Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide.
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Reconciling the regulatory role of Munc18 proteins in SNARE-complex assemblyConformational states of syntaxin-1 govern the necessity of N-peptide binding in exocytosis of PC12 cells and Caenorhabditis elegansCrystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformationSyntaxin binding mechanism and disease-causing mutations in Munc18-2Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate.Crucial role of the hydrophobic pocket region of Munc18 protein in mast cell degranulation.Munc18-1 and the Syntaxin-1 N Terminus Regulate Open-Closed States in a t-SNARE Complex.Allosteric control of syntaxin 1a by Munc18-1: characterization of the open and closed conformations of syntaxin.Munc18c: a controversial regulator of peripheral insulin action.Milligram quantities of homogeneous recombinant full-length mouse Munc18c from Escherichia coli cultures.Doc2b serves as a scaffolding platform for concurrent binding of multiple Munc18 isoforms in pancreatic islet β-cellsThe trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosisMunc18-1 controls SNARE protein complex assembly during human sperm acrosomal exocytosis.Munc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis.Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.Small angle neutron scattering for the study of solubilised membrane proteins.The Sec1/Munc18 Protein Groove Plays a Conserved Role in Interaction with Sec9p/SNAP-25.To protect or reject.Binding of SEC11 indicates its role in SNARE recycling after vesicle fusion and identifies two pathways for vesicular traffic to the plasma membrane.The nature of the Syntaxin4 C-terminus affects Munc18c-supported SNARE assembly.Revisiting interaction specificity reveals neuronal and adipocyte Munc18 membrane fusion regulatory proteins differ in their binding interactions with partner SNARE Syntaxins.Evidence for a conserved inhibitory binding mode between the membrane fusion assembly factors Munc18 and syntaxin in animals.Munc18a clusters SNARE-bearing liposomes prior to trans-SNARE zippering.Conformational change of syntaxin linker region induced by Munc13s initiates SNARE complex formation in synaptic exocytosis.
P2860
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P2860
Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@ast
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@en
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@nl
type
label
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@ast
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@en
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@nl
prefLabel
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@ast
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@en
Low-resolution solution struct ...... ven by the Syntaxin N-peptide.
@nl
P2093
P2860
P50
P356
P1476
Low-resolution solution struct ...... iven by the Syntaxin N-peptide
@en
P2093
Gordon J King
Philip Callow
Shu-Hong Hu
P2860
P304
P356
10.1073/PNAS.1116975109
P407
P50
P577
2012-06-05T00:00:00Z