In vitro reconstitution of interactions in the CARD9 signalosome.

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In vitro reconstitution of interactions in the CARD9 signalosome.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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In vitro reconstitution of interactions in the CARD9 signalosome.

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In vitro reconstitution of interactions in the CARD9 signalosome.

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In vitro reconstitution of interactions in the CARD9 signalosome.

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P1476

In vitro reconstitution of interactions in the CARD9 signalosome.

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P2093

Hyun Ho Park

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Jae Young Choi

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Jin Hee Park

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Mir Faisal Mustafa

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P2860

Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1

Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma

Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation

The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations

Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO

T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20

The Fas-FADD death domain complex structure unravels signalling by receptor clustering

The adaptor protein CARD9 is required for innate immune responses to intracellular pathogens

SWISS-MODEL: An automated protein homology-modeling server

The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD

P304

3910-3916

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P31

scholarly article

P356

10.3892/MMR.2017.7116

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P433

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P478

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

P577

2017-07-31T00:00:00Z

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P698

28765954

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P932

5646969

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