Document Detail


Studies of the ubiquitin proteasome system.
MedLine Citation:
PMID:  18228479     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A concept that has arisen over the last decade is that proteins can, in general, be covalently modified by polypeptides, resulting in alterations in their fate and function. The first-identified and most well studied of these modifying polypeptides is ubiquitin. Although targeting for proteasomal degradation is the best studied outcome of ubiquitylation, we now understand that modification of proteins with ubiquitin has numerous other cellular roles that alter protein function and that are unrelated to proteasomal degradation. Ubiquitylation is a complex process that is regulated at the level of both addition and removal of ubiquitin from target proteins. This unit includes a number of different basic protocols that will facilitate the study of components of the ubiquitin system and substrate ubiquitylation both in vitro and in cells. Because another protein modifier, NEDD8, itself regulates aspects of the ubiquitin system, basic protocols on neddylation are also included in this unit.
Authors:
Kevin L Lorick; Yili Yang; Jane P Jensen; Kazuhiro Iwai; Allan M Weissman
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Current protocols in cell biology / editorial board, Juan S. Bonifacino ... [et al.]     Volume:  Chapter 15     ISSN:  1934-2616     ISO Abbreviation:  Curr Protoc Cell Biol     Publication Date:  2006 Jul 
Date Detail:
Created Date:  2008-01-29     Completed Date:  2008-05-13     Revised Date:  2009-12-11    
Medline Journal Info:
Nlm Unique ID:  101287856     Medline TA:  Curr Protoc Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  Unit 15.9     Citation Subset:  IM    
Affiliation:
National Cancer Institute, Frederick, Maryland, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Proteasome Endopeptidase Complex / analysis*
Rabbits
Ubiquitin / analysis*
Ubiquitin-Activating Enzymes / analysis
Ubiquitin-Conjugating Enzymes / analysis
Ubiquitin-Protein Ligase Complexes / analysis
Ubiquitin-Protein Ligases / analysis
Ubiquitination*
Chemical
Reg. No./Substance:
0/Ubiquitin; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 6.3.2.19/Ubiquitin-Activating Enzymes; EC 6.3.2.19/Ubiquitin-Conjugating Enzymes; EC 6.3.2.19/Ubiquitin-Protein Ligase Complexes; EC 6.3.2.19/Ubiquitin-Protein Ligases

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


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