| pubmed-article:9148966 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C0058836 | lld:lifeskim |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C0170270 | lld:lifeskim |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C0282535 | lld:lifeskim |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C1514490 | lld:lifeskim |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C0079160 | lld:lifeskim |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:9148966 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:9148966 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:9148966 | pubmed:dateCreated | 1997-6-19 | lld:pubmed |
| pubmed-article:9148966 | pubmed:abstractText | Amphiphysin is an SH3 domain-containing neuronal protein that is highly concentrated in nerve terminals where it interacts via its SH3 domain with dynamin I, a GTPase implicated in synaptic vesicle endocytosis. We show here that the SH3 domain of amphiphysin, but not a mutant SH3 domain, bound with high affinity to a single site in the long proline-rich region of human dynamin I, that this site was distinct from the binding sites for other SH3 domains, and that the mutation of two adjacent amino acids in dynamin I was sufficient to abolish binding. The dynamin I sequence critically required for amphiphysin binding (PSRPNR) fits in the novel SH3 binding consensus identified for the SH3 domain of amphiphysin via a combinatorial peptide library approach: PXRPXR(H)R(H). Our data demonstrate that the long proline-rich stretch present in dynamin I contained multiple SH3 domain binding sites that recognize interacting proteins with high specificity. | lld:pubmed |
| pubmed-article:9148966 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9148966 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9148966 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9148966 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9148966 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9148966 | pubmed:month | May | lld:pubmed |
| pubmed-article:9148966 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9148966 | pubmed:author | pubmed-author:DavidCC | lld:pubmed |
| pubmed-article:9148966 | pubmed:author | pubmed-author:LynchMM | lld:pubmed |
| pubmed-article:9148966 | pubmed:author | pubmed-author:CantleyL CLC | lld:pubmed |
| pubmed-article:9148966 | pubmed:author | pubmed-author:De CamilliPP | lld:pubmed |
| pubmed-article:9148966 | pubmed:author | pubmed-author:SlepnevV IVI | lld:pubmed |
| pubmed-article:9148966 | pubmed:author | pubmed-author:GrabsDD | lld:pubmed |
| pubmed-article:9148966 | pubmed:author | pubmed-author:SongyangZZ | lld:pubmed |
| pubmed-article:9148966 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9148966 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:9148966 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:9148966 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9148966 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9148966 | pubmed:pagination | 13419-25 | lld:pubmed |
| pubmed-article:9148966 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9148966 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9148966 | pubmed:articleTitle | The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence. | lld:pubmed |
| pubmed-article:9148966 | pubmed:affiliation | Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, Boyer Center for Molecular Medicine, New Haven, Connecticut 06510, USA. | lld:pubmed |
| pubmed-article:9148966 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9148966 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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