FADD self-association is required for stable interaction with an activated death receptor (Q40277983)

19 September 2017

FADD self-association is required for stable interaction with an activated death receptor (English)

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19 September 2017

C Sandu

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19 September 2017

G Morisawa

2

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19 September 2017

I Wegorzewska

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19 September 2017

T Huang

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19 September 2017

A F Arechiga

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19 September 2017

J M Hill

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19 September 2017

T Kim

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19 September 2017

C M Walsh

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19 September 2017

M H Werner

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19 September 2017

language of work or name

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19 May 2006

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Cell Death & Differentiation

19 September 2017

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19 September 2017

13

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19 September 2017

12

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19 September 2017

2052-2061

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https://scigraph.springernature.com/pub.10.1038/sj.cdd.4401966

19 September 2017

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A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain

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NMR structure and mutagenesis of the FADD (Mort1) death-effector domain

21 January 2018

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

21 January 2018

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Insights into programmed cell death through structural biology

21 January 2018

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FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex

21 January 2018

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

21 January 2018

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Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8

21 January 2018

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Caspase-10 is an initiator caspase in death receptor signaling

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Death receptors: signaling and modulation

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Two CD95 (APO-1/Fas) signaling pathways

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Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation

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Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5

21 January 2018

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Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation

21 January 2018

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FADD/MORT1 is a common mediator of CD95 (Fas/APO-1) and tumor necrosis factor receptor-induced apoptosis

21 January 2018

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A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis

21 January 2018

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Regulation of Fas-associated death domain interactions by the death effector domain identified by a modified reverse two-hybrid screen

21 January 2018

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Direct binding of Fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD.

21 January 2018

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A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes

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A role for FADD in T cell activation and development

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A mechanism for death receptor discrimination by death adaptors

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

21 January 2018

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Crystal structure of an isoleucine-zipper trimer

21 January 2018

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Fas- and tumor necrosis factor-mediated apoptosis uses the same binding surface of FADD to trigger signal transduction. A typical model for convergent signal transduction

21 January 2018

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

21 January 2018

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The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability

21 January 2018

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

21 January 2018

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Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis

21 January 2018

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Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain

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21 January 2018

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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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21 January 2018

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p53-dependent impairment of T-cell proliferation in FADD dominant-negative transgenic mice

21 January 2018

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Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling

21 January 2018

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Crystal structure of a viral FLIP: insights into FLIP-mediated inhibition of death receptor signaling

21 January 2018

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21 January 2018

Identifiers

DOI

10.1038/SJ.CDD.4401966

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Dimensions Publication ID

19 September 2017

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