{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,13]],"date-time":"2026-03-13T16:16:10Z","timestamp":1773418570682,"version":"3.50.1"},"reference-count":43,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2007,2,1]],"date-time":"2007-02-01T00:00:00Z","timestamp":1170288000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2007,2,1]],"date-time":"2007-02-01T00:00:00Z","timestamp":1170288000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2007,2,1]],"date-time":"2007-02-01T00:00:00Z","timestamp":1170288000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2007,2,1]],"date-time":"2007-02-01T00:00:00Z","timestamp":1170288000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2007,2,1]],"date-time":"2007-02-01T00:00:00Z","timestamp":1170288000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2007,2,1]],"date-time":"2007-02-01T00:00:00Z","timestamp":1170288000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2007,2,1]],"date-time":"2007-02-01T00:00:00Z","timestamp":1170288000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2007,2]]},"DOI":"10.1016\/j.jmb.2006.11.036","type":"journal-article","created":{"date-parts":[[2006,11,14]],"date-time":"2006-11-14T10:23:50Z","timestamp":1163499830000},"page":"244-257","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":62,"title":["Structural Analysis of the Plakin Domain of Bullous Pemphigoid Antigen1 (BPAG1) Suggests that Plakins Are Members of the Spectrin Superfamily"],"prefix":"10.1016","volume":"366","author":[{"given":"Julius J.","family":"Jefferson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carlo","family":"Ciatto","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lawrence","family":"Shapiro","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ronald K.H.","family":"Liem","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2006.11.036_bib1","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1038\/nrm1425","article-title":"Plakins: goliaths that link cell junctions and the cytoskeleton","volume":"5","author":"Jefferson","year":"2004","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2006.11.036_bib2","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0962-8924(01)02180-8","article-title":"Plakins: a family of versatile cytolinker proteins","volume":"12","author":"Leung","year":"2002","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.jmb.2006.11.036_bib3","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1083\/jcb.200012098","article-title":"The BPAG1 locus: alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles","volume":"154","author":"Leung","year":"2001","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jmb.2006.11.036_bib4","first-page":"612","article-title":"Structures of two intermediate filament-binding fragments of desmoplakin Rev.eal a unique repeat motif structure","volume":"9","author":"Choi","year":"2002","journal-title":"Nature Struct. Biol."},{"key":"10.1016\/j.jmb.2006.11.036_bib5","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1038\/nrm1356","article-title":"Working out the strength and flexibility of desmosomes","volume":"5","author":"Getsios","year":"2004","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2006.11.036_bib6","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1242\/jcs.00241","article-title":"Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly","volume":"116","author":"Koster","year":"2003","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jmb.2006.11.036_bib7","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1073\/pnas.89.2.544","article-title":"Molecular structure of the human desmoplakin I and II amino terminus","volume":"89","author":"Virata","year":"1992","journal-title":"Proc. Natl Acad Sci. USA"},{"key":"10.1016\/j.jmb.2006.11.036_bib8","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0065-3233(05)70006-1","article-title":"Intermediate filament associated proteins","volume":"70","author":"Green","year":"2005","journal-title":"Advan. Protein Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib9","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/0022-2836(87)90297-X","article-title":"Structure and hydrodynamic properties of plectin molecules","volume":"198","author":"Foisner","year":"1987","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2006.11.036_bib10","doi-asserted-by":"crossref","first-page":"9716","DOI":"10.1074\/jbc.271.16.9716","article-title":"Structural analysis of the predicted coiled-coil rod domain of the cytoplasmic bullous pemphigoid antigen (BPAG1). Empirical localization of the N-terminal globular domain-rod boundary","volume":"271","author":"Tang","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib11","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S0065-3233(05)70007-3","article-title":"Spectrin, alpha-actinin, and dystrophin","volume":"70","author":"Broderick","year":"2005","journal-title":"Advan. Protein Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib12","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/j.str.2004.02.022","article-title":"Structural insights into the stability and flexibility of unusual erythroid spectrin repeats","volume":"12","author":"Kusunoki","year":"2004","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2006.11.036_bib13","first-page":"234","article-title":"Crystal structure of the alpha-actinin rod: four spectrin repeats forming a tight dimer","volume":"6","author":"Ylanne","year":"2001","journal-title":"Cell Mol. Biol. Letters"},{"key":"10.1016\/j.jmb.2006.11.036_bib14","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/S0092-8674(00)81980-7","article-title":"Structures of two repeats of spectrin suggest models of flexibility","volume":"98","author":"Grum","year":"1999","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2006.11.036_bib15","doi-asserted-by":"crossref","first-page":"21052","DOI":"10.1074\/jbc.272.34.21052","article-title":"Site-directed mutagenesis of either the highly conserved Trp-22 or the moderately conserved Trp-95 to a large, hydrophobic residue reduces the thermodynamic stability of a spectrin repeating unit","volume":"272","author":"Pantazatos","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib16","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1073\/pnas.91.4.1299","article-title":"Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin","volume":"91","author":"MacDonald","year":"1994","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2006.11.036_bib17","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1002\/(SICI)1097-0134(199610)26:2<134::AID-PROT3>3.0.CO;2-G","article-title":"Heptad breaks in alpha-helical coiled coils: stutters and stammers","volume":"26","author":"Brown","year":"1996","journal-title":"Proteins: Struct. Funct. Genet."},{"key":"10.1016\/j.jmb.2006.11.036_bib18","doi-asserted-by":"crossref","first-page":"D257","DOI":"10.1093\/nar\/gkj079","article-title":"SMART 5: domains in the context of genomes and networks","volume":"34","author":"Letunic","year":"2006","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jmb.2006.11.036_bib19","doi-asserted-by":"crossref","first-page":"D247","DOI":"10.1093\/nar\/gkj149","article-title":"Pfam: clans, web tools and services","volume":"34","author":"Finn","year":"2006","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jmb.2006.11.036_bib20","doi-asserted-by":"crossref","first-page":"D192","DOI":"10.1093\/nar\/gki069","article-title":"CDD: a conserved domain database for protein classification","volume":"33","author":"Marchler-Bauer","year":"2005","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jmb.2006.11.036_bib21","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1002\/prot.1168","article-title":"Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM","volume":"5","author":"Bates","year":"2001","journal-title":"Proteins: Struct Funct. Genet. Suppl."},{"key":"10.1016\/j.jmb.2006.11.036_bib22","doi-asserted-by":"crossref","first-page":"4215","DOI":"10.1242\/jcs.00157","article-title":"The \u2018spectraplakins\u2019: cytoskeletal giants with characteristics of both spectrin and plakin families","volume":"115","author":"Roper","year":"2002","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jmb.2006.11.036_bib23","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1038\/35043032","article-title":"Are desmosomes more than tethers for intermediate filaments?","volume":"1","author":"Green","year":"2000","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2006.11.036_bib24","doi-asserted-by":"crossref","first-page":"7735","DOI":"10.1074\/jbc.M210988200","article-title":"c-Src binds alpha II spectrin's Src homology 3 (SH3) domain and blocks calpain susceptibility by phosphorylating Tyr1176","volume":"278","author":"Nedrelow","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib25","doi-asserted-by":"crossref","first-page":"10481","DOI":"10.1074\/jbc.274.15.10481","article-title":"Proline-rich motifs of the Na+\/H+ exchanger 2 isoform. Binding of Src homology domain 3 and role in apical targeting in epithelia","volume":"274","author":"Chow","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib26","doi-asserted-by":"crossref","first-page":"4440","DOI":"10.1002\/j.1460-2075.1994.tb06766.x","article-title":"An SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane","volume":"13","author":"Rotin","year":"1994","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2006.11.036_bib27","doi-asserted-by":"crossref","first-page":"3527","DOI":"10.1128\/MCB.22.10.3527-3536.2002","article-title":"Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain","volume":"22","author":"Nicolas","year":"2002","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2006.11.036_bib28","doi-asserted-by":"crossref","first-page":"13681","DOI":"10.1074\/jbc.273.22.13681","article-title":"Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton","volume":"273","author":"Ziemnicka-Kotula","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib29","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1242\/jcs.01625","article-title":"SH3 domain of spectrin participates in the activation of Rac in specialized calpain-induced integrin signaling complexes","volume":"118","author":"Bialkowska","year":"2005","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jmb.2006.11.036_bib30","doi-asserted-by":"crossref","first-page":"32427","DOI":"10.1074\/jbc.M011005200","article-title":"The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression","volume":"276","author":"Favre","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib31","doi-asserted-by":"crossref","first-page":"23018","DOI":"10.1074\/jbc.M502530200","article-title":"Identification of spectrin-like repeats required for high affinity utrophin-actin interaction","volume":"280","author":"Rybakova","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2006.11.036_bib32","first-page":"276","article-title":"Methods in Enzymology. Macromolecular Crystallography","author":"Doublie","year":"1997"},{"key":"10.1016\/j.jmb.2006.11.036_bib33","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1107\/S0021889893005588","article-title":"Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants","volume":"21","author":"Kabsch","year":"1993","journal-title":"J. Appl. Crystallog."},{"key":"10.1016\/j.jmb.2006.11.036_bib34","doi-asserted-by":"crossref","first-page":"2288","DOI":"10.1107\/S0907444904023716","article-title":"Developments in the CCP4 molecular-graphics project","volume":"60","author":"Potterton","year":"2004","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.11.036_bib35","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.11.036_bib36","doi-asserted-by":"crossref","first-page":"1772","DOI":"10.1107\/S0907444902011678","article-title":"Substructure solution with SHELXD","volume":"58","author":"Schneider","year":"2002","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.11.036_bib37","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1107\/S0907444900013263","article-title":"General quadratic functions in real and reciprocal space and their application to likelihood phasing","volume":"56","author":"Cowtan","year":"2000","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.11.036_bib38","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1107\/S0907444906022116","article-title":"The Buccaneer software for automated model building. 1. Tracing protein chains","volume":"62","author":"Cowtan","year":"2006","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.11.036_bib39","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"COOT: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.11.036_bib40","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography and NMR system: a new software suite for macromolecular structure determination","volume":"54","author":"Brunger","year":"1998","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.11.036_bib41","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/S0076-6879(03)74014-2","article-title":"Macromolecular TLS refinement in REFMAC at moderate resolutions","volume":"374","author":"Winn","year":"2003","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jmb.2006.11.036_bib42","doi-asserted-by":"crossref","first-page":"3300","DOI":"10.1093\/nar\/gkg508","article-title":"The PredictProtein server","volume":"31","author":"Rost","year":"2003","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jmb.2006.11.036_bib43","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/S0141-8130(05)80004-2","article-title":"Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: members of a new gene family involved in organization of intermediate filaments","volume":"14","author":"Green","year":"1992","journal-title":"Int. J. Biol. Macromol."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283606015762?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283606015762?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T06:07:30Z","timestamp":1762668450000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283606015762"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,2]]},"references-count":43,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2007,2]]}},"alternative-id":["S0022283606015762"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2006.11.036","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1098444.554519","asserted-by":"object"}]},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2007,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural Analysis of the Plakin Domain of Bullous Pemphigoid Antigen1 (BPAG1) Suggests that Plakins Are Members of the Spectrin Superfamily","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2006.11.036","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2006 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}