The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production - Wikidata - awgldk - TriplyDB

The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production

The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production

http://www.wikidata.org/entity/Q34684433

about

TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*)The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment The efficacy of anakinra in an adolescent with colchicine-resistant familial Mediterranean fever The Relationship between NALP3 and Autoinflammatory Syndromes Update on Pyrin Functions and Mechanisms of Familial Mediterranean Fever Familial Mediterranean fever: current perspectives Treating rheumatological diseases and co-morbidities with interleukin-1 blocking therapies Lighting the fires within: the cell biology of autoinflammatory diseases Pyrin- and CARD-only Proteins as Regulators of NLR Functions A clear and present danger: inflammasomes DAMPing down disorders of pregnancy Beyond the NLRP3 inflammasome: autoinflammatory diseases reach adolescence Immunology in clinic review series; focus on autoinflammatory diseases: inflammasomes: mechanisms of activation The inflammasome pyrin contributes to pertussis toxin-induced IL-1β synthesis, neutrophil intravascular crawling and autoimmune encephalomyelitis COPs and POPs: modulators of inflammasome activity Co-regulation of NF-kappaB and inflammasome-mediated inflammatory responses by myxoma virus pyrin domain-containing protein M013 Pyrin inflammasome activation and RhoA signaling in the autoinflammatory diseases FMF and HIDS The inflammasome NLRs in immunity, inflammation, and associated diseases The AIM2 inflammasome is critical for innate immunity to Francisella tularensis Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants Identification of multifaceted binding modes for pyrin and ASC pyrin domains gives insights into pyrin inflammasome assembly.A genomic view of the NOD-like receptor family in teleost fish: identification of a novel NLR subfamily in zebrafish.Development of interleukin-1 receptor antagonist mutants with enhanced antagonistic activity in vitro and improved therapeutic efficacy in collagen-induced arthritis.Predominant role of host genetics in controlling the composition of gut microbiota.Elevated systemic antibodies towards commensal gut microbiota in autoinflammatory condition.Genetic variation in the familial Mediterranean fever gene (MEFV) and risk for Crohn's disease and ulcerative colitis.IL-1beta processing in host defense: beyond the inflammasomes.Potential of IL-1, IL-18 and Inflammasome Inhibition for the Treatment of Inflammatory Skin Diseases.Extraordinary antigenicity of the human Ro52 autoantigen.Monogenic IL-1 mediated autoinflammatory and immunodeficiency syndromes: finding the right balance in response to danger signals Rapidly progressive Creutzfeldt-Jakob disease in patients with Familial Mediterranean Fever Analysis of MEFV exon methylation and expression patterns in familial Mediterranean fever IL-1 blockade in autoinflammatory syndromes.Caspase functions in cell death and disease.Monogenic autoinflammatory diseases: new insights into clinical aspects and pathogenesis.Genetic loss of murine pyrin, the Familial Mediterranean Fever protein, increases interleukin-1β levels Pathogenesis of familial periodic fever syndromes or hereditary autoinflammatory syndromes.Advances in the understanding of familial Mediterranean fever and possibilities for targeted therapy.MEFV mutations affecting pyrin amino acid 577 cause autosomal dominant autoinflammatory disease.

P2860

2a94ab5b30297122aded4d003f3414bbbe27a1ad c02b91b6f78c32ff0c9b573027a85f2df883f2d9

P248

Q24294243-2A34308E-2D34-4DC1-8CA6-E65611E2B2DD Q24338801-F1416951-2BC3-44F5-ABE7-8011180661E4 Q24631660-8BA62B7C-2B09-41BF-B312-2FEDF627D455 Q24642151-A3D54800-9370-423A-8F7F-1AF3CA762A7C Q24656095-008A7026-3DAB-41D6-A034-947B6029FE7A Q26749025-1A7C68E4-4EFF-4625-9D14-7ED79022C8C6 Q26749573-00227F90-9560-4BF2-9094-E73675C21DA0 Q26751292-2C10E64B-4A07-4278-A05B-E46B46248703 Q26799747-9EC37369-38F4-4C2C-BADB-2C2449EE8989 Q26827163-FF38F4D0-998D-49AF-BAD4-05104E8D0323 Q26827832-7608BA4A-1F1B-4978-B589-5B33633917C6 Q27007734-CE7D1EA0-4278-4D3B-AB53-2011763541F0 Q27011650-D05434D6-B43C-4C43-A9F1-FBD04BFB18BC Q27021688-D8B6C9FF-2808-4FA5-9E57-0C65C6288714 Q27325503-BF7D853E-C914-461A-9E1D-E95B994B0081 Q28387485-6625DB6E-4C26-405B-B386-ADC75EC8BDF9 Q28391594-3EC06714-2447-46AE-9F40-08BDD835166B Q28596027-9A6F1D1C-8266-423D-840F-BF5D5E4A49DF Q29616025-65BCBD0E-376C-4968-BE30-251BABD936A8 Q29622833-BB20EE6E-286B-403E-991D-332D5876784C Q30489231-507E919A-F1F1-4B33-841F-533396AEFC4D Q30668589-349A02C3-4E44-41E9-B0BC-80A857CB53A6 Q33318582-3A564199-109C-46E2-BBF3-34C13AC0032A Q33345449-5B523777-B2A4-4630-BB47-D832CA17FD4D Q33363139-FCEBC555-7E8A-4DE6-9868-467731F33266 Q33367939-A287AEA2-83F6-4811-94CE-5E47B1B8C916 Q33507084-DBCEB200-424B-4070-A169-672C0F5FE748 Q33535878-A75DB4C8-227C-4AFE-80FE-86ABC521AE10 Q33710807-709832DE-AEA1-44F2-B4CF-CC5B6F4D0D0D Q33793461-CD02CF0D-B367-48A0-A2EB-DDD6EFB6E979 Q33798590-ED4A756A-0592-48DD-8CEB-D393C2B543D1 Q33955559-68FBC80D-11B9-49FD-B7F4-A6E19A50ECF5 Q33984080-500ADC48-4154-4CCA-91CF-A7EF8E57E9F6 Q34262561-9A02765A-3156-47B2-8EC8-3D31842F0011 Q34336335-92354EF9-7BDC-461F-A896-3FC07A84494D Q34489840-1C0C0528-8438-49E8-8202-6144F7F8E17A Q34506303-899DCF53-EAF2-4893-93DE-F3026B1B2F60 Q34560380-1FDA5199-0444-4A79-9DB6-FC94FB46D74C Q34608120-272F8C8E-499E-473F-A059-F92F9E5C2602 Q34625197-CF31EB2D-6732-49A5-BC5C-3DFE02D07BCC

P2860

The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production

http://www.wikidata.org/entity/Q34684433

description

2006 nî lūn-bûn

@nan

2006 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հունիսին հրատարակված գիտական հոդված

@hy

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

name

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@ast

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@en

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@nl

type

label

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@ast

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@en

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@nl

prefLabel

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@ast

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@en

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@nl

P1433

Q34684433-E922FCDF-F21D-4109-97D0-EBA75BEFD14C

P1476

Q34684433-CE327001-0D94-4AD8-96F5-7A7621669D0E

P2093

Q34684433-06B63E34-7E60-4D9E-8196-A7B181BCA110

Q34684433-5FFB6EF6-AB79-4706-B389-81855C1C1ABA

Q34684433-9B80134C-238E-4BA6-9305-D3D76F8ADAA9

Q34684433-CE8180E7-61E9-4E08-93ED-7CB9CAE1A411

Q34684433-E38D7DB5-EC1C-4254-953F-9300808AC7E0

P2860

Q34684433-00590456-E0E0-4226-AECE-DDD68F031A55

Q34684433-00C379C4-AA4C-456C-BDD5-2EEDDF58E223

Q34684433-00FF72CC-52B2-45B4-8CD4-350613B991C6

Q34684433-08E5FC89-DF26-483D-B2CF-6F607932D84A

Q34684433-0AD9E225-DAAB-407A-9E94-73FE9D5ABC17

Q34684433-11A25B53-4700-4B99-A380-EDF9330896C9

Q34684433-1B308A0C-D7FF-42CF-AA33-6E7A78C77D23

Q34684433-2EA1D2EF-1A38-4A53-801C-382000E3D4F3

Q34684433-2FEBBC81-ADF8-4E6B-B082-12CA397453BB

Q34684433-34BDECEB-E066-4EF5-A8D5-4BB64E2DFBB0

P304

Q34684433-8EC7B885-DBC8-4504-8F77-E24E623B0EE9

P31

Q34684433-0659B2C7-1B8E-453F-9B47-3A70133AFD2F

P356

Q34684433-01DEF437-76F8-498E-9315-6FAA7327F9BE

P407

Q34684433-8029C3E9-F388-42F7-A0E6-879412A61A6B

P433

Q34684433-D354D764-0459-4E83-B2BE-C29C213D608B

P478

Q34684433-B828AF60-B962-4716-97F8-1FD1A36BA6AD

P50

Q34684433-890E073C-5A30-493B-B706-59F5CB94E810

Q34684433-E1DEB029-BFA1-45BD-A1DE-87EA2F4D2461

P577

Q34684433-987B4063-CD7B-47E9-A641-5D4B24321566

P5875

Q34684433-C7C31669-8CA2-4A09-A841-F95522ABC571

P698

Q34684433-98F3EF2C-CA73-4132-86D8-7500EA25CE05

P932

Q34684433-3FF744B1-AD4B-4DF3-A0F8-D468D15F6304

P356

PNAS.0602081103

P1433

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

P1476

The B30.2 domain of pyrin, the ...... o modulate IL-1beta production

@en

P2093

Daniel L Kastner

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

Geryl Wood

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

Grace Park

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

Jae Jin Chae

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

Katharina Richard

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

P2860

ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells

Human CARD12 is a novel CED4/Apaf-1 family member that induces apoptosis

Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1

CLAN, a novel human CED-4-like gene

ASC is an activating adaptor for NF-kappa B and caspase-8-dependent apoptosis

The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta

RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase

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

Identification of CARDIAK, a RIP-like kinase that associates with caspase-1

The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor kappaB activation pathways

P304

9982-9987

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

P31

scholarly article

P356

10.1073/PNAS.0602081103

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

P407

P433

26

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

P478

103

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

P50

P577

2006-06-19T00:00:00Z

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

P5875

6999395

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

P698

16785446

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

P932

1479864

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