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Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formationA drug delivery strategy: binding enkephalin to asialoglycoprotein receptor by enzymatic galactosylationLow-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.Biophysical characterization of lectin-glycan interactions for therapeutics, vaccines and targeted drug-delivery.Peptide based DNA nanocarriers incorporating a cell-penetrating peptide derived from neurturin protein and poly-L-lysine dendrons.The nature of the Syntaxin4 C-terminus affects Munc18c-supported SNARE assembly.Nanosized, peptide-based multicomponent DNA delivery systems: optimization of endosome escape activity.Revisiting interaction specificity reveals neuronal and adipocyte Munc18 membrane fusion regulatory proteins differ in their binding interactions with partner SNARE Syntaxins.The Munc18-1 domain 3a loop is essential for neuroexocytosis but not for syntaxin-1A transport to the plasma membrane.
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description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Michelle P Christie
@nl
Michelle P Christie
@sl
Michelle P. Christie
@en
Michelle P. Christie
@es
type
label
Michelle P Christie
@nl
Michelle P Christie
@sl
Michelle P. Christie
@en
Michelle P. Christie
@es
prefLabel
Michelle P Christie
@nl
Michelle P Christie
@sl
Michelle P. Christie
@en
Michelle P. Christie
@es
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0000-0002-7001-3400