Source:http://linkedlifedata.com/resource/pubmed/id/12612637
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2003-3-3
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pubmed:abstractText |
The endoplasmic reticulum (ER) has a quality-control system for 'proof-reading' newly synthesized proteins, so that only native conformers reach their final destinations. Non-native conformers and incompletely assembled oligomers are retained, and, if misfolded persistently, they are degraded. As a large fraction of ER-synthesized proteins fail to fold and mature properly, ER quality control is important for the fidelity of cellular functions. Here, we discuss recent progress in understanding the conformation-specific sorting of proteins at the level of ER retention and export.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1471-0072
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
181-91
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12612637-Animals,
pubmed-meshheading:12612637-Calnexin,
pubmed-meshheading:12612637-Calreticulin,
pubmed-meshheading:12612637-Endoplasmic Reticulum,
pubmed-meshheading:12612637-Golgi Apparatus,
pubmed-meshheading:12612637-Humans,
pubmed-meshheading:12612637-Models, Biological,
pubmed-meshheading:12612637-Protein Conformation,
pubmed-meshheading:12612637-Protein Folding,
pubmed-meshheading:12612637-Proteins,
pubmed-meshheading:12612637-Saccharomyces cerevisiae
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pubmed:year |
2003
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pubmed:articleTitle |
Quality control in the endoplasmic reticulum.
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pubmed:affiliation |
Institute of Biochemistry, Swiss Federal Institute of Technology (ETH) Zürich, Hönggerberg, CH - 8093 Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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