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Bernard Brais
Researcher at Montreal Neurological Institute and Hospital
Publications - 190
Citations - 7827
Bernard Brais is an academic researcher from Montreal Neurological Institute and Hospital. The author has contributed to research in topics: Oculopharyngeal muscular dystrophy & Ataxia. The author has an hindex of 42, co-authored 157 publications receiving 6830 citations. Previous affiliations of Bernard Brais include McGill University & Montreal General Hospital.
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Journal ArticleDOI
Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy
Bernard Brais,Jean-Pierre Bouchard,Ya-Gang Xie,Daniel Rochefort,Nathalie Chretien,Fernando M.S. Tomé,Ronald G. Lafrenière,Johanna M. Rommens,E. Uyama,O. Nohira,Sergiu C. Blumen,Amos D. Korczyn,Peter Heutink,Jean Mathieu,André Duranceau,François Codère,Michel Fardeau,Guy A. Rouleau +17 more
TL;DR: Pathological expansions of the polyalanine tract may cause mutated PABP2 oligomers to accumulate as filament inclusions in nuclei to cause autosomal recessive OPMD.
Journal ArticleDOI
A dominant-negative mutation in the TRESK potassium channel is linked to familial migraine with aura.
Ronald G. Lafrenière,M. Zameel Cader,M. Zameel Cader,Jean-François Poulin,Isabelle Andres-Enguix,Maryse Simoneau,Namrata Gupta,Karine Boisvert,François Lafrenière,Shannon McLaughlan,Marie-Pierre Dubé,Martin M Marcinkiewicz,Sreeram V. Ramagopalan,Olaf Ansorge,Bernard Brais,Jorge Sequeiros,José Pereira-Monteiro,Lyn R. Griffiths,Stephen J. Tucker,George C. Ebers,Guy A. Rouleau +20 more
TL;DR: A frameshift mutation, F139WfsX24, is reported, which segregates perfectly with typical migraine with aura in a large pedigree and demonstrates that it causes a complete loss of TRESK function and that the mutant subunit suppresses wild-type channel function through a dominant-negative effect, thus explaining the dominant penetrance of this allele.
Journal ArticleDOI
Utility of whole-exome sequencing for those near the end of the diagnostic odyssey: time to address gaps in care.
Sara L. Sawyer,Taila Hartley,David A. Dyment,Chandree L. Beaulieu,Jeremy Schwartzentruber,Amanda C. Smith,H M Bedford,Geneviève Bernard,Francois P. Bernier,Bernard Brais,Dennis E. Bulman,J. Warman Chardon,David Chitayat,Johnny Deladoëy,Bridget A. Fernandez,Patrick Frosk,Michael T. Geraghty,Brenda Gerull,William T. Gibson,Robert M. Gow,Gail E. Graham,Jane Green,Elise Héon,Gabriella Horvath,A.M. Innes,Nada Jabado,Raymond H. Kim,Robert K. Koenekoop,Aneal Khan,Ordan J. Lehmann,Roberto Mendoza-Londono,Jacques L. Michaud,Sarah M. Nikkel,L S Penney,Constantin Polychronakos,Julie Richer,Guy A. Rouleau,Mark E. Samuels,Victoria Mok Siu,Oksana Suchowersky,Mark A. Tarnopolsky,Grace Yoon,Farah R. Zahir,Jacek Majewski,Kym M. Boycott +44 more
TL;DR: The analysis of this dataset showed that these known disease genes were not identified prior to WES enrollment for two key reasons: genetic heterogeneity associated with a clinical diagnosis and atypical presentation of known, clinically recognized diseases.
A dominant-negative mutation in the TRESK potassium channel is linked to familial migraine with aura
Ronald G. Lafrenière,M. Zameel Cader,M. Zameel Cader,Jean-François Poulin,Isabelle Andres-Enguix,Maryse Simoneau,Namrata Gupta,Karine Boisvert,François Lafrenière,Shannon McLaughlan,Marie-Pierre Dubé,Martin M Marcinkiewicz,Sreeram V. Ramagopalan,Olaf Ansorge,Bernard Brais,Jorge Sequeiros,José Pereira-Monteiro,Lyn R. Griffiths,Stephen J. Tucker,George C. Ebers,Guy A. Rouleau +20 more
TL;DR: In this article, a frameshift mutation, F139WfsX24, was found to cause complete loss of TRESK function and that the mutant subunit suppresses wild-type channel function through a dominant negative effect, thus explaining the dominant penetrance of this allele.
Journal ArticleDOI
Recessive Mutations in the Putative Calcium-Activated Chloride Channel Anoctamin 5 Cause Proximal LGMD2L and Distal MMD3 Muscular Dystrophies
V. Bolduc,Gareth Marlow,Kym M. Boycott,Khalil Saleki,Hiroshi Inoue,Johan T.M. Kroon,Mitsuo Itakura,Yves Robitaille,Lucie Parent,Frank Baas,Kuniko Mizuta,Nobuyuki Kamata,Isabelle Richard,W. H. J. P. Linssen,Ibrahim Mahjneh,Marianne de Visser,Rumaisa Bashir,Bernard Brais +17 more
TL;DR: Though the function of the ANO5 protein is still unknown, its putative calcium-activated chloride channel function may lead to important insights into the role of deficient skeletal muscle membrane repair in muscular dystrophies.