Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structure - Wikidata - awgldk - TriplyDB

Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structure

Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structure

http://www.wikidata.org/entity/Q28268641

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Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18 A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function SNARE zippering SNAP-25, a Known Presynaptic Protein with Emerging Postsynaptic Functions Distinct initial SNARE configurations underlying the diversity of exocytosis Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a Helical extension of the neuronal SNARE complex into the membrane Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p.Identification of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiae The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly Pulling force generated by interacting SNAREs facilitates membrane hemifusion.Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes.Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex.Strategies for prokaryotic expression of eukaryotic membrane proteins.Functional and physical coupling of voltage-sensitive calcium channels with exocytotic proteins: ramifications for the secretion mechanism.SNARE-mediated lipid mixing depends on the physical state of the vesicles.What is the role of SNARE proteins in membrane fusion?SNARE proteins contribute to calcium cooperativity of synaptic transmission.Kinetics of complexin binding to the SNARE complex: correcting single molecule FRET measurements for hidden events Regulation of membrane fusion by the membrane-proximal coil of the t-SNARE during zippering of SNAREpins SNAREpins are functionally resistant to disruption by NSF and alphaSNAP.Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain.Lipid-anchored Synaptobrevin Provides Little or No Support for Exocytosis or Liposome Fusion.The SNARE complex from yeast is partially unstructured on the membrane.Syntaxin-17 delivers PINK1/parkin-dependent mitochondrial vesicles to the endolysosomal system.Mechanisms of biphasic insulin-granule exocytosis - roles of the cytoskeleton, small GTPases and SNARE proteins.The role of zinc binding in the biological activity of botulinum toxin.Review: Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes.Supramolecular pellicle precursors.SNARE protein trafficking in polarized MDCK cells.The cellular and developmental expression of hrs-2 in rat.SNAP-25 is targeted to the plasma membrane through a novel membrane-binding domain.SNARE interactions are not selective. Implications for membrane fusion specificity.SNARE complex zipping as a driving force in the dilation of proteinaceous fusion pores.Characterization of VAMP-2 in the lung: implication in lung surfactant secretion.Regulation of Exocytotic Fusion Pores by SNARE Protein Transmembrane Domains.Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling.The four-helix bundle of the neuronal target membrane SNARE complex is neither disordered in the middle nor uncoiled at the C-terminal region.Syntaxin 1A modulates the voltage-gated L-type calcium channel (Ca(v)1.2) in a cooperative manner.Differential phosphorylation of syntaxin and synaptosome-associated protein of 25 kDa (SNAP-25) isoforms.

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P2860

Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structure

http://www.wikidata.org/entity/Q28268641

description

1998 nî lūn-bûn

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1998 թուականի Մայիսին հրատարակուած գիտական յօդուած

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1998 թվականի մայիսին հրատարակված գիտական հոդված

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1998年の論文

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Protease resistance of syntaxi ...... ons for assembly and structure

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C Chan

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D S King

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Predicting coiled coils from protein sequences

Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase

Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones

Specificity and regulation of a synaptic vesicle docking complex

Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking

A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion

The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin

Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy

Coiled coils: new structures and new functions

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273

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