Document Detail

Palmitoylation of influenza virus proteins.
MedLine Citation:
PMID:  23356257     Owner:  NLM     Status:  In-Data-Review    
Influenza viruses contain two palmitoylated (S-acylated) proteins: the major spike protein HA (haemagglutinin) and the proton-channel M2. The present review describes the fundamental biochemistry of palmitoylation of HA: the location of palmitoylation sites and the fatty acid species bound to HA. Finally, the functional consequences of palmitoylation of HA and M2 are discussed regarding association with membrane rafts, entry of viruses into target cells by HA-mediated membrane fusion as well as the release of newly assembled virus particles from infected cells.
Michael Veit; Marina V Serebryakova; Larisa V Kordyukova
Related Documents :
23536547 - Discovering new medicines targeting helicases: challenges and recent progress.
14047227 - L-cystine requirement for production of coxsackie b3 virus in cultured monkey heart cells.
24283137 - Isolation of influenza a viruses from wild ducks and feathers in minnesota (2010-2011).
23140247 - Serological and molecular investigation into the role of wild birds in the epidemiology...
9506817 - A new assay for classical swine fever virus based on cytopathogenicity in porcine kidne...
18770207 - Studies on the persistence and excretion of egg drop syndrome 1976 virus in chickens.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemical Society transactions     Volume:  41     ISSN:  1470-8752     ISO Abbreviation:  Biochem. Soc. Trans.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7506897     Medline TA:  Biochem Soc Trans     Country:  England    
Other Details:
Languages:  eng     Pagination:  50-5     Citation Subset:  IM    
*Department of Immunology and Molecular Biology Veterinary Faculty, Free University, Philippstr. 13, 10115 Berlin, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

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

Previous Document:  Chemical approaches for profiling dynamic palmitoylation.
Next Document:  Chemical proteomics: a powerful tool for exploring protein lipidation.