{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,26]],"date-time":"2026-06-26T04:29:45Z","timestamp":1782448185933,"version":"3.54.5"},"reference-count":61,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,4,1]],"date-time":"2018-04-01T00:00:00Z","timestamp":1522540800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,1,22]],"date-time":"2018-01-22T00:00:00Z","timestamp":1516579200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01-DK36425"],"award-info":[{"award-number":["R01-DK36425"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Matrix Biology"],"published-print":{"date-parts":[[2018,4]]},"DOI":"10.1016\/j.matbio.2018.01.012","type":"journal-article","created":{"date-parts":[[2018,3,3]],"date-time":"2018-03-03T00:16:28Z","timestamp":1520036188000},"page":"32-46","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":17,"special_numbering":"C","title":["Chimeric protein identification of dystrophic, Pierson and other laminin polymerization residues"],"prefix":"10.1016","volume":"67","author":[{"given":"Karen K.","family":"McKee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maya","family":"Aleksandrova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter D.","family":"Yurchenco","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"2","key":"10.1016\/j.matbio.2018.01.012_bb0005","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1016\/j.jsb.2010.02.004","article-title":"Laminin chain assembly is regulated by specific coiled-coil interactions","volume":"170","author":"Macdonald","year":"2010","journal-title":"J. Struct. Biol."},{"issue":"7","key":"10.1016\/j.matbio.2018.01.012_bb0010","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1083\/jcb.200203073","article-title":"Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation","volume":"157","author":"Li","year":"2002","journal-title":"J. Cell Biol."},{"issue":"5","key":"10.1016\/j.matbio.2018.01.012_bb0015","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1083\/jcb.150.5.1215","article-title":"Regulation of programmed cell death by basement membranes in embryonic development","volume":"150","author":"Murray","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.matbio.2018.01.012_bb0020","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.matbio.2016.12.009","article-title":"The nature and biology of basement membranes","volume":"57\u201358","author":"Pozzi","year":"2017","journal-title":"Matrix Biol."},{"issue":"1","key":"10.1016\/j.matbio.2018.01.012_bb0025","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1083\/jcb.200501098","article-title":"Laminin-sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts","volume":"169","author":"Li","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.matbio.2018.01.012_bb0030","doi-asserted-by":"crossref","first-page":"11573","DOI":"10.1074\/jbc.M607886200","article-title":"Loss of nidogen-1 and -2 results in syndactyly and changes in limb development","volume":"281","author":"Bose","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"7","key":"10.1016\/j.matbio.2018.01.012_bb0035","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1242\/dev.01037","article-title":"Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development","volume":"131","author":"Poschl","year":"2004","journal-title":"Development"},{"issue":"5","key":"10.1016\/j.matbio.2018.01.012_bb0040","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1083\/jcb.147.5.1109","article-title":"Perlecan maintains the integrity of cartilage and some basement membranes","volume":"147","author":"Costell","year":"1999","journal-title":"J. Cell Biol."},{"issue":"4","key":"10.1016\/j.matbio.2018.01.012_bb0045","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/S0092-8674(00)81253-2","article-title":"Defective neuromuscular synaptogenesis in agrin-deficient mutant mice","volume":"85","author":"Gautam","year":"1996","journal-title":"Cell"},{"issue":"3","key":"10.1016\/j.matbio.2018.01.012_bb0050","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1111\/jnc.13241","article-title":"Laminin promotes metalloproteinase-mediated dystroglycan processing to regulate oligodendrocyte progenitor cell proliferation","volume":"135","author":"Leiton","year":"2015","journal-title":"J. Neurochem."},{"issue":"1","key":"10.1016\/j.matbio.2018.01.012_bb0055","doi-asserted-by":"crossref","first-page":"256","DOI":"10.2353\/ajpath.2009.080522","article-title":"Laminin-111 restores regenerative capacity in a mouse model for alpha7 integrin congenital myopathy","volume":"174","author":"Rooney","year":"2009","journal-title":"Am. J. Pathol."},{"issue":"19","key":"10.1016\/j.matbio.2018.01.012_bb0060","doi-asserted-by":"crossref","first-page":"4609","DOI":"10.1242\/jcs.107995","article-title":"Schwann cell myelination requires integration of laminin activities","volume":"125","author":"McKee","year":"2012","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.matbio.2018.01.012_bb0065","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.ctm.2015.05.001","article-title":"Integrating activities of laminins that drive basement membrane assembly and function","volume":"76","author":"Yurchenco","year":"2015","journal-title":"Curr. Top. Membr."},{"key":"10.1016\/j.matbio.2018.01.012_bb0070","doi-asserted-by":"crossref","first-page":"3137","DOI":"10.1002\/j.1460-2075.1991.tb04875.x","article-title":"Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV","volume":"10","author":"Fox","year":"1991","journal-title":"EMBO J."},{"issue":"1","key":"10.1016\/j.matbio.2018.01.012_bb0075","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1006\/jmbi.1998.2004","article-title":"Nidogen-2: a new basement membrane protein with diverse binding properties","volume":"282","author":"Kohfeldt","year":"1998","journal-title":"J. Mol. Biol."},{"issue":"3","key":"10.1016\/j.matbio.2018.01.012_bb0080","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1046\/j.1432-1327.1999.00127.x","article-title":"Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin","volume":"259","author":"Hopf","year":"1999","journal-title":"Eur. J. Biochem."},{"issue":"3","key":"10.1016\/j.matbio.2018.01.012_bb0085","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1006\/jmbi.2001.4878","article-title":"Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparin to different IG modules of perlecan","volume":"311","author":"Hopf","year":"2001","journal-title":"J. Mol. Biol."},{"issue":"2","key":"10.1016\/j.matbio.2018.01.012_bb0090","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1111\/j.1432-1033.1981.tb05690.x","article-title":"A network model for the organization of type IV collagen molecules in basement membranes","volume":"120","author":"Timpl","year":"1981","journal-title":"Eur. J. Biochem."},{"issue":"8","key":"10.1016\/j.matbio.2018.01.012_bb0095","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.1021\/bi00303a040","article-title":"Self-assembly of basement membrane collagen","volume":"23","author":"Yurchenco","year":"1984","journal-title":"Biochemistry"},{"issue":"6 Pt 1","key":"10.1016\/j.matbio.2018.01.012_bb0100","doi-asserted-by":"crossref","first-page":"2559","DOI":"10.1083\/jcb.105.6.2559","article-title":"Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network","volume":"105","author":"Yurchenco","year":"1987","journal-title":"J. Cell Biol."},{"issue":"1","key":"10.1016\/j.matbio.2018.01.012_bb0105","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1111\/j.1432-1033.1985.tb09186.x","article-title":"Amino acid sequence of the N-terminal aggregation and cross-linking region (7S domain) of the alpha 1 (IV) chain of human basement membrane collagen","volume":"152","author":"Glanville","year":"1985","journal-title":"Eur. J. Biochem."},{"issue":"3","key":"10.1016\/j.matbio.2018.01.012_bb0110","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1111\/j.1432-1033.1987.tb13455.x","article-title":"Construction of a model for the aggregation and cross-linking region (7S domain) of type IV collagen based upon an evaluation of the primary structure of the alpha 1 and alpha 2 chains in this region","volume":"168","author":"Siebold","year":"1987","journal-title":"Eur. J. Biochem."},{"issue":"5945","key":"10.1016\/j.matbio.2018.01.012_bb0115","doi-asserted-by":"crossref","first-page":"1230","DOI":"10.1126\/science.1176811","article-title":"A sulfilimine bond identified in collagen IV","volume":"325","author":"Vanacore","year":"2009","journal-title":"Science"},{"issue":"4","key":"10.1016\/j.matbio.2018.01.012_bb0120","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1016\/S0896-6273(00)80096-3","article-title":"Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor","volume":"16","author":"Gesemann","year":"1996","journal-title":"Neuron"},{"issue":"38","key":"10.1016\/j.matbio.2018.01.012_bb0125","doi-asserted-by":"crossref","first-page":"23418","DOI":"10.1074\/jbc.271.38.23418","article-title":"Dystroglycan is a dual receptor for agrin and laminin-2 in Schwann cell membrane","volume":"271","author":"Yamada","year":"1996","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.matbio.2018.01.012_bb0130","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1083\/jcb.137.3.671","article-title":"Agrin binds to the nerve-muscle basal lamina via laminin","volume":"137","author":"Denzer","year":"1997","journal-title":"J. Cell Biol."},{"issue":"2","key":"10.1016\/j.matbio.2018.01.012_bb0135","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1093\/emboj\/17.2.335","article-title":"Electron microscopic structure of agrin and mapping of its binding site in laminin-1","volume":"17","author":"Denzer","year":"1998","journal-title":"EMBO J."},{"issue":"1","key":"10.1016\/j.matbio.2018.01.012_bb0140","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1074\/jbc.273.1.600","article-title":"Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue","volume":"273","author":"Gesemann","year":"1998","journal-title":"J. Biol. Chem."},{"issue":"50","key":"10.1016\/j.matbio.2018.01.012_bb0145","doi-asserted-by":"crossref","first-page":"41449","DOI":"10.1074\/jbc.M508939200","article-title":"Conjugation of LG domains of agrins and perlecan to polymerizing laminin-2 promotes acetylcholine receptor clustering","volume":"280","author":"Smirnov","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.matbio.2018.01.012_bb0150","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/S1097-2765(00)80388-3","article-title":"The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin","volume":"4","author":"Hohenester","year":"1999","journal-title":"Mol. Cell"},{"issue":"50","key":"10.1016\/j.matbio.2018.01.012_bb0155","doi-asserted-by":"crossref","first-page":"31525","DOI":"10.1074\/jbc.272.50.31525","article-title":"Self-assembly of laminin isoforms","volume":"272","author":"Cheng","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.matbio.2018.01.012_bb0160","doi-asserted-by":"crossref","first-page":"17286","DOI":"10.1016\/S0021-9258(19)85334-6","article-title":"Self-assembly and calcium-binding sites in laminin. A three-arm interaction model","volume":"268","author":"Yurchenco","year":"1993","journal-title":"J. Biol. Chem."},{"issue":"29","key":"10.1016\/j.matbio.2018.01.012_bb0165","doi-asserted-by":"crossref","first-page":"21437","DOI":"10.1074\/jbc.M702963200","article-title":"Role of laminin terminal globular domains in basement membrane assembly","volume":"282","author":"McKee","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"13","key":"10.1016\/j.matbio.2018.01.012_bb0170","doi-asserted-by":"crossref","first-page":"8984","DOI":"10.1074\/jbc.M809719200","article-title":"Scaffold-forming and adhesive contributions of synthetic laminin-binding proteins to basement membrane assembly","volume":"284","author":"McKee","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"7","key":"10.1016\/j.matbio.2018.01.012_bb0175","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0042473","article-title":"Crystal structures of the network-forming short-arm tips of the laminin beta1 and gamma1 chains","volume":"7","author":"Carafoli","year":"2012","journal-title":"PLoS One"},{"issue":"3","key":"10.1016\/j.matbio.2018.01.012_bb0180","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1038\/embor.2011.3","article-title":"Determinants of laminin polymerization revealed by the structure of the alpha5 chain amino-terminal region","volume":"12","author":"Hussain","year":"2011","journal-title":"EMBO Rep."},{"issue":"5","key":"10.1016\/j.matbio.2018.01.012_bb0185","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1002\/mus.22132","article-title":"Clinical and molecular characterization of limb-girdle muscular dystrophy due to LAMA2 mutations","volume":"44","author":"Gavassini","year":"2011","journal-title":"Muscle Nerve"},{"issue":"10","key":"10.1016\/j.matbio.2018.01.012_bb0190","doi-asserted-by":"crossref","first-page":"1582","DOI":"10.1001\/archneur.62.10.1582","article-title":"LAMA2 gene analysis in congenital muscular dystrophy: new mutations, prenatal diagnosis, and founder effect","volume":"62","author":"Di Blasi","year":"2005","journal-title":"Arch. Neurol."},{"issue":"Pt. 10","key":"10.1016\/j.matbio.2018.01.012_bb0195","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1242\/jcs.015354","article-title":"A single point mutation in the LN domain of LAMA2 causes muscular dystrophy and peripheral amyelination","volume":"121","author":"Patton","year":"2008","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.matbio.2018.01.012_bb0200","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1186\/1471-213X-14-26","article-title":"Distinct functions of the laminin beta LN domain and collagen IV during cardiac extracellular matrix formation and stabilization of alary muscle attachments revealed by EMS mutagenesis in Drosophila","volume":"14","author":"Hollfelder","year":"2014","journal-title":"BMC Dev. Biol."},{"issue":"9","key":"10.1016\/j.matbio.2018.01.012_bb0205","doi-asserted-by":"crossref","first-page":"992","DOI":"10.1002\/humu.21304","article-title":"Mutations in the human laminin beta2 (LAMB2) gene and the associated phenotypic spectrum","volume":"31","author":"Matejas","year":"2010","journal-title":"Hum. Mutat."},{"issue":"22","key":"10.1016\/j.matbio.2018.01.012_bb0210","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1016\/S0960-9822(00)80056-1","article-title":"The laminin alpha2 expressed by dystrophic dy(2J) mice is defective in its ability to form polymers","volume":"9","author":"Colognato","year":"1999","journal-title":"Curr. Biol."},{"key":"10.1016\/j.matbio.2018.01.012_bb0215","doi-asserted-by":"crossref","DOI":"10.1016\/j.matbio.2017.11.009","article-title":"Laminin-deficient muscular dystrophy: molecular pathogenesis and structural repair strategies","author":"Yurchenco","year":"2017","journal-title":"Matrix Biol."},{"issue":"6","key":"10.1016\/j.matbio.2018.01.012_bb0220","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1016\/j.ophtha.2010.10.009","article-title":"A novel mutation of LAMB2 in a multigenerational mennonite family reveals a new phenotypic variant of Pierson syndrome","volume":"118","author":"Mohney","year":"2011","journal-title":"Ophthalmology"},{"key":"10.1016\/j.matbio.2018.01.012_bb0225","doi-asserted-by":"crossref","first-page":"1879","DOI":"10.1002\/j.1460-2075.1993.tb05836.x","article-title":"A single EGF-like motif of laminin is responsible for high affinity nidogen binding","volume":"12","author":"Mayer","year":"1993","journal-title":"EMBO J."},{"issue":"3","key":"10.1016\/j.matbio.2018.01.012_bb0230","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1006\/jmbi.1996.0191","article-title":"Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site","volume":"257","author":"Stetefeld","year":"1996","journal-title":"J. Mol. Biol."},{"issue":"7","key":"10.1016\/j.matbio.2018.01.012_bb0235","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1038\/89683","article-title":"Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1","volume":"8","author":"Hopf","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.matbio.2018.01.012_bb0240","doi-asserted-by":"crossref","first-page":"10881","DOI":"10.1016\/S0021-9258(18)82067-1","article-title":"Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan, and zinc","volume":"268","author":"Reinhardt","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.matbio.2018.01.012_bb0245","doi-asserted-by":"crossref","DOI":"10.1681\/ASN.2017090997","article-title":"Pathogenicity of a human laminin beta2 mutation revealed in models of Alport syndrome","author":"Funk","year":"2017","journal-title":"J. Am. Soc. Nephrol."},{"issue":"5","key":"10.1016\/j.matbio.2018.01.012_bb0250","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1007\/s00467-011-2088-2","article-title":"Pierson syndrome in an adolescent girl with nephrotic range proteinuria but a normal GFR","volume":"27","author":"Lehnhardt","year":"2012","journal-title":"Pediatr. Nephrol."},{"issue":"53","key":"10.1016\/j.matbio.2018.01.012_bb0255","doi-asserted-by":"crossref","first-page":"44270","DOI":"10.1074\/jbc.M112.418426","article-title":"Laminin network formation studied by reconstitution of ternary nodes in solution","volume":"287","author":"Purvis","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.matbio.2018.01.012_bb0260","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1681\/ASN.2010060632","article-title":"A missense LAMB2 mutation causes congenital nephrotic syndrome by impairing laminin secretion","volume":"22","author":"Chen","year":"2011","journal-title":"J. Am. Soc. Nephrol."},{"issue":"8","key":"10.1016\/j.matbio.2018.01.012_bb0265","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1681\/ASN.2012121149","article-title":"Laminin beta2 gene missense mutation produces endoplasmic reticulum stress in podocytes","volume":"24","author":"Chen","year":"2013","journal-title":"J. Am. Soc. Nephrol."},{"issue":"1","key":"10.1016\/j.matbio.2018.01.012_bb0270","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1083\/jcb.144.1.151","article-title":"Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation","volume":"144","author":"Smyth","year":"1999","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.matbio.2018.01.012_bb0275","doi-asserted-by":"crossref","first-page":"7636","DOI":"10.1016\/S0021-9258(17)39656-4","article-title":"Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity","volume":"260","author":"Yurchenco","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.matbio.2018.01.012_bb0280","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0022-2836(81)90326-0","article-title":"Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix","volume":"150","author":"Engel","year":"1981","journal-title":"J. Mol. Biol."},{"issue":"3","key":"10.1016\/j.matbio.2018.01.012_bb0285","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1172\/JCI90854","article-title":"Chimeric protein repair of laminin polymerization ameliorates muscular dystrophy phenotype","volume":"127","author":"McKee","year":"2017","journal-title":"J. Clin. Invest."},{"issue":"396","key":"10.1016\/j.matbio.2018.01.012_bb0290","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.aal4649","article-title":"Linker proteins restore basement membrane and correct LAMA2-related muscular dystrophy in mice","volume":"9","author":"Reinhard","year":"2017","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.matbio.2018.01.012_bb0295","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1002\/cpps.20","article-title":"Comparative protein structure modeling using MODELLER","volume":"86","author":"Webb","year":"2016","journal-title":"Curr. Protoc. Protein Sci."},{"key":"10.1016\/j.matbio.2018.01.012_bb0300","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms13515","article-title":"Structural decoding of netrin-4 reveals a regulatory function towards mature basement membranes","volume":"7","author":"Reuten","year":"2016","journal-title":"Nat. Commun."},{"issue":"2","key":"10.1016\/j.matbio.2018.01.012_bb0305","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.ccell.2016.01.001","article-title":"Structural decoding of the Netrin-1\/UNC5 interaction and its therapeutical implications in cancers","volume":"29","author":"Grandin","year":"2016","journal-title":"Cancer Cell"}],"container-title":["Matrix Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0945053X17304894?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0945053X17304894?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,8,15]],"date-time":"2022-08-15T01:08:29Z","timestamp":1660525709000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0945053X17304894"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,4]]},"references-count":61,"alternative-id":["S0945053X17304894"],"URL":"https:\/\/doi.org\/10.1016\/j.matbio.2018.01.012","relation":{},"ISSN":["0945-053X"],"issn-type":[{"value":"0945-053X","type":"print"}],"subject":[],"published":{"date-parts":[[2018,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Chimeric protein identification of dystrophic, Pierson and other laminin polymerization residues","name":"articletitle","label":"Article Title"},{"value":"Matrix Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.matbio.2018.01.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}