The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations (Q24302236)

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

Language	Label	Description	Also known as
English	The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations	scientific article	The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations

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scholarly article

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

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structural biology

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Fas cell surface death receptor

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GOA release 2020-03-11

Fas associated via death domain

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GOA release 2020-03-11

positive regulation of apoptotic process

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GOA release 2020-03-11

Fas (TNF receptor superfamily member 6)

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GOA release 2020-03-11

Richard M Siegel

object named as

Richard M Siegel

12

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object named as

Stefan Raunser

10

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Carol V. Robinson

object named as

Carol V Robinson

11

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author name string

Liwei Wang

1

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Jin Kuk Yang

2

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Venkataraman Kabaleeswaran

3

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Amanda J Rice

4

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Anthony C Cruz

5

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Ah Young Park

6

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Qian Yin

7

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Ermelinda Damko

8

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Se Bok Jang

9

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Thomas Walz

13

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Hao Wu

14

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language of work or name

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publication date

November 2010

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Nature Structural & Molecular Biology

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17

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1324-9

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11

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

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Negative staining and image classification — powerful tools in modern electron microscopy

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Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations

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

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

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19 March 2017

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

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Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex

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The three-dimensional solution structure and dynamic properties of the human FADD death domain

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Three-dimensional structure of a complex between the death domains of Pelle and Tube

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

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NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain

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The Fas signaling pathway: more than a paradigm

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The many roles of FAS receptor signaling in the immune system

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Fire and death: the pyrin domain joins the death-domain superfamily

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SPOTS: signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane

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Identification of an expanded binding surface on the FADD death domain responsible for interaction with CD95/Fas

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The death effector domain protein family: regulators of cellular homeostasis

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Autoimmune lymphoproliferative syndromes: genetic defects of apoptosis pathways

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Two adjacent trimeric Fas ligands are required for Fas signaling and formation of a death-inducing signaling complex

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21 January 2018

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12 December 2020

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10.1038/NSMB.1920

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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Springer Nature article ID

10.1038/nsmb.1920

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