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Brain Sciences|June 26, 2014
Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionGuylaine Hoffner, Philippe DjianMolecular Neurobiology|October 23, 2014
Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?Guylaine Hoffner, Philippe DjianFrontiers in Bioscience : a Journal and Virtual Library|June 23, 2005
Transglutaminase and diseases of the central nervous systemGuylaine Hoffner, Philippe DjianPrion|January 28, 2009
Aggregation of expanded huntingtin in the brains of patients with Huntington diseaseGuylaine Hoffner, Sylvie Souès, Philippe DjianJournal of Cell Science|March 1, 2002
Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's diseaseGuylaine Hoffner, Pascal Kahlem, Philippe DjianJournal of Neurochemistry|September 27, 2005
Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymersGuylaine Hoffner, Marie-Laure Island, Philippe DjianAnalytical Chemistry|March 6, 2013
Structure of inclusions of Huntington's disease brain revealed by synchrotron infrared microspectroscopy: polymorphism and relevance to cytotoxicityWilliam André, Christophe Sandt, Paul Dumas, et al.Analytical Chemistry|April 12, 2017
Inclusions of R6/2 Mice Are Not Amyloid and Differ Structurally from Those of Huntington Disease BrainWilliam André, Christophe Sandt, Isabelle Nondier, et al.The Journal of Biological Chemistry|November 7, 2008
Misfolding of proteins with a polyglutamine expansion is facilitated by proteasomal chaperonesErwann Rousseau, Rieko Kojima, Guylaine Hoffner, et al.Pageof 3