Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins - Test2 - elhamkhani - TriplyDB

Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins

Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins

http://www.wikidata.org/entity/Q36179296

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Recent advances in understanding apicomplexan parasites Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First Horizontally Transferred Ubiquitin Gene from a Mosquito Host Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily Interferon-induced guanylate-binding proteins in inflammasome activation and host defense TRIM21 is critical for survival of Toxoplasma gondii infection and localises to GBP-positive parasite vacuoles.Loss of the interferon-γ-inducible regulatory immunity-related GTPase (IRG), Irgm1, causes activation of effector IRG proteins on lysosomes, damaging lysosomal function and predicting the dramatic susceptibility of Irgm1-deficient mice to infection.K63-Linked Ubiquitination Targets Toxoplasma gondii for Endo-lysosomal Destruction in IFNγ-Stimulated Human Cells.Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages.Detection of a microbial metabolite by STING regulates inflammasome activation in response to Chlamydia trachomatis infection.Guanylate binding proteins directly attack Toxoplasma gondii via supramolecular complexes.Chlamydia cell biology and pathogenesis Human GBP1 does not localize to pathogen vacuoles but restricts Toxoplasma gondii Chlamydia trachomatis Is Resistant to Inclusion Ubiquitination and Associated Host Defense in Gamma Interferon-Primed Human Epithelial Cells.Galectin-3 directs antimicrobial guanylate binding proteins to vacuoles furnished with bacterial secretion systems.Sensing the enemy, containing the threat: cell-autonomous immunity to Chlamydia trachomatis.Subversion of Cell-Autonomous Host Defense by Chlamydia Infection.Ubiquitination of pathogen-containing vacuoles promotes host defense to Chlamydia trachomatis and Toxoplasma gondii.Interferon-inducible GTPases in cell autonomous and innate immunity.Immune Response: Intracellular pathogens under attack Viral Replication Complexes Are Targeted by LC3-Guided Interferon-Inducible GTPases.Tumor Necrosis Factor Receptor-Associated Factor 6 (TRAF6) Mediates Ubiquitination-Dependent STAT3 Activation upon Salmonella enterica Serovar Typhimurium Infection.Interferon-Inducible GTPases in Host Resistance, Inflammation and Disease.Quo vadis? Interferon-inducible GTPases go to their target membranes via the LC3-conjugation system of autophagy.Guanylate-binding protein 1 (GBP1) contributes to the immunity of human mesenchymal stromal cells against Toxoplasma gondii.The Ubiquitin Ligase Smurf1 Functions in Selective Autophagy of Mycobacterium tuberculosis and Anti-tuberculous Host Defense.The Rhoptry Pseudokinase ROP54 Modulates Toxoplasma gondii Virulence and Host GBP2 Loading.Broad recruitment of mGBP family members to Chlamydia trachomatis inclusions.Mechanisms and functions of guanylate-binding proteins and related interferon-inducible GTPases: roles in intracellular lysis of pathogens.Innate Immunity to Intracellular Pathogens: Balancing Microbial Elimination and Inflammation.Detection of Cytosolic Shigella flexneri via a C-Terminal Triple-Arginine Motif of GBP1 Inhibits Actin-Based Motility.The human guanylate-binding proteins hGBP-1 and hGBP-5 cycle between monomers and dimers only.Stable Isotope Labeling Reveals Novel Insights Into Ubiquitin-Mediated Protein Aggregation With Age, Calorie Restriction, and Rapamycin Treatment.Eat Prey, Live: Dictyostelium discoideum As a Model for Cell-Autonomous Defenses.Sweet host revenge: Galectins and GBPs join forces at broken membranes.Characterisation of the in vitro Chlamydia pecorum response to IFN-γ.LPS targets host guanylate-binding proteins to the bacterial outer membrane for non-canonical inflammasome activation.Demarcation of Viral Shelters Results in Destruction by Membranolytic GTPases: Antiviral Function of Autophagy Proteins and Interferon-Inducible GTPases.Murine Gbp1 and Gbp2 are ubiquitinated independent of Toxoplasma gondii infection.Lipid Droplet, a Key Player in Host-Parasite Interactions.

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P2860

Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins

http://www.wikidata.org/entity/Q36179296

description

2015 nî lūn-bûn

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

Ubiquitin systems mark pathoge ...... by guanylate binding proteins

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Ubiquitin systems mark pathoge ...... by guanylate binding proteins

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type

label

Ubiquitin systems mark pathoge ...... by guanylate binding proteins

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Ubiquitin systems mark pathoge ...... by guanylate binding proteins

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prefLabel

Ubiquitin systems mark pathoge ...... by guanylate binding proteins

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Ubiquitin systems mark pathoge ...... by guanylate binding proteins

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PNAS.1515966112

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Ubiquitin systems mark pathoge ...... by guanylate binding proteins

@en

P2093

Anthony S Piro

http://www.w3.org/2001/XMLSchema#string

Arun K Haldar

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Danielle M Pilla-Moffett

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Eva-Maria Frickel

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Jörn Coers

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Masaki Komatsu

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Ryan Finethy

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P2860

The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of the cell autonomous resistance mechanism in the human lineage.

Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNgamma-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death

IFN-gamma-inducible Irga6 mediates host resistance against Chlamydia trachomatis via autophagy

Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-resistance GTPases.

Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice

p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha.

The LRR and RING domain protein LRSAM1 is an E3 ligase crucial for ubiquitin-dependent autophagy of intracellular Salmonella Typhimurium

GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals

p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins

Coordinated loading of IRG resistance GTPases on to the Toxoplasma gondii parasitophorous vacuole

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E5628-37

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scholarly article

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10.1073/PNAS.1515966112

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41

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P478

112

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Clémence Foltz

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2015-09-28T00:00:00Z

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282292775

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26417105

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4611635

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