TRAMP, a novel apoptosis-mediating receptor with sequence homology to tumor necrosis factor receptor 1 and Fas(Apo-1/CD95) (Q24323902)

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1 November 2019

title

TRAMP, a novel apoptosis-mediating receptor with sequence homology to tumor necrosis factor receptor 1 and Fas(Apo-1/CD95) (English)

1 reference

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TNF receptor superfamily member 25

1 November 2019

main subject

apoptotic process

0 references

1 reference

cell surface receptor signaling pathway

GOA release 2020-03-11

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GOA release 2020-03-11

author

Pascal Schneider

3

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1 November 2019

Margot Thome

6

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1 November 2019

Lars E. French

12

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1 November 2019

Jeffrey L. Browning

13

1 reference

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1 November 2019

15

J Tschopp

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1 November 2019

J L Bodmer

1

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1 November 2019

K Burns

2

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1 November 2019

K Hofmann

4

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1 November 2019

V Steiner

5

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1 November 2019

T Bornand

7

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1 November 2019

M Hahne

8

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1 November 2019

M Schröter

9

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1 November 2019

K Becker

10

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1 November 2019

A Wilson

11

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1 November 2019

H R MacDonald

14

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1 November 2019

publication date

1 January 1997

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1 November 2019

language of work or name

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1 November 2019

volume

6

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1 November 2019

issue

1

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1 November 2019

page(s)

79-88

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

1 November 2019

cites work

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Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects

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7 January 2021

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

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The protein bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis

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Lymphotoxin beta, a novel member of the TNF family that forms a heteromeric complex with lymphotoxin on the cell surface

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Preparation and characterization of soluble recombinant heterotrimeric complexes of human lymphotoxins alpha and beta.

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

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The death domain: a module shared by proteins with diverse cellular functions.

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In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains

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Structure of the human TNF receptor 1 (p60) gene (TNFR1) and localization to chromosome 12p13 [corrected]

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7 January 2021

Melanoma cell expression of Fas(Apo-1/CD95) ligand: implications for tumor immune escape

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7 January 2021

Analysis of the role of bcl-2 in apoptosis.

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7 January 2021

Modes of DAPI banding and simultaneous in situ hybridization

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7 January 2021

ICE family proteases: mediators of all apoptotic cell death?

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7 January 2021

The death domain motif found in Fas (Apo-1) and TNF receptor is present in proteins involved in apoptosis and axonal guidance

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7 January 2021

The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation

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7 January 2021

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

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7 January 2021

Regulators of cell death

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The role of APO-1-mediated apoptosis in the immune system

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ICE-like proteases in apoptosis

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7 January 2021

Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor

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Requirement of an ICE/CED-3 protease for Fas/APO-1-mediated apoptosis

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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

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