Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study. (Q48329932)

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scientific article published in December 1998

Language	Label	Description	Also known as
English	Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study.	scientific article published in December 1998

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scholarly article

1 reference

Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study. (English)

1 reference

Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

author name string

Cánaves JM

1

1 reference

Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

Montal M

2

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Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

language of work or name

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publication date

1 December 1998

1 reference

Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

Journal of Biological Chemistry

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Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

273

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Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

34214-34221

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Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

51

1 reference

Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

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

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Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation.

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The synaptic vesicle cycle: a cascade of protein-protein interactions

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SNAP receptors implicated in vesicle targeting and fusion

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

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SNAREpins: minimal machinery for membrane fusion

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An alpha-helical minimal binding domain within the H3 domain of syntaxin is required for SNAP-25 binding

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Structural organization of the synaptic exocytosis core complex

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Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic function

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Peptide 'Velcro': design of a heterodimeric coiled coil.

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Predicting coiled coils from protein sequences

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Prediction and analysis of coiled-coil structures

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Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release

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Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds

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Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins.

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Botulinum neurotoxin type G proteolyses the Ala81-Ala82 bond of rat synaptobrevin 2.

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Inhibition of neurotransmitter release by synthetic proline-rich peptides shows that the N-terminal domain of vesicle-associated membrane protein/synaptobrevin is critical for neuro-exocytosis

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A post-docking role for synaptobrevin in synaptic vesicle fusion

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Inhibition of insulin release by synthetic peptides shows that the H3 region at the C-terminal domain of syntaxin-1 is crucial for Ca(2+)- but not for guanosine 5'-[gamma-thio]triphosphate-induced secretion.

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The 26-mer peptide released from SNAP-25 cleavage by botulinum neurotoxin E inhibits vesicle docking

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Endocytosis of VAMP is facilitated by a synaptic vesicle targeting signal

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DNA recognition by GAL4: structure of a protein-DNA complex.

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Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin

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Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements

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Intermolecular beta-sheet results from trifluoroethanol-induced nonnative alpha-helical structure in beta-sheet predominant proteins: infrared and circular dichroism spectroscopic study.

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Non-specific helix-induction in charged homopolypeptides by alcohols.

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Structure, function and application of the coiled-coil protein folding motif

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A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A

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Structural analysis of peptides encompassing all alpha-helices of three alpha/beta parallel proteins: Che-Y, flavodoxin and P21-ras: implications for alpha-helix stability and the folding of alpha/beta parallel proteins

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Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the alpha-helix fragment

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The stability of tropomyosin, a two-stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface.

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A Structural Change Occurs upon Binding of Syntaxin to SNAP-25

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Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25

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A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells

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Stabilization of the ribonuclease S-peptide alpha-helix by trifluoroethanol

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Identifiers

10.1074/JBC.273.51.34214

1 reference

Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

1 reference

Europe PubMed Central

10 February 2018

http://europepmc.org/abstract/MED/9852083

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