Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition - Wikidata - wikimedia - TriplyDB

Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition

Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition

http://www.wikidata.org/entity/Q34012966

about

The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations DED or alive: assembly and regulation of the death effector domain complexes On the Quest of Cellular Functions of PEA-15 and the Therapeutic Opportunities Helical assembly in the death domain (DD) superfamily Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex E2 interaction and dimerization in the crystal structure of TRAF6 Structure and Interdomain Dynamics of Apoptosis-associated Speck-like Protein Containing a CARD (ASC)Crystal Structure of NALP3 Protein Pyrin Domain (PYD) and Its Implications in Inflammasome Assembly Structure of the Absent in Melanoma 2 (AIM2) Pyrin Domain Provides Insights into the Mechanisms of AIM2 Autoinhibition and Inflammasome Assembly Structure of the caspase-recruitment domain from a zebrafish guanylate-binding protein Crystal Structure of the F27G AIM2 PYD Mutant and Similarities of Its Self-Association to DED/DED Interactions Molecular architecture of the DED chains at the DISC: regulation of procaspase-8 activation by short DED proteins c-FLIP and procaspase-8 prodomain FLIP and the death effector domain family Modeling a snap-action, variable-delay switch controlling extrinsic cell death Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex.The death domain superfamily in intracellular signaling of apoptosis and inflammation.A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death.In vitro reconstitution of the interactions in the PIDDosome An updated view on the structure and function of PYRIN domains.Substantial conformational change mediated by charge-triad residues of the death effector domain in protein-protein interactions The MC159 protein from the molluscum contagiosum poxvirus inhibits NF-κB activation by interacting with the IκB kinase complex.Identification and Characterization of the Interaction Site between cFLIPL and Calmodulin Identification of an acetylation-dependant Ku70/FLIP complex that regulates FLIP expression and HDAC inhibitor-induced apoptosis The molluscum contagiosum virus death effector domain containing protein MC160 RxDL motifs are not required for its known viral immune evasion functions.The Inflammasome Adaptor ASC Induces Procaspase-8 Death Effector Domain Filaments Caspase-containing complexes in the regulation of cell death and inflammation.Viral subversion of apoptotic enzymes: escape from death row.Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF).c-FLIP knockdown induces ligand-independent DR5-, FADD-, caspase-8-, and caspase-9-dependent apoptosis in breast cancer cells.FLIP as an anti-cancer therapeutic target.Structural basis of signal transduction in the TNF receptor superfamily Inhibition of interferon gene activation by death-effector domain-containing proteins from the molluscum contagiosum virus.Going up in flames: necrotic cell injury and inflammatory diseases.Role of Bcl-2 family proteins and caspases in the regulation of apoptosis.PYRIN domains and their interactions in the apoptosis and inflammation signaling pathway.Tandem DEDs and CARDs suggest novel mechanisms of signaling complex assembly.Death effecter domain for the assembly of death-inducing signaling complex.Structural basis of cell apoptosis and necrosis in TNFR signaling.Cellular FLICE-Inhibitory Protein Regulates Tissue Homeostasis.Gene expression profiles and signaling mechanisms in α2B-adrenoceptor-evoked proliferation of vascular smooth muscle cells.

P2860

Q24302236-0C568337-DC6B-4548-8F52-8D7880F607F5 Q26796544-AEABB26D-43FC-45FD-8293-DB3D68318075 Q26799216-05AB6F07-A858-405F-B8FC-32AF8B023824 Q27025156-95C7A5E8-9503-4AC3-883E-CACEA7F78706 Q27643768-53EB00D8-86C7-47A3-9693-4C0A33BC28C7 Q27655601-DD44A0BB-9EC5-4E0D-943B-FF5EE6892DB0 Q27657442-F69E11A9-A116-4DE0-A24B-0A9533BD0486 Q27672559-70037D30-C8FF-4220-9964-282C5F0C7272 Q27677057-111B249A-5B30-43A3-B45A-FE2CC0A7D813 Q27679338-B87186F4-17FD-40AF-949F-09C16E79C4C3 Q27681248-3B1A974D-1A99-465B-9D5B-D0D1AEA46C80 Q28268989-9D526835-2DDC-463D-84F9-8E651519A376 Q28297969-BCF284B8-2C94-4D4F-9FFD-E902F4F2DA24 Q28474253-C6D056F7-CE26-48AE-9C77-93C6888BA03E Q30275663-FBB40435-BB3B-4C91-95B4-9EAC8B2D8077 Q33996534-259BADA9-2ADB-414D-AE49-2DD5F228FA2E Q34032310-263BED4B-A821-4F8A-8A53-07EABA9B337B Q34711482-330439C3-B9D3-4862-9989-391807915D63 Q34978343-DE8F1674-35D3-4ABE-A6D0-90DBA0A677B9 Q35082465-1C1F1024-AAC0-4CC9-99EF-8816862A2C3E Q35785785-88E25CCE-AC56-4AC8-BED2-7EABA17C619D Q35830561-AFBA15E8-D6D8-4904-AF22-D08919E3A12E Q36084498-916A0F87-CB21-4DF8-A1C8-CBCB1A80C365 Q36351550-7E83A32A-7409-4979-8CA5-250EF17A69F0 Q36444012-BD11D9CF-00C8-4BFD-ABB7-4D570D985ED1 Q36559701-9C70B283-8741-444D-A7A5-BF367E448E3E Q36925632-6A937F00-E354-4952-A616-0F551E1B49E0 Q37024785-46717797-1E09-4F25-8EDA-B24343AB5ED9 Q37029417-65A06CDC-09A1-4925-A4D9-D5DF679A8F16 Q37096732-287691D1-E7C1-480D-A1FB-D50595382443 Q37194681-8FF1F992-9437-4B15-9544-C6BC587B421A Q37495190-CA911414-DC75-4639-A4EA-7CB6290AD213 Q37763609-B20DD7C2-3664-4C19-8013-E9CDC1F358DC Q37826384-D4C71E01-39B8-4D76-BE25-A3876E1B4321 Q38055709-FB272114-CFC0-434E-8872-17F31643DB76 Q38268330-7904B449-E96D-43FF-AA1F-4E1A734CEA6C Q38275781-2A6DDAFA-9B77-46AD-84AA-0FB4A5FC04B9 Q38275782-9C35DE07-8D74-4F8B-BEE5-6840E43EDBF0 Q38544605-79BE72FA-4179-455A-9D82-AAA81D9E4AEB Q38698722-51CE5595-C698-43CF-A662-589A2291EFF7

P2860

Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition

http://www.wikidata.org/entity/Q34012966

description

2005 nî lūn-bûn

@nan

2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@ast

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@en

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@nl

type

label

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@ast

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@en

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@nl

prefLabel

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@ast

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@en

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@nl

P1433

Q34012966-C0A91BE9-E82B-49E2-A6CB-DBF204AB83FA

P1476

Q34012966-BCD0E945-BF70-4580-A5B7-B2204EAC44DA

P2093

Q34012966-041ACE5F-5C3F-4DE7-9FBE-32B130DED82C

Q34012966-29D3388D-117C-4CFD-8A68-374140FCE8FE

Q34012966-3EE1EC73-6A81-44B9-BE54-BFEF0AE24FDB

Q34012966-4F141CE2-C05F-4C09-AACC-120E8FED196C

Q34012966-C6E3BC19-4C16-4CC3-8FE4-5E6CA49D4A1A

Q34012966-D5D4F08C-7ACF-4349-B80A-B85DD18EDF4F

Q34012966-DA00D732-E12D-43C6-959F-DD202C1C8DBE

P2860

Q34012966-0BBE7A71-5154-443F-B8AC-8F4FA1627552

Q34012966-0E74440B-516D-4533-82F8-94C6967663BF

Q34012966-13ABC6EA-C01E-4D70-A4C4-589B4025C2A6

Q34012966-14474572-3CA2-4D80-9A20-E8E098BF6E4B

Q34012966-198962CD-BE70-44D7-B1CE-5FA177407E66

Q34012966-1A2B86B1-5A81-4C2B-966E-F5DCBE9CF69F

Q34012966-1F594924-6AF4-45FD-B224-C1ED2890AE16

Q34012966-278AFE4E-EF6A-4630-9EDA-BA8EB4276149

Q34012966-296B01EB-180E-463C-8A86-506338EC37EE

Q34012966-2C0A7D36-1CDD-46D3-B75A-81C54CBB0683

P304

Q34012966-955DB447-D179-40DD-866E-B6EF1BDB1478

P31

Q34012966-34702379-02B5-4E79-BD45-646405EEA1F8

P356

Q34012966-32634373-CB16-46C8-A4DB-C2755CEABE11

P433

Q34012966-42C7074C-A0D9-44AA-A082-44DC8C7E594C

P478

Q34012966-8C593C58-EF9C-4E6C-B4A2-D340622CA176

P577

Q34012966-855D4583-3A7A-47FE-8CE8-6A7296DB31D7

P5875

Q34012966-7FA5A9EC-8476-4CA7-9E37-DF0474B4401A

P698

Q34012966-183E9154-E9AB-4CAF-A069-3240D6536DD8

P921

Q34012966-F81D728A-0508-4322-AA19-F6E8172BDCA8

P932

Q34012966-9209AAC2-3C09-429F-BC2C-0FC5B8AB9462

P356

J.MOLCEL.2005.10.023

P1433

P1476

Crystal structure of MC159 rev ...... C assembly and FLIP inhibition

@en

P2093

Fengyi Wan

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

Hao Wu

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

Jin Kuk Yang

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

Liwei Wang

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

Lixin Zheng

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

Michael J Lenardo

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

Misonara Ahmed

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

P2860

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

FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes

Casper is a FADD- and caspase-related inducer of apoptosis

Inhibition of death receptor signals by cellular FLIP

The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress

Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor

MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death

Improved methods for building protein models in electron density maps and the location of errors in these models

P304

939-949

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

P31

scholarly article

P356

10.1016/J.MOLCEL.2005.10.023

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

P433

6

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

P478

20

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

P577

2005-12-01T00:00:00Z

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

P5875

7405542

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

P698

16364918

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

P921

crystal structure

P932

2908330

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