Nod-like proteins in immunity, inflammation and disease. - sprookjes - yvandenbroek - TriplyDB

Nod-like proteins in immunity, inflammation and disease.

Nod-like proteins in immunity, inflammation and disease.

http://www.wikidata.org/entity/Q36655897

about

Inflammasome-mediated cell death in response to bacterial pathogens that access the host cell cytosol: lessons from legionella pneumophila A commensal Helicobacter sp. of the rodent intestinal flora activates TLR2 and NOD1 responses in epithelial cells Evolution and functional divergence of NLRP genes in mammalian reproductive systems A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response Effects of NOD-like receptors in human B lymphocytes and crosstalk between NOD1/NOD2 and Toll-like receptors ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways The Salmonella type III effector SspH2 specifically exploits the NLR co-chaperone activity of SGT1 to subvert immunity c-Abl tyrosine kinase interacts with MAVS and regulates innate immune response GEF-H1 mediated control of NOD1 dependent NF-kappaB activation by Shigella effectors PPM1B negatively regulates antiviral response via dephosphorylating TBK1 A novel motif in the Crohn's disease susceptibility protein, NOD2, allows TRAF4 to down-regulate innate immune responses An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix A role for the human nucleotide-binding domain, leucine-rich repeat-containing family member NLRC5 in antiviral responses The NLR gene family: a standard nomenclature Activation of innate immune antiviral responses by Nod2 Genomic analysis of the immune gene repertoire of amphioxus reveals extraordinary innate complexity and diversity A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-kappaB and JNK pathways by inducing reactive oxygen species production NLRX1: friend or foe?Cytolysin-dependent escape of the bacterium from the phagosome is required but not sufficient for induction of the Th1 immune response against Listeria monocytogenes infection: distinct role of Listeriolysin O determined by cytolysin gene replacement The Nucleotide Oligomerization Domain-Like Receptors in Kidney Injury The Modulation of Apoptotic Pathways by Gammaherpesviruses Modulation of liver tolerance by conventional and nonconventional antigen-presenting cells and regulatory immune cells NLRC5, at the Heart of Antigen Presentation Genetic update on inflammatory factors in ulcerative colitis: Review of the current literature Biochemical and structural aspects of the ATP-binding domain in inflammasome-forming human NLRP proteins Innate immune signaling in defense against intestinal microbes RIP2 activity in inflammatory disease and implications for novel therapeutics Comparative genomic analysis of buffalo (Bubalus bubalis) NOD1 and NOD2 receptors and their functional role in in-vitro cellular immune response Salmonella Typhimurium type III secretion effectors stimulate innate immune responses in cultured epithelial cells Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa Structural Basis of Recognition of Pathogen-associated Molecular Patterns and Inhibition of Proinflammatory Cytokines by Camel Peptidoglycan Recognition Protein Structural and Functional Analysis of the NLRP4 Pyrin Domain The NLRP12 Pyrin Domain: Structure, Dynamics, and Functional Insights Metainflammation in Diabetic Coronary Artery Disease: Emerging Role of Innate and Adaptive Immune Responses Danger signals, inflammasomes, and the intricate intracellular lives of chlamydiae Modulation of the host innate immune and inflammatory response by translocated bacterial proteins Polymorphisms in inflammasome genes and risk of coal workers' pneumoconiosis in a Chinese population The Nod-like receptor (NLR) family: a tale of similarities and differences Type IV secretion-dependent activation of host MAP kinases induces an increased proinflammatory cytokine response to Legionella pneumophila

P2860

Q21131296-F423A550-7FC0-4849-AB3A-CF91D7F5D007 Q21143791-81B0D8C9-9062-48BD-B1C8-CA76F83FA3F7 Q21283838-58E44048-6087-4032-9939-F5524CEF92DA Q22001534-C29CB23F-D6D7-401F-918D-0F9670190EA8 Q24299913-DAAC2476-0D1E-4B55-875B-790683E4F47F Q24313068-34D39514-AFF2-4E90-8D11-D7041D12C6F3 Q24317043-2CE47088-5A4F-4CBB-B2EB-56B6B638ED29 Q24317392-3507DD47-F3AC-40D6-B0D9-74147A045469 Q24319756-764E977C-6E56-42AC-9B3C-94759B4E56AF Q24339402-60E657B9-DB46-46B1-BB06-707047ADF94D Q24594581-77808D8A-ED8D-40A8-B177-B4FE234CC92D Q24616584-9FA23D3F-4905-4BF6-9973-E881809AF688 Q24630474-C36A8B50-E0D9-4275-8713-DB4EE9ADBF11 Q24645445-C72C2552-B12D-4A39-B865-5A8208053639 Q24646833-59FBCCE8-893A-4FCF-8D93-955F18102F4F Q24650676-E57926BC-45C0-4353-9191-8CAA39E92A26 Q24652200-AF0944DC-AEE7-435A-A6DF-DB3D1BC8F8BF Q24654451-21E8BBEF-128E-4251-84AC-B8D2DE87A7C9 Q24654601-11A6779E-369E-4145-BD94-DB1472C3329C Q24675620-52253234-72EB-4043-B9AF-BB4817CBE9C1 Q26740429-B76061A7-07DD-44C2-85E5-347175B4D89C Q26747452-1D4B2197-C3B1-4A80-8DAA-5DB022D0A498 Q26753022-017D07BC-09C4-4EC0-BF7F-8627DC4C216D Q26823400-77D4EE47-D578-4906-B722-81D5806A25ED Q26852514-3DB00FE1-5B0A-48DF-8FB5-08B854E5E549 Q26852840-C8686040-684E-4D4A-BDB5-0CD63F116E83 Q27002611-6993A680-A3CE-4D03-895B-352C357E2C11 Q27025050-79BFB2A4-5B12-42AA-ABFC-F4C3678EC4B0 Q27312426-FAD5AB29-9B86-4110-A8C3-16FFA5A0EFF0 Q27316415-9890212D-9A99-4B2B-A72B-080D3C4C453B Q27645881-FDFBBD73-9EB4-4212-A331-CB3AC7EA2DFE Q27667386-9112B4E1-E8CE-4E8E-9D8F-65AF68E99C77 Q27671760-F1856274-87E1-4272-9537-82DF2D28897E Q27674765-67634359-62FC-46B2-A87C-C7CA40822B3E Q28075968-C432B7FD-451F-43B5-9A1F-F589DCD5CFD4 Q28076278-CD8B7305-1B90-4628-A065-271BF21E7AE7 Q28083042-A4D00F73-3053-4C77-975E-1464FD2FFFD2 Q28390069-25BF73C2-96CE-40FF-B6CC-D0079CCC612D Q28472636-523E5F7F-653B-49C4-9E1A-83316AA6E534 Q28474072-1858A157-E205-40C2-B7D1-C11FFAB31029

P2860

Nod-like proteins in immunity, inflammation and disease.

http://www.wikidata.org/entity/Q36655897

description

2006 nî lūn-bûn

@nan

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

2006年论文

@zh

2006年论文

@zh-cn

name

Nod-like proteins in immunity, inflammation and disease.

@ast

Nod-like proteins in immunity, inflammation and disease.

@en

type

label

Nod-like proteins in immunity, inflammation and disease.

@ast

Nod-like proteins in immunity, inflammation and disease.

@en

prefLabel

Nod-like proteins in immunity, inflammation and disease.

@ast

Nod-like proteins in immunity, inflammation and disease.

@en

P1433

Q36655897-3CB1AA8B-B6DB-45F4-89B6-F4AA172D6429

P1476

Q36655897-89880164-C03B-40E9-993E-5A9B7A8C37FD

P2093

Q36655897-80CF4BE2-FBB5-459E-9E9E-0C9A6748015B

Q36655897-92E54D2E-E6A2-4E0F-B2EF-3C5FBD86DD01

Q36655897-BA770851-82E4-4955-8D48-D0B72193A09A

Q36655897-D37115B9-1BD6-4E9D-8E30-829F4CB4A6A0

P2860

Q36655897-04263DAC-CBD6-482C-B335-7B24C2CEA0A3

Q36655897-1215B4A7-3DEC-4DE9-BB9B-8F2510AAA059

Q36655897-12D24F85-D53F-4F4D-9EDE-86256652AC4C

Q36655897-12DADEC7-D959-4994-B0D3-DC0CFABA0AFF

Q36655897-14DEFA2D-67D0-4F2E-90C4-202F9B1DE904

Q36655897-193FFECA-C026-4A56-8201-C9F30AACE579

Q36655897-1E5FDAAA-BB1F-4CC6-8877-6BB69F7CC7CE

Q36655897-23E0EBB8-66CD-4DFA-BB3E-50D7253F92A7

Q36655897-26F82BFD-4DAE-4C54-A6D1-FF3629BD2FE3

Q36655897-28E0FF29-1673-442F-96AC-4AE4CAE156EF

P304

Q36655897-2563E113-66CC-497B-B2A2-4F5084CB5CCD

P31

Q36655897-F5EE78EA-7375-41F9-A005-7F75D11B97B5

P356

Q36655897-C6387A8F-9E96-4A2F-9437-DD2BE1D6D656

P407

Q36655897-25009530-B189-49C0-886C-84317FB2B89C

P433

Q36655897-156DF8AE-616C-49DC-95C5-89678B16D7A5

P478

Q36655897-ECCE2EA1-CDC5-4D6B-8F9C-14B6246FA12C

P577

Q36655897-57992E0F-5BDC-4F04-8554-DA09596AB7AB

P5875

Q36655897-AC01CF27-94BC-4953-B4B6-D4AC38734AD5

P698

Q36655897-FDD214AB-7C43-407C-A52E-871CF3BB701F

P356

P1433

Nature Immunology

P1476

Nod-like proteins in immunity, inflammation and disease.

@en

P2093

Dana J Philpott

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

Jörg H Fritz

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

Richard L Ferrero

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

Stephen E Girardin

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

P2860

A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease

Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection

GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells

Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition

NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder

Reciprocal cross-talk between Nod2 and TAK1 signaling pathways

The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO

A role for Erbin in the regulation of Nod2-dependent NF-kappaB signaling

Role for erbin in bacterial activation of Nod2

Nod1-mediated endothelial cell activation by Chlamydophila pneumoniae

P304

1250-1257

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

P31

scholarly article

P356

10.1038/NI1412

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

P407

P433

12

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

P478

7

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

P577

2006-12-01T00:00:00Z

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

P5875

6686822

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

P698

17110941

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