pubmed-article:17448445 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C0008633 | lld:lifeskim |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
pubmed-article:17448445 | lifeskim:mentions | umls-concept:C1706765 | lld:lifeskim |
pubmed-article:17448445 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:17448445 | pubmed:dateCreated | 2007-5-2 | lld:pubmed |
pubmed-article:17448445 | pubmed:abstractText | Chromosome segregation and proper alignment in mitosis relies on cohesion between sister chromatids and the interaction of the kinetochore with spindle microtubules. Vertebrate Sgo 1 localizes to kinetochores and is required to prevent premature sister centromere separation in mitosis. Sgo 1 is degraded by the anaphase-promoting complex, allowing the separation of sister centromeres in anaphase. However, little is known about the molecular basis of Sgo 1 degradation and its temporal control during mitosis. Here, we show that APC/C targets human Sgo 1 for degradation through a destruction box motif (D-box) in its C-terminus. Mutation in the D-box causes transient metaphase arrest, and mutation in the D-box leads to defects in chromosome alignment and segregation through its effect on the localization of Aurora B and CENP-E. These results provide a link between sister centromere cohesion and bipolar attachment of kinetochores. | lld:pubmed |
pubmed-article:17448445 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:language | eng | lld:pubmed |
pubmed-article:17448445 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17448445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17448445 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17448445 | pubmed:month | Jun | lld:pubmed |
pubmed-article:17448445 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:17448445 | pubmed:author | pubmed-author:HILDWW | lld:pubmed |
pubmed-article:17448445 | pubmed:author | pubmed-author:YaoXuebiaoX | lld:pubmed |
pubmed-article:17448445 | pubmed:author | pubmed-author:GuoZhenZ | lld:pubmed |
pubmed-article:17448445 | pubmed:author | pubmed-author:YangYongY | lld:pubmed |
pubmed-article:17448445 | pubmed:author | pubmed-author:FuGuoshengG | lld:pubmed |
pubmed-article:17448445 | pubmed:author | pubmed-author:WardTarshaT | lld:pubmed |
pubmed-article:17448445 | pubmed:author | pubmed-author:HuaShashaS | lld:pubmed |
pubmed-article:17448445 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17448445 | pubmed:day | 8 | lld:pubmed |
pubmed-article:17448445 | pubmed:volume | 357 | lld:pubmed |
pubmed-article:17448445 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17448445 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17448445 | pubmed:pagination | 672-8 | lld:pubmed |
pubmed-article:17448445 | pubmed:dateRevised | 2011-7-11 | lld:pubmed |
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pubmed-article:17448445 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17448445 | pubmed:articleTitle | D-box is required for the degradation of human Shugoshin and chromosome alignment. | lld:pubmed |
pubmed-article:17448445 | pubmed:affiliation | Laboratory of Cellular Dynamics, University of Science & Technology of China, Hefei National Laboratory, Hefei 230027, China. | lld:pubmed |
pubmed-article:17448445 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17448445 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:17448445 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:151648 | entrezgene:pubmed | pubmed-article:17448445 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17448445 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17448445 | lld:pubmed |