Document Detail


Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha1-antitrypsin deficiency.
MedLine Citation:
PMID:  23197448     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
CONCLUSION: Changes in protein diffusion provide an explanation for the cellular consequences of ER protein overload in mutants that cause inclusion body formation and α1AT deficiency.
Authors:
Adriana Ordóñez; Erik L Snapp; Lu Tan; Elena Miranda; Stefan J Marciniak; David A Lomas
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2013-03-14
Journal Detail:
Title:  Hepatology (Baltimore, Md.)     Volume:  57     ISSN:  1527-3350     ISO Abbreviation:  Hepatology     Publication Date:  2013 May 
Date Detail:
Created Date:  2013-04-23     Completed Date:  2013-07-05     Revised Date:  2014-07-31    
Medline Journal Info:
Nlm Unique ID:  8302946     Medline TA:  Hepatology     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2049-60     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 American Association for the Study of Liver Diseases.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line
Cricetinae
Cricetulus
Endoplasmic Reticulum Stress / physiology*
Female
Inclusion Bodies / physiology
Models, Animal
Mutation / genetics
Polymers / metabolism*
Proteins / metabolism*
Stress, Physiological / physiology*
Unfolded Protein Response / physiology
alpha 1-Antitrypsin / genetics,  metabolism
alpha 1-Antitrypsin Deficiency / genetics,  metabolism,  physiopathology*
Grant Support
ID/Acronym/Agency:
100140//Wellcome Trust; G0601840//Medical Research Council; G0901786//Medical Research Council; GGP11057//Telethon; R01 GM086530/GM/NIGMS NIH HHS; R01GM086530-01/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Polymers; 0/Proteins; 0/alpha 1-Antitrypsin
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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