{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T17:13:41Z","timestamp":1762190021160,"version":"build-2065373602"},"reference-count":90,"publisher":"Elsevier BV","issue":"12","license":[{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,11,13]],"date-time":"2024-11-13T00:00:00Z","timestamp":1731456000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100017908","name":"ALSAM Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100017908","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2024,12]]},"DOI":"10.1016\/j.jbc.2024.108002","type":"journal-article","created":{"date-parts":[[2024,11,17]],"date-time":"2024-11-17T15:00:40Z","timestamp":1731855640000},"page":"108002","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Biophysical characterization of the dystrophin C-terminal domain: Dystrophin interacts differentially with dystrobrevin isoforms"],"prefix":"10.1016","volume":"300","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0916-6408","authenticated-orcid":false,"given":"Vaibhav","family":"Upadhyay","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8838-398X","authenticated-orcid":false,"given":"Shashikant","family":"Ray","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8413-2913","authenticated-orcid":false,"given":"Sudipta","family":"Panja","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6890-512X","authenticated-orcid":false,"given":"Anthony J.","family":"Saviola","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nasib Karl","family":"Maluf","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8308-5318","authenticated-orcid":false,"given":"Krishna M.G.","family":"Mallela","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2024.108002_bib1","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/0092-8674(87)90579-4","article-title":"Dystrophin: the protein product of the Duchenne muscular dystrophy locus","volume":"51","author":"Hoffman","year":"1987","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.108002_bib2","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1002\/humu.21114","article-title":"Mutational spectrum of DMD mutations in dystrophinopathy patients: application of modern diagnostic techniques to a large cohort","volume":"30","author":"Flanigan","year":"2009","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.jbc.2024.108002_bib3","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/S1474-4422(03)00585-4","article-title":"Dystrophin and mutations: one gene, several proteins, multiple phenotypes","volume":"2","author":"Muntoni","year":"2003","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.jbc.2024.108002_bib4","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.2147\/NDT.S93873","article-title":"Current and emerging treatment strategies for Duchenne muscular dystrophy","volume":"12","author":"Mah","year":"2016","journal-title":"Neuropsychiatr. Dis. Treat."},{"key":"10.1016\/j.jbc.2024.108002_bib5","doi-asserted-by":"crossref","first-page":"9161","DOI":"10.1016\/S0021-9258(18)31565-5","article-title":"Purification of dystrophin from skeletal muscle","volume":"266","author":"Ervasti","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.108002_bib6","doi-asserted-by":"crossref","first-page":"7851","DOI":"10.1073\/pnas.87.20.7851","article-title":"Isolated dystrophin molecules as seen by electron microscopy","volume":"87","author":"Pons","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"10.1016\/j.jbc.2024.108002_bib7","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1111\/j.1432-1033.1994.tb18958.x","article-title":"Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside","volume":"222","author":"Yoshida","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2024.108002_bib8","first-page":"639","article-title":"Role of dystrophin isoforms and associated proteins in muscular dystrophy (review)","volume":"2","author":"Culligan","year":"1998","journal-title":"Int. J. Mol. Med."},{"key":"10.1016\/j.jbc.2024.108002_bib9","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1038\/338509a0","article-title":"Alternative splicing of human dystrophin mRNA generates isoforms at the carboxy terminus","volume":"338","author":"Feener","year":"1989","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.108002_bib10","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1016\/j.bbapap.2010.05.001","article-title":"Dystrophin: more than just the sum of its parts","volume":"1804","author":"Le Rumeur","year":"2010","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.jbc.2024.108002_bib11","doi-asserted-by":"crossref","first-page":"3647","DOI":"10.1093\/hmg\/ddw210","article-title":"Dystrophin contains multiple independent membrane-binding domains","volume":"25","author":"Zhao","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2024.108002_bib12","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.bbadis.2006.05.010","article-title":"Dystrophin, its interactions with other proteins, and implications for muscular dystrophy","volume":"1772","author":"Ervasti","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2024.108002_bib13","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1002\/j.2040-4603.2015.tb00638.x","article-title":"The dystrophin complex: structure, function, and","volume":"5","author":"Gao","year":"2015","journal-title":"Implications. Ther. Compr. Physiol."},{"key":"10.1016\/j.jbc.2024.108002_bib14","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1152\/physrev.00028.2001","article-title":"Function and genetics of dystrophin and dystrophin-related proteins in muscle","volume":"82","author":"Blake","year":"2002","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.jbc.2024.108002_bib15","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.bbamem.2013.08.023","article-title":"Dystrophin complex functions as a scaffold for signalling proteins","volume":"1838","author":"Constantin","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2024.108002_bib16","doi-asserted-by":"crossref","first-page":"5561","DOI":"10.1021\/bi00016a030","article-title":"Characterization of the recombinant C-terminal domain of dystrophin: phosphorylation by calmodulin-dependent protein kinase II and dephosphorylation by type 2B protein phosphatase","volume":"34","author":"Walsh","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.108002_bib17","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1038\/s41434-022-00317-6","article-title":"Evaluation of the dystrophin carboxy-terminal domain for micro-dystrophin gene therapy in cardiac and skeletal muscles in the DMD(mdx) rat model","volume":"29","author":"Bourdon","year":"2022","journal-title":"Gene. Ther."},{"issue":"Pt 3","key":"10.1016\/j.jbc.2024.108002_bib18","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1042\/bj2881037","article-title":"Isolation and characterization of different C-terminal fragments of dystrophin expressed in Escherichia coli","volume":"288","author":"Milner","year":"1992","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2024.108002_bib19","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/0022-510X(91)90039-A","article-title":"Preservation of the C-terminus of dystrophin molecule in the skeletal muscle from Becker muscular dystrophy","volume":"101","author":"Arahata","year":"1991","journal-title":"J.\u00a0Neurol. Sci."},{"key":"10.1016\/j.jbc.2024.108002_bib20","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1006\/abbi.1999.1172","article-title":"Alpha-actinin-2 is a new component of the dystrophin-glycoprotein complex","volume":"365","author":"Hance","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2024.108002_bib21","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1083\/jcb.150.6.1399","article-title":"Assembly of the dystrophin-associated protein complex does not require the dystrophin COOH-terminal domain","volume":"150","author":"Crawford","year":"2000","journal-title":"J.\u00a0Cell. Biol."},{"key":"10.1016\/j.jbc.2024.108002_bib22","doi-asserted-by":"crossref","first-page":"S303","DOI":"10.3233\/JND-210678","article-title":"Gene therapy for duchenne muscular dystrophy","volume":"8","author":"Elangkovan","year":"2021","journal-title":"J.\u00a0Neuromuscul. Dis."},{"key":"10.1016\/j.jbc.2024.108002_bib23","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.ymthe.2019.01.002","article-title":"Development of novel micro-dystrophins with enhanced functionality","volume":"27","author":"Ramos","year":"2019","journal-title":"Mol. Ther."},{"key":"10.1016\/j.jbc.2024.108002_bib24","doi-asserted-by":"crossref","first-page":"2355","DOI":"10.1093\/hmg\/11.20.2355","article-title":"Gene therapy of muscular dystrophy","volume":"11","author":"Chamberlain","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2024.108002_bib25","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.ymthe.2006.01.007","article-title":"C-terminal-truncated microdystrophin recruits dystrobrevin and syntrophin to the dystrophin-associated glycoprotein complex and reduces muscular dystrophy in symptomatic utrophin\/dystrophin double-knockout mice","volume":"14","author":"Yue","year":"2006","journal-title":"Mol. Ther."},{"key":"10.1016\/j.jbc.2024.108002_bib26","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1016\/S0960-9822(00)00760-0","article-title":"Alternative splicing of dystrobrevin regulates the stoichiometry of syntrophin binding to the dystrophin protein complex","volume":"10","author":"Newey","year":"2000","journal-title":"Curr. Biol."},{"key":"10.1016\/j.jbc.2024.108002_bib27","doi-asserted-by":"crossref","first-page":"12413","DOI":"10.1073\/pnas.94.23.12413","article-title":"Dystrobrevin and dystrophin: an interaction through coiled-coil motifs","volume":"94","author":"Sadoulet-Puccio","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"10.1016\/j.jbc.2024.108002_bib28","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1083\/jcb.128.3.363","article-title":"Syntrophin binds to an alternatively spliced exon of dystrophin","volume":"128","author":"Ahn","year":"1995","journal-title":"J.\u00a0Cell. Biol"},{"key":"10.1016\/j.jbc.2024.108002_bib29","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1083\/jcb.128.3.373","article-title":"Mammalian alpha 1- and beta 1-syntrophin bind to the alternative splice-prone region of the dystrophin COOH terminus","volume":"128","author":"Suzuki","year":"1995","journal-title":"J.\u00a0Cell. Biol."},{"key":"10.1016\/j.jbc.2024.108002_bib30","doi-asserted-by":"crossref","first-page":"2724","DOI":"10.1074\/jbc.271.5.2724","article-title":"The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives","volume":"271","author":"Ahn","year":"1996","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.108002_bib31","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1093\/hmg\/1.7.505","article-title":"Expression of four alternative dystrophin transcripts in brain regions regulated by different promoters","volume":"1","author":"Gorecki","year":"1992","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2024.108002_bib32","doi-asserted-by":"crossref","first-page":"1877","DOI":"10.1093\/hmg\/2.11.1877","article-title":"Point mutations at the carboxy terminus of the human dystrophin gene: implications for an association with mental retardation in DMD patients","volume":"2","author":"Lenk","year":"1993","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2024.108002_bib33","unstructured":"The human gene mutation database 2024"},{"key":"10.1016\/j.jbc.2024.108002_bib34","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1179\/016164104773026589","article-title":"Dystrophin deletions and cognitive impairment in Duchenne\/Becker muscular dystrophy","volume":"26","author":"Giliberto","year":"2004","journal-title":"Neurol. Res."},{"key":"10.1016\/j.jbc.2024.108002_bib35","first-page":"25","article-title":"Intellectual ability in the duchenne muscular dystrophy and dystrophin gene mutation location Balkan","volume":"17","author":"Milic Rasic","year":"2014","journal-title":"J.\u00a0Med. Genet."},{"key":"10.1016\/j.jbc.2024.108002_bib36","doi-asserted-by":"crossref","first-page":"3779","DOI":"10.1093\/hmg\/ddp320","article-title":"Analysis of Dp71 contribution in the severity of mental retardation through comparison of Duchenne and Becker patients differing by mutation consequences on Dp71 expression","volume":"18","author":"Daoud","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2024.108002_bib37","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1038\/s41572-021-00248-3","article-title":"Duchenne muscular dystrophy","volume":"7","author":"Duan","year":"2021","journal-title":"Nat. Rev. Dis. Primers."},{"key":"10.1016\/j.jbc.2024.108002_bib38","doi-asserted-by":"crossref","first-page":"1813","DOI":"10.1007\/s00424-021-02623-1","article-title":"Complexity of skeletal muscle degeneration: multi-systems pathophysiology and organ crosstalk in dystrophinopathy","volume":"473","author":"Ohlendieck","year":"2021","journal-title":"Pflugers. Arch."},{"key":"10.1016\/j.jbc.2024.108002_bib39","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1093\/bioinformatics\/bti797","article-title":"Paircoil2: improved prediction of coiled coils from sequence","volume":"22","author":"McDonnell","year":"2006","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jbc.2024.108002_bib40","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.108002_bib41","doi-asserted-by":"crossref","first-page":"W315","DOI":"10.1093\/nar\/gky497","article-title":"BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra","volume":"46","author":"Micsonai","year":"2018","journal-title":"Nucleic. Acids. Res."},{"key":"10.1016\/j.jbc.2024.108002_bib42","doi-asserted-by":"crossref","first-page":"2138","DOI":"10.1002\/pro.5560041020","article-title":"Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding","volume":"4","author":"Myers","year":"1995","journal-title":"Protein. Sci."},{"key":"10.1016\/j.jbc.2024.108002_bib43","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1093\/protein\/14.8.583","article-title":"An approach for protein to be completely reversible to thermal denaturation even at autoclave temperatures","volume":"14","author":"Iwakura","year":"2001","journal-title":"Protein. Eng."},{"key":"10.1016\/j.jbc.2024.108002_bib44","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1002\/bip.360321209","article-title":"Alpha-helix to random coil transitions: determination of peptide concentration from the CD at the isodichroic point","volume":"32","author":"Holtzer","year":"1992","journal-title":"Biopolymers"},{"key":"10.1016\/j.jbc.2024.108002_bib45","doi-asserted-by":"crossref","first-page":"29470","DOI":"10.1074\/jbc.M111.221267","article-title":"Truncation, randomization, and selection: generation of a reduced length c-Jun antagonist that retains high interaction stability","volume":"286","author":"Crooks","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.108002_bib46","article-title":"Protein complex prediction with AlphaFold-Multimer","author":"Evans","year":"2022","journal-title":"bioRxiv"},{"key":"10.1016\/j.jbc.2024.108002_bib47","first-page":"67","article-title":"The 10th Oligonucleotide therapy approved: Golodirsen for duchenne muscular dystrophy Nucleic acid","volume":"30","author":"Aartsma-Rus","year":"2020","journal-title":"Ther"},{"key":"10.1016\/j.jbc.2024.108002_bib48","first-page":"1","article-title":"FDA Approves eteplirsen for duchenne muscular dystrophy: the Next Chapter in the eteplirsen saga Nucleic acid","volume":"27","author":"Aartsma-Rus","year":"2017","journal-title":"Ther"},{"key":"10.1016\/j.jbc.2024.108002_bib49","doi-asserted-by":"crossref","first-page":"S343","DOI":"10.3233\/JND-210682","article-title":"Exon-skipping in duchenne muscular dystrophy","volume":"8","author":"Takeda","year":"2021","journal-title":"J.\u00a0Neuromuscul. Dis."},{"key":"10.1016\/j.jbc.2024.108002_bib50","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1038\/s41582-018-0033-8","article-title":"Why dystrophin quantification is key in the eteplirsen saga","volume":"14","author":"Aartsma-Rus","year":"2018","journal-title":"Nat. Rev. Neurol."},{"key":"10.1016\/j.jbc.2024.108002_bib51","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1038\/345315a0","article-title":"Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle","volume":"345","author":"Ervasti","year":"1990","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.108002_bib52","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1093\/oxfordjournals.jbchem.a123276","article-title":"Glycoprotein complex anchoring dystrophin to sarcolemma","volume":"108","author":"Yoshida","year":"1990","journal-title":"J.\u00a0Biochem."},{"key":"10.1016\/j.jbc.2024.108002_bib53","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1002\/(SICI)1097-0169(1997)36:3<246::AID-CM5>3.0.CO;2-5","article-title":"Physical properties of dystrophin rod domain Cell","volume":"36","author":"Kahana","year":"1997","journal-title":"Motil. Cytoskeleton."},{"key":"10.1016\/j.jbc.2024.108002_bib54","doi-asserted-by":"crossref","first-page":"15069","DOI":"10.1073\/pnas.1008818107","article-title":"Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates","volume":"107","author":"Singh","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"10.1016\/j.jbc.2024.108002_bib55","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/0014-5793(95)00398-S","article-title":"Dystrophin and utrophin: the missing links","volume":"369","author":"Winder","year":"1995","journal-title":"FEBS. Lett."},{"key":"10.1016\/j.jbc.2024.108002_bib56","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/0014-5793(92)80249-G","article-title":"Expression of the N-terminal domain of dystrophin in E.\u00a0coli and demonstration of binding to F-actin","volume":"301","author":"Way","year":"1992","journal-title":"FEBS. Lett."},{"key":"10.1016\/j.jbc.2024.108002_bib57","doi-asserted-by":"crossref","first-page":"1970","DOI":"10.1016\/j.bpj.2012.08.066","article-title":"The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin","volume":"103","author":"Singh","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2024.108002_bib58","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1002\/prot.24033","article-title":"Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin","volume":"80","author":"Singh","year":"2012","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2024.108002_bib59","doi-asserted-by":"crossref","first-page":"2159","DOI":"10.1021\/acsomega.9b02911","article-title":"Tissue-Specificity of dystrophin-actin interactions: isoform-specific thermodynamic stability and actin-binding function of tandem calponin-homology domains","volume":"5","author":"Upadhyay","year":"2020","journal-title":"ACS. Omega."},{"key":"10.1016\/j.jbc.2024.108002_bib60","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1093\/hmg\/3.6.919","article-title":"Half the dystrophin gene is apparently enough for a mild clinical course: confirmation of its potential use for gene therapy","volume":"3","author":"Passos-Bueno","year":"1994","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2024.108002_bib61","first-page":"498","article-title":"The molecular basis for Duchenne versus Becker muscular dystrophy: correlation of severity with type of deletion","volume":"45","author":"Koenig","year":"1989","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.jbc.2024.108002_bib62","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/343180a0","article-title":"Very mild muscular dystrophy associated with the deletion of 46% of dystrophin","volume":"343","author":"England","year":"1990","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.108002_bib63","doi-asserted-by":"crossref","first-page":"27305","DOI":"10.1074\/jbc.270.45.27305","article-title":"Identification and characterization of the dystrophin anchoring site on beta-dystroglycan","volume":"270","author":"Jung","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.108002_bib64","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1172\/JCI115909","article-title":"An intact cysteine-rich domain is required for dystrophin function","volume":"90","author":"Bies","year":"1992","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2024.108002_bib65","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/0014-5793(92)81265-N","article-title":"Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxy-terminal domain","volume":"308","author":"Suzuki","year":"1992","journal-title":"FEBS. Lett."},{"key":"10.1016\/j.jbc.2024.108002_bib66","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1002\/bip.360261104","article-title":"Protein stability curves","volume":"26","author":"Becktel","year":"1987","journal-title":"Biopolymers"},{"key":"10.1016\/j.jbc.2024.108002_bib67","doi-asserted-by":"crossref","first-page":"11345","DOI":"10.1073\/pnas.1635051100","article-title":"Role of residual structure in the unfolded state of a thermophilic protein","volume":"100","author":"Robic","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"10.1016\/j.jbc.2024.108002_bib68","doi-asserted-by":"crossref","first-page":"4489","DOI":"10.1016\/j.bpj.2023.10.026","article-title":"Biophysical evolution of the receptor-binding domains of SARS-CoVs","volume":"122","author":"Upadhyay","year":"2023","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2024.108002_bib69","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0014-5793(97)00454-7","article-title":"In\u00a0vitro expressed dystrophin fragments do not associate with each other","volume":"410","author":"Chan","year":"1997","journal-title":"FEBS. Lett."},{"key":"10.1016\/j.jbc.2024.108002_bib70","doi-asserted-by":"crossref","first-page":"28771","DOI":"10.1074\/jbc.272.45.28771","article-title":"Dystrophin-glycoprotein complex is monomeric and stabilizes actin filaments in\u00a0vitro through a lateral association","volume":"272","author":"Rybakova","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.108002_bib71","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1093\/oxfordjournals.jbchem.a123951","article-title":"Molecular shape of dystrophin","volume":"112","author":"Sato","year":"1992","journal-title":"J.\u00a0Biochem."},{"key":"10.1016\/j.jbc.2024.108002_bib72","doi-asserted-by":"crossref","DOI":"10.1111\/cpr.12562","article-title":"Syntrophins entangled in cytoskeletal meshwork: Helping to hold it all together","volume":"52","author":"Bhat","year":"2019","journal-title":"Cell. Prolif."},{"key":"10.1016\/j.jbc.2024.108002_bib73","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/S0014-5793(98)00097-0","article-title":"Identification and characterization of a novel member of the dystrobrevin gene family","volume":"425","author":"Puca","year":"1998","journal-title":"FEBS. Lett."},{"key":"10.1016\/j.jbc.2024.108002_bib74","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.3390\/ijms12031660","article-title":"The role of alpha-dystrobrevin in striated muscle","volume":"12","author":"Nakamori","year":"2011","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2024.108002_bib75","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1038\/12034","article-title":"Role for alpha-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies","volume":"1","author":"Grady","year":"1999","journal-title":"Nat. Cell. Biol."},{"key":"10.1016\/j.jbc.2024.108002_bib76","doi-asserted-by":"crossref","first-page":"1770","DOI":"10.1136\/heartjnl-2017-311269","article-title":"A\u00a0current approach to heart failure in Duchenne muscular dystrophy","volume":"103","author":"D'Amario","year":"2017","journal-title":"Heart"},{"key":"10.1016\/j.jbc.2024.108002_bib77","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1093\/brain\/awf012","article-title":"Brain function in Duchenne muscular dystrophy","volume":"125","author":"Anderson","year":"2002","journal-title":"Brain"},{"key":"10.1016\/j.jbc.2024.108002_bib78","doi-asserted-by":"crossref","first-page":"7442","DOI":"10.1128\/MCB.21.21.7442-7448.2001","article-title":"Role of beta-dystrobrevin in nonmuscle dystrophin-associated protein complex-like complexes in kidney and liver","volume":"21","author":"Loh","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.jbc.2024.108002_bib79","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1073\/pnas.95.1.241","article-title":"Beta-dystrobrevin, a member of the dystrophin-related protein family","volume":"95","author":"Blake","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U S A."},{"key":"10.1016\/j.jbc.2024.108002_bib80","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.nmd.2006.11.003","article-title":"Dystrobrevins in muscle and non-muscle tissues","volume":"17","author":"Rees","year":"2007","journal-title":"Neuromuscul. Disord."},{"key":"10.1016\/j.jbc.2024.108002_bib81","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1002\/bies.950120702","article-title":"The functional importance of multiple actin isoforms","volume":"12","author":"Rubenstein","year":"1990","journal-title":"Bioessays"},{"key":"10.1016\/j.jbc.2024.108002_bib82","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/0960-8966(94)90072-8","article-title":"Cognitive impairment in Duchenne muscular dystrophy","volume":"4","author":"Bresolin","year":"1994","journal-title":"Neuromuscul. Disord."},{"key":"10.1016\/j.jbc.2024.108002_bib83","doi-asserted-by":"crossref","first-page":"e8803","DOI":"10.1371\/journal.pone.0008803","article-title":"Dystrophin gene mutation location and the risk of cognitive impairment in Duchenne muscular dystrophy","volume":"5","author":"Taylor","year":"2010","journal-title":"PLoS. One."},{"key":"10.1016\/j.jbc.2024.108002_bib84","doi-asserted-by":"crossref","first-page":"e6574","DOI":"10.1371\/journal.pone.0006574","article-title":"Role of mental retardation-associated dystrophin-gene product Dp71 in excitatory synapse organization, synaptic plasticity and behavioral functions","volume":"4","author":"Daoud","year":"2008","journal-title":"PLoS. One."},{"key":"10.1016\/j.jbc.2024.108002_bib85","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1002\/cbic.200300781","article-title":"Coiled coil domains: stability,\u00a0specificity, and biological implications","volume":"5","author":"Mason","year":"2004","journal-title":"ChemBioChem"},{"key":"10.1016\/j.jbc.2024.108002_bib86","doi-asserted-by":"crossref","first-page":"8063","DOI":"10.1021\/bi00421a014","article-title":"Unfolding free-energy changes determined by the linear extrapolation method .1. unfolding phenylmethanesulfonyl alpha-chymotrypsin using different denaturants","volume":"27","author":"Santoro","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.108002_bib87","doi-asserted-by":"crossref","first-page":"4901","DOI":"10.1021\/bi00135a022","article-title":"A\u00a0test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range","volume":"31","author":"Santoro","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.108002_bib88","doi-asserted-by":"crossref","first-page":"2527","DOI":"10.1038\/nprot.2006.204","article-title":"Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions","volume":"1","author":"Greenfield","year":"2006","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.jbc.2024.108002_bib89","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0183975","article-title":"Biophysical analysis of the effect of chemical modification by 4-oxononenal on the structure, stability, and function of binding immunoglobulin protein (BiP)","volume":"12","author":"Shah","year":"2017","journal-title":"PLoS. One."},{"key":"10.1016\/j.jbc.2024.108002_bib90","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1038\/nmeth.4256","article-title":"MSFragger: ultrafast and comprehensive peptide identification in mass spectrometry-based proteomics","volume":"14","author":"Kong","year":"2017","journal-title":"Nat. Methods."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824025043?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824025043?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T16:53:13Z","timestamp":1762188793000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925824025043"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,12]]},"references-count":90,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2024,12]]}},"alternative-id":["S0021925824025043"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2024.108002","relation":{},"ISSN":["0021-9258"],"issn-type":[{"type":"print","value":"0021-9258"}],"subject":[],"published":{"date-parts":[[2024,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Biophysical characterization of the dystrophin C-terminal domain: Dystrophin interacts differentially with dystrobrevin isoforms","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2024.108002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"108002"}}