| pubmed-article:10446175 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10446175 | lifeskim:mentions | umls-concept:C0061928 | lld:lifeskim |
| pubmed-article:10446175 | lifeskim:mentions | umls-concept:C0005290 | lld:lifeskim |
| pubmed-article:10446175 | lifeskim:mentions | umls-concept:C1158106 | lld:lifeskim |
| pubmed-article:10446175 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:10446175 | lifeskim:mentions | umls-concept:C0178555 | lld:lifeskim |
| pubmed-article:10446175 | lifeskim:mentions | umls-concept:C1156022 | lld:lifeskim |
| pubmed-article:10446175 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:10446175 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:10446175 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:10446175 | pubmed:dateCreated | 1999-9-9 | lld:pubmed |
| pubmed-article:10446175 | pubmed:abstractText | In vivo, many proteins must interact with molecular chaperones to attain their native conformation. In the case of tubulin, newly synthesized alpha- and beta-subunits are partially folded by cytosolic chaperonin, a double-toroidal ATPase with homologs in all kingdoms of life and in most cellular compartments. alpha- and beta-tubulin folding intermediates are then brought together by tubulin-specific chaperone proteins (named cofactors A-E) in a cofactor-containing supercomplex with GTPase activity. Here we show that tubulin subunit exchange can only occur by passage through this supercomplex, thus defining it as a dimer-making machine. We also show that hydrolysis of GTP by beta-tubulin in the supercomplex acts as a switch for the release of native tubulin heterodimer. In this folding reaction and in the related reaction of tubulin-folding cofactors with native tubulin, the cofactors behave as GTPase-activating proteins, stimulating the GTP-binding protein beta-tubulin to hydrolyze its GTP. | lld:pubmed |
| pubmed-article:10446175 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10446175 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10446175 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10446175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10446175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10446175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10446175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10446175 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10446175 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10446175 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10446175 | pubmed:author | pubmed-author:LewisS ASA | lld:pubmed |
| pubmed-article:10446175 | pubmed:author | pubmed-author:CowanN JNJ | lld:pubmed |
| pubmed-article:10446175 | pubmed:author | pubmed-author:TianGG | lld:pubmed |
| pubmed-article:10446175 | pubmed:author | pubmed-author:BhamidipatiAA | lld:pubmed |
| pubmed-article:10446175 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10446175 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:10446175 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:10446175 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10446175 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10446175 | pubmed:pagination | 24054-8 | lld:pubmed |
| pubmed-article:10446175 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10446175 | pubmed:meshHeading | pubmed-meshheading:10446175... | lld:pubmed |
| pubmed-article:10446175 | pubmed:meshHeading | pubmed-meshheading:10446175... | lld:pubmed |
| pubmed-article:10446175 | pubmed:meshHeading | pubmed-meshheading:10446175... | lld:pubmed |
| pubmed-article:10446175 | pubmed:meshHeading | pubmed-meshheading:10446175... | lld:pubmed |
| pubmed-article:10446175 | pubmed:meshHeading | pubmed-meshheading:10446175... | lld:pubmed |
| pubmed-article:10446175 | pubmed:meshHeading | pubmed-meshheading:10446175... | lld:pubmed |
| pubmed-article:10446175 | pubmed:meshHeading | pubmed-meshheading:10446175... | lld:pubmed |
| pubmed-article:10446175 | pubmed:meshHeading | pubmed-meshheading:10446175... | lld:pubmed |
| pubmed-article:10446175 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10446175 | pubmed:articleTitle | Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer. | lld:pubmed |
| pubmed-article:10446175 | pubmed:affiliation | Department of Biochemistry, New York University Medical Center, New York, New York 10016, USA. | lld:pubmed |
| pubmed-article:10446175 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10446175 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10446175 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:10446175 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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