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The C Isoform of Dictyostelium Tetraspanins Localizes to the Contractile Vacuole and Contributes to Resistance against Osmotic StressAttenuation of phospholipid signaling provides a novel mechanism for the action of valproic acid.Fluid-phase uptake by macropinocytosis in Dictyostelium.Fluid-phase uptake and transit in axenic Dictyostelium cells.A Dictyostelium mutant with reduced lysozyme levels compensates by increased phagocytic activity.Fusion and fission events in the endocytic pathway of Dictyostelium.Organelle transport: a park-and-ride system for melanosomes.Mechanisms of gene regulation by endogenous and artificially introduced antisense RNA.Dictyostelium discoideum Dgat2 can substitute for the essential function of Dgat1 in triglyceride production but not in ether lipid synthesis.Dictyostelium as a model for human lysosomal and trafficking diseases.Ethane-freezing/methanol-fixation of cell monolayers: a procedure for improved preservation of structure and antigenicity for light and electron microscopies.Lipid droplet dynamics at early stages of Mycobacterium marinum infection in Dictyostelium.pISAR, a tool for cloning genomic sequences adjacent to the site of vector integration.Two separable promoters control different aspects of expression of a Dictyostelium gene.Evidence for a feedback regulated back-up promoter which controls permanent expression of a Dictyostelium gene.Fat-containing cells are eliminated during Dictyostelium development.DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1, is involved in endocytosis, cytokinesis, and motility.Talin-null cells of Dictyostelium are strongly defective in adhesion to particle and substrate surfaces and slightly impaired in cytokinesis.Dictyostelium lipid droplets host novel proteins.Competition between targeting signals in hybrid proteins provides information on their relative in vivo affinities for subcellular compartments.Coronin and vacuolin identify consecutive stages of a late, actin-coated endocytic compartment in Dictyostelium.The BEACH protein LvsB is localized on lysosomes and postlysosomes and limits their fusion with early endosomes.The isoform B of the Dictyostelium long-chain fatty-acyl-coenzyme A synthetase is initially inserted into the ER and subsequently provides peroxisomes with an activity important for efficient phagocytosis.Targeting the actin-binding protein VASP to late endosomes induces the formation of giant actin aggregates.Developmental regulation of antisense-mediated gene silencing in Dictyostelium.Chemoattractant-controlled accumulation of coronin at the leading edge of Dictyostelium cells monitored using a green fluorescent protein-coronin fusion protein.Quantitative and microscopic methods for studying the endocytic pathway.Dictyostelium discoideumprotein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL-type retrieval signalVacuolin, a flotillin/reggie-related protein from Dictyostelium oligomerizes for endosome associationA colony-blot technique for the detection of specific transcripts in eukaryotes3' processing in Dictyostelium: unusual sequence requirements and interaction with a downstream promoterCoronin involved in phagocytosis: dynamics of particle-induced relocalization visualized by a green fluorescent protein TagGreen fluorescent protein in the visualization of particle uptake and fluid-phase endocytosisTargeted gene disruption reveals a role for vacuolin B in the late endocytic pathway and exocytosisA coat of filamentous actin prevents clustering of late-endosomal vacuoles in vivoA Dictyostelium long chain fatty acyl coenzyme A-synthetase mediates fatty acid retrieval from endosomes
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
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հետազոտող
@hy
name
Markus Maniak
@ast
Markus Maniak
@en
Markus Maniak
@es
Markus Maniak
@nl
Markus Maniak
@sl
type
label
Markus Maniak
@ast
Markus Maniak
@en
Markus Maniak
@es
Markus Maniak
@nl
Markus Maniak
@sl
prefLabel
Markus Maniak
@ast
Markus Maniak
@en
Markus Maniak
@es
Markus Maniak
@nl
Markus Maniak
@sl
P106
P21
P31
P496
0000-0001-6442-5372