(Q40624013)

22 September 2017

title

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

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22 September 2017

Justine M Hill

1

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22 September 2017

Gaku Morisawa

2

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22 September 2017

Tad Kim

3

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22 September 2017

Ted Huang

4

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22 September 2017

Yu Wei

5

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22 September 2017

Yufeng Wei

6

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22 September 2017

Milton H Werner

7

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22 September 2017

language of work or name

English

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publication date

22 October 2003

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Journal of Biological Chemistry

22 September 2017

published in

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22 September 2017

volume

279

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22 September 2017

issue

2

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22 September 2017

page(s)

1474-1481

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Death receptors: signaling and modulation

22 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Caspase-10 is an initiator caspase in death receptor signaling

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

NMR structure of the death domain of the p75 neurotrophin receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Solution structure of the tumor necrosis factor receptor-1 death domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Systematic mutational analysis of the death domain of the tumor necrosis factor receptor 1-associated protein TRADD.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Crystal structure of an isoleucine-zipper trimer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Insights into programmed cell death through structural biology

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

A novel domain within the 55 kd TNF receptor signals cell death

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Two CD95 (APO-1/Fas) signaling pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Protein structure comparison by alignment of distance matrices

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

Mutational analysis and NMR studies of the death domain of the tumor necrosis factor receptor-1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

A docking model of key components of the DISC complex: death domain superfamily interactions redefined

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304996200

21 January 2018

Identifiers

DOI

10.1074/JBC.M304996200

1 reference

22 September 2017

1 reference