Correlation of the phosphorylation states of pp60c-src with tyrosine kinase activity: the intramolecular pY530-SH2 complex retains significant activity if Y419 is phosphorylated.
Boerner, R J
Correlation of the phosphorylation states of pp60c-src with tyrosine kinase activity: the intramolecular pY530-SH2 complex retains significant activity if Y419 is phosphorylated. [electronic resource] - Biochemistry Jul 1996 - 9519-25 p. digital
Publication Type: Journal Article
0006-2960
10.1021/bi960248u doi
Adenosine Triphosphate--metabolism
Amino Acid Sequence
Chromatography, Affinity
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Kinetics
Mass Spectrometry
Molecular Sequence Data
Phosphopeptides--chemistry
Phosphorylation
Protein-Tyrosine Kinases--metabolism
Proto-Oncogene Proteins pp60(c-src)--metabolism
Recombinant Proteins--metabolism
Spectrophotometry
Trypsin--metabolism
Tyrosine--metabolism
src Homology Domains
Correlation of the phosphorylation states of pp60c-src with tyrosine kinase activity: the intramolecular pY530-SH2 complex retains significant activity if Y419 is phosphorylated. [electronic resource] - Biochemistry Jul 1996 - 9519-25 p. digital
Publication Type: Journal Article
0006-2960
10.1021/bi960248u doi
Adenosine Triphosphate--metabolism
Amino Acid Sequence
Chromatography, Affinity
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Kinetics
Mass Spectrometry
Molecular Sequence Data
Phosphopeptides--chemistry
Phosphorylation
Protein-Tyrosine Kinases--metabolism
Proto-Oncogene Proteins pp60(c-src)--metabolism
Recombinant Proteins--metabolism
Spectrophotometry
Trypsin--metabolism
Tyrosine--metabolism
src Homology Domains