| pubmed-article:20007713 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C1537395 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:20007713 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:20007713 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:20007713 | pubmed:dateCreated | 2010-2-15 | lld:pubmed |
| pubmed-article:20007713 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20007713 | pubmed:abstractText | E3 ubiquitin ligases catalyze the final step of ubiquitin conjugation and regulate numerous cellular processes. The HECT class of E3 ubiquitin (Ub) ligases directly transfers Ub from bound E2 enzyme to a myriad of substrates. The catalytic domain of HECT Ub ligases has a bilobal architecture that separates the E2 binding region and catalytic site. An important question regarding HECT domain function is the control of ligase activity and specificity. Here we present a functional analysis of the HECT domain of the E3 ligase HUWE1 based on crystal structures and show that a single N-terminal helix significantly stabilizes the HECT domain. We observe that this element modulates HECT domain activity, as measured by self-ubiquitination induced in the absence of this helix, as distinct from its effects on Ub conjugation of substrate Mcl-1. Such subtle changes to the protein may be at the heart of the vast spectrum of substrate specificities displayed by HECT domain E3 ligases. | lld:pubmed |
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| pubmed-article:20007713 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20007713 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20007713 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20007713 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20007713 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20007713 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20007713 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20007713 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:20007713 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20007713 | pubmed:author | pubmed-author:PloeghHidde... | lld:pubmed |
| pubmed-article:20007713 | pubmed:author | pubmed-author:SchwartzThoma... | lld:pubmed |
| pubmed-article:20007713 | pubmed:author | pubmed-author:LoveKerry... | lld:pubmed |
| pubmed-article:20007713 | pubmed:author | pubmed-author:PandyaRenuka... | lld:pubmed |
| pubmed-article:20007713 | pubmed:author | pubmed-author:PartridgeJame... | lld:pubmed |
| pubmed-article:20007713 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20007713 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:20007713 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20007713 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20007713 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20007713 | pubmed:pagination | 5664-73 | lld:pubmed |
| pubmed-article:20007713 | pubmed:dateRevised | 2011-7-25 | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:meshHeading | pubmed-meshheading:20007713... | lld:pubmed |
| pubmed-article:20007713 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20007713 | pubmed:articleTitle | A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities. | lld:pubmed |
| pubmed-article:20007713 | pubmed:affiliation | Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142, USA. | lld:pubmed |
| pubmed-article:20007713 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20007713 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:20007713 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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