Structural basis of membrane bending by the N-BAR protein endophilin - Wikidata - awgldk - TriplyDB

Structural basis of membrane bending by the N-BAR protein endophilin

Structural basis of membrane bending by the N-BAR protein endophilin

http://www.wikidata.org/entity/Q30010148

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Molecular basis for SNX-BAR-mediated assembly of distinct endosomal sorting tubules Versatile membrane deformation potential of activated pacsin Endophilin, Lamellipodin, and Mena cooperate to regulate F-actin-dependent EGF-receptor endocytosis.When Physics Takes Over: BAR Proteins and Membrane Curvature Dynamics and instabilities of lipid bilayer membrane shapes Membrane curvature and its generation by BAR proteins Curvature-undulation coupling as a basis for curvature sensing and generation in bilayer membranes PICK1 deficiency impairs secretory vesicle biogenesis and leads to growth retardation and decreased glucose tolerance Membrane-mediated interaction between strongly anisotropic protein scaffolds IRSp53 senses negative membrane curvature and phase separates along membrane tubules.Membrane sculpting by F-BAR domains studied by molecular dynamics simulations Structural Insights into Membrane Interaction and Caveolar Targeting of Dynamin-like EHD2 A Dynamin Mutant Defines a Superconstricted Prefission State Calmodulin Promotes N-BAR Domain-Mediated Membrane Constriction and Endocytosis.Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein Membrane fission by dynamin: what we know and what we need to know Mutations in BIN1 associated with centronuclear myopathy disrupt membrane remodeling by affecting protein density and oligomerization Membrane tension and peripheral protein density mediate membrane shape transitions Association of Endophilin B1 with Cytoplasmic Vesicles.Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and Autoregulation Structural insights into the cooperative remodeling of membranes by amphiphysin/BIN1.Vesicle uncoating regulated by SH3-SH3 domain-mediated complex formation between endophilin and intersectin at synapses Intradimer/Intermolecular interactions suggest autoinhibition mechanism in endophilin A1 The Bin/amphiphysin/Rvs (BAR) domain protein endophilin B2 interacts with plectin and controls perinuclear cytoskeletal architecture.Autoinhibition of endophilin in solution via interdomain interactions.A PH domain in ACAP1 possesses key features of the BAR domain in promoting membrane curvature Direct interaction of actin filaments with F-BAR protein pacsin2.Coarse-Grained Models for Protein-Cell Membrane Interactions.Membrane fission by protein crowding Formation of membrane ridges and scallops by the F-BAR protein Nervous Wreck.Linear aggregation of proteins on the membrane as a prelude to membrane remodeling Membrane tension controls the assembly of curvature-generating proteins.Endophilin A1 induces different membrane shapes using a conformational switch that is regulated by phosphorylation.α-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry.Monomeric synucleins generate membrane curvature.Coupling between endocytosis and sphingosine kinase 1 recruitment.Mesoscale computational studies of membrane bilayer remodeling by curvature-inducing proteins.Defining the free-energy landscape of curvature-inducing proteins on membrane bilayers Visualizing the functional architecture of the endocytic machinery.Endocytic accessory factors and regulation of clathrin-mediated endocytosis

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Structural basis of membrane bending by the N-BAR protein endophilin

http://www.wikidata.org/entity/Q30010148

description

2012 nî lūn-bûn

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2012 թուականի Մարտին հրատարակուած գիտական յօդուած

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2012 թվականի մարտին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Structural basis of membrane bending by the N-BAR protein endophilin

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Structural basis of membrane bending by the N-BAR protein endophilin

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Structural basis of membrane bending by the N-BAR protein endophilin

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Structural basis of membrane bending by the N-BAR protein endophilin

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Structural basis of membrane bending by the N-BAR protein endophilin

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Structural basis of membrane bending by the N-BAR protein endophilin

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J.CELL.2012.01.048

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P1476

Structural basis of membrane bending by the N-BAR protein endophilin

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P2093

Adam Frost

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Carsten Mim

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Edward Lyman

http://www.w3.org/2001/XMLSchema#string

Haosheng Cui

http://www.w3.org/2001/XMLSchema#string

Joseph A Gawronski-Salerno

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Vinzenz M Unger

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P2860

Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis

Structural basis of membrane invagination by F-BAR domains.

Pinkbar is an epithelial-specific BAR domain protein that generates planar membrane structures

Rho mediates endocytosis of epidermal growth factor receptor through phosphorylation of endophilin A1 by Rho-kinase

A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke

The BAR domain proteins: molding membranes in fission, fusion, and phagy

The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain

The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis

BAR domains as sensors of membrane curvature: the amphiphysin BAR structure

SH3 domains from a subset of BAR proteins define a Ubl-binding domain and implicate parkin in synaptic ubiquitination

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137-145

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1717551

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10.1016/J.CELL.2012.01.048

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1

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149

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Gregory A. Voth

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2012-03-01T00:00:00Z

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223992907

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22464326

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3319357

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