Physiology AJP: Gastrointestinal and Liver Physiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


News Physiol Sci 18: 191-195, 2003; doi:10.1152/nips.01445.2003
1548-9213/03 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (5)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Altenberg, G. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Altenberg, G. A.
News in Physiological Sciences, Vol. 18, No. 5, 191-195, October 2003
© 2003 Int. Union Physiol. Sci./Am. Physiol. Soc.

The Engine of ABC Proteins

Guillermo A. Altenberg

Membrane Protein Laboratory, Sealy Center for Structural Biology, and Department of Physiology and Biophysics, The University of Texas Medical Branch, Galveston, Texas 77555-0437
Proteins that belong to the ATP-binding cassette superfamily span from bacteria to humans and comprise one of the largest protein families. These proteins are characterized by the presence of two nucleotide-binding domains, and recent studies suggest that association and dissociation of these domains is a common basic molecular mechanism of operation that couples ATP binding/hydrolysis to substrate transport across membranes.




This article has been cited by other articles:


Home page
J. Bacteriol.Home page
J. S. Richardson and I. J. Oresnik
L-Rhamnose Transport Is Sugar Kinase (RhaK) Dependent in Rhizobium leguminosarum bv. trifolii
J. Bacteriol., December 1, 2007; 189(23): 8437 - 8446.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. Cuthbertson, J. Powers, and C. Whitfield
The C-terminal Domain of the Nucleotide-binding Domain Protein Wzt Determines Substrate Specificity in the ATP-binding Cassette Transporter for the Lipopolysaccharide O-antigens in Escherichia coli Serotypes O8 and O9a
J. Biol. Chem., August 26, 2005; 280(34): 30310 - 30319.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2003 by the Int. Union Physiol. Sci./Am. Physiol. Soc.