about
Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative foldingStructural and functional characterization of the oxidoreductase alpha-DsbA1 from Wolbachia pipientisStructural and functional characterization of three DsbA paralogues from Salmonella enterica serovar TyphimuriumPossible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formationMembrane Curvature Protein Exhibits Interdomain Flexibility and Binds a Small GTPaseThe antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumpingCloning, expression, purification and characterization of a DsbA-like protein from Wolbachia pipientis.Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide.Milligram quantities of homogeneous recombinant full-length mouse Munc18c from Escherichia coli cultures.Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis.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.Studying Munc18:Syntaxin Interactions Using Small-Angle Scattering
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P50
description
researcher ORCID ID = 0000-0003-4326-1203
@en
wetenschapper
@nl
name
Russell Jarrott
@ast
Russell Jarrott
@en
Russell Jarrott
@es
Russell Jarrott
@nl
type
label
Russell Jarrott
@ast
Russell Jarrott
@en
Russell Jarrott
@es
Russell Jarrott
@nl
prefLabel
Russell Jarrott
@ast
Russell Jarrott
@en
Russell Jarrott
@es
Russell Jarrott
@nl
P1153
23972782300
P31
P496
0000-0003-4326-1203