Mechanism of Coupling of Transport to Hydrolysis in Bacterial ATP-Binding Cassette Transporters-Reference-Cited by-同舟云学术

Mechanism of Coupling of Transport to Hydrolysis in Bacterial ATP-Binding Cassette Transporters

Published:2002-03 Issue:5 Volume:184 Page:1225-1233
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Davidson Amy L.¹

Affiliation:

1. Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.184.5.1225-1233.2002

Reference136 articles.

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2. Al-Shawi, M. K., and A. E. Senior. 1993. Characterization of the adenosine triphosphatase activity of Chinese hamster P-glycoprotein. J. Biol. Chem.268:4197-4206.

3. Al-Shawi, M. K., I. L. Urbatsch, and A. E. Senior. 1994. Covalent inhibitors of P-glycoprotein ATPase activity. J. Biol. Chem.269:8986-8992.

4. Ames, G. F., C. S. Mimura, and V. Shyamala. 1990. Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to humans: traffic ATPases. FEMS Microbiol. Rev.6:429-446.

5. Ames, G. F. L., C. E. Liu, A. K. Joshi, and K. Nikaido. 1996. Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases. J. Biol. Chem.271:14264-14270.

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