CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members (Q28201693)

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Theodore Tsichritzis

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Hannah Farmer

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George Mosialos

Identification of the familial cylindromatosis tumour-suppressor gene

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language of work or name

English

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publication date

14 August 2003

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published in

Nature

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volume

424

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issue

6950

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page(s)

793-6

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cites work

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Missing pieces in the NF-kappaB puzzle

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Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia

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Regulation of ubiquitin-dependent processes by deubiquitinating enzymes

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Involvement of a novel Tnf receptor homologue in hair follicle induction

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Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors

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Cellular signaling pathways engaged by the Epstein-Barr virus transforming protein LMP1.

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TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses.

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TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling

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Identification of a novel death domain-containing adaptor molecule for ectodysplasin-A receptor that is mutated in crinkled mice

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TRAF6-deficient mice display hypohidrotic ectodermal dysplasia

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Tumor necrosis factor receptor associated factor 2 is a mediator of NF-kappa B activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein

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TRAF6 is a critical mediator of signal transduction by the viral oncogene latent membrane protein 1

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Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain

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TAK1 is a ubiquitin-dependent kinase of MKK and IKK

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Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2).

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An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis

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The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation

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The alpha and beta subunits of IkappaB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF

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Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation

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Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde

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NF-kappaB in cancer: from innocent bystander to major culprit

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Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB

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The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family

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Ultraspiracle, a Drosophila retinoic X receptor alpha homologue, can mobilize the human thyroid hormone receptor to transactivate a human promoter.

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Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-kappaB activation

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