| pubmed-article:10493591 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10493591 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:10493591 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:10493591 | pubmed:dateCreated | 2000-1-13 | lld:pubmed |
| pubmed-article:10493591 | pubmed:abstractText | Self-association of ClpB (a mixture of 95- and 80-kDa subunits) has been studied with gel filtration chromatography, analytical ultracentrifugation, and electron microscopy. Monomeric ClpB predominates at low protein concentration (0.07 mg/mL), while an oligomeric form is highly populated at >4 mg/mL. The oligomer formation is enhanced in the presence of 2 mM ATP or adenosine 5'-O-thiotriphosphate (ATPgammaS). In contrast, 2 mM ADP inhibits full oligomerization of ClpB. The apparent size of the ATP- or ATPgammaS-induced oligomer, as determined by gel filtration, sedimentation velocity and electron microscopy image averaging, and the molecular weight, as determined by sedimentation equilibrium, are consistent with those of a ClpB hexamer. These results indicate that the oligomerization reactions of ClpB are similar to those of other Hsp100 proteins. | lld:pubmed |
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| pubmed-article:10493591 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10493591 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493591 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10493591 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10493591 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10493591 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:10493591 | pubmed:author | pubmed-author:GinsburgAA | lld:pubmed |
| pubmed-article:10493591 | pubmed:author | pubmed-author:KesselMM | lld:pubmed |
| pubmed-article:10493591 | pubmed:author | pubmed-author:MauriziM RMR | lld:pubmed |
| pubmed-article:10493591 | pubmed:author | pubmed-author:ZolkiewskiMM | lld:pubmed |
| pubmed-article:10493591 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10493591 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:10493591 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10493591 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10493591 | pubmed:pagination | 1899-903 | lld:pubmed |
| pubmed-article:10493591 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10493591 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10493591 | pubmed:articleTitle | Nucleotide-dependent oligomerization of ClpB from Escherichia coli. | lld:pubmed |
| pubmed-article:10493591 | pubmed:affiliation | Department of Biochemistry, Kansas State University, Manhattan 66506, USA. michalz@ksu.edu | lld:pubmed |
| pubmed-article:10493591 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10493591 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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