pubmed-article:15546659 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15546659 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
pubmed-article:15546659 | pubmed:issue | 1-3 | lld:pubmed |
pubmed-article:15546659 | pubmed:dateCreated | 2004-11-19 | lld:pubmed |
pubmed-article:15546659 | pubmed:abstractText | In bacteria, the translocase mediates the translocation of proteins into or across the cytosolic membrane. It consists of a membrane embedded protein-conducting channel and a peripherally associated motor domain, the ATPase SecA. The channel is formed by SecYEG, a multimeric protein complex that assembles into oligomeric forms. The structure and subunit composition of this protein-conducting channel is evolutionary conserved and a similar system is found in the endoplasmic reticulum of eukaryotes and the cytoplasmic membrane of archaea. The ribosome and other membrane proteins can associate with the protein-conducting channel complex and affect its activity or functionality. | lld:pubmed |
pubmed-article:15546659 | pubmed:language | eng | lld:pubmed |
pubmed-article:15546659 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15546659 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15546659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15546659 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15546659 | pubmed:month | Nov | lld:pubmed |
pubmed-article:15546659 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:15546659 | pubmed:author | pubmed-author:van der... | lld:pubmed |
pubmed-article:15546659 | pubmed:author | pubmed-author:DriessenArnol... | lld:pubmed |
pubmed-article:15546659 | pubmed:author | pubmed-author:VeenendaalAnd... | lld:pubmed |
pubmed-article:15546659 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15546659 | pubmed:day | 11 | lld:pubmed |
pubmed-article:15546659 | pubmed:volume | 1694 | lld:pubmed |
pubmed-article:15546659 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15546659 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15546659 | pubmed:pagination | 81-95 | lld:pubmed |
pubmed-article:15546659 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:15546659 | pubmed:meshHeading | pubmed-meshheading:15546659... | lld:pubmed |
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pubmed-article:15546659 | pubmed:meshHeading | pubmed-meshheading:15546659... | lld:pubmed |
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pubmed-article:15546659 | pubmed:meshHeading | pubmed-meshheading:15546659... | lld:pubmed |
pubmed-article:15546659 | pubmed:meshHeading | pubmed-meshheading:15546659... | lld:pubmed |
pubmed-article:15546659 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15546659 | pubmed:articleTitle | The protein-conducting channel SecYEG. | lld:pubmed |
pubmed-article:15546659 | pubmed:affiliation | Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9750 AA Haren, The Netherlands. | lld:pubmed |
pubmed-article:15546659 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15546659 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:15546659 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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