IRG and GBP host resistance factors target aberrant, "non-self" vacuoles characterized by the missing of "self" IRGM proteins - Test2 - elhamkhani - TriplyDB

IRG and GBP host resistance factors target aberrant, "non-self" vacuoles characterized by the missing of "self" IRGM proteins

IRG and GBP host resistance factors target aberrant, "non-self" vacuoles characterized by the missing of "self" IRGM proteins

http://www.wikidata.org/entity/Q34778494

about

The gut mucosal immune response to Toxoplasma gondii Identification of the microsporidian Encephalitozoon cuniculi as a new target of the IFNγ-inducible IRG resistance system Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily Evolution of Cell-Autonomous Effector Mechanisms in Macrophages versus Non-Immune Cells Interferon-induced guanylate-binding proteins in inflammasome activation and host defense The 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.The Toxoplasma pseudokinase ROP5 is an allosteric inhibitor of the immunity-related GTPases.Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases.Self and non-self discrimination of intracellular membranes by the innate immune system.Palmitoylation of the immunity related GTPase, Irgm1: impact on membrane localization and ability to promote mitochondrial fission Toxoplasma gondii superinfection and virulence during secondary infection correlate with the exact ROP5/ROP18 allelic combination.IRGM3 contributes to immunopathology and is required for differentiation of antigen-specific effector CD8+ T cells in experimental cerebral malaria RabGDIα is a negative regulator of interferon-γ-inducible GTPase-dependent cell-autonomous immunity to Toxoplasma gondii 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.Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins 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 Secretion of Rhoptry and Dense Granule Effector Proteins by Nonreplicating Toxoplasma gondii Uracil Auxotrophs Controls the Development of Antitumor Immunity.Human GBP1 does not localize to pathogen vacuoles but restricts Toxoplasma gondii The Toxoplasma gondii rhoptry protein ROP18 is an Irga6-specific kinase and regulated by the dense granule protein GRA7.Chlamydia 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.Galectin-3 directs antimicrobial guanylate binding proteins to vacuoles furnished with bacterial secretion systems.Innate resistance against Toxoplasma gondii: an evolutionary tale of mice, cats, and men.Sensing the enemy, containing the threat: cell-autonomous immunity to Chlamydia trachomatis.Chlamydia-host cell interaction not only from a bird's eye view: some lessons from Chlamydia psittaci.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.Toxoplasma Effectors Targeting Host Signaling and Transcription.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.Targeting by AutophaGy proteins (TAG): Targeting of IFNG-inducible GTPases to membranes by the LC3 conjugation system of autophagy.Guanylate Binding Proteins regulate inflammasome activation in response to hyper-injected Yersinia translocon components.Metabolic Alterations Contribute to Enhanced Inflammatory Cytokine Production in Irgm1-deficient Macrophages.Guanylate-binding protein 1 (GBP1) contributes to the immunity of human mesenchymal stromal cells against Toxoplasma gondii.

P2860

Q26863747-4FEAB18B-43DA-4338-B6BE-71C6FDC33124 Q27323191-75A553BB-5984-4631-B9F5-54306334CD56 Q28079024-5C4CAE3F-9B6D-4A33-A1CD-BE8F3BA68843 Q28559840-1F0D5D99-B540-45CC-A58B-F96F07AE4497 Q28595838-AF4D6E9A-08ED-4D48-8706-E7A7AB5148AD Q31148891-5B10EA1A-1FEF-4EB2-B642-2C3FEDB35382 Q33861156-61DEB646-B49C-40A2-AEE7-2E025FA34301 Q33938258-45AF7F3D-BD64-4766-A8E0-764984BBDA89 Q34283543-5AE9A283-9F0B-404E-933A-AAB84801D6CB Q34415551-ADEF6296-F0AF-4254-B427-8FA4DC71B811 Q34998188-77D9C99E-8DF9-43E1-86CA-B2A77D15FF0F Q35153885-699EE5B4-4388-4EF7-875C-25A14007586A Q35172341-27B38C04-AEC8-4D15-AA51-7932C901A136 Q35187600-1BBEB839-6DE5-45AD-8607-044D9B5B6D13 Q35989946-83D80D04-2F3B-49FC-BD12-89AC0F8B4E0E Q35995190-89BB4DF4-A1E6-4698-89DE-5994ED4EE2C9 Q36179296-5978244C-BD9B-49CE-84AE-8894A9D3849D Q36281253-FFDF1E7D-CE64-42A2-B529-2922F072479C Q36389473-0BD356C4-4CB2-4931-8981-8744368B7904 Q36673756-D8C72A16-6D13-45D1-994F-C9B6C5ACA51A Q36950792-07203779-C330-4563-BF5F-122B1D527FFB Q37119146-336C1569-1F9C-4EF1-AE08-9A53D212900C Q37127539-B5D1F243-6E62-4071-8A6B-20EF826B7362 Q37334013-D97C80C9-AE08-4138-850D-1B32AD8332AA Q37502917-5130B37A-3F84-43D1-9F45-DFEC3B083B6F Q37519590-47B4A4AE-0FE0-43FA-B7CD-0DC42E097462 Q37682433-86A3F55C-F278-489D-B1CF-EF66144FB6A1 Q37735128-126295E7-C3D9-4A92-958C-09A8FF2D4DC0 Q37834944-29AAFF28-1A92-4FFA-B105-8E3648982FF5 Q37836009-BF47B5E5-F1F8-48D8-BC62-8F25B48074AC Q37836415-06DB4BE4-090C-43E8-9C2E-596F1AA90CFF Q37836804-A9F2B366-794D-4931-98C4-8207C2D6D99E Q38634433-2E021F1D-C82D-4430-A780-F282B7EF301C Q38731005-F41C22E8-6EA9-4456-9D4F-F4238F1331F8 Q38834935-D23EA6DF-52AF-41DE-A880-6586198B9CA4 Q39591613-0B902C65-67EE-427B-84DA-8E9B54672D45 Q39771819-5C73921B-86B6-4253-9583-852E254F907E Q40103031-DBA4F2CA-E1E6-4BE3-9F04-DC04FDBD7DFE Q40348070-754CF439-A774-4699-B717-115078275F26 Q40358072-6AC02111-ABBC-478E-8157-7AE9A135BD8F

P2860

IRG and GBP host resistance factors target aberrant, "non-self" vacuoles characterized by the missing of "self" IRGM proteins

http://www.wikidata.org/entity/Q34778494

description

2013 nî lūn-bûn

@nan

2013 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@ast

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@en

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@nl

type

label

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@ast

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@en

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@nl

prefLabel

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@ast

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@en

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@nl

P1433

Q34778494-F777975A-7356-4F57-9200-8C35577B0B45

P1476

Q34778494-45B02CFE-B12C-47BA-BFBF-992475BB747F

P2093

Q34778494-2C8F43C3-2EDB-44E5-B307-FB47FD7C8155

Q34778494-33B7DFAE-71ED-4710-8607-E79DD98DB77E

Q34778494-53193904-DBC8-4567-A3DF-0141344FD8C4

Q34778494-5F560BF2-D2CC-410B-92A9-BC28F084939E

Q34778494-BF82DB57-7275-4155-8A7A-6C1F9F855815

Q34778494-C408EE3A-AD25-46A5-AFD4-A4259F1C65F0

Q34778494-CCA5537A-B704-45CA-9403-D79E37E63E30

Q34778494-D6AD7DD4-2682-4735-82D7-04D3C5CF4354

Q34778494-DF13DA27-3B86-41EC-93DC-1C7607A873F8

P2860

Q34778494-05A87791-0089-460F-8ACD-48364066A6ED

Q34778494-08D0EDA5-BAD0-422C-9B51-06A29E94595A

Q34778494-1423DB1E-61EF-42A1-AC62-1E1983EC8624

Q34778494-1906FDDB-A9E7-4CE3-8D4A-1B11D1655D5A

Q34778494-1E9A1080-CC99-4205-A3FD-437844A2246F

Q34778494-23C33550-BA39-4660-83D6-D1481DDFDF8F

Q34778494-270A80F5-CB95-4CB3-9AAE-9DEEA44255BD

Q34778494-288EFE0E-FCFF-4CC8-A240-87938F198E0D

Q34778494-2A333FE2-DCDD-4B98-A495-B8C517D483DC

Q34778494-4138A450-E2CF-44C4-84E0-75466F03488E

P304

Q34778494-8AE474E6-A8BD-4851-BDB1-5894A76773A9

P31

Q34778494-1CB6F2FF-8D51-4A57-A075-F48D14855D88

P356

Q34778494-26BD30CE-9BB5-49BB-ACE2-46C4A852BB2A

P433

Q34778494-470EFF6C-7B3B-4941-B93F-2E8CDD4A9D60

P478

Q34778494-4CD1B161-D5C4-41EC-8CA2-02BB6B5CD3DD

P577

Q34778494-2CE488CF-53BC-4E2F-BEFE-F4702063BFDC

P5875

Q34778494-8C2E012E-236D-4C15-BE41-73A88EB68EB9

P698

Q34778494-19D0EB89-529B-4D5E-9255-7B6D479373FF

P932

Q34778494-B0B0186F-F867-4345-99BF-C260E11A8DD3

P356

JOURNAL.PPAT.1003414

P1433

P1476

IRG and GBP host resistance fa ...... issing of "self" IRGM proteins

@en

P2093

Anthony S Piro

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

Arun K Haldar

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

Eva M Frickel

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

Gregory A Taylor

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

Hector A Saka

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

Joe Dan Dunn

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

Jörn Coers

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

Raphael H Valdivia

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

Stanley C Henry

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

P2860

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

Guidelines for the use and interpretation of assays for monitoring autophagy

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

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

Human IRGM regulates autophagy and cell-autonomous immunity functions through mitochondria

Targeting of the GTPase Irgm1 to the phagosomal membrane via PtdIns(3,4)P(2) and PtdIns(3,4,5)P(3) promotes immunity to mycobacteria.

Determinants of GBP recruitment to Toxoplasma gondii vacuoles and the parasitic factors that control it

Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins

Interferon-gamma: an overview of signals, mechanisms and functions

Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis

P304

e1003414

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

P31

scholarly article

P356

10.1371/JOURNAL.PPAT.1003414

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

P433

6

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

P478

9

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

P577

2013-06-13T00:00:00Z

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

P5875

240306905

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

P698

23785284

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

P932

3681737

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