Toxoplasma MIC2 is a major determinant of invasion and virulence
about
The roles of intramembrane proteases in protozoan parasitesThe inner membrane complex through development of Toxoplasma gondii and PlasmodiumFunctional characterization of a redundant Plasmodium TRAP family invasin, TRAP-like protein, by aldolase binding and a genetic complementation testParasite Calcineurin Regulates Host Cell Recognition and Attachment by ApicomplexansGliding motility of Babesia bovis merozoites visualized by time-lapse video microscopyConcerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondiiIdentification and characterization of Toxoplasma SIP, a conserved apicomplexan cytoskeleton protein involved in maintaining the shape, motility and virulence of the parasite.Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondiiThe toxoplasma Acto-MyoA motor complex is important but not essential for gliding motility and host cell invasionThe Conoid Associated Motor MyoH Is Indispensable for Toxoplasma gondii Entry and Exit from Host CellsDisruption of TgPHIL1 alters specific parameters of Toxoplasma gondii motility measured in a quantitative, three-dimensional live motility assayThe motility of a human parasite, Toxoplasma gondii, is regulated by a novel lysine methyltransferaseStructure of the micronemal protein 2 A/I domain fromToxoplasma gondiiStructures of the Toxoplasma gliding motility adhesinA tetracycline-repressible transactivator system to study essential genes in malaria parasitesApical membrane antigen 1 mediates apicomplexan parasite attachment but is dispensable for host cell invasion.Identification of T. gondii myosin light chain-1 as a direct target of TachypleginA-2, a small-molecule inhibitor of parasite motility and invasionA conserved apicomplexan microneme protein contributes to Toxoplasma gondii invasion and virulenceA DOC2 protein identified by mutational profiling is essential for apicomplexan parasite exocytosisToxoplasma gondii protease TgSUB1 is required for cell surface processing of micronemal adhesive complexes and efficient adhesion of tachyzoites.Structural basis for chirality and directional motility of Plasmodium sporozoites.Parasites lacking the micronemal protein MIC2 are deficient in surface attachment and host cell egress, but remain virulent in vivoProteomic analysis of calcium-dependent secretion in Toxoplasma gondii.Adenylyl cyclase alpha and cAMP signaling mediate Plasmodium sporozoite apical regulated exocytosis and hepatocyte infection.TgICMAP1 is a novel microtubule binding protein in Toxoplasma gondii.Toxoplasma gondii: 25 years and 25 major advances for the fieldHow apicomplexan parasites move in and out of cells.Toxoplasma gondii transmembrane microneme proteins and their modular design.Functional analysis of rhomboid proteases during Toxoplasma invasion.An overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemesIdentification of host proteins interacting with the integrin-like A domain of Toxoplasma gondii micronemal protein MIC2 by yeast-two-hybrid screening.Small-molecule inhibition of a depalmitoylase enhances Toxoplasma host-cell invasion.A Toxoplasma gondii protein with homology to intracellular type Na⁺/H⁺ exchangers is important for osmoregulation and invasion.Forward targeting of Toxoplasma gondii proproteins to the micronemes involves conserved aliphatic amino acids.Toxoplasma gondii-induced activation of EGFR prevents autophagy protein-mediated killing of the parasite.Structural basis of Toxoplasma gondii MIC2-associated protein interaction with MIC2Identification of genes expressed during Toxoplasma gondii infection by in vivo-induced antigen technology (IVIAT) with positive porcine sera.RON5 is critical for organization and function of the Toxoplasma moving junction complexA cleavable propeptide influences Toxoplasma infection by facilitating the trafficking and secretion of the TgMIC2-M2AP invasion complexThe apical complex provides a regulated gateway for secretion of invasion factors in Toxoplasma.
P2860
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P2860
Toxoplasma MIC2 is a major determinant of invasion and virulence
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Toxoplasma MIC2 is a major determinant of invasion and virulence
@ast
Toxoplasma MIC2 is a major determinant of invasion and virulence
@en
Toxoplasma MIC2 is a major determinant of invasion and virulence
@nl
type
label
Toxoplasma MIC2 is a major determinant of invasion and virulence
@ast
Toxoplasma MIC2 is a major determinant of invasion and virulence
@en
Toxoplasma MIC2 is a major determinant of invasion and virulence
@nl
prefLabel
Toxoplasma MIC2 is a major determinant of invasion and virulence
@ast
Toxoplasma MIC2 is a major determinant of invasion and virulence
@en
Toxoplasma MIC2 is a major determinant of invasion and virulence
@nl
P2860
P1433
P1476
Toxoplasma MIC2 is a major determinant of invasion and virulence
@en
P2093
My-Hang Huynh
P2860
P356
10.1371/JOURNAL.PPAT.0020084
P407
P577
2006-08-01T00:00:00Z