Document Detail


Structure and mechanism of FoF1-type ATP synthases and ATPases.
MedLine Citation:
PMID:  1828930     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Authors:
H S Penefsky; R L Cross
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Advances in enzymology and related areas of molecular biology     Volume:  64     ISSN:  0065-258X     ISO Abbreviation:  Adv. Enzymol. Relat. Areas Mol. Biol.     Publication Date:  1991  
Date Detail:
Created Date:  1991-07-24     Completed Date:  1991-07-24     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0337243     Medline TA:  Adv Enzymol Relat Areas Mol Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  173-214     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, SUNY Health Science Center, Syracuse.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / metabolism*
Animals
Binding Sites
Cattle
Escherichia coli / enzymology
Kinetics
Mitochondria, Heart / enzymology
Proton-Translocating ATPases / metabolism*
Saccharomyces cerevisiae / enzymology
Grant Support
ID/Acronym/Agency:
GM-21737/GM/NIGMS NIH HHS; GM-23152/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.3.14/Proton-Translocating ATPases

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


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