Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism - Wikidata - awgldk - TriplyDB

Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Optimizing water permeability through the hourglass shape of aquaporins TMPad: an integrated structural database for helix-packing folds in transmembrane proteins MIPModDB: a central resource for the superfamily of major intrinsic proteins Computational electrophysiology: the molecular dynamics of ion channel permeation and selectivity in atomistic detail Detecting Aquaporin Function and Regulation Optimal permeability of aquaporins: a question of shape?Structure and mechanism of a pentameric formate channel Subangstrom Resolution X-Ray Structure Details Aquaporin-Water Interactions Mercury increases water permeability of a plant aquaporin through a non-cysteine-related mechanism Yeast aquaglyceroporins use the transmembrane core to restrict glycerol transport.Electrostatics of aquaporin and aquaglyceroporin channels correlates with their transport selectivity.Structures of membrane proteins.The New York Consortium on Membrane Protein Structure (NYCOMPS): a high-throughput platform for structural genomics of integral membrane proteins.Tuning microbial hosts for membrane protein production.Aquaporins: important but elusive drug targets.Characterization of Leishmania donovani aquaporins shows presence of subcellular aquaporins similar to tonoplast intrinsic proteins of plants Biocrystallography: past, present, future.Cloning and characterization of a zebrafish homologue of human AQP1: a bifunctional water and gas channel Phosphorylation of aquaporin-2 regulates its water permeability The gating mechanism of the human aquaporin 5 revealed by molecular dynamics simulations.Regulation of macrophage motility by the water channel aquaporin-1: crucial role of M0/M2 phenotype switch.Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways.Single amino acid substitutions in the selectivity filter render NbXIP1;1α aquaporin water permeable NMR quantification of diffusional exchange in cell suspensions with relaxation rate differences between intra and extracellular compartments.Water permeation through the internal water pathway in activated GPCR rhodopsin.Unlocking the eukaryotic membrane protein structural proteome.Exploring transmembrane diffusion pathways with molecular dynamics Influences of membrane mimetic environments on membrane protein structures.A functional BH3 domain in an aquaporin from Leishmania infantum.Pore waters regulate ion permeation in a calcium release-activated calcium channel.Structural insights into eukaryotic aquaporin regulation.Yeast water channels: an overview of orthodox aquaporins.The evolutionary aspects of aquaporin family.Advances in the production of membrane proteins in Pichia pastoris.An emerging consensus on aquaporin translocation as a regulatory mechanism.Molecular dynamics of water in the neighborhood of aquaporins.Further advances in the production of membrane proteins in Pichia pastoris.Ion selectivity and gating mechanisms of FNT channels.Fungal aquaporins: cellular functions and ecophysiological perspectives.Aquaglyceroporins: implications in adipose biology and obesity.

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

http://www.wikidata.org/entity/Q27655977

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2009 nî lūn-bûn

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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2009 թվականի հունիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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Crystal Structure of a Yeast Aquaporin at 1.15 Å Reveals a Novel Gating Mechanism

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JOURNAL.PBIO.1000130

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Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism

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Kristina Hedfalk

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Madelene Palmgren

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Richard Neutze

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Urszula Kosinska-Eriksson

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P2860

Lipid-protein interactions in double-layered two-dimensional AQP0 crystals.

Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z

A short history of SHELX

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structural determinants of water permeation through aquaporin-1

Structure of a glycerol-conducting channel and the basis for its selectivity

Structural basis of water-specific transport through the AQP1 water channel

Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum

High-resolution x-ray structure of human aquaporin 5

Coot: model-building tools for molecular graphics

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e1000130

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10.1371/JOURNAL.PBIO.1000130

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6

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Camilo Aponte-Santamaría

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Karin Lindkvist-Petersson

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19529756

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crystal structure

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