scispace - formally typeset
C

Carsten Scaffidi

Researcher at German Cancer Research Center

Publications -  23
Citations -  12992

Carsten Scaffidi is an academic researcher from German Cancer Research Center. The author has contributed to research in topics: Fas receptor & Caspase 8. The author has an hindex of 20, co-authored 23 publications receiving 12787 citations. Previous affiliations of Carsten Scaffidi include National Institutes of Health.

Papers
More filters
Journal ArticleDOI

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

TL;DR: This work utilized nano-electrospray tandem mass spectrometry to identify CAP3 and CAP4, components of the CD95 (Fas/APO-1) death-inducing signaling complex, and found a novel 55 kDa protein, designated FLICE, which has homology to both FADD and the ICE/CED-3 family of cysteine proteases.
Journal ArticleDOI

Two CD95 (APO-1/Fas) signaling pathways

TL;DR: In the presence of caspase‐3 the amount of active casp enzyme‐8 generated at the DISC determines whether a mitochondria‐independent apoptosis pathway is used (type I cells) or not (type II cells).
Journal ArticleDOI

Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors

TL;DR: A new family of viral inhibitors (v-FLIPs) which interfere with apoptosis signalled through death receptors3 and which are present in several γ-herpesviruses (including Kaposi's-sarcoma-associated human herpesvirus-8), as well as in the tumorigenic human molluscipoxvirus4.
Journal ArticleDOI

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

TL;DR: The data indicate that FLICE is the first in a cascade of ICE‐like proteases activated by CD95 and that this activation requires a functional CD95 DISC.
Journal ArticleDOI

The Role of c-FLIP in Modulation of CD95-induced Apoptosis *

TL;DR: It is shown that c-FLIP is expressed in two isoforms, both of which, like FADD and caspase-8, are recruited to the CD95 DISC in a stimulation-dependent fashion and inhibits CD95-mediated apoptosis.