Biophysical and cell-based evidence for differential interactions between the death domains of CD95/Fas and FADD (Q58449593)

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1 January 2020

title

Biophysical and cell-based evidence for differential interactions between the death domains of CD95/Fas and FADD (English)

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1 January 2020

5

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1 January 2020

author name string

B J Ferguson

1

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1 January 2020

D Esposito

2

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1 January 2020

J Jovanović

3

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1 January 2020

A Sankar

4

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1 January 2020

H Mehmet

6

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1 January 2020

publication date

29 June 2007

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Cell Death & Differentiation

1 January 2020

published in

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1 January 2020

volume

14

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1 January 2020

issue

9

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1 January 2020

page(s)

1717-1719

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Signaling by the TNF receptor superfamily and T cell homeostasis

1 January 2020

cites work

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

Apoptosis by death factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

Molecular ordering of the initial signaling events of CD95.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

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/10.1038%2FSJ.CDD.4402191

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

Defective CD95/APO-1/Fas signal complex formation in the human autoimmune lymphoproliferative syndrome, type Ia.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

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/10.1038%2FSJ.CDD.4402191

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/10.1038%2FSJ.CDD.4402191

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

21 January 2018

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https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

The death domain superfamily: a tale of two interfaces?

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

7 January 2021

Drug-induced apoptosis in hepatoma cells is mediated by the CD95 (APO-1/Fas) receptor/ligand system and involves activation of wild-type p53.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

7 January 2021

The molecular basis for apoptotic defects in patients with CD95 (Fas/Apo-1) mutations

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

7 January 2021

Extensive regions of the FADD death domain are required for binding to the TRAIL receptor DR5

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402191

7 January 2021

Identifiers

DOI

10.1038/SJ.CDD.4402191

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1 January 2020

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