Literature DB >> 10950303

The plasma membrane proton-translocating ATPase.

G A Scarborough1.   

Abstract

Living cells require membranes and membrane transporters for the maintenance of life. After decades of biochemical scrutiny, the structures and molecular mechanisms by which membrane transporters catalyze transmembrane solute movements are beginning to be understood. The plasma membrane proton-translocating adenosine triphosphatase (ATPase) is an archetype of the P-type ATPase family of membrane transporters, which are important in a wide variety of cellular processes. The H+-ATPase has been crystallized and its structure determined to a resolution of 8 angstrom in the membrane plane. When considered together with the large body of biochemical information that has been accumulated for this transporter, and for enzymes in general, this new structural information is providing tantalizing insights regarding the molecular mechanism of active ion transport catalyzed by this enzyme.

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Year:  2000        PMID: 10950303     DOI: 10.1007/PL00000730

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  3 in total

Review 1.  Molecular mechanism of the P-type ATPases.

Authors:  Gene A Scarborough
Journal:  J Bioenerg Biomembr       Date:  2002-08       Impact factor: 2.945

2.  Early, H+-V-ATPase-dependent proton flux is necessary for consistent left-right patterning of non-mammalian vertebrates.

Authors:  Dany S Adams; Kenneth R Robinson; Takahiro Fukumoto; Shipeng Yuan; R Craig Albertson; Pamela Yelick; Lindsay Kuo; Megan McSweeney; Michael Levin
Journal:  Development       Date:  2006-03-22       Impact factor: 6.868

3.  Bioinformatic characterization of p-type ATPases encoded within the fully sequenced genomes of 26 eukaryotes.

Authors:  Mark D Thever; Milton H Saier
Journal:  J Membr Biol       Date:  2009-06-23       Impact factor: 1.843

  3 in total

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