Varaico: Literature-Extracted Genetic Variants

Gene:CASP8
Variant:p.C360S
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CASP8

NM_001372051.1:p.C360S

Associated Papers

Caspase-8 is a novel modulator of Homologous Recombination Repair in response to ionizing radiations in glioblastoma.

Ferri A et al.

Cancer Letters, 2026

N4BP1 functions as a dimerization-dependent linear ubiquitin reader which regulates TNF signalling.

Kliza KW et al.

Cell Death Discovery, 2024

Caspase-8 is the molecular switch for apoptosis, necroptosis and pyroptosis.

Fritsch M et al.

Nature, 2019

Q482H mutation of procaspase-8 in acute myeloid leukemia abolishes caspase-8-mediated apoptosis by impairing procaspase-8 dimerization.

Li M et al.

Biochemical and Biophysical Research Communications, 2018

RELT family members activate p38 and induce apoptosis by a mechanism distinct from TNFR1.

Moua P et al.

Biochemical and Biophysical Research Communications, 2017

The molluscum contagiosum virus death effector domain containing protein MC160 RxDL motifs are not required for its known viral immune evasion functions.

Beaury M et al.

Virus Genes, 2017

Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex.

Fu TM et al.

Molecular Cell, 2016

Intramolecular Interactions and Regulation of Cofactor Binding by the Four Repressive Elements in the Caspase Recruitment Domain-containing Protein 11 (CARD11) Inhibitory Domain.

Jattani RP et al.

The Journal of Biological Chemistry, 2016

The Inflammasome Adaptor ASC Induces Procaspase-8 Death Effector Domain Filaments.

Vajjhala PR et al.

The Journal of Biological Chemistry, 2015

Casp8p41 generated by HIV protease kills CD4 T cells through direct Bak activation.

Sainski AM et al.

The Journal of Cell Biology, 2014

A coupled protein and probe engineering approach for selective inhibition and activity-based probe labeling of the caspases.

Xiao J et al.

Journal of the American Chemical Society, 2013

Oncogenic CARD11 mutations induce hyperactive signaling by disrupting autoinhibition by the PKC-responsive inhibitory domain.

Lamason RL et al.

Biochemistry, 2010

Poxvirus MC160 protein utilizes multiple mechanisms to inhibit NF-kappaB activation mediated via components of the tumor necrosis factor receptor 1 signal transduction pathway.

Nichols DB et al.

Journal of Virology, 2009

The Parkinson disease protein leucine-rich repeat kinase 2 transduces death signals via Fas-associated protein with death domain and caspase-8 in a cellular model of neurodegeneration.

Ho CC et al.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2009

Cardiolipin provides an essential activating platform for caspase-8 on mitochondria.

Gonzalvez F et al.

The Journal of Cell Biology, 2008

The protein kinase C-responsive inhibitory domain of CARD11 functions in NF-kappaB activation to regulate the association of multiple signaling cofactors that differentially depend on Bcl10 and MALT1 for association.

McCully RR et al.

Molecular and Cellular Biology, 2008

FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies.

Milovic-Holm K et al.

The Embo Journal, 2007

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

Yang JK et al.

Molecular Cell, 2005

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

Garvey TL et al.

Journal of Virology, 2002

The ectodermal dysplasia receptor activates the nuclear factor-kappaB, JNK, and cell death pathways and binds to ectodysplasin A.

Kumar A et al.

The Journal of Biological Chemistry, 2001

TAJ, a novel member of the tumor necrosis factor receptor family, activates the c-Jun N-terminal kinase pathway and mediates caspase-independent cell death.

Eby MT et al.

The Journal of Biological Chemistry, 2000

DAP-kinase participates in TNF-alpha- and Fas-induced apoptosis and its function requires the death domain.

Cohen O et al.

The Journal of Cell Biology, 1999

Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling.

Vincenz C et al.

The Journal of Biological Chemistry, 1997

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Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."