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

By R. Graham, Yu Deng, E. Slow, Brendan Haigh, N. Bissada, G. Lu, J. Pearson, Jacqueline Shehadeh, L. Bertram, Z. Murphy and 8 more. Cell, 2006

713 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology, Neurology

View Paper: https://www.semanticscholar.org/paper/763b743fc9ad38a87fb5588b625ccb5d000ba6e2

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

1. E. Carafoli
2. Tito Calì
3. Denis Ottolini
4. M. Brini

In Molecular Biology

1. E. Carafoli
2. Tito Calì
3. Denis Ottolini
4. M. Brini
5. P. Mehlen

Citations in the corpus

• Cell death in the nervous system (2006, background): “In an analogous study with an HD-transgenic mouse model, mutation of the caspase-6 site (but not the caspase-3 sites) in polyglutamine-expanded huntingtin prevented both the neurodegeneration and motor abnormalities characteristic of Huntington's diseas”
• Neuronal calcium signaling: function and dysfunction (2014, background): “pase 6 [153], producing N-terminal fragments that accumu-”
• Full-Length Human Mutant Huntingtin with a Stable Polyglutamine Repeat Can Elicit Progressive and Selective Neuropathogenesis in BACHD Mice (2008, methodology): “Proteolysis of fl-mhtt to generate toxic mhtt N-terminal fragments has been postulated as a critical mechanism for HD pathogenesis (Ross, 2004; Graham et al., 2006).”