Regulation of SHP-1 tyrosine phosphatase in human platelets by serine phosphorylation at its C terminus

Journal of Biological Chemistry

Volumn 279, Issue 39, 2004, Pages 40475-40483

  Jones, Matthew L ^a   Craik, Johnathan D ^a   Gibbins, Jonathan M ^b   Poole, Alastair W ^a  

^a SCHOOL OF MEDICAL SCIENCES   (United Kingdom)

^b UNIVERSITY OF READING   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CELLS; ENZYME INHIBITION; HUMAN ENGINEERING; IMMUNOLOGY; SUBSTRATES;

HUMAN PLATELETS; PHOSPHORYLATION; TYROSINE PHOSPHATASE;

ENZYMES;

AMINO ACID; EGTAZIC ACID; MONOCLONAL ANTIBODY; PHORBOL 13 ACETATE 12 MYRISTATE; PLASMID DNA; PROTEIN KINASE C ALPHA; PROTEIN SH2; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEINASE ACTIVATED RECEPTOR 1; PROTEINASE ACTIVATED RECEPTOR 4; SERINE; THROMBIN; THROMBIN RECEPTOR; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ASSAY; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; HUMAN; HUMAN CELL; IMMUNOBLOTTING; IMMUNOPRECIPITATION; MUTAGENESIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PURIFICATION; THROMBOCYTE;

AMINO ACID SEQUENCE; BLOOD PLATELETS; CELL LINE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENE EXPRESSION REGULATION; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTATHIONE TRANSFERASE; GREEN FLUORESCENT PROTEINS; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; LUMINESCENT PROTEINS; MICROSCOPY, CONFOCAL; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; ONCOGENE PROTEINS; PHOSPHORYLATION; PRECIPITIN TESTS; PROTEIN KINASE C; PROTEIN KINASE C-ALPHA; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; PROTEIN-TYROSINE-PHOSPHATASE; PROTO-ONCOGENE PROTEINS C-VAV; RECEPTOR, PAR-1; RECEPTORS, THROMBIN; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; SHP1 PROTEIN TYROSINE PHOSPHATASE; SRC HOMOLOGY DOMAINS; SUBSTRATE SPECIFICITY; THROMBIN; TYROSINE;

ESCHERICHIA COLI;

EID: 4644314870     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M402970200     Document Type: Article

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