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41001
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Purification of mouse liver benzene dihydrodiol dehydrogenases
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41002
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Purification of mouse liver benzene dihydrodiol dehydrogenases
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41003
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Purification of mouse liver benzene dihydrodiol dehydrogenases
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41004
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Purification of mouse liver benzene dihydrodiol dehydrogenases
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41005
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41006
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41007
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41008
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41009
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41010
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41011
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41012
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41013
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41014
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myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb
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41015
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41016
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41017
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41018
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41019
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41020
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41021
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41022
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41023
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41024
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41025
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41026
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41027
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41028
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41029
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41030
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41031
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41032
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41033
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41034
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41035
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41036
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41037
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41038
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41039
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41040
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41041
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41042
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41043
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41044
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41045
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41046
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41047
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41048
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41049
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41050
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41051
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41052
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41053
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41054
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41055
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41056
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41057
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41058
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41059
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41060
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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
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41061
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Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
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41062
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Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
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41063
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Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
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41064
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Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
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41065
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Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
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41066
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Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
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41067
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Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
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41068
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Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
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41069
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41070
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41071
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41072
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41073
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41074
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41075
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41076
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41077
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41078
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41079
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41080
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41081
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41082
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41083
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41084
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41085
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41086
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41087
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41088
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41089
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41090
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41091
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41092
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41093
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41094
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41095
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41096
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41097
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41098
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41099
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41100
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41101
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41102
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41103
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41104
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Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from ...
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41105
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Identification of the catalytic nucleophile in Family 42 beta-galactosidases by intermediate trapping and ...
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41106
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Identification of the catalytic nucleophile in Family 42 beta-galactosidases by intermediate trapping and ...
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41107
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Identification of the catalytic nucleophile in Family 42 beta-galactosidases by intermediate trapping and ...
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41108
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Identification of the catalytic nucleophile in Family 42 beta-galactosidases by intermediate trapping and ...
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41109
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Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at ...
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41110
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Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at ...
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41111
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Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at ...
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41112
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41113
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41114
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41115
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41116
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41117
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41118
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41119
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41120
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41121
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41122
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41123
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41124
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41125
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41126
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Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of catalytically essential ...
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41127
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Adenosine triphosphate-adenosine-5`-monophosphate phosphotransferase from normal human liver mitochondria. ...
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41128
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Adenosine triphosphate-adenosine-5`-monophosphate phosphotransferase from normal human liver mitochondria. ...
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41129
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Adenosine triphosphate-adenosine-5`-monophosphate phosphotransferase from normal human liver mitochondria. ...
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41130
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Adenosine triphosphate-adenosine-5`-monophosphate phosphotransferase from normal human liver mitochondria. ...
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41131
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41132
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41133
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41134
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41135
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41136
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41137
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41138
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41139
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41140
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41141
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41142
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41143
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41144
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41145
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41146
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41147
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41148
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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|
41149
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An acyl-coenzyme A chain length dependent assay for 3-oxoacyl-coenzyme A thiolases employing ...
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41150
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41151
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41152
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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|
41153
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41154
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41155
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41156
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41157
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41158
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41159
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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41160
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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|
41161
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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|
41162
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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|
41163
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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|
41164
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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|
41165
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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|
41166
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
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|
41167
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41168
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41169
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41170
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41171
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41172
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41173
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41174
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41175
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41176
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41177
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41178
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41179
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41180
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41181
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41182
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41183
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41184
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41185
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41186
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41187
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41188
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41189
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41190
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41191
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41192
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41193
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41194
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41195
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41196
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41197
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41198
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41199
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41200
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41201
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41202
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41203
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41204
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41205
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41206
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41207
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41208
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41209
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41210
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41211
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41212
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41213
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41214
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41215
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41216
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41217
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41218
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41219
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41220
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41221
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41222
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41223
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41224
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41225
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41226
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41227
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41228
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41229
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41230
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41231
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41232
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41233
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41234
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41235
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41236
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41237
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41238
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41239
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41240
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41241
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41242
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41243
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41244
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41245
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41246
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41247
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41248
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41249
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41250
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41251
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41252
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41253
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41254
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41255
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41256
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41257
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41258
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41259
|
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase ...
|
|
41260
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41261
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41262
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41263
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41264
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41265
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41266
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41267
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41268
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41269
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41270
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41271
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41272
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41273
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41274
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41275
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41276
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41277
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41278
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41279
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41280
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41281
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41282
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41283
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41284
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41285
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41286
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41287
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41288
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41289
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41290
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41291
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41292
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41293
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41294
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41295
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41296
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41297
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41298
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41299
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41300
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41301
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41302
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41303
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41304
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41305
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41306
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41307
|
The kinetics, substrate and inhibitor specificity of the lactate transporter of Ehrlich-Lettre tumour cells ...
|
|
41308
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41309
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41310
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41311
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41312
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41313
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41314
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41315
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41316
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41317
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41318
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41319
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41320
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41321
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41322
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41323
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41324
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41325
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41326
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41327
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41328
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41329
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41330
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41331
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41332
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41333
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41334
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41335
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41336
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41337
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41338
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41339
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41340
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41341
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41342
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41343
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41344
|
The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver ...
|
|
41345
|
Characterization of the inactivation of rat fatty acid synthase by C75: Inhibition of partial reactions and ...
|
|
41346
|
Characterization of the inactivation of rat fatty acid synthase by C75: Inhibition of partial reactions and ...
|
|
41347
|
Characterization of the inactivation of rat fatty acid synthase by C75: Inhibition of partial reactions and ...
|
|
41348
|
Characterization of the inactivation of rat fatty acid synthase by C75: Inhibition of partial reactions and ...
|
|
41349
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41350
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41351
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41352
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41353
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41354
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41355
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41356
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41357
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41358
|
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by ...
|
|
41359
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41360
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41361
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41362
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41363
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41364
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41365
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41366
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41367
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41368
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41369
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41370
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41371
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41372
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41373
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41374
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41375
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41376
|
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol ...
|
|
41377
|
Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated ...
|
|
41378
|
Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated ...
|
|
41379
|
Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated ...
|
|
41380
|
Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated ...
|
|
41381
|
Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting as a novel auxiliary enzyme in ...
|
|
41382
|
Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting as a novel auxiliary enzyme in ...
|
|
41383
|
Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting as a novel auxiliary enzyme in ...
|
|
41384
|
Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and ...
|
|
41385
|
Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and ...
|
|
41386
|
Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and ...
|
|
41387
|
Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and ...
|
|
41388
|
Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and ...
|
|
41389
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41390
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41391
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41392
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41393
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41394
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41395
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41396
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41397
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41398
|
The purification and properties of myo-inositol monophosphatase from bovine brain.
|
|
41399
|
Aerobic benzoyl-coenzyme A (CoA) catabolic pathway in Azoarcus evansii: conversion of ring cleavage product by ...
|
|
41400
|
Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in ...
|
|
41401
|
Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in ...
|
|
41402
|
The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate
|
|
41403
|
Malolactic enzyme of Lactobacillus plantarum. Purification, properties, and distribution among bacteria
|
|
41404
|
Malolactic enzyme of Lactobacillus plantarum. Purification, properties, and distribution among bacteria
|
|
41405
|
Malolactic enzyme of Lactobacillus plantarum. Purification, properties, and distribution among bacteria
|
|
41406
|
Intramolecular regulation of the opposing (p)ppGpp catalytic activities of Rel(Seq), the Rel/Spo enzyme from ...
|
|
41407
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41408
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41409
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41410
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41411
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41412
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41413
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41414
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41415
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41416
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41417
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41418
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41419
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41420
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41421
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41422
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41423
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41424
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41425
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41426
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41427
|
Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
|
|
41428
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41429
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41430
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41431
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41432
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41433
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41434
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41435
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41436
|
Influence of water-miscible organic solvents on kinetics and enantioselectivity of the (R)-specific alcohol ...
|
|
41437
|
The macrophage migration inhibitory factor MIF is a phenylpyruvate tautomerase
|
|
41438
|
The macrophage migration inhibitory factor MIF is a phenylpyruvate tautomerase
|
|
41439
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41440
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41441
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41442
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41443
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41444
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41445
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41446
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41447
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41448
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41449
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41450
|
Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine ...
|
|
41451
|
C-terminal end and aminoacid Lys48 in HMG-CoA lyase are involved in substrate binding and enzyme activity
|
|
41452
|
C-terminal end and aminoacid Lys48 in HMG-CoA lyase are involved in substrate binding and enzyme activity
|
|
41453
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41454
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41455
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41456
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41457
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41458
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41459
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41460
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41461
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41462
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41463
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41464
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41465
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41466
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41467
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41468
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41469
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41470
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41471
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41472
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41473
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41474
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41475
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41476
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41477
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41478
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41479
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41480
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41481
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41482
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41483
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41484
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41485
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41486
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41487
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41488
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41489
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41490
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41491
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41492
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41493
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41494
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41495
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41496
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41497
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41498
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41499
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41500
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41501
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41502
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41503
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41504
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41505
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41506
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41507
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41508
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41509
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41510
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41511
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41512
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41513
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41514
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41515
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41516
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41517
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41518
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41519
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41520
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41521
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41522
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41523
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41524
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41525
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41526
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41527
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41528
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41529
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41530
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41531
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41532
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41533
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41534
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41535
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41536
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41537
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41538
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41539
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41540
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41541
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41542
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41543
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41544
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41545
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41546
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41547
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41548
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41549
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41550
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41551
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41552
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41553
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41554
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41555
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41556
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41557
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41558
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41559
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41560
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41561
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41562
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41563
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41564
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41565
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41566
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41567
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41568
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41569
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41570
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41571
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41572
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41573
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41574
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41575
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41576
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41577
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41578
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41579
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41580
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41581
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41582
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41583
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41584
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41585
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41586
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41587
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41588
|
Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and ...
|
|
41589
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41590
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41591
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41592
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41593
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41594
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41595
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41596
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41597
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41598
|
Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate ...
|
|
41599
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41600
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41601
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41602
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41603
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41604
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41605
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41606
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41607
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41608
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41609
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41610
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41611
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41612
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41613
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41614
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41615
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41616
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41617
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41618
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41619
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41620
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41621
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41622
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41623
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41624
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41625
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41626
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41627
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41628
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41629
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41630
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41631
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41632
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41633
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41634
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41635
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41636
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41637
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41638
|
Phosphoramidate pronucleotides: a comparison of the phosphoramidase substrate specificity of human and ...
|
|
41639
|
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto ...
|
|
41640
|
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto ...
|
|
41641
|
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto ...
|
|
41642
|
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto ...
|
|
41643
|
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto ...
|
|
41644
|
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto ...
|
|
41645
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41646
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41647
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41648
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41649
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41650
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41651
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41652
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41653
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41654
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41655
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41656
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41657
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41658
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41659
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41660
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41661
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41662
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41663
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41664
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41665
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41666
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41667
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41668
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41669
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41670
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41671
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41672
|
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
|
|
41673
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41674
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41675
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41676
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41677
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41678
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41679
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41680
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41681
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41682
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41683
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41684
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41685
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41686
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41687
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41688
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41689
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41690
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41691
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41692
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41693
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41694
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41695
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41696
|
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially ...
|
|
41697
|
Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction ...
|
|
41698
|
Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction ...
|
|
41699
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41700
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41701
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41702
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41703
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41704
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41705
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41706
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41707
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41708
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41709
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41710
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41711
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41712
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41713
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41714
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41715
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41716
|
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
|
|
41717
|
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
|
|
41718
|
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
|
|
41719
|
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
|
|
41720
|
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
|
|
41721
|
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
|
|
41722
|
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
|
|
41723
|
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
|
|
41724
|
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
|
|
41725
|
A novel beta-galactosidase capable of glycosyl transfer from Enterobacter agglomerans B1
|
|
41726
|
A novel beta-galactosidase capable of glycosyl transfer from Enterobacter agglomerans B1
|
|
41727
|
Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme
|
|
41728
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41729
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41730
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41731
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41732
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41733
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41734
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41735
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41736
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41737
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41738
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41739
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41740
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41741
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41742
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41743
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41744
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41745
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41746
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41747
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41748
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41749
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41750
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41751
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41752
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41753
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41754
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41755
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41756
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41757
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41758
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41759
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41760
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41761
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41762
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41763
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41764
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41765
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41766
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41767
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41768
|
Diverging Substrate Specificity of Pure Human Thymidine Kinases 1 and 2 Against Antiviral Dideoxynucleosides
|
|
41769
|
Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase
|
|
41770
|
Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase
|
|
41771
|
Nuclear export of the DEAD box An3 protein by CRM1 is coupled to An3 helicase activity
|
|
41772
|
Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of ...
|
|
41773
|
Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of ...
|
|
41774
|
Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of ...
|
|
41775
|
Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of ...
|
|
41776
|
Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of ...
|
|
41777
|
Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of ...
|
|
41778
|
An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces ...
|
|
41779
|
An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces ...
|
|
41780
|
Purification and properties of lactaldehyde dehydrogenase from Escherichia coli
|
|
41781
|
Purification and properties of lactaldehyde dehydrogenase from Escherichia coli
|
|
41782
|
Biochemical characterization of androgen receptor-interacting protein 4
|
|
41783
|
Biochemical characterization of androgen receptor-interacting protein 4
|
|
41784
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41785
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41786
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41787
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41788
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41789
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41790
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41791
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41792
|
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is ...
|
|
41793
|
Gene expression and characterization of a stress-induced tyrosine decarboxylase from Arabidopsis thaliana
|
|
41794
|
Continuous spectrophotometric assay of peptide deformylase
|
|
41795
|
Continuous spectrophotometric assay of peptide deformylase
|
|
41796
|
Continuous spectrophotometric assay of peptide deformylase
|
|
41797
|
Continuous spectrophotometric assay of peptide deformylase
|
|
41798
|
Continuous spectrophotometric assay of peptide deformylase
|
|
41799
|
Continuous spectrophotometric assay of peptide deformylase
|
|
41800
|
Some kinetic properties of Bacillus subtilis glutamine synthetase
|
|
41801
|
Some kinetic properties of Bacillus subtilis glutamine synthetase
|
|
41802
|
Some kinetic properties of Bacillus subtilis glutamine synthetase
|
|
41803
|
Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27
|
|
41804
|
Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27
|
|
41805
|
Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus ...
|
|
41806
|
Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus ...
|
|
41807
|
Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus ...
|
|
41808
|
Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus ...
|
|
41809
|
Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus ...
|
|
41810
|
Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus ...
|
|
41811
|
Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus ...
|
|
41812
|
Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus ...
|
|
41813
|
Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilus
|
|
41814
|
Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilus
|
|
41815
|
Identification and purification of glucose phosphate isomerase of Plasmodium falciparum
|
|
41816
|
Identification and purification of glucose phosphate isomerase of Plasmodium falciparum
|
|
41817
|
Identification and purification of glucose phosphate isomerase of Plasmodium falciparum
|
|
41818
|
Identification and purification of glucose phosphate isomerase of Plasmodium falciparum
|
|
41819
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41820
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41821
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41822
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41823
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41824
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41825
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41826
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41827
|
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, ...
|
|
41828
|
Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase
|
|
41829
|
Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase
|
|
41830
|
Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase
|
|
41831
|
Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase
|
|
41832
|
Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase
|
|
41833
|
An operon from Lactobacillus helveticus composed of a proline iminopeptidase gene (pepI) and two genes coding ...
|
|
41834
|
An h.p.l.c. assay for protoporphyrinogen oxidase activity in rat liver
|
|
41835
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41836
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41837
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41838
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41839
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41840
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41841
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41842
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41843
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41844
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41845
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41846
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41847
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41848
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41849
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41850
|
Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5`-phosphate
|
|
41851
|
Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus
|
|
41852
|
Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus
|
|
41853
|
Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus
|
|
41854
|
Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus
|
|
41855
|
Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus
|
|
41856
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41857
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41858
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41859
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41860
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41861
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41862
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41863
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41864
|
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL ...
|
|
41865
|
Alpha-amylase from germinating soybean (Glycine max) seeds--purification, characterization and sequential ...
|
|
41866
|
Alpha-amylase from germinating soybean (Glycine max) seeds--purification, characterization and sequential ...
|
|
41867
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41868
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41869
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41870
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41871
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41872
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41873
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41874
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41875
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41876
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41877
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41878
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41879
|
Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site
|
|
41880
|
Novel flavonol 3-sulfotransferase. Purification, kinetic properties, and partial amino acid sequence
|
|
41881
|
Novel flavonol 3-sulfotransferase. Purification, kinetic properties, and partial amino acid sequence
|
|
41882
|
Novel flavonol 3-sulfotransferase. Purification, kinetic properties, and partial amino acid sequence
|
|
41883
|
Novel flavonol 3-sulfotransferase. Purification, kinetic properties, and partial amino acid sequence
|
|
41884
|
Novel flavonol 3-sulfotransferase. Purification, kinetic properties, and partial amino acid sequence
|
|
41885
|
Novel flavonol 3-sulfotransferase. Purification, kinetic properties, and partial amino acid sequence
|
|
41886
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41887
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41888
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41889
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41890
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41891
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41892
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41893
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41894
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41895
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41896
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41897
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41898
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41899
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41900
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41901
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41902
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41903
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41904
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41905
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41906
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41907
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41908
|
The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for ...
|
|
41909
|
Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to ...
|
|
41910
|
Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to ...
|
|
41911
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41912
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41913
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41914
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41915
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41916
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41917
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41918
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41919
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41920
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41921
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41922
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41923
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41924
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41925
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41926
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41927
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41928
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41929
|
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
|
|
41930
|
Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii ...
|
|
41931
|
Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii ...
|
|
41932
|
Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii ...
|
|
41933
|
Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii ...
|
|
41934
|
Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii ...
|
|
41935
|
Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii ...
|
|
41936
|
Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family
|
|
41937
|
Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family
|
|
41938
|
Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarum
|
|
41939
|
Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarum
|
|
41940
|
Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8
|
|
41941
|
Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8
|
|
41942
|
Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8
|
|
41943
|
Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8
|
|
41944
|
Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from ...
|
|
41945
|
Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from ...
|
|
41946
|
Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization ...
|
|
41947
|
Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization ...
|
|
41948
|
Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization ...
|
|
41949
|
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of ...
|
|
41950
|
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of ...
|
|
41951
|
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of ...
|
|
41952
|
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of ...
|
|
41953
|
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of ...
|
|
41954
|
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of ...
|
|
41955
|
Bovine pyruvate kinases. II. Purification of the liver isozyme and its hybridization with skeletal muscle ...
|
|
41956
|
Bovine pyruvate kinases. II. Purification of the liver isozyme and its hybridization with skeletal muscle ...
|
|
41957
|
Bovine pyruvate kinases. II. Purification of the liver isozyme and its hybridization with skeletal muscle ...
|
|
41958
|
Bovine pyruvate kinases. II. Purification of the liver isozyme and its hybridization with skeletal muscle ...
|
|
41959
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41960
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41961
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41962
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41963
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41964
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41965
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41966
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41967
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41968
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41969
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41970
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41971
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41972
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41973
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41974
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41975
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41976
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41977
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41978
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41979
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41980
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41981
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41982
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41983
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41984
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41985
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41986
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41987
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41988
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41989
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41990
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41991
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41992
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41993
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41994
|
Mutational analysis of domain II of flavonol 3-sulfotransferase
|
|
41995
|
Histidine decarboxylase of Lactobacillus 30a. VI. Mechanism of action and kinetic properties
|
|
41996
|
Histidine decarboxylase of Lactobacillus 30a. VI. Mechanism of action and kinetic properties
|
|
41997
|
Histidine decarboxylase of Lactobacillus 30a. VI. Mechanism of action and kinetic properties
|
|
41998
|
Identification of amino acid residues critical for catalysis and cosubstrate binding in the flavonol ...
|
|
41999
|
Identification of amino acid residues critical for catalysis and cosubstrate binding in the flavonol ...
|
|
42000
|
Identification of amino acid residues critical for catalysis and cosubstrate binding in the flavonol ...
|
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