Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Analysis of mutation effects on PIDDosome core complex.

Applied biochemistry and biotechnology - 1 May 2013

Jang Tae-Ho, Seo En Kyung, Park Hyun Ho

Abstract excerpt

PIDDosome is a recently-identified caspase-2-activating molecular complex formed by genotoxic stress that leads to caspase-2-dependent apoptosis. PIDD, RAIDD, and caspase-2 are three protein components of PIDDosome. The core portion of PIDDosome is formed by the unique screw rotation of seven RAIDD DD and five PIDD DD. In the current study, we found that two mutations generated during structural-based mutagenesis...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Apoptosis
Share to Cysteine Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Damage

Share to Escherichia coli

Share to Protein Multimerization

Share to Recombinant Fusion Proteins

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 23494218
DOI: 10.1007/s12010-013-0184-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Analysis of mutation effects on PIDDosome core complex.PMID 23494218Read ↗

Dissecting caspase-2-mediated cell death: from intrinsic PIDDosome activation to chemical modulationSemantic proximity Read ↗

Solution Structure of the CIDE-N Domain of CIDE-B and a Model for CIDE-N/CIDE-N Interactions in the DNA Fragmentation Pathway of ApoptosisSemantic proximity Read ↗

NPM1 directs PIDDosome-dependent caspase-2 activation in the nucleolus.Semantic proximity Read ↗

Evolutionary conservation of the intrinsic disorder-based Radical-Induced Cell Death1 hub interactomeSemantic proximity Read ↗

In silico scanning of structural and functional deleterious nsSNPs in Arabidopsis thaliana's SOG1 protein, using molecular dynamic simulation approaches.Semantic proximity Read ↗

General interaction mode of CIDE:CIDE complex revealed by a mutation study of the Drep2 CIDE domain.Semantic proximity Read ↗

Prediction and expression analysis of deleterious nonsynonymous SNPs of Arabidopsis ACD11 gene by combining computational algorithms and molecular docking approach.Semantic proximity Read ↗

Computational and Molecular Dynamics Simulation Approach To Analyze the Impact of <i>XPD</i> Gene Mutation on Protein Stability and FunctionSemantic proximity Read ↗

A Computational Approach for Structural and Functional Analyses of Disease-associated Mutations in the Human <i>CYLD</i> GeneSemantic proximity Read ↗

Stepwise phosphorylation and SUMOylation of PIDD1 drive PIDDosome assembly in response to DNA repair failureSemantic proximity Read ↗

Structural localization of pathogenic mutations in the central nucleotide-binding domain (NBD) of nucleotide-binding oligomerization domain-2 (NOD2) protein and their inference in inflammatory disorders.Semantic proximity Read ↗

Flavonoids as potential reactivators of structural mutation p53Y220C by computational and cell-based studies.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.