DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB (Q24312840)

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English	DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB	scientific article

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instance of

scholarly article

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title

DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB (English)

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main subject

NF-κB

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based on heuristic

inferred from title

author

Jürg Tschopp

series ordinal

9

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Etienne Meylan

object named as

Etienne Meylan

series ordinal

3

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Manuele Rebsamen

object named as

Manuele Rebsamen

series ordinal

1

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Kate Schroder

object named as

Kate Schroder

series ordinal

5

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Leonhard Heinz

series ordinal

2

object named as

Leonhard X Heinz

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Marie-Cécile Michallet

series ordinal

4

object named as

Marie-Cécile Michallet

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author name string

Kay Hofmann

series ordinal

6

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Jessica Vazquez

series ordinal

7

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Chris A Benedict

series ordinal

8

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language of work or name

English

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publication date

August 2009

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published in

EMBO Reports

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volume

10

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issue

8

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page(s)

916-22

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cites work

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DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response

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Receptor-interacting protein homotypic interaction motif-dependent control of NF-kappa B activation via the DNA-dependent activator of IFN regulatory factors

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Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1.

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Regulation of innate immune responses by DAI (DLM-1/ZBP1) and other DNA-sensing molecules

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Antiviral defense: interferons and beyond

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RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation

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Kappa B-type enhancers are involved in lipopolysaccharide-mediated transcriptional activation of the tumor necrosis factor alpha gene in primary macrophages

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Toll-like receptor-independent gene induction program activated by mammalian DNA escaped from apoptotic DNA degradation

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The antiviral adaptor proteins Cardif and Trif are processed and inactivated by caspases

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TANK-binding kinase-1 delineates innate and adaptive immune responses to DNA vaccines

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TRADD Protein Is an Essential Component of the RIG-like Helicase Antiviral Pathway

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Identifiers

DOI

10.1038/EMBOR.2009.109

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PMC publication ID

2726668

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PubMed publication ID

19590578

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ResearchGate publication ID

26659593

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