about
Guidelines for the use and interpretation of assays for monitoring autophagyA dibasic motif in the tail of a class XIV apicomplexan myosin is an essential determinant of plasma membrane localizationRab GDI: a solubilizing and recycling factor for rab9 proteinToxoplasma gondii myosins B/C: one gene, two tails, two localizations, and a role in parasite divisionReactive oxygen species and mitochondria: A nexus of cellular homeostasisSocial amoebae trap and kill bacteria by casting DNA netsOpen Source Drug Discovery with the Malaria Box Compound Collection for Neglected Diseases and BeyondRab7 and Rab9 are recruited onto late endosomes by biochemically distinguishable processesExploring anti-bacterial compounds against intracellular LegionellaEstablishment and validation of whole-cell based fluorescence assays to identify anti-mycobacterial compounds using the Acanthamoeba castellanii-Mycobacterium marinum host-pathogen systemLysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi networkRab9 functions in transport between late endosomes and the trans Golgi networkDual targeting of antioxidant and metabolic enzymes to the mitochondrion and the apicoplast of Toxoplasma gondiiMyosin-I nomenclature.Morphology and dynamics of the endocytic pathway in Dictyostelium discoideumA potentially exhaustive screening strategy reveals two novel divergent myosins in Dictyostelium.Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motorMycobacterium marinum antagonistically induces an autophagic response while repressing the autophagic flux in a TORC1- and ESX-1-dependent manner.European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS).A myosin IK-Abp1-PakB circuit acts as a switch to regulate phagocytosis efficiency.Vps13F links bacterial recognition and intracellular killing in DictyosteliumEat, kill or die: when amoeba meets bacteria.Regulation of aggregate size and pattern by adenosine and caffeine in cellular slime molds.High-resolution dissection of phagosome maturation reveals distinct membrane trafficking phasesEvolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifsMolecular characterization of the evolution of phagosomes.Infection by tubercular mycobacteria is spread by nonlytic ejection from their amoeba hosts.Actin polymerization driven by WASH causes V-ATPase retrieval and vesicle neutralization before exocytosis.The autophagic machinery ensures nonlytic transmission of mycobacteria.Unconventional myosins, actin dynamics and endocytosis: a ménage à trois?Involvement of the AP-1 adaptor complex in early steps of phagocytosis and macropinocytosisRab8a regulates the exocyst-mediated kiss-and-run discharge of the Dictyostelium contractile vacuoleAmoebae-Based Screening Reveals a Novel Family of Compounds Restricting Intracellular Legionella pneumophila.Mycobacterium marinum Degrades Both Triacylglycerols and Phospholipids from Its Dictyostelium Host to Synthesise Its Own Triacylglycerols and Generate Lipid InclusionsThe balance in the delivery of ER components and the vacuolar proton pump to the phagosome depends on myosin IK in Dictyostelium.Prison break: pathogens' strategies to egress from host cells.Powering membrane traffic in endocytosis and recycling.Of Amoebae and Men: Extracellular DNA Traps as an Ancient Cell-Intrinsic Defense Mechanism.WASH is required for lysosomal recycling and efficient autophagic and phagocytic digestion.WASH drives early recycling from macropinosomes and phagosomes to maintain surface phagocytic receptors
P50
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P50
description
hulumtues
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researcher
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wetenschapper
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հետազոտող
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name
Thierry Soldati
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Thierry Soldati
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Thierry Soldati
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Thierry Soldati
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Thierry Soldati
@sl
type
label
Thierry Soldati
@ast
Thierry Soldati
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Thierry Soldati
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Thierry Soldati
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Thierry Soldati
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prefLabel
Thierry Soldati
@ast
Thierry Soldati
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Thierry Soldati
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Thierry Soldati
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Thierry Soldati
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P1053
A-2902-2009
P106
P1153
7003724048
P21
P31
P3829
P496
0000-0002-2056-7931