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Aquaporins

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Published by Academic Press in San Diego .
Written in English

Subjects:

  • Aquaporins,
  • Aquaporins

Book details:

Edition Notes

Includes bibliographical references and index.

Statementedited by Stefan Hohmann, Søren Nielsen, Peter Agre.
SeriesCurrent topics in membranes ;, v. 51
ContributionsHohmann, Stefan, 1956-, Nielsen, Søren, 1962-, Agre, Peter, 1949-
Classifications
LC ClassificationsQP552.A65 A68 2001
The Physical Object
Paginationxvii, 390 p., [8] p. of plates :
Number of Pages390
ID Numbers
Open LibraryOL3968996M
ISBN 100121533514
LC Control Number2001275332
OCLC/WorldCa46764295

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Aquaporins (Advances in Experimental Medicine and Biology Book ) - Kindle edition by Yang, Baoxue. Download it once and read it on your Kindle device, PC, phones or tablets. Use features like bookmarks, note taking and highlighting while reading Aquaporins (Advances in Experimental Medicine and Biology Book ).Manufacturer: Springer. Aquaporins are membrane proteins that form the channels by which water travels into and between cells across all organ systems (Badaut et al., , ; Hill et al., ). In the BBB, aquaporin-4 is the channel protein that facilitates movement of water into the CNS.   Aquaporins are multifunctional water and solute transporters highly divergent in living organisms. Biochimica et Biophysica Acta (BBA) - . The structure of this volume on aquaporins follows the points laid out above and thus covers the developments from basic research to potential pharmacological use. Situated between pharmacology textbooks and recent scientific papers this book provides a timely overview for readers from the fundamental as well as the applied disciplines.

This book provides a state-of-the-art report on our current understanding of aquaporins and the future direction of the field. Aquaporins (AQPs) are a group of water-channel proteins that are specifically permeable to water and other small molecules, such as . ISBN: OCLC Number: Description: xvi, pages: illustrations. Contents: Discovery of the aquaporins and development of the field --Aquaporin protein structure and selectivity mechanisms --AQP structure and functional implications --Dynamics and energetics of permeation through do .   The three-dimensional structures of the human water-channel protein AQP1 [] and the bacterial aquaglyceroporin GlpF [] are highly similar, although the sequence identity between them is less than 30% at the amino-acid indicates that the overall structure of aquaporins (classical aquaporins and aquaglyceroporins) is conserved over 2 to 3 billion years . Aquaporins / This book provides a state-of-the-art report on our current understanding of aquaporins and the future direction of the field. Aquaporins (AQPs) are a group of water-channel proteins that are specifically permeable to water and other small molecules, such as .

The aquaporins are a family of small ( kDa) pore-forming integral membrane proteins. This ancient protein family was first named after its archetype, the major intrinsic protein (MIP) of mammalian lens fibers [1, 2], which is now designated AQP0 (see Table 1).When, later on, MIP homologs were shown to function as water channels, the term 'aquaporin' was suggested for .   Aquaporins are typically composed of identical subunit proteins. Water molecules traverse the narrowest portion of the water channel in single file. The presence of water channels increases the permeability of membranes to water by as much as ten-fold. Aquaporins prevent us from dying of dehydration by reabsorbing 99% of the water in the kidney. channel [chan´el] a passage, cut, or groove through which something can pass or flow across a solid structure. calcium channel (calcium-sodium channel) a slow voltage-gated channel very permeable to calcium ions and slightly permeable to sodium ions, existing in three subtypes designated L, M, and N and located throughout the body; calcium channels are. An innovative water filter technology, billion years in the making. Our Aquaporin Inside® hollow fiber forward osmosis biomimetic membranes use natural aquaporins to improve water reuse and concentration processes, with low back diffusion and using only osmotic pressure.