| pubmed-article:21496645 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21496645 | lifeskim:mentions | umls-concept:C1655065 | lld:lifeskim |
| pubmed-article:21496645 | lifeskim:mentions | umls-concept:C0040715 | lld:lifeskim |
| pubmed-article:21496645 | lifeskim:mentions | umls-concept:C1522702 | lld:lifeskim |
| pubmed-article:21496645 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:21496645 | lifeskim:mentions | umls-concept:C0599718 | lld:lifeskim |
| pubmed-article:21496645 | lifeskim:mentions | umls-concept:C0599813 | lld:lifeskim |
| pubmed-article:21496645 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
| pubmed-article:21496645 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:21496645 | pubmed:dateCreated | 2011-4-18 | lld:pubmed |
| pubmed-article:21496645 | pubmed:abstractText | All cells employ ATP-powered proteases for protein-quality control and regulation. In the ClpXP protease, ClpX is a AAA+ machine that recognizes specific protein substrates, unfolds these molecules, and then translocates the denatured polypeptide through a central pore and into ClpP for degradation. Here, we use optical-trapping nanometry to probe the mechanics of enzymatic unfolding and translocation of single molecules of a multidomain substrate. Our experiments demonstrate the capacity of ClpXP and ClpX to perform mechanical work under load, reveal very fast and highly cooperative unfolding of individual substrate domains, suggest a translocation step size of 5-8 amino acids, and support a power-stroke model of denaturation in which successful enzyme-mediated unfolding of stable domains requires coincidence between mechanical pulling by the enzyme and a transient stochastic reduction in protein stability. We anticipate that single-molecule studies of the mechanical properties of other AAA+ proteolytic machines will reveal many shared features with ClpXP. | lld:pubmed |
| pubmed-article:21496645 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21496645 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21496645 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21496645 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21496645 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21496645 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21496645 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21496645 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21496645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21496645 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21496645 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21496645 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:21496645 | pubmed:issn | 1097-4172 | lld:pubmed |
| pubmed-article:21496645 | pubmed:author | pubmed-author:BakerTania... | lld:pubmed |
| pubmed-article:21496645 | pubmed:author | pubmed-author:SauerRobert... | lld:pubmed |
| pubmed-article:21496645 | pubmed:author | pubmed-author:LangMatthew... | lld:pubmed |
| pubmed-article:21496645 | pubmed:author | pubmed-author:OlivaresAdria... | lld:pubmed |
| pubmed-article:21496645 | pubmed:author | pubmed-author:Aubin-TamMari... | lld:pubmed |
| pubmed-article:21496645 | pubmed:copyrightInfo | Copyright © 2011 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:21496645 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21496645 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:21496645 | pubmed:volume | 145 | lld:pubmed |
| pubmed-article:21496645 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21496645 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21496645 | pubmed:pagination | 257-67 | lld:pubmed |
| pubmed-article:21496645 | pubmed:dateRevised | 2011-10-17 | lld:pubmed |
| pubmed-article:21496645 | pubmed:meshHeading | pubmed-meshheading:21496645... | lld:pubmed |
| pubmed-article:21496645 | pubmed:meshHeading | pubmed-meshheading:21496645... | lld:pubmed |
| pubmed-article:21496645 | pubmed:meshHeading | pubmed-meshheading:21496645... | lld:pubmed |
| pubmed-article:21496645 | pubmed:meshHeading | pubmed-meshheading:21496645... | lld:pubmed |
| pubmed-article:21496645 | pubmed:meshHeading | pubmed-meshheading:21496645... | lld:pubmed |
| pubmed-article:21496645 | pubmed:meshHeading | pubmed-meshheading:21496645... | lld:pubmed |
| pubmed-article:21496645 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21496645 | pubmed:articleTitle | Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. | lld:pubmed |
| pubmed-article:21496645 | pubmed:affiliation | Department of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. | lld:pubmed |
| pubmed-article:21496645 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21496645 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:21496645 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21496645 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:21496645 | lld:pubmed |
