(Q24310283)

Baculoviral IAP repeat containing 2

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

zinc ion binding

1 reference

GOA release 2020-03-11

author

Callum Smits

2

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Peter D. Mace

Peter D Mace

1

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Catherine L. Day

Catherine L Day

5

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John Silke

John Silke

4

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David L Vaux

David L Vaux

Journal of Molecular Biology

3

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language of work or name

English

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publication date

2 July 2010

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published in

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volume

400

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page(s)

8-15

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issue

1

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cites work

The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

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IAP antagonists induce autoubiquitination of c-IAPs, NF-kappaB activation, and TNFalpha-dependent apoptosis

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IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis

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Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2.

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XIAP Induces NF-κB Activation via the BIR1/TAB1 Interaction and BIR1 Dimerization

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cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination

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Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction

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A tangled web of ubiquitin chains: breaking news in TNF-R1 signaling.

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A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction

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Structural Basis for the Lack of E2 Interaction in the RING Domain of TRAF2

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Structural basis for self-association and receptor recognition of human TRAF2

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Regulation of death receptor signaling by the ubiquitin system

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RIPK1 is not essential for TNFR1-induced activation of NF-kappaB.

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Noncanonical NF-kappaB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK.

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IAPs, RINGs and ubiquitylation

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E2 interaction and dimerization in the crystal structure of TRAF6

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Avid interactions underlie the Lys63-linked polyubiquitin binding specificities observed for UBA domains

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Both cIAP1 and cIAP2 regulate TNFalpha-mediated NF-kappaB activation

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Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors

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TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (tnf) to efficiently activate nf-{kappa}b and to prevent tnf-induced apoptosis.

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The inhibitor of apoptosis protein fusion c-IAP2.MALT1 stimulates NF-kappaB activation independently of TRAF1 AND TRAF2.

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Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment

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