Aquaporins by Jennifer M. Carbrey, Peter Agre (auth.), Prof. Dr. Eric

By Jennifer M. Carbrey, Peter Agre (auth.), Prof. Dr. Eric Beitz (eds.)

The aquaporin box has matured at an incredibly speedy speed and we're on the verge to advance critical suggestions to therapeutically modulate aquaporin functionality without delay or through regulatory networks. Key necessities can be found this day: i. a substantial (and turning out to be) variety of aquaporin crystal constructions for the rational layout of inhibitory molecules, ii. complex molecular dynamics simulation strategies for theoretical analyses of selectivity mechanisms and docking experiments, iii. finished facts on aquaporin immunohistochemistry, iv. aquaporin knockout animals for physiological experiences, and v. assay structures for compound library screenings. The constitution of this quantity on aquaporins follows the issues laid out above and therefore covers the advancements from easy study to power pharmacological use. positioned among pharmacology textbooks and up to date clinical papers this booklet offers a well timed review for readers from the basic in addition to the utilized disciplines.

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Coli Bovine lens E. coli Bovine lens Water channel Water channel Water channel Water channel; open conform Methanobacterium Water channel thermoautotrophicum Methanobacterium Water channel thermoautotrophicum Bovine lens Water channel Spinach Water channel; closed conform Spinach Water channel; open conform Human Water channel E. coli E. 2 A 13-Feb-07 13-Feb-07 E. coli E. 9 A 13-Feb-07 13-Feb-07 isoforms in maize (Chaumont et al. 2001). Phylogenetically these proteins can be divided into four different subfamilies, which to some extent correspond to distinct subcellular localizations (Johanson et al.

1 Functional Characterization . . . . . . . . . . . . . . . . . . . . . . . 3 The Structure of AQPs . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1 The AQP Fold . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2 The Structure of the Pore . . . . . . . . . . . . . . . . . . . . . . . . 3 Surface Structure of AQPs Involved in Membrane Junctions . . . .

Am J Physiol Cell Physiol 289:C1303–C1311 Jahn TP, Møller AL, Zeuthen T, Holm LM, Klaerke DA, Mohsin B, K¨uhlbrandt W, Schjoerring JK (2004) Aquaporin homologues in plants and mammals transport ammonia. FEBS Lett 574: 31–36 Jung JS, Preston GM, Smith BL, Guggino WB, Agre P (1994) Molecular structure of the water channel through aquaporin CHIP: The hourglass model. J Biol Chem 269:14648–14654 Kachadorian WA, Wade JB, DiScala VA (2000) Vasopressin: Induced structural changes in toad bladder luminal membrane.

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