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Conserved prefusion protein assembly in regulated exocytosis.

Conserved prefusion protein assembly in regulated exocytosis.

http://www.wikidata.org/entity/Q41820253

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The diversity of calcium sensor proteins in the regulation of neuronal function Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution Push-and-pull regulation of the fusion pore by synaptotagmin-7 Differential but convergent functions of Ca2+ binding to synaptotagmin-1 C2 domains mediate neurotransmitter release Distinct initial SNARE configurations underlying the diversity of exocytosis The importance of an asymmetric distribution of acidic lipids for synaptotagmin 1 function as a Ca2+ sensor Synaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strength Cross-linking of phospholipid membranes is a conserved property of calcium-sensitive synaptotagmins An electrostatically preferred lateral orientation of SNARE complex suggests novel mechanisms for driving membrane fusion.Interaction of synaptotagmin with lipid bilayers, analyzed by single-molecule force spectroscopy.Synaptotagmin interaction with SNAP-25 governs vesicle docking, priming, and fusion triggering.Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex.Ca2+-dependent, phospholipid-binding residues of synaptotagmin are critical for excitation-secretion coupling in vivo Solution single-vesicle assay reveals PIP2-mediated sequential actions of synaptotagmin-1 on SNAREs.Synaptotagmin-7 is an asynchronous calcium sensor for synaptic transmission in neurons expressing SNAP-23 C2B polylysine motif of synaptotagmin facilitates a Ca2+-independent stage of synaptic vesicle priming in vivo.Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Post-translational modifications and lipid binding profile of insect cell-expressed full-length mammalian synaptotagmin 1 A role for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex dimerization during neurosecretion.The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function.Analysis of SNARE complex/synaptotagmin-1 interactions by one-dimensional NMR spectroscopy.Morphological docking of secretory vesicles.The blockade of the neurotransmitter release apparatus by botulinum neurotoxins.Binary polypeptide system for permanent and oriented protein immobilization.Functionally and spatially distinct modes of munc18-syntaxin 1 interaction A quaternary SNARE-synaptotagmin-Ca2+-phospholipid complex in neurotransmitter release.Calcineurin-mediated dephosphorylation of synaptotagmin VI is necessary for acrosomal exocytosis.Dissecting docking and tethering of secretory vesicles at the target membrane.Doc2B acts as a calcium sensor for vesicle priming requiring synaptotagmin-1, Munc13-2 and SNAREs.Mechanism of neurotransmitter release coming into focus

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P2860

Conserved prefusion protein assembly in regulated exocytosis.

http://www.wikidata.org/entity/Q41820253

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

2005年论文

@zh

2005年论文

@zh-cn

name

Conserved prefusion protein assembly in regulated exocytosis.

@en

type

label

Conserved prefusion protein assembly in regulated exocytosis.

@en

prefLabel

Conserved prefusion protein assembly in regulated exocytosis.

@en

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MBC.E05-07-0620

P1433

Molecular Biology of the Cell

P1476

Conserved prefusion protein assembly in regulated exocytosis.

@en

P2093

Bazbek Davletov

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

Deborah A Archer

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

José L Jiménez

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

Margaret E Graham

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

Mikhail Soloviev

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

Robert D Burgoyne

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

P2860

Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly

Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine

Three-dimensional structure of the complexin/SNARE complex

Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold

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

The atomic structure of protein-protein recognition sites

SNAP receptors implicated in vesicle targeting and fusion

Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties

Synaptotagmin I functions as a calcium regulator of release probability

Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis

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283-294

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10.1091/MBC.E05-07-0620

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1

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17

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16267273

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