about
A mechanism for retromer endosomal coat complex assembly with cargoGolgi localization of glycosyltransferases requires a Vps74p oligomerMembrane insertion of the FYVE domain is modulated by pHRiding the R Train into the CellPtdIns4 P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi traffickingStructural Insights into Assembly and Regulation of the Plasma Membrane Phosphatidylinositol 4-Kinase ComplexBiogenesis of endosome-derived transport carriers.Conserved structures and diversity of functions of RNA-binding proteinsMolecular mechanism of membrane docking by the Vam7p PX domain.Local control of phosphatidylinositol 4-phosphate signaling in the Golgi apparatus by Vps74 and Sac1 phosphoinositide phosphataseRab GTPase regulation of retromer-mediated cargo export during endosome maturation.Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component.Arf-like GTPases: not so Arf-like after all.FYVE domain targets Pib1p ubiquitin ligase to endosome and vacuolar membranes.Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling.Global mapping of the yeast genetic interaction network.Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3.Golgi targeting of ARF-like GTPase Arl3p requires its Nalpha-acetylation and the integral membrane protein Sys1p.Saccharomyces cerevisiae Rab-GDI displacement factor ortholog Yip3p forms distinct complexes with the Ypt1 Rab GTPase and the reticulon Rtn1p.Fission of SNX-BAR-coated endosomal retrograde transport carriers is promoted by the dynamin-related protein Vps1.The GAP activity of Msb3p and Msb4p for the Rab GTPase Sec4p is required for efficient exocytosis and actin organization.tGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing centreDirect binding of retromer to human papillomavirus type 16 minor capsid protein L2 mediates endosome exit during viral infectionAlpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiaePhosphatidylserine flipping enhances membrane curvature and negative charge required for vesicular transport.A CDC25 family protein phosphatase gates cargo recognition by the Vps26 retromer subunit.Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switchSac1-Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus.The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity.Retromer: a master conductor of endosome sorting.Coordination of Golgi functions by phosphatidylinositol 4-kinases.Physiology and pathology of endosome-to-Golgi retrograde sorting.Acidic di-leucine motif essential for AP-3-dependent sorting and restriction of the functional specificity of the Vam3p vacuolar t-SNARE.Opposing activities of the Snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosomeRNA binding specificity of hnRNP A1: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicingDeterminants of NPC1 expression and action: key promoter regions, posttranscriptional control, and the importance of a "cysteine-rich" loop.Receptor signalling and the regulation of endocytic membrane transport.Molecular dissection of guanine nucleotide dissociation inhibitor function in vivo. Rab-independent binding to membranes and role of Rab recycling factors.GDP dissociation inhibitor domain II required for Rab GTPase recycling.Novel pathways, membrane coats and PI kinase regulation in yeast lysosomal trafficking.
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Christopher G Burd
@ast
Christopher G Burd
@en
Christopher G Burd
@es
Christopher G Burd
@nl
Christopher G Burd
@sl
type
label
Christopher G Burd
@ast
Christopher G Burd
@en
Christopher G Burd
@es
Christopher G Burd
@nl
Christopher G Burd
@sl
prefLabel
Christopher G Burd
@ast
Christopher G Burd
@en
Christopher G Burd
@es
Christopher G Burd
@nl
Christopher G Burd
@sl
P106
P21
P31
P496
0000-0003-1831-8706