Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity.
Boerner, R J
Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity. [electronic resource] - Biochemistry Nov 1995 - 15351-8 p. digital
Publication Type: Journal Article
0006-2960
10.1021/bi00046a044 doi
Amino Acid Sequence
Binding Sites
Calcium--pharmacology
Catalysis
Chromatography, High Pressure Liquid
Disulfides--metabolism
Edetic Acid--pharmacology
Enzyme Inhibitors--pharmacology
Humans
Isoelectric Focusing
Kinetics
Magnesium--pharmacology
Magnetic Resonance Spectroscopy
Mass Spectrometry
Molecular Sequence Data
Mutagenesis, Site-Directed
Peptide Fragments--metabolism
Phosphoric Monoester Hydrolases--antagonists & inhibitors
Phosphorylation
Proto-Oncogene Proteins pp60(c-src)--chemistry
Recombinant Proteins--metabolism
Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity. [electronic resource] - Biochemistry Nov 1995 - 15351-8 p. digital
Publication Type: Journal Article
0006-2960
10.1021/bi00046a044 doi
Amino Acid Sequence
Binding Sites
Calcium--pharmacology
Catalysis
Chromatography, High Pressure Liquid
Disulfides--metabolism
Edetic Acid--pharmacology
Enzyme Inhibitors--pharmacology
Humans
Isoelectric Focusing
Kinetics
Magnesium--pharmacology
Magnetic Resonance Spectroscopy
Mass Spectrometry
Molecular Sequence Data
Mutagenesis, Site-Directed
Peptide Fragments--metabolism
Phosphoric Monoester Hydrolases--antagonists & inhibitors
Phosphorylation
Proto-Oncogene Proteins pp60(c-src)--chemistry
Recombinant Proteins--metabolism