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| pubmed-article:8107851 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
| pubmed-article:8107851 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:8107851 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:8107851 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:8107851 | lifeskim:mentions | umls-concept:C2347858 | lld:lifeskim |
| pubmed-article:8107851 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:8107851 | pubmed:issue | 6464 | lld:pubmed |
| pubmed-article:8107851 | pubmed:dateCreated | 1994-3-23 | lld:pubmed |
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| pubmed-article:8107851 | pubmed:abstractText | Protein translocation into the mammalian endoplasmic reticulum requires the Sec61p complex, which consists of three membrane proteins. The alpha-subunit, the homologue of Sec61p of yeast, shows some similarity to SecYp, a key component of the protein export apparatus of bacteria. In Escherichia coli, SecYp is also associated with two other proteins (SecEp and band-1 protein). We have now determined the sequences of the beta- and gamma-subunits of the mammalian Sec61p complex. Sec61-gamma is homologous to SSS1p, a suppressor of sec61 mutants in Saccharomyces cerevisiae, and can functionally replace it in yeast cells. Moreover, Sec61-gamma and SSS1p are structurally related to SecEp of E. coli and to putative homologues in various other bacteria. At least two subunits of the Sec61/SecYp complex therefore seem to be key components of the protein translocation apparatus in all classes of organisms. | lld:pubmed |
| pubmed-article:8107851 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8107851 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8107851 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8107851 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8107851 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8107851 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8107851 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:8107851 | pubmed:author | pubmed-author:RapoportT ATA | lld:pubmed |
| pubmed-article:8107851 | pubmed:author | pubmed-author:HartmannEE | lld:pubmed |
| pubmed-article:8107851 | pubmed:author | pubmed-author:PrehnSS | lld:pubmed |
| pubmed-article:8107851 | pubmed:author | pubmed-author:SommerTT | lld:pubmed |
| pubmed-article:8107851 | pubmed:author | pubmed-author:JentschSS | lld:pubmed |
| pubmed-article:8107851 | pubmed:author | pubmed-author:GörlichDD | lld:pubmed |
| pubmed-article:8107851 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8107851 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:8107851 | pubmed:volume | 367 | lld:pubmed |
| pubmed-article:8107851 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8107851 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8107851 | pubmed:pagination | 654-7 | lld:pubmed |
| pubmed-article:8107851 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8107851 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8107851 | pubmed:articleTitle | Evolutionary conservation of components of the protein translocation complex. | lld:pubmed |
| pubmed-article:8107851 | pubmed:affiliation | Max-Delbrück Centre for Molecular Medicine, Berlin-Buch, Germany. | lld:pubmed |
| pubmed-article:8107851 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8107851 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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