The IRG protein-based resistance mechanism in mice and its relation to virulence in Toxoplasma gondii.
about
Phagocyte responses to protozoan infection and how Toxoplasma gondii meets the challengeImmune response and immunopathology during toxoplasmosisRecent advances in understanding apicomplexan parasitesThe gut mucosal immune response to Toxoplasma gondiiIdentification of the microsporidian Encephalitozoon cuniculi as a new target of the IFNγ-inducible IRG resistance systemMAP kinase phosphatase-2 plays a key role in the control of infection with Toxoplasma gondii by modulating iNOS and arginase-1 activities in miceStructure of the Toxoplasma gondii ROP18 Kinase Domain Reveals a Second Ligand Binding Pocket Required for Acute VirulenceA Toxoplasma gondii pseudokinase inhibits host IRG resistance proteinsThe E2-like conjugation enzyme Atg3 promotes binding of IRG and Gbp proteins to Chlamydia- and Toxoplasma-containing vacuoles and host resistance.The Toxoplasma pseudokinase ROP5 forms complexes with ROP18 and ROP17 kinases that synergize to control acute virulence in mice.The parasitophorous vacuole membrane of Toxoplasma gondii is targeted for disruption by ubiquitin-like conjugation systems of autophagy.Modulation of innate immunity by Toxoplasma gondii virulence effectors.Toxoplasma co-opts host cells it does not invadeGuanylate-binding protein 1 (Gbp1) contributes to cell-autonomous immunity against Toxoplasma gondii.Enzymatically active Rho and Rac small-GTPases are involved in the establishment of the vacuolar membrane after Toxoplasma gondii invasion of host cells.IRG and GBP host resistance factors target aberrant, "non-self" vacuoles characterized by the missing of "self" IRGM proteinsSelf and non-self discrimination of intracellular membranes by the innate immune system.Border maneuvers: deployment of mucosal immune defenses against Toxoplasma gondii.Parasite fate and involvement of infected cells in the induction of CD4+ and CD8+ T cell responses to Toxoplasma gondii.Palmitoylation of the immunity related GTPase, Irgm1: impact on membrane localization and ability to promote mitochondrial fissionAMA1-deficient Toxoplasma gondii parasites transiently colonize mice and trigger an innate immune response that leads to long-lasting protective immunity.miR-146a and miR-155 delineate a MicroRNA fingerprint associated with Toxoplasma persistence in the host brain.Predominant role of interferon-γ in the host protective effect of CD8(+) T cells against Neospora caninum infection.A Noncanonical Autophagy Pathway Restricts Toxoplasma gondii Growth in a Strain-Specific Manner in IFN-γ-Activated Human Cells.Murine guanylate binding protein 2 (mGBP2) controls Toxoplasma gondii replicationCombined action of nucleic acid-sensing Toll-like receptors and TLR11/TLR12 heterodimers imparts resistance to Toxoplasma gondii in mice.Functional dissection of Toxoplasma gondii perforin-like protein 1 reveals a dual domain mode of membrane binding for cytolysis and parasite egressSecretion of Rhoptry and Dense Granule Effector Proteins by Nonreplicating Toxoplasma gondii Uracil Auxotrophs Controls the Development of Antitumor Immunity.A Toxoplasma dense granule protein, GRA24, modulates the early immune response to infection by promoting a direct and sustained host p38 MAPK activation.Toxoplasma gondii TgIST co-opts host chromatin repressors dampening STAT1-dependent gene regulation and IFN-γ-mediated host defenses.Repeated exposure to Lutzomyia intermedia sand fly saliva induces local expression of interferon-inducible genes both at the site of injection in mice and in human bloodChlamydia trachomatis Is Resistant to Inclusion Ubiquitination and Associated Host Defense in Gamma Interferon-Primed Human Epithelial Cells.Toxoplasma GRA7 effector increases turnover of immunity-related GTPases and contributes to acute virulence in the mouse.Virulent and avirulent strains of Toxoplasma gondii which differ in their glycosylphosphatidylinositol content induce similar biological functions in macrophages.Dual role for inflammasome sensors NLRP1 and NLRP3 in murine resistance to Toxoplasma gondii.Innate resistance against Toxoplasma gondii: an evolutionary tale of mice, cats, and men.Insights into inflammatory bowel disease using Toxoplasma gondii as an infectious trigger.Complex immune cell interplay in the gamma interferon response during Toxoplasma gondii infectionIdentification of small molecule inhibitors that block the Toxoplasma gondii rhoptry kinase ROP18.Interferon-inducible GTPases in cell autonomous and innate immunity.
P2860
Q22255519-0BA642ED-889F-49D6-A8C4-892456D15B6FQ24612341-16D1E345-D381-41C0-B9FB-89273B9979D9Q26747055-0B7C2971-39D3-4C24-AD3F-2C89B804DF73Q26863747-3FC84F0F-1917-4AEA-92C1-7C4D51A40BFEQ27323191-0FCA9317-1488-4DCF-BBF2-EDCD766517B7Q27334138-255BAA81-862E-4E86-85DC-4BC03FAAB911Q27680375-FD156A97-1B53-459D-A65D-C43287769D5AQ28481222-E49C1DA1-6A8C-4ADD-9BB2-575A07006672Q31148891-5ABE719A-8E54-46EF-9BB0-DD27282BC75EQ33861156-1CF732D8-F991-4199-90F1-56D38F95E22CQ33938258-46B9C107-F3AB-4E3D-A56C-D56218F96116Q34033981-D0206543-C1C6-4D84-A462-4DC1A252A271Q34387102-7F069C99-9223-47A5-A4A0-ECB73CE2D1E7Q34697891-FE56E52A-9956-4ED6-A445-1F01F8B4DD42Q34747385-A0535825-BE8B-43C8-8223-5AB1A28ACBEAQ34778494-08D0EDA5-BAD0-422C-9B51-06A29E94595AQ34998188-071187CE-1DFE-4BCB-BE49-417019E7E59CQ35143581-9D3E0EBA-72F0-4652-A2B7-19F7A105C1BEQ35145091-68FD2D4D-C227-4C31-8EBD-177A93C14E51Q35153885-3078974F-75C9-4D6A-AA40-FD5C2DFA533FQ35609307-B3D14525-4153-4148-B8AD-1C2C1E3AEA20Q35764747-C4E4A926-F02E-4B36-B5B5-29BD809BB4A3Q36139419-821B67ED-A896-4488-BC7C-89FE0CEC8ED5Q36143601-7F3E0415-7354-4503-93DC-E6DA3F09C08DQ36512191-93AD01D2-0B90-4897-A325-203607870C82Q36553712-D52AEDA6-572B-4089-96C4-3ECDEC28D81AQ36708689-AE65C255-AD09-46D4-B77A-F49418BCFD73Q37119146-E4722ACE-AB1C-4788-A56F-0097F33D50C5Q37194952-47388DAA-1356-4CC0-AB53-84AFE26F8832Q37197979-7B6C0FB4-E671-44A8-9E56-D7CE2BED52D1Q37464870-AF5D8B1A-7ECF-4139-B1D0-E5CFF45B2DE1Q37502917-B0FDCF68-BF4C-4A93-BF61-731A498DEEFAQ37519590-FE9C1782-D659-4E0C-8311-9F268256B5A5Q37525068-6C7A7D80-FF6D-41FA-B852-5F5F20866945Q37621648-63D9F841-69AF-4077-8052-11CB8586335CQ37735128-0C081CEC-ADD3-451E-B69D-66C6419E8F4CQ37953824-0954826A-50B7-4BC9-A35D-9A0D3DED2D35Q38215371-920F0F84-A74E-4C48-8A20-6FB3242A247AQ38437242-30C593AB-6A9E-4BFD-B778-FFB938343EDEQ38634433-2510491C-38BC-4F7C-869F-4CA0C611B5DB
P2860
The IRG protein-based resistance mechanism in mice and its relation to virulence in Toxoplasma gondii.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 23 July 2011
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The IRG protein-based resistan ...... irulence in Toxoplasma gondii.
@en
The IRG protein-based resistan ...... irulence in Toxoplasma gondii.
@nl
type
label
The IRG protein-based resistan ...... irulence in Toxoplasma gondii.
@en
The IRG protein-based resistan ...... irulence in Toxoplasma gondii.
@nl
prefLabel
The IRG protein-based resistan ...... irulence in Toxoplasma gondii.
@en
The IRG protein-based resistan ...... irulence in Toxoplasma gondii.
@nl
P1476
The IRG protein-based resistan ...... irulence in Toxoplasma gondii.
@en
P2093
Julia P Hunn
Tobias Steinfeldt
P304
P356
10.1016/J.MIB.2011.07.002
P577
2011-07-23T00:00:00Z