期刊
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
卷 18, 期 6, 页码 751-761出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2007.09.001
关键词
heat shock proteins; ERAD; proteasome; lectin; degradation
资金
- NIGMS NIH HHS [R01 GM075061, R01 GM075061-01A1, R01 GM075061-02] Funding Source: Medline
Most proteins in the secretory pathway are translated, folded, and subjected to quality control at the endoplasmic reticulum (ER). These processes must be flexible enough to process diverse protein conformations, yet specific enough to recognize when a protein should be degraded. Molecular chaperones are responsible for this decision making process. ER associated chaperones assist in polypeptide translocation, protein folding, and ER associated degradation (ERAD). Nevertheless, we are only beginning to understand how chaperones function, how they are recruited to specific substrates and assist in folding/degradation, and how unique chaperone classes make quality control decisions. (C) 2007 Elsevier Ltd. All rights reserved.
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