t-SNARE protein conformations patterned by the lipid microenvironment. - sprookjes - yvandenbroek - TriplyDB

t-SNARE protein conformations patterned by the lipid microenvironment.

t-SNARE protein conformations patterned by the lipid microenvironment.

http://www.wikidata.org/entity/Q30494220

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Distinct initial SNARE configurations underlying the diversity of exocytosis Organization and dynamics of SNARE proteins in the presynaptic membrane Vesicle fusion probability is determined by the specific interactions of munc18 Regulation of Ca2+ channels by SNAP-25 via recruitment of syntaxin-1 from plasma membrane clusters A molecular toggle after exocytosis sequesters the presynaptic syntaxin1a molecules involved in prior vesicle fusion.Nanometric depth resolution from multi-focal images in microscopy.Multi-protein assemblies underlie the mesoscale organization of the plasma membrane.Super-resolution imaging reveals the internal architecture of nano-sized syntaxin clusters.Secretory vesicles are preferentially targeted to areas of low molecular SNARE density Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.Contact-induced clustering of syntaxin and munc18 docks secretory granules at the exocytosis site.Islet cholesterol accumulation due to loss of ABCA1 leads to impaired exocytosis of insulin granules.Dynamical Organization of Syntaxin-1A at the Presynaptic Active Zone Two-photon fluorescence lifetime imaging of primed SNARE complexes in presynaptic terminals and β cells Nanoscale Landscape of Phosphoinositides Revealed by Specific Pleckstrin Homology (PH) Domains Using Single-molecule Superresolution Imaging in the Plasma Membrane.Calcium Promotes the Formation of Syntaxin 1 Mesoscale Domains through Phosphatidylinositol 4,5-Bisphosphate.Lipids in Regulated Exocytosis: What are They Doing?Navigation through the Plasma Membrane Molecular Landscape Shapes Random Organelle Movement Molecular strategies to read and write at the nanoscale with far-field optics.Vesicle trafficking and membrane remodelling in cytokinesis.Analytical tools to monitor exocytosis: a focus on new fluorescent probes and methods.SNARE requirements en route to exocytosis: from many to few.Imaging large cohorts of single ion channels and their activity.Exocytosis through the Lens Super-resolution microscopy in studying neuroendocrine cell function.Cholesterol-enriched membrane rafts and insulin secretion.PI(4,5)P₂-binding effector proteins for vesicle exocytosis.The packing density of a supramolecular membrane protein cluster is controlled by cytoplasmic interactions.The Multifaceted Role of SNARE Proteins in Membrane Fusion.Munc18-1 protein molecules move between membrane molecular depots distinct from vesicle docking sites.Ca2+ induces clustering of membrane proteins in the plasma membrane via electrostatic interactions The L-type Voltage-Gated Calcium Channel co-localizes with Syntaxin 1A in nano-clusters at the plasma membrane.Vesicle Docking Is a Key Target of Local PI(4,5)P2 Metabolism in the Secretory Pathway of INS-1 Cells.Fluorescence Lifetime Imaging Microscopy reveals rerouting of SNARE trafficking driving dendritic cell activation

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t-SNARE protein conformations patterned by the lipid microenvironment.

http://www.wikidata.org/entity/Q30494220

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

t-SNARE protein conformations patterned by the lipid microenvironment.

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t-SNARE protein conformations patterned by the lipid microenvironment.

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type

label

t-SNARE protein conformations patterned by the lipid microenvironment.

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t-SNARE protein conformations patterned by the lipid microenvironment.

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prefLabel

t-SNARE protein conformations patterned by the lipid microenvironment.

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t-SNARE protein conformations patterned by the lipid microenvironment.

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JBC.M109.091058

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Journal of Biological Chemistry

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t-SNARE protein conformations patterned by the lipid microenvironment.

@en

P2093

Alison R Dun

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

Claire N Medine

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

David J Moulton

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

Luke H Chamberlain

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

Nagaraj D Halemani

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

Ondrej Mandula

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

Silvio O Rizzoli

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

P2860

Two-photon fluorescence microscopy of laurdan generalized polarization domains in model and natural membranes.

Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs

Ultra-high resolution imaging by fluorescence photoactivation localization microscopy

Helical extension of the neuronal SNARE complex into the membrane

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

Imaging intracellular fluorescent proteins at nanometer resolution

Self-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition.

SNAP receptors implicated in vesicle targeting and fusion

SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis

Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells

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10.1074/JBC.M109.091058

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18

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285

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2010-01-21T00:00:00Z

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20093362

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2859514

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