| pubmed-article:19933328 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C0040715 | lld:lifeskim |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C1522702 | lld:lifeskim |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C0599718 | lld:lifeskim |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C0599813 | lld:lifeskim |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
| pubmed-article:19933328 | lifeskim:mentions | umls-concept:C1283195 | lld:lifeskim |
| pubmed-article:19933328 | pubmed:issue | 49 | lld:pubmed |
| pubmed-article:19933328 | pubmed:dateCreated | 2010-8-17 | lld:pubmed |
| pubmed-article:19933328 | pubmed:abstractText | Many bacterial proteins, including most secretory proteins, are translocated across the plasma membrane by the interplay of the cytoplasmic SecA ATPase and a protein-conducting channel formed by the SecY complex. SecA catalyzes the sequential movement of polypeptide segments through the SecY channel. How SecA interacts with a broad range of polypeptide segments is unclear, but structural data raise the possibility that translocation substrates bind into a "clamp" of SecA. Here, we have used disulfide bridge cross-linking to test this hypothesis. To analyze polypeptide interactions of SecA during translocation, two cysteines were introduced into a translocation intermediate: one that cross-links to the SecY channel and the other one for cross-linking to a cysteine placed at various positions in SecA. Our results show that a translocating polypeptide is indeed captured inside SecA's clamp and moves in an extended conformation through the clamp into the SecY channel. These results define the polypeptide path during SecA-mediated protein translocation and suggest a mechanism by which ATP hydrolysis by SecA is used to move a polypeptide chain through the SecY channel. | lld:pubmed |
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| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19933328 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19933328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19933328 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19933328 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:19933328 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:19933328 | pubmed:author | pubmed-author:RapoportTom... | lld:pubmed |
| pubmed-article:19933328 | pubmed:author | pubmed-author:BauerBenedikt... | lld:pubmed |
| pubmed-article:19933328 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19933328 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:19933328 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:19933328 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19933328 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19933328 | pubmed:pagination | 20800-5 | lld:pubmed |
| pubmed-article:19933328 | pubmed:dateRevised | 2010-9-28 | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:meshHeading | pubmed-meshheading:19933328... | lld:pubmed |
| pubmed-article:19933328 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19933328 | pubmed:articleTitle | Mapping polypeptide interactions of the SecA ATPase during translocation. | lld:pubmed |
| pubmed-article:19933328 | pubmed:affiliation | Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:19933328 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19933328 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19933328 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19933328 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19933328 | lld:pubmed |
