ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
about
Inflammasomes: too big to missFunction of Nod-like receptors in microbial recognition and host defenseBiochemical and structural aspects of the ATP-binding domain in inflammasome-forming human NLRP proteinsAn Update on PYRIN Domain-Containing Pattern Recognition Receptors: From Immunity to PathologyATP binding by NLRP7 is required for inflammasome activation in response to bacterial lipopeptidesThe Nod-like receptor (NLR) family: a tale of similarities and differencesNLRP12 suppresses colon inflammation and tumorigenesis through the negative regulation of noncanonical NF-κB signalingStructural models of zebrafish (Danio rerio) NOD1 and NOD2 NACHT domains suggest differential ATP binding orientations: insights from computational modeling, docking and molecular dynamics simulationsMeta-analysis of rare and common exome chip variants identifies S1PR4 and other loci influencing blood cell traits.Assessing ATP binding and hydrolysis by NLR proteinsClassical and/or alternative NF-kappaB pathway activation in multiple myeloma.Inflammasomes and their activation.Clinical presentation and pathogenesis of cold-induced autoinflammatory disease in a family with recurrence of an NLRP12 mutation.Inflammasomes and the microbiota--partners in the preservation of mucosal homeostasis.Emerging significance of NLRs in inflammatory bowel disease.NLRP12 provides a critical checkpoint for osteoclast differentiationPathogen sensing by nucleotide-binding oligomerization domain-containing protein 2 (NOD2) is mediated by direct binding to muramyl dipeptide and ATP.Regulation of class I major histocompatibility complex (MHC) by nucleotide-binding domain, leucine-rich repeat-containing (NLR) proteins.The nod-like receptor, Nlrp12, plays an anti-inflammatory role in experimental autoimmune encephalomyelitis.A new eye on NLR proteins: focused on clarity or diffused by complexity?Formation and structure of a NAIP5-NLRC4 inflammasome induced by direct interactions with conserved N- and C-terminal regions of flagellin.Unsolved Mysteries in NLR Biology.Functions of NOD-Like Receptors in Human Diseases.Blimp-1/PRDM1 mediates transcriptional suppression of the NLR gene NLRP12/Monarch-1NOD-like receptor (NLR) signaling beyond the inflammasomeNF-κB inducing kinase: a key regulator in the immune system and in cancerThe kinase NIK as a therapeutic target in multiple myeloma.The rhapsody of NLRPs: master players of inflammation...and a lot more.The role of interferon-β in the treatment of multiple sclerosis and experimental autoimmune encephalomyelitis - in the perspective of inflammasomes.Non-Inflammasome Forming NLRs in Inflammation and Tumorigenesis.The dual role of nod-like receptors in mucosal innate immunity and chronic intestinal inflammation.NLR-regulated pathways in cancer: opportunities and obstacles for therapeutic interventions.Pathogen perception by NLRs in plants and animals: Parallel worlds.Innate Immune Cell Recovery Is Positively Regulated by NLRP12 during Emergency Hematopoiesis.The inflammasome as a target for pain therapy.Understanding chemical allergen potency: role of NLRP12 and Blimp-1 in the induction of IL-18 in human keratinocytes.Side population cells have the characteristics of cancer stem-like cells/cancer-initiating cells in bone sarcomas.Identification and functional consequences of a recurrent NLRP12 missense mutation in periodic fever syndromes.Innate Immune Receptors.Is the inflammasome a potential therapeutic target in renal disease?
P2860
Q24647337-551F3F8B-FEC3-417E-817D-169EE2D477C0Q24647448-887F3A9C-26AF-45B4-BC56-C471EFF67975Q26852840-DBC1BEB3-8791-4DF1-A76A-26092941AB4FQ27004333-3066017D-9AA2-49CF-940B-9A4D0A232A46Q28388318-8C890B60-4694-4328-A7DD-57DAFA5319BBQ28472636-A0C1F015-7E1F-47AA-9996-B4E69435A1BDQ28505592-DDF4AB4E-607E-439D-B653-5B44C52DE5B3Q28545008-28633247-8BF7-4A3E-9BEA-7C37AFC796E6Q30354462-44295F13-67ED-4472-B50F-720E6E6EC72DQ33563515-2B028CC7-FA2A-4030-8C4C-DFC7FA351D3CQ33839840-8C3576B7-A098-438D-896B-4FF6807471DEQ34905606-2A4A6DCF-C3F9-4079-A248-030679C62C01Q35038760-ED5B89A5-8CF5-4A9F-8CB4-C94CC035C7C8Q35332035-D447B392-8304-4B85-914D-7FA6BC2F4D92Q35414220-5329A75F-3844-4A1A-AD40-8A6470DA810DQ35989917-5A153BA5-CC5B-4750-833C-E9AC841E1A6EQ36080388-7FB67B6F-8CA9-40A7-851E-20A0F0BF869FQ36097953-B9866455-9115-4080-84E6-71163FC8ECA1Q36234920-05A305DD-6D42-405D-BBE7-CCFE4CA40A07Q36351436-8400B7B5-9DC2-41A7-B1AE-C01949DB8CF3Q36385761-35396812-C199-4763-9E23-D7236D552873Q37176714-5C6F6C2E-25A9-4604-AE68-EA7CBE207003Q37231612-7BF3E3B9-0824-423C-894B-77FE1B19BF03Q37239308-CFE50EA7-F9A9-41F6-BAB7-E25B0840F402Q37702146-3AA1414E-064E-414A-89EC-B6326FFFC623Q37777775-A245A5B1-33CB-4E5B-AD0F-D7D587F8248AQ37825898-C6A2A113-4F84-4F76-A162-E0F7E6D94F46Q37994620-A6C6A539-342C-431C-99DB-BC1DCBAB6777Q38077590-1B46F508-0084-471D-97C5-3A5A39A5FB8EQ38209323-E8A609E2-DCDA-4381-A2A3-260A58B0C347Q38234947-554E9F2B-2513-4D15-A8AC-DBC210C9EFF8Q38680628-60CEDDB9-CB2D-4A0F-9C01-0936E92B50E0Q38875166-AD610E91-490B-4CBE-9420-DE987AA993ADQ38979899-189CB311-CDE6-4029-A727-DDE4FD134D97Q39036848-F9E4BE52-AB55-4694-BE91-F92A9E2F3820Q39431484-94BE9F9C-39BB-4159-9A5D-A4C148F88590Q39787753-0D127415-EC38-4DCD-9A27-96A24B599C0AQ40326197-C444F481-CF9A-4558-94A1-D6A1D407804FQ40661175-ACB6E8ED-1CA5-4774-9593-421F22E2BDF3Q41934684-D492F4EF-92EA-4195-817A-0BF8569AEE79
P2860
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
description
2008 nî lūn-bûn
@nan
2008 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մարտին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@ast
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@en
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@nl
type
label
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@ast
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@en
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@nl
prefLabel
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@ast
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@en
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@nl
P2093
P2860
P3181
P356
P1476
ATP binding by monarch-1/NLRP12 is critical for its inhibitory function
@en
P2093
Chris B Moore
Jenny P-Y Ting
John D Lich
Joseph A Duncan
Kristi L Williams
Zhengmao Ye
P2860
P304
P3181
P356
10.1128/MCB.01468-07
P407
P577
2008-03-01T00:00:00Z