Document Detail


MultIDIMensionality of IDIMs: Intrinsic Disorder in Autoinhibition.
MedLine Citation:
PMID:  23473663     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Intrinsic disorder (ID) is crucial for the function of many proteins. The activity of some proteins is autoinhibited by their inhibitory modules (IMs). In this issue of Structure, Trudeau and colleagues showed multifarious roles of ID in controlling agility of IMs.
Authors:
Vladimir N Uversky
Related Documents :
23473663 - Multidimensionality of idims: intrinsic disorder in autoinhibition.
24376903 - Matrix metalloproteinases (mmp-2 and mmp-9) activity in corneal ulcer and ocular surfac...
22303623 - Loneliness and eating disorders.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Structure (London, England : 1993)     Volume:  21     ISSN:  1878-4186     ISO Abbreviation:  Structure     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-03-11     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101087697     Medline TA:  Structure     Country:  United States    
Other Details:
Languages:  eng     Pagination:  315-6     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 Elsevier Ltd. All rights reserved.
Affiliation:
Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA; Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia. Electronic address: vuversky@health.usf.edu.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

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


Previous Document:  Prevalence and resistance of commensal Staphylococcus aureus, including meticillin-resistant S aureu...
Next Document:  Variations on glutamate binding in channel-gated receptors.