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rdf:type |
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lifeskim:mentions |
umls-concept:C0004927,
umls-concept:C0033684,
umls-concept:C0038592,
umls-concept:C0085536,
umls-concept:C0443199,
umls-concept:C0851285,
umls-concept:C1335280,
umls-concept:C1335283,
umls-concept:C1705637,
umls-concept:C1706044,
umls-concept:C1710082
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pubmed:issue |
4
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pubmed:dateCreated |
2002-2-8
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pubmed:abstractText |
The substrate specificity of catalytic domains and the activation of full length protein tyrosine phosphatases, SHP-1 and SHP-2 have been investigated using synthetic phosphotyrosyl peptides derived from SIPRalpha1. We found that the catalytic domains of SHP-1 and SHP-2 exhibit different substrate specificity towards a longer trideca-peptide pY(469+3) ((-7)RPEDTLTpYADLDM(+5)) and not to the shorter decapeptide pY(469) ((-5)EDTLTpYADLD(+4)), the former being the substrate of SHP-2 only. Furthermore, the activation of full-length SHP-1 and not the SHP-2 by the deca/trideca-peptides suggested SIRPalpha 1 to be possibly acting as both an upstream activator and a substrate for SHP-1, and merely as the downstream substrate for SHP-2 in signaling events.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neural Cell Adhesion Molecule L1,
http://linkedlifedata.com/resource/pubmed/chemical/Neural Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic
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pubmed:status |
MEDLINE
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pubmed:issn |
0730-2312
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2002 Wiley?Liss, Inc.
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pubmed:issnType |
Print
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
840-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11835408-Antigens, Differentiation,
pubmed-meshheading:11835408-Catalytic Domain,
pubmed-meshheading:11835408-Enzyme Activation,
pubmed-meshheading:11835408-Humans,
pubmed-meshheading:11835408-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:11835408-Kinetics,
pubmed-meshheading:11835408-Membrane Glycoproteins,
pubmed-meshheading:11835408-Neural Cell Adhesion Molecule L1,
pubmed-meshheading:11835408-Neural Cell Adhesion Molecules,
pubmed-meshheading:11835408-Oligopeptides,
pubmed-meshheading:11835408-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:11835408-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:11835408-Protein Tyrosine Phosphatases,
pubmed-meshheading:11835408-Receptors, Immunologic,
pubmed-meshheading:11835408-Substrate Specificity
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pubmed:year |
2002
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pubmed:articleTitle |
Substrate specificity of protein tyrosine phosphatase: differential behavior of SHP-1 and SHP-2 towards signal regulation protein SIRPalpha1.
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pubmed:affiliation |
Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, Massachusetts 01605, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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