About: Interleukin-33 is biologically active independently of caspase-1 cleavage

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scientific article published on 22 May 2009

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 2009 (ast) наукова стаття, опублікована в травні 2009 (uk) مقالة علمية نشرت في 22 مايو 2009 (ar) scientific article published on 22 May 2009 (en)
publication date	wds:Q37339298-2B6052AE-2418-4387-A7C4-EF22FE1B263C
publication date	2009-05-22 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37339298-F310FD6A-A4F5-47F5-A780-6F529E2B1CDE
language of work or name	English
cites work	wds:Q37339298-1EB02F8E-EE11-4DEC-BBBA-C4EBA995909E wds:Q37339298-1F04E013-5929-4AEE-9DB1-80BDD66F3BCA wds:Q37339298-1FDB5402-BC10-4124-9B85-76AB00CF7EEF wds:Q37339298-229847C4-9F4B-4104-A6F9-67FAF2384FCD wds:Q37339298-27090DA0-0FF4-41A4-AF39-F9D907E52B6D wds:Q37339298-43A341DA-6D3E-45FC-9596-3CE622BECE2B wds:Q37339298-49260423-3502-411A-8FDE-3B612E0FBFDA wds:Q37339298-5586FEFA-1E9E-4DB4-9F9B-E6E96C890548 wds:Q37339298-6DEEF0B8-51A8-44BA-ACB6-3AFA2F9A296A wds:Q37339298-7A564B9E-6BFF-4005-967C-5ECDC7872E94 wds:Q37339298-A1B0F141-FFFE-451F-B827-717B69774973 wds:Q37339298-A3852198-7653-4D58-8C06-D227998A89FF wds:Q37339298-B926E3D6-078D-4287-A393-2061BE200E63 wds:Q37339298-BAAFD556-163D-4F96-A74E-3B3D97A93E4F wds:Q37339298-BE616AC8-8C9E-4BAF-BD62-06961F8206F7 wds:Q37339298-C5A00D53-349D-4C67-88F0-5AAB6EA5594F wds:Q37339298-C98DF374-E055-4D2F-AE1E-5924D5F0DB17 wds:Q37339298-CB65FE37-4B71-44C9-8FE8-C1F33C4A93D0 wds:Q37339298-E6364F63-3A6F-47B9-B5F2-7E0A1F7B9F93
cites work	IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines The IL-1-like cytokine IL-33 is constitutively expressed in the nucleus of endothelial cells and epithelial cells in vivo: a novel 'alarmin'? IL-33, the IL-1-like cytokine ligand for ST2 receptor, is a chromatin-associated nuclear factor in vivo Cutting edge: inflammasome activation by alum and alum's adjuvant effect are mediated by NLRP3. T1/ST2-deficient mice demonstrate the importance of T1/ST2 in developing primary T helper cell type 2 responses Active caspase-1 is a regulator of unconventional protein secretion Conditional suppression of cellular genes: lentivirus vector-mediated drug-inducible RNA interference The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity Caspase-1 activity is required for neuronal differentiation of PC12 cells: cross-talk between the caspase and calpain systems Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration Interleukin (IL)-33 induces the release of pro-inflammatory mediators by mast cells Targeted peptidecentric proteomics reveals caspase-7 as a substrate of the caspase-1 inflammasomes Production of IL-1 receptor antagonist by hepatocytes is regulated as an acute-phase proteinin vivo Induction of IL-33 expression and activity in central nervous system glia IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1 beta precursor at two distinct sites and does not cleave 31-kDa IL-1 alpha Cleavage of human cytosolic phospholipase A2 by caspase-1 (ICE) and caspase-8 (FLICE). Nuclear interleukin-33 is generally expressed in resting endothelium but rapidly lost upon angiogenic or proinflammatory activation. Alterations in NF-kappaB and RBP-Jkappa by arenavirus infection of macrophages in vitro and in vivo Pre-interleukin-1alpha expression reduces cell growth and increases interleukin-6 production in SaOS-2 osteosarcoma cells: Differential inhibitory effect of interleukin-1 receptor antagonist (icIL-1Ra1).
author name string	wds:Q37339298-7D745599-D1A6-4472-B85B-11A4D7FEF9AB wds:Q37339298-BF85D4D5-3584-44E3-A992-DE4E2AA5416E wds:Q37339298-DA885BE3-BC99-4532-A282-CD4FA7ED3A9B
author name string	Gaby Palmer Dominique Talabot-Ayer Céline Lamacchia
rdfs:label	Interleukin-33 is biologically active independently of caspase-1 cleavage (en) Interleukin-33 is biologically active independently of caspase-1 cleavage (nl) Interleukin-33 is biologically active independently of caspase-1 cleavage (ast)
skos:prefLabel	Interleukin-33 is biologically active independently of caspase-1 cleavage (en) Interleukin-33 is biologically active independently of caspase-1 cleavage (nl) Interleukin-33 is biologically active independently of caspase-1 cleavage (ast)
name	Interleukin-33 is biologically active independently of caspase-1 cleavage (en) Interleukin-33 is biologically active independently of caspase-1 cleavage (nl) Interleukin-33 is biologically active independently of caspase-1 cleavage (ast)
author	wds:Q37339298-6FEC0636-98E2-4192-BDF3-B8848E280029
author	Cem Gabay
title	wds:Q37339298-3D3B3536-449F-486B-8A33-8F9423B4D79D
title	Interleukin-33 is biologically active independently of caspase-1 cleavage (en)
page(s)	wds:Q37339298-4049EBA1-7744-4D9A-8728-6A408552BEF5
page(s)	19420-19426
instance of	wds:Q37339298-15A3BA17-15DD-46C6-BF76-86561E993764
instance of	scholarly article
main subject	wds:Q37339298-4f7e9ad1-cb7c-4802-8dc3-a45e2a1727d3
main subject	interleukins
PubMed ID	wds:Q37339298-FB328FF5-8346-4E2F-83DC-27DBE23852B3
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19465481
PubMed ID	19465481
published in	wds:Q37339298-8F41FDD4-9259-4B81-ACD9-83E2FF131DEF
published in	Journal of Biological Chemistry
issue	wds:Q37339298-61F9FD49-6FC9-4E1E-B466-52D805B50C40
volume	wds:Q37339298-1F5AA6CE-693E-4BF8-A3C0-D94C8ADA7A5E
issue	29
volume	284
DOI	wds:Q37339298-C1F65D3A-22D1-4ED1-8DA6-4F692D97B6F8
DOI	http://dx.doi.org/10.1074/JBC.M901744200
DOI	10.1074/JBC.M901744200
PMCID	wds:Q37339298-64C9795B-2A67-4BDC-971E-BD6FEE9B5570
PMCID	2740567
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q37339298
is cites work of	Intramyocardial fibroblast myocyte communication

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