| pubmed-article:11478859 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C1880352 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C1707798 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C0183362 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:11478859 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:11478859 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11478859 | pubmed:dateCreated | 2001-7-31 | lld:pubmed |
| pubmed-article:11478859 | pubmed:abstractText | p47 is the major protein identified in complex with the cytosolic AAA ATPase p97. It functions as an essential cofactor of p97-regulated membrane fusion, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of membrane fusion. Here, we report the high-resolution NMR structure of the C-terminal domain from p47. It comprises a UBX domain and a 13 residue long structured N-terminal extension. The UBX domain adopts a characteristic ubiquitin fold with a betabetaalphabetabetaalphabeta secondary structure arrangement. Three hydrophobic residues from the N-terminal extension pack closely against a cleft in the UBX domain. We also identify, for the first time, the p97 interaction surface using NMR chemical shift perturbation studies. | lld:pubmed |
| pubmed-article:11478859 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478859 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11478859 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11478859 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11478859 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11478859 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11478859 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:11478859 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:11478859 | pubmed:author | pubmed-author:KondoHH | lld:pubmed |
| pubmed-article:11478859 | pubmed:author | pubmed-author:ShawAA | lld:pubmed |
| pubmed-article:11478859 | pubmed:author | pubmed-author:LallyJJ | lld:pubmed |
| pubmed-article:11478859 | pubmed:author | pubmed-author:MatthewsSS | lld:pubmed |
| pubmed-article:11478859 | pubmed:author | pubmed-author:ZhangXX | lld:pubmed |
| pubmed-article:11478859 | pubmed:author | pubmed-author:FreemontP SPS | lld:pubmed |
| pubmed-article:11478859 | pubmed:author | pubmed-author:YuanXX | lld:pubmed |
| pubmed-article:11478859 | pubmed:copyrightInfo | Copyright 2001 Academic Press. | lld:pubmed |
| pubmed-article:11478859 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11478859 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:11478859 | pubmed:volume | 311 | lld:pubmed |
| pubmed-article:11478859 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11478859 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11478859 | pubmed:pagination | 255-63 | lld:pubmed |
| pubmed-article:11478859 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:11478859 | pubmed:meshHeading | pubmed-meshheading:11478859... | lld:pubmed |
| pubmed-article:11478859 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11478859 | pubmed:articleTitle | Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly. | lld:pubmed |
| pubmed-article:11478859 | pubmed:affiliation | Department of Biological Sciences, Wolfson Laboratories, Imperial College of Science Technology and Medicine, London, South Kensington, SW7 2AY, UK. | lld:pubmed |
| pubmed-article:11478859 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11478859 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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