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

Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays.

The Journal of biological chemistry - 4 May 2012

Cao Qin, Wang Xiao-Jun, Liu Cheng-Wen, Liu Dai-Fei, Li Lan-Fen, Gao Yi-Qin, Su Xiao-Dong

Abstract excerpt

The apoptotic effector caspase-6 (CASP6) has been clearly identified as a drug target due to its strong association with neurodegeneration and axonal pruning events as well as its crucial roles in Huntington disease and Alzheimer disease. CASP6 activity is suppressed by ARK5-mediated phosphorylation at Ser(257) with an unclear mechanism. In this work, we solved crystal structures of ΔproCASP6S257E and...

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 Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Enzyme Activation

Share to Molecular Dynamics Simulation

Share to Phosphorylation

Share to Protein Structure, Tertiary

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 22433863
DOI: 10.1074/jbc.M112.351213
PMCID: PMC3346075

Genes

CASP6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays.PMID 22433863Read ↗

The regulatory mechanism of the caspase 6 pro-domain revealed by crystal structure and biochemical assays.Semantic proximity Read ↗

Allosteric regulation of the proteasome’s catalytic sites by the proteasome activator PA28γ /REGγSemantic proximity Read ↗

Designing peptide inhibitors targeting LRP6 co-receptor to restrict its association to DKK1; an Alzheimer’s disease therapeutic strategySemantic proximity Read ↗

'Polymorphism-aided' Selective Targeting and Inhibition of Caspase-6 by a Novel Allosteric Inhibitor Towards Efficient Alzheimer's Disease Treatment.Semantic proximity Read ↗

Delta-Secretase Phosphorylation by SRPK2 Enhances Its Enzymatic Activity, Provoking Pathogenesis in Alzheimer's Disease.Semantic proximity Read ↗

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches.Semantic proximity Read ↗

Structural Insight for Roles of DR5 Death Domain Mutations on Oligomerization of DR5 Death Domain-FADD Complex in the Death-Inducing Signaling Complex Formation: A Computational Study.Semantic proximity Read ↗

Microfluidic deep mutational scanning of the human executioner caspases reveals differences in structure and regulationSemantic proximity Read ↗

Effect of phosphorylation and single nucleotide polymorphisms on caspase substrates processing.Semantic proximity Read ↗

CDK5 mediated phosphorylation of cytosolic phospholipase A2 regulates its activity and neuroinflammation in Parkinson’s DiseaseSemantic proximity Read ↗

Rare human Caspase-6-R65W and Caspase-6-G66R variants identify a novel regulatory region of Caspase-6 activity.Semantic proximity Read ↗

Catalytic activity in vitro of the human protein kinase ASK1 mutants: Experimental and molecular simulation study.Semantic proximity Read ↗

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