{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Delalande O"],"funding":["Centre National de la Recherche Scientifique","Association Française contre les Myopathies","Conseil Régional de Bretagne","Université Européenne de Bretagne"],"pagination":["6637-6646"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5936807"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["293(18)"],"pubmed_abstract":["Dystrophin, encoded by the <i>DMD</i> gene, is critical for maintaining plasma membrane integrity during muscle contraction events. Mutations in the <i>DMD</i> gene disrupting the reading frame prevent dystrophin production and result in severe Duchenne muscular dystrophy (DMD); in-frame internal deletions allow production of partly functional internally deleted dystrophin and result in less severe Becker muscular dystrophy (BMD). Many known BMD deletions occur in dystrophin's central domain, generally considered to be a monotonous rod-shaped domain based on the knowledge of spectrin family proteins. However, the effects caused by these deletions, ranging from asymptomatic to severe BMD, argue against the central domain serving only as a featureless scaffold. We undertook structural studie"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions."],"pmcid":["PMC5936807"],"funding_grant_id":["AN Fellowship"],"pubmed_authors":["Guilbaud M","Pietri-Rouxel F","Dos Santos Morais R","Bondon A","Le Rumeur E","Hubert JF","Pollet E","Molza AE","Roblin P","Raguenes-Nicol C","Giudice E","Czjzek M","Ferey N","Cheron A","Baaden M","Leturcq F","Tascon C","Delalande O","Perez J","Nicolas A"],"additional_accession":[]},"is_claimable":false,"name":"Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.","description":"Dystrophin, encoded by the <i>DMD</i> gene, is critical for maintaining plasma membrane integrity during muscle contraction events. Mutations in the <i>DMD</i> gene disrupting the reading frame prevent dystrophin production and result in severe Duchenne muscular dystrophy (DMD); in-frame internal deletions allow production of partly functional internally deleted dystrophin and result in less severe Becker muscular dystrophy (BMD). Many known BMD deletions occur in dystrophin's central domain, generally considered to be a monotonous rod-shaped domain based on the knowledge of spectrin family proteins. However, the effects caused by these deletions, ranging from asymptomatic to severe BMD, argue against the central domain serving only as a featureless scaffold. We undertook structural studie","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 May","modification":"2026-05-05T23:34:01.169Z","creation":"2019-06-06T23:03:26Z"},"accession":"S-EPMC5936807","cross_references":{"pubmed":["29535188"],"doi":["10.1074/jbc.M117.809798","10.1074/jbc.m117.809798"]}}