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

Cleavage at the 586 Amino Acid Caspase-6 Site in Mutant huntingtin Influences Caspase-6 ActivationIn Vivo

10 Nov 2010

Abstract excerpt

Caspase cleavage of huntingtin (htt) and nuclear htt accumulation represent early neuropathological changes in brains of patients with Huntington's disease (HD). However, the relationship between caspase cleavage of htt and caspase activation patterns in the pathogenesis of HD remains poorly understood. The lack of a phenotype in YAC mice expressing caspase-6-resistant (C6R) mutant htt (mhtt) highlights...

Read the complete abstract on PubMed

Topics

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

Share to Genetic Neurodegenerative Diseases
Share to Mitochondrial Function and Pathology
Share to Neurological disorders and treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 21068307
DOI: 10.1523/jneurosci.2071-10.2010

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cleavage at the 586 Amino Acid Caspase-6 Site in Mutant huntingtin Influences Caspase-6 ActivationIn VivoPMID 21068307Read ↗

Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin.Semantic proximity Read ↗

Identification of a novel caspase cleavage site in huntingtin that regulates mutant huntingtin clearanceSemantic proximity Read ↗

Activated caspase-6 and caspase-6-cleaved fragments of huntingtin specifically colocalize in the nucleus.Semantic proximity Read ↗

Transgenic mice expressing caspase-6-derived N-terminal fragments of mutant huntingtin develop neurologic abnormalities with predominant cytoplasmic inclusion pathology composed largely of a smaller proteolytic derivativeSemantic proximity Read ↗

A Huntingtin-based peptide inhibitor of caspase-6 provides protection from mutant Huntingtin-induced motor and behavioral deficits.Semantic proximity Read ↗

Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease.Semantic proximity Read ↗

Transgenic Mouse Model Expressing the Caspase 6 Fragment of Mutant HuntingtinSemantic proximity Read ↗

Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease.Semantic proximity Read ↗

Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus.Semantic proximity Read ↗

p53 increases caspase-6 expression and activation in muscle tissue expressing mutant huntingtin.Semantic proximity Read ↗

Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis.Semantic proximity Read ↗

Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions.Semantic proximity Read ↗

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