Document Detail


The tail end of membrane insertion.
MedLine Citation:
PMID:  17382875     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Many membrane proteins are inserted into cellular membranes via a carboxy-terminal tail-anchor segment, but the mechanism of insertion is poorly understood. In this issue of Cell, Stefanovic and Hegde (2007) report the identification and initial characterization of a soluble ATP-dependent receptor for the insertion of newly synthesized tail-anchored membrane proteins.
Authors:
Elisabet C Mandon; Reid Gilmore
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Publication Detail:
Type:  Comment; Journal Article    
Journal Detail:
Title:  Cell     Volume:  128     ISSN:  0092-8674     ISO Abbreviation:  Cell     Publication Date:  2007 Mar 
Date Detail:
Created Date:  2007-03-26     Completed Date:  2007-05-08     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0413066     Medline TA:  Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1031-2     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605-2324, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Arsenite Transporting ATPases / chemistry,  metabolism*
Endoplasmic Reticulum / metabolism*
Eukaryotic Cells
Intracellular Membranes / chemistry,  metabolism*
Membrane Proteins / chemistry,  metabolism*
Protein Structure, Tertiary
Chemical
Reg. No./Substance:
0/Membrane Proteins; EC 3.6.3.16/Arsenite Transporting ATPases
Comments/Corrections
Comment On:
Cell. 2007 Mar 23;128(6):1147-59   [PMID:  17382883 ]

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


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