{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T01:11:29Z","timestamp":1790730689446,"version":"4.1.0"},"reference-count":63,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,5,4]],"date-time":"2021-05-04T00:00:00Z","timestamp":1620086400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["NY90\/2-1"],"award-info":[{"award-number":["NY90\/2-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["NY90\/5-1"],"award-info":[{"award-number":["NY90\/5-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["BE 4086\/5-1"],"award-info":[{"award-number":["BE 4086\/5-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["CRC850"],"award-info":[{"award-number":["CRC850"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["CRC877"],"award-info":[{"award-number":["CRC877"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Matrix Biology Plus"],"published-print":{"date-parts":[[2021,8]]},"DOI":"10.1016\/j.mbplus.2021.100065","type":"journal-article","created":{"date-parts":[[2021,5,13]],"date-time":"2021-05-13T12:27:50Z","timestamp":1620908870000},"page":"100065","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":22,"special_numbering":"C","title":["Distinct contributions of meprins to skin regeneration after injury \u2013 Meprin \u03b1 a physiological processer of pro-collagen VII"],"prefix":"10.1016","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2024-0402","authenticated-orcid":false,"given":"Daniel","family":"Kruppa","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8529-2326","authenticated-orcid":false,"given":"Florian","family":"Peters","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olivier","family":"Bornert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mareike D.","family":"Maler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan F.","family":"Martin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5100-9916","authenticated-orcid":false,"given":"Christoph","family":"Becker-Pauly","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Nystr\u00f6m","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.mbplus.2021.100065_b0005","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1016\/j.jid.2016.03.036","article-title":"Fibroblast-derived MMP-14 regulates collagen homeostasis in adult skin","volume":"136","author":"Zigrino","year":"2016","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mbplus.2021.100065_b0010","doi-asserted-by":"crossref","first-page":"100019","DOI":"10.1016\/j.mbplus.2019.100019","article-title":"Kallikreins: essential epidermal messengers for regulation of the skin microenvironment during homeostasis, repair and disease","volume":"6\u20137","author":"Nauroy","year":"2020","journal-title":"Matrix Biol. Plus."},{"key":"10.1016\/j.mbplus.2021.100065_b0015","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1177\/0963689717725755","article-title":"Fighting against skin aging: the way from bench to bedside","volume":"27","author":"Zhang","year":"2018","journal-title":"Cell Transplant."},{"key":"10.1016\/j.mbplus.2021.100065_b0020","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1089\/wound.2013.0485","article-title":"Extracellular matrix reorganization during wound healing and its impact on abnormal scarring","volume":"4","author":"Xue","year":"2015","journal-title":"Adv. Wound Care"},{"key":"10.1016\/j.mbplus.2021.100065_b0025","doi-asserted-by":"crossref","first-page":"265sr6","DOI":"10.1126\/scitranslmed.3009337","article-title":"Wound repair and regeneration: mechanisms, signaling, and translation","volume":"6","author":"Eming","year":"2014","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.mbplus.2021.100065_b0030","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1038\/sj.jid.5700675","article-title":"The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation","volume":"127","author":"Becker-Pauly","year":"2007","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mbplus.2021.100065_b0035","doi-asserted-by":"crossref","first-page":"2727","DOI":"10.1038\/jid.2010.202","article-title":"Processing of procollagen III by meprins: new players in extracellular matrix assembly?","volume":"130","author":"Kronenberg","year":"2010","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mbplus.2021.100065_b0040","doi-asserted-by":"crossref","first-page":"26372","DOI":"10.1074\/jbc.M203247200","article-title":"Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen","volume":"277","author":"Rattenholl","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0045","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.matbio.2016.06.004","article-title":"BMP1-like proteinases are essential to the structure and wound healing of skin","volume":"56","author":"Muir","year":"2016","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0050","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1083\/jcb.200606058","article-title":"BMP1 controls TGF\u03b21 activation via cleavage of latent TGF\u03b2-binding protein","volume":"175","author":"Ge","year":"2006","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0055","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.aba3880","article-title":"BMP-1 disrupts cell adhesion and enhances TGF-\u03b2 activation through cleavage of the matricellular protein thrombospondin-1","volume":"13","author":"Anastasi","year":"2020","journal-title":"Sci. Signal."},{"key":"10.1016\/j.mbplus.2021.100065_b0060","doi-asserted-by":"crossref","first-page":"27051","DOI":"10.1074\/jbc.M102921200","article-title":"Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer","volume":"276","author":"Kessler","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0065","doi-asserted-by":"crossref","first-page":"27511","DOI":"10.1074\/jbc.273.42.27511","article-title":"Bone morphogenetic protein-1 processes the NH2-terminal propeptide, and a furin-like proprotein convertase processes the COOH-terminal propeptide of pro-alpha1(V) collagen","volume":"273","author":"Imamura","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0070","doi-asserted-by":"crossref","first-page":"41626","DOI":"10.1074\/jbc.M406630200","article-title":"Bone morphogenetic protein-1\/tolloid-related metalloproteinases process osteoglycin and enhance its ability to regulate collagen fibrillogenesis","volume":"279","author":"Ge","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0075","doi-asserted-by":"crossref","first-page":"22537","DOI":"10.1074\/jbc.M102352200","article-title":"Multiple bone morphogenetic protein 1-related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures","volume":"276","author":"Uzel","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0080","doi-asserted-by":"crossref","first-page":"22728","DOI":"10.1074\/jbc.M002345200","article-title":"Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 \u03b32 chain","volume":"275","author":"Amano","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0085","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.matbio.2016.07.012","article-title":"Cell therapy for basement membrane-linked diseases","volume":"57\u201358","author":"Nystr\u00f6m","year":"2017","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0090","doi-asserted-by":"crossref","first-page":"32572","DOI":"10.1016\/S0021-9258(18)31672-7","article-title":"Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues","volume":"269","author":"Takahara","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0095","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1007\/s00018-012-1106-2","article-title":"The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin \u03b2 and ADAM10","volume":"70","author":"Jefferson","year":"2013","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.mbplus.2021.100065_b0100","doi-asserted-by":"crossref","first-page":"14219","DOI":"10.1073\/pnas.1305464110","article-title":"Metalloproteases meprin \u03b1 and meprin \u03b2 are C- and N-procollagen proteinases important for collagen assembly and tensile strength","volume":"110","author":"Broder","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.mbplus.2021.100065_b0105","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M111.009233","article-title":"Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates","volume":"10","author":"Becker-Pauly","year":"2011","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mbplus.2021.100065_b0110","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.matbio.2015.01.010","article-title":"Meprin \u03b1 and meprin \u03b2: procollagen proteinases in health and disease","volume":"44\u201346","author":"Prox","year":"2015","journal-title":"Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0115","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1006\/abbi.1997.0453","article-title":"Maturation of secreted meprin \u03b1 during biosynthesis: role of the furin site and identification of the COOH-terminal amino acids of the mouse kidney metalloprotease subunit","volume":"349","author":"Tang","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.mbplus.2021.100065_b0120","doi-asserted-by":"crossref","first-page":"13308","DOI":"10.1074\/jbc.M114.559088","article-title":"ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A","volume":"289","author":"Herzog","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0125","first-page":"11925","article-title":"Meprin \u03b2 induces activities of A disintegrin and metalloproteinases 9, 10, and 17 by specific prodomain cleavage, FASEB","volume":"33","author":"Wichert","year":"2019","journal-title":"J. Off. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0130","first-page":"7490","article-title":"Tethering soluble meprin \u03b1 in an enzyme complex to the cell surface affects IBD-associated genes, FASEB","volume":"33","author":"Peters","year":"2019","journal-title":"J. Off. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0135","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.cyto.2018.11.032","article-title":"Role of meprin metalloproteinases in cytokine processing and inflammation","volume":"114","author":"Herzog","year":"2019","journal-title":"Cytokine"},{"key":"10.1016\/j.mbplus.2021.100065_b0140","doi-asserted-by":"crossref","first-page":"44053","DOI":"10.1038\/srep44053","article-title":"Meprin metalloproteases generate biologically active soluble interleukin-6 receptor to induce trans-signaling","volume":"7","author":"Arnold","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mbplus.2021.100065_b0145","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20153677","article-title":"Differences in shedding of the interleukin-11 receptor by the proteases ADAM9, ADAM10, ADAM17, meprin \u03b1, meprin \u03b2 and MT1-MMP","volume":"20","author":"Sammel","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.mbplus.2021.100065_b0150","doi-asserted-by":"crossref","first-page":"7580","DOI":"10.1074\/jbc.M113.546309","article-title":"Meprin metalloproteases inactivate interleukin 6","volume":"289","author":"Keiffer","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0155","doi-asserted-by":"crossref","DOI":"10.1126\/science.1260419","article-title":"Tissue-based map of the human proteome","volume":"347","author":"Uhlen","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.mbplus.2021.100065_b0160","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1034\/j.1600-0560.2001.028004191.x","article-title":"E-cadherin expression in wound healing of mouse skin","volume":"28","author":"Kuwahara","year":"2001","journal-title":"J. Cutan. Pathol."},{"key":"10.1016\/j.mbplus.2021.100065_b0165","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1083\/jcb.201501076","article-title":"Polarized E-cadherin endocytosis directs actomyosin remodeling during embryonic wound repair","volume":"210","author":"Hunter","year":"2015","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0170","doi-asserted-by":"crossref","first-page":"e2153","DOI":"10.1371\/journal.pone.0002153","article-title":"The metalloprotease meprin\u03b2 processes E-cadherin and weakens intercellular adhesion","volume":"3","author":"Huguenin","year":"2008","journal-title":"PLoS One"},{"key":"10.1016\/j.mbplus.2021.100065_b0175","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.matbio.2017.04.003","article-title":"The provisional matrix: setting the stage for tissue repair outcomes","volume":"60\u201361","author":"Barker","year":"2017","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0180","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.matbio.2015.05.006","article-title":"The extracellular matrix and transforming growth factor-\u03b21: tale of a strained relationship","volume":"47","author":"Hinz","year":"2015","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0185","doi-asserted-by":"crossref","first-page":"100046","DOI":"10.1016\/j.mbplus.2020.100046","article-title":"Fibronectin fibers are highly tensed in healthy organs in contrast to tumors and virus-infected lymph nodes","volume":"8","author":"Fonta","year":"2020","journal-title":"Matrix Biol. Plus"},{"key":"10.1016\/j.mbplus.2021.100065_b0190","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1083\/jcb.131.2.551","article-title":"Immunohistochemical and mutation analyses demonstrate that procollagen VII is processed to collagen VII through removal of the NC-2 domain","volume":"131","author":"Bruckner-Tuderman","year":"1995","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0195","unstructured":"MEROPS -\u2013 the Peptidase Database, n.d., https:\/\/www.ebi.ac.uk\/merops\/cgi-bin\/pepsum?id=M12.002;type=P (accessed March 8, 2021)."},{"key":"10.1016\/j.mbplus.2021.100065_b0200","doi-asserted-by":"crossref","DOI":"10.1016\/j.matbio.2017.01.002","article-title":"Stromal microenvironment in type VII collagen-deficient skin: te ground for squamous cell carcinoma development","author":"Guerra","year":"2017","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0205","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.matbio.2018.01.016","article-title":"Injury- and inflammation-driven skin fibrosis: the paradigm of epidermolysis bullosa","volume":"68\u201369","author":"Nystr\u00f6m","year":"2018","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0210","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/j.matbio.2017.12.010","article-title":"Therapies for genetic extracellular matrix diseases of the skin","volume":"71\u201372","author":"Nystr\u00f6m","year":"2018","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0215","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1038\/s41598-018-37024-5","article-title":"Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases","volume":"9","author":"Karmilin","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mbplus.2021.100065_b0220","unstructured":"R. Bernasconi, K. Thriene, E. Romero-Fern\u00e1ndez, C. Gretzmeier, T. K\u00fchl, Proinflammatory immunity drives injury-induced fibrosis, n.d."},{"key":"10.1016\/j.mbplus.2021.100065_b0225","first-page":"3964","article-title":"Differential roles of macrophages in diverse phases of skin repair","volume":"184","author":"Lucas","year":"2010","journal-title":"J. Immunol. Baltim. Md 1950"},{"key":"10.1016\/j.mbplus.2021.100065_b0230","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1111\/imr.12615","article-title":"Function and regulation of IL-1\u03b1 in inflammatory diseases and cancer","volume":"281","author":"Malik","year":"2018","journal-title":"Immunol. Rev."},{"key":"10.1016\/j.mbplus.2021.100065_b0235","doi-asserted-by":"crossref","first-page":"39969","DOI":"10.1038\/srep39969","article-title":"Meprin \u03b2 contributes to collagen deposition in lung fibrosis","volume":"7","author":"Biasin","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mbplus.2021.100065_b0240","doi-asserted-by":"crossref","first-page":"2096","DOI":"10.1016\/j.bbamcr.2017.05.011","article-title":"Meprin metalloproteases: molecular regulation and function in inflammation and fibrosis","volume":"1864","author":"Arnold","year":"2017","journal-title":"Biochim. Biophys. Acta, Mol. Cell. Res."},{"key":"10.1016\/j.mbplus.2021.100065_b0245","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.omtn.2019.11.018","article-title":"Inhibition of miR-155-5p exerts anti-fibrotic effects in silicotic mice by regulating meprin \u03b1","volume":"19","author":"Chen","year":"2019","journal-title":"Mol. Ther. Nucleic Acids"},{"key":"10.1016\/j.mbplus.2021.100065_b0250","first-page":"1075","article-title":"A novel dimeric thymosin beta 4 with enhanced activities accelerates the rate of wound healing","volume":"7","author":"Xu","year":"2013","journal-title":"Drug Des. Dev. Ther."},{"key":"10.1016\/j.mbplus.2021.100065_b0255","doi-asserted-by":"crossref","first-page":"24188","DOI":"10.1074\/jbc.M501486200","article-title":"Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1","volume":"280","author":"Moali","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mbplus.2021.100065_b0260","doi-asserted-by":"crossref","first-page":"1579","DOI":"10.1039\/C003962D","article-title":"Comparative quantitation of proteome alterations induced by aging or immortalization in primary human fibroblasts and keratinocytes for clinical applications","volume":"6","author":"Sprenger","year":"2010","journal-title":"Mol. BioSyst."},{"key":"10.1016\/j.mbplus.2021.100065_b0265","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1128\/MCB.23.4.1221-1230.2003","article-title":"Targeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles","volume":"23","author":"Norman","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0270","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1038\/mi.2009.3","article-title":"MEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel disease","volume":"2","author":"Banerjee","year":"2009","journal-title":"Mucosal Immunol."},{"key":"10.1016\/j.mbplus.2021.100065_b0275","doi-asserted-by":"crossref","first-page":"G273","DOI":"10.1152\/ajpgi.00504.2009","article-title":"Balance of meprin A and B in mice affects the progression of experimental inflammatory bowel disease","volume":"300","author":"Banerjee","year":"2011","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"10.1016\/j.mbplus.2021.100065_b0280","doi-asserted-by":"crossref","first-page":"e1000412","DOI":"10.1371\/journal.pbio.1000412","article-title":"Improving bioscience research reporting: the ARRIVE guidelines for reporting animal research","volume":"8","author":"Kilkenny","year":"2010","journal-title":"PLoS Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0285","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.15252\/emmm.201505061","article-title":"Losartan ameliorates dystrophic epidermolysis bullosa and uncovers new disease mechanisms","volume":"7","author":"Nystr\u00f6m","year":"2015","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.mbplus.2021.100065_b0290","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.1038\/mt.2015.58","article-title":"High local concentrations of intradermal MSCs restore skin integrity and facilitate wound healing in dystrophic epidermolysis bullosa","volume":"23","author":"K\u00fchl","year":"2015","journal-title":"Mol. Ther. J. Am. Soc. Gene Ther."},{"key":"10.1016\/j.mbplus.2021.100065_b0295","doi-asserted-by":"crossref","first-page":"3498","DOI":"10.1172\/JCI68127","article-title":"Collagen VII plays a dual role in wound healing","volume":"123","author":"Nystr\u00f6m","year":"2013","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.mbplus.2021.100065_b0300","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1016\/j.jid.2016.02.002","article-title":"Collagen VII Half-life at the dermal-epidermal junction zone: implications for mechanisms and therapy of genodermatoses","volume":"136","author":"K\u00fchl","year":"2016","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.mbplus.2021.100065_b0305","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.matbio.2018.12.001","article-title":"Decorin counteracts disease progression in mice with recessive dystrophic epidermolysis bullosa","volume":"81","author":"Cianfarani","year":"2019","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"10.1016\/j.mbplus.2021.100065_b0310","doi-asserted-by":"crossref","first-page":"100017","DOI":"10.1016\/j.mbplus.2019.100017","article-title":"Generation of rabbit polyclonal human and murine collagen VII monospecific antibodies: a useful tool for dystrophic epidermolysis bullosa therapy studies","volume":"4","author":"Bornert","year":"2019","journal-title":"Matrix Biol. Plus."},{"key":"10.1016\/j.mbplus.2021.100065_b0315","article-title":"QR-313, an antisense oligonucleotide, shows therapeutic efficacy for treatment of dominant and recessive dystrophic epidermolysis bullosa: a preclinical study","author":"Bornert","year":"2020","journal-title":"J. Invest. Dermatol."}],"container-title":["Matrix Biology Plus"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2590028521000090?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2590028521000090?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T04:39:41Z","timestamp":1778906381000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2590028521000090"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,8]]},"references-count":63,"alternative-id":["S2590028521000090"],"URL":"https:\/\/doi.org\/10.1016\/j.mbplus.2021.100065","relation":{},"ISSN":["2590-0285"],"issn-type":[{"value":"2590-0285","type":"print"}],"subject":[],"published":{"date-parts":[[2021,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Distinct contributions of meprins to skin regeneration after injury \u2013 Meprin \u03b1 a physiological processer of pro-collagen VII","name":"articletitle","label":"Article Title"},{"value":"Matrix Biology Plus","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mbplus.2021.100065","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"100065"}}