| pubmed-article:8631758 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8631758 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:8631758 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:8631758 | lifeskim:mentions | umls-concept:C0090388 | lld:lifeskim |
| pubmed-article:8631758 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:8631758 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8631758 | lifeskim:mentions | umls-concept:C0282604 | lld:lifeskim |
| pubmed-article:8631758 | lifeskim:mentions | umls-concept:C0086816 | lld:lifeskim |
| pubmed-article:8631758 | lifeskim:mentions | umls-concept:C0300500 | lld:lifeskim |
| pubmed-article:8631758 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:8631758 | pubmed:dateCreated | 1996-7-3 | lld:pubmed |
| pubmed-article:8631758 | pubmed:abstractText | The zeta-form 14-3-3 protein (14-3-3zeta) regulates protein kinases and interacts with several signaling molecules. We reported previously that a platelet adhesion receptor, glycoprotein (GP) Ib-IX, was associated with a 29-kDa protein with partial sequences identical to 14-3-3zeta. In this study, the interaction between GPIb-IX and recombinant 14-3-3zeta is reconstituted. Further, we show that the 14-3-3zeta binding site in GPIb is within a 15 residue sequence at the C terminus of GPIb-alpha, as indicated by antibody inhibition and direct binding of 14-3-3zeta to synthetic GPIb-alpha cytoplasmic domain peptides. The 14-3-3zeta binds to recombinant wild type GPIb-IX but not to the GPIb-alpha mutants lacking C-terminal 5 or more residues, suggesting that the C-terminal 5 residues of GPIb-alpha are critical. Similarity between the GPIb-alpha C-terminal sequence and the serine-rich regions of Raf and Bcr kinases suggests a possible serine-rich recognition motif for the 14-3-3 protein. | lld:pubmed |
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| pubmed-article:8631758 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8631758 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8631758 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8631758 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8631758 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8631758 | pubmed:author | pubmed-author:FoxJ EJE | lld:pubmed |
| pubmed-article:8631758 | pubmed:author | pubmed-author:ZhuZ TZT | lld:pubmed |
| pubmed-article:8631758 | pubmed:author | pubmed-author:PelPP | lld:pubmed |
| pubmed-article:8631758 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8631758 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:8631758 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8631758 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8631758 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8631758 | pubmed:pagination | 7362-7 | lld:pubmed |
| pubmed-article:8631758 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8631758 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8631758 | pubmed:articleTitle | Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ib alpha. | lld:pubmed |
| pubmed-article:8631758 | pubmed:affiliation | Department of Vascular Biology, Scripps Research Institute, La Jolla, California 92037, USA. | lld:pubmed |
| pubmed-article:8631758 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8631758 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8631758 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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