Document Detail


Cleaning up: ER-associated degradation to the rescue.
MedLine Citation:
PMID:  23217703     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
All cellular proteins are subject to quality control "decisions," which help to prevent or delay a myriad of diseases. Quality control within the secretory pathway creates a special challenge, as aberrant polypeptides are recognized and returned to the cytoplasm for proteasomal degradation. This process is termed endoplasmic-reticulum (ER)-associated degradation (ERAD).
Authors:
Jeffrey L Brodsky
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Cell     Volume:  151     ISSN:  1097-4172     ISO Abbreviation:  Cell     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-10     Completed Date:  2013-02-06     Revised Date:  2014-10-28    
Medline Journal Info:
Nlm Unique ID:  0413066     Medline TA:  Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1163-7     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Inc. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Animals
Endoplasmic Reticulum / physiology*
Endoplasmic Reticulum-Associated Degradation*
Humans
Protein Folding
Protein Transport
Proteins / metabolism*
Secretory Pathway*
Grant Support
ID/Acronym/Agency:
P30 DK072506/DK/NIDDK NIH HHS; P30 DK079307/DK/NIDDK NIH HHS; R01 GM075061/GM/NIGMS NIH HHS; R01 HL058541/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Proteins
Comments/Corrections

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