Determinants of liposome fusion mediated by synaptic SNARE proteins. - Wikidata - awgldk - TriplyDB

Determinants of liposome fusion mediated by synaptic SNARE proteins.

Determinants of liposome fusion mediated by synaptic SNARE proteins.

http://www.wikidata.org/entity/Q36852539

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Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes Open syntaxin docks synaptic vesicles Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies Helical extension of the neuronal SNARE complex into the membrane Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate.Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum.Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous expression SNARE-fusion mediated insertion of membrane proteins into native and artificial membranes.Assembly and Comparison of Plasma Membrane SNARE Acceptor Complexes High cholesterol obviates a prolonged hemifusion intermediate in fast SNARE-mediated membrane fusion The SNARE motif of synaptobrevin exhibits an aqueous-interfacial partitioning that is modulated by membrane curvature.In vitro assay using engineered yeast vacuoles for neuronal SNARE-mediated membrane fusion.Rapid fusion of synaptic vesicles with reconstituted target SNARE membranes Docking and fast fusion of synaptobrevin vesicles depends on the lipid compositions of the vesicle and the acceptor SNARE complex-containing target membrane.Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion.Supported double membranes Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4,5-bisphosphate and cholesterol.Single molecule observation of liposome-bilayer fusion thermally induced by soluble N-ethyl maleimide sensitive-factor attachment protein receptors (SNAREs)SNARE-driven, 25-millisecond vesicle fusion in vitro.Kinetics of DNA-mediated docking reactions between vesicles tethered to supported lipid bilayers Productive hemifusion intermediates in fast vesicle fusion driven by neuronal SNAREs.SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes Single molecule mechanical probing of the SNARE protein interactions.Atomic force microscope spectroscopy reveals a hemifusion intermediate during soluble N-ethylmaleimide-sensitive factor-attachment protein receptors-mediated membrane fusion Intracellular bacteria encode inhibitory SNARE-like proteins Single-molecule studies of the neuronal SNARE fusion machinery.Docking, not fusion, as the rate-limiting step in a SNARE-driven vesicle fusion assay Molecular interaction studies using microscale thermophoresis.Model systems for membrane fusion.Novel interactions of CAPS (Ca2+-dependent activator protein for secretion) with the three neuronal SNARE proteins required for vesicle fusion.SNARE-mediated lipid mixing depends on the physical state of the vesicles.Homotypic fusion of early endosomes: SNAREs do not determine fusion specificity Are there too many or too few SNAREs in proteoliposomes?Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.Asymmetric phospholipid distribution drives in vitro reconstituted SNARE-dependent membrane fusion.Resolving single membrane fusion events on planar pore-spanning membranes Determinants of synaptobrevin regulation in membranes.Molecular Basis of the Membrane Interaction of the β2e Subunit of Voltage-Gated Ca(2+) Channels.Towards reconstitution of membrane fusion mediated by SNAREs and other synaptic proteins

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P2860

Determinants of liposome fusion mediated by synaptic SNARE proteins.

http://www.wikidata.org/entity/Q36852539

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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2004年论文

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2004年论文

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name

Determinants of liposome fusion mediated by synaptic SNARE proteins.

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type

label

Determinants of liposome fusion mediated by synaptic SNARE proteins.

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prefLabel

Determinants of liposome fusion mediated by synaptic SNARE proteins.

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PNAS.0400044101

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Determinants of liposome fusion mediated by synaptic SNARE proteins.

@en

P2093

Christina G Schuette

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

Dietmar Riedel

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Kiyotaka Hatsuzawa

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

Marcelle König

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

Martin Margittai

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

Petra Küster

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P2860

A conformational switch in syntaxin during exocytosis: role of munc18.

A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function

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

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs

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

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

Topological restriction of SNARE-dependent membrane fusion.

Compartmental specificity of cellular membrane fusion encoded in SNARE proteins.

SNAREpins: minimal machinery for membrane fusion

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9

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P478

101

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Alexander Stein

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2004-02-23T00:00:00Z

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5248535

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14981239

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365710

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