Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
about
Molecular dynamics simulations of membrane proteins and their interactions: from nanoscale to mesoscaleCurrent approaches to studying membrane organizationOrganization and dynamics of SNARE proteins in the presynaptic membraneThe role of cholesterol in membrane fusionIn vivo single-molecule imaging of syntaxin1A reveals polyphosphoinositide- and activity-dependent trapping in presynaptic nanoclusters.Nucleolin-targeted Extracellular Vesicles as a Versatile Platform for Biologics Delivery to Breast Cancer.Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.SNARE-mediated membrane fusion trajectories derived from force-clamp experimentsCalcium Promotes the Formation of Syntaxin 1 Mesoscale Domains through Phosphatidylinositol 4,5-Bisphosphate.Cholesterol Increases the Openness of SNARE-Mediated Flickering Fusion PoresPre-transition effects mediate forces of assembly between transmembrane proteins.Nanodisc-cell fusion: control of fusion pore nucleation and lifetimes by SNARE protein transmembrane domains.CELF RNA binding proteins promote axon regeneration in C. elegans and mammals through alternative splicing of Syntaxins.Roles of Interleaflet Coupling and Hydrophobic Mismatch in Lipid Membrane Phase-Separation Kinetics.The packing density of a supramolecular membrane protein cluster is controlled by cytoplasmic interactions.Why cells need intramembrane proteases - a mechanistic perspective.The Multifaceted Role of SNARE Proteins in Membrane Fusion.Super-Resolution Microscopy: Shedding Light on the Cellular Plasma Membrane.Membrane lipids and cell signaling.Shaping intercellular channels of plasmodesmata: the structure-to-function missing link.Regulation of Exocytotic Fusion Pores by SNARE Protein Transmembrane Domains.Changes in Cholesterol Level Alter Integrin Sequestration in Raft-Mimicking Lipid Mixtures.Transmembrane region of bacterial chemoreceptor is capable of promoting protein clustering.The shape of the transmembrane domain is a novel endocytosis signal for single-spanning membrane proteins.Membrane lipid order of sub-synaptic T cell vesicles correlates with their dynamics and function.Directed Supramolecular Organization of N-BAR Proteins through Regulation of H0 Membrane Immersion Depth
P2860
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P2860
Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
description
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2015 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2015 թվականի հունվարին հրատարակված գիտական հոդված
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2015年の論文
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年學術文章
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Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
@ast
Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
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type
label
Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
@ast
Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
@en
prefLabel
Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
@ast
Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
@en
P2093
P2860
P50
P356
P1476
Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.
@en
P2093
Gesa Pähler
Helmut Grubmüller
Herre J Risselada
Meike Junius
Seiichi Koike
Stefan Müllar
P2860
P2888
P356
10.1038/NCOMMS6984
P407
P50
P577
2015-01-30T00:00:00Z