{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T00:17:31Z","timestamp":1793146651805,"version":"4.5.0"},"reference-count":247,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2017,11,1]],"date-time":"2017-11-01T00:00:00Z","timestamp":1509494400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,11,1]],"date-time":"2018-11-01T00:00:00Z","timestamp":1541030400000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["CA98799"],"award-info":[{"award-number":["CA98799"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AR063795"],"award-info":[{"award-number":["AR063795"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["MH078948"],"award-info":[{"award-number":["MH078948"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["268201000036C"],"award-info":[{"award-number":["268201000036C"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Multiple Sclerosis National Research Institute"},{"DOI":"10.13039\/100000928","name":"Robert A. Welch Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100000928","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100005979","name":"Lustgarten Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005979","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"published-print":{"date-parts":[[2017,11]]},"DOI":"10.1016\/j.bbamcr.2017.04.015","type":"journal-article","created":{"date-parts":[[2017,4,26]],"date-time":"2017-04-26T05:15:44Z","timestamp":1493183744000},"page":"1940-1951","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":193,"special_numbering":"PA","title":["Matrix metalloproteinase collagenolysis in health and disease"],"prefix":"10.1016","volume":"1864","author":[{"given":"Sabrina","family":"Amar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lyndsay","family":"Smith","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregg B.","family":"Fields","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamcr.2017.04.015_bb0005","doi-asserted-by":"crossref","first-page":"1014","DOI":"10.1073\/pnas.48.6.1014","article-title":"Collagenolytic activity in amphibian tissues: a tissue culture assay","volume":"48","author":"Gross","year":"1962","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0010","doi-asserted-by":"crossref","first-page":"2735","DOI":"10.1021\/cr9804543","article-title":"Design and therapeutic application of matrix metalloproteinase inhibitors","volume":"99","author":"Whittaker","year":"1999","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0015","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1517\/13543776.15.3.253","article-title":"Recent non-hydroxamate matrix metalloproteinase inhibitors","volume":"15","author":"Breuer","year":"2005","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0020","doi-asserted-by":"crossref","first-page":"31","DOI":"10.2147\/MNM.S65143","article-title":"Matrix metalloproteinase protein inhibitors: highlighting a new beginning for metalloproteinases in medicine","volume":"3","author":"Mohan","year":"2016","journal-title":"Metalloproteinases Med."},{"issue":"4","key":"10.1016\/j.bbamcr.2017.04.015_bb0025","first-page":"30","article-title":"European roundup: no anticancer benefit in trials of marimastat","volume":"20","author":"Fox","year":"2000","journal-title":"Gen. Eng. News"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0030","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1007\/BF02574483","article-title":"Matrix metalloproteinases and their role in pancreatic cancer: a review of preclinical studies and clinical trials","volume":"9","author":"Bloomston","year":"2002","journal-title":"Ann. Surg. Oncol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0035","doi-asserted-by":"crossref","first-page":"3805","DOI":"10.2174\/092986709789178037","article-title":"Selective matrix metalloproteinase inhibitors for cancer","volume":"16","author":"Li","year":"2009","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0040","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/nrc1821","article-title":"Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy","volume":"6","author":"Overall","year":"2006","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0045","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1007\/s10555-007-9089-4","article-title":"The other side of MMPs: protective roles in tumor progression","volume":"26","author":"Martin","year":"2007","journal-title":"Cancer Metastasis Rev."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0050","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1111\/j.1582-4934.2011.01302.x","article-title":"Matrix metalloproteinases: protective roles in cancer","volume":"15","author":"Decock","year":"2011","journal-title":"J. Cell. Mol. Med."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0055","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.tips.2013.02.004","article-title":"Missing the target: matrix metalloproteinase antitargets in inflammation and cancer","volume":"34","author":"Dufour","year":"2013","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0060","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1038\/nrc745","article-title":"New functions for the matrix metalloproteinases in cancer progression","volume":"2","author":"Egeblad","year":"2002","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0065","doi-asserted-by":"crossref","first-page":"263","DOI":"10.2174\/138161207779313524","article-title":"Proteomic validation of protease drug targets: pharmacoproteomics of matrix metalloproteinase inhibitor drugs using isotope-coded affinity tag labelling and tandem mass spectrometry","volume":"13","author":"Butler","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0070","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1080\/10409230701340019","article-title":"The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases","volume":"42","author":"Cauwe","year":"2007","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0075","doi-asserted-by":"crossref","first-page":"10830","DOI":"10.1021\/bi901656f","article-title":"Updated biological roles for matrix metalloproteinases and new \u201cintracellular\u201d substrates revealed by degradomics","volume":"48","author":"Butler","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0080","doi-asserted-by":"crossref","first-page":"351","DOI":"10.3109\/10409238.2010.501783","article-title":"Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases","volume":"45","author":"Cauwe","year":"2010","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0085","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.bbamcr.2009.09.015","article-title":"Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics","volume":"1803","author":"Rodr\u00edguez","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0090","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1001869","article-title":"Network analyses reveal pervasive functional regulation between proteases in the human protease web","volume":"12","author":"Fortelny","year":"2014","journal-title":"PLoS Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0095","doi-asserted-by":"crossref","first-page":"2100","DOI":"10.1021\/ja208338j","article-title":"Structural basis for matrix metalloproteinase 1 catalyzed collagenolysis","volume":"134","author":"Bertini","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0100","doi-asserted-by":"crossref","first-page":"30659","DOI":"10.1074\/jbc.M113.477240","article-title":"Examination of matrix metalloproteinase-1 (MMP-1) in solution: a preference for the pre-collagenolysis state","volume":"288","author":"Cerofolini","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0105","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.str.2014.11.021","article-title":"Transient collagen triple helix binding to a key metalloproteinase in invasion and development","volume":"23","author":"Zhao","year":"2015","journal-title":"Structure"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0110","doi-asserted-by":"crossref","first-page":"7","DOI":"10.3109\/07853890109002055","article-title":"Collagen and collagen-related diseases","volume":"33","author":"Myllyharju","year":"2001","journal-title":"Ann. Med."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0115","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1093\/emboj\/21.7.1524","article-title":"CLAC: a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P\/collagen type XXV","volume":"21","author":"Hashimoto","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0120","series-title":"Comprehensive Natural Products II","first-page":"469","article-title":"Collagen formation and structure","author":"B\u00e4chinger","year":"2010"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0125","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1126\/science.7695699","article-title":"Crystal and molecular structure of a collagen-like peptide at 1.9\u00c5 resolution","volume":"266","author":"Bella","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0130","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1038\/33573","article-title":"Code for collagen's stability deciphered","volume":"392","author":"Holmgren","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0135","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1126\/science.1099179","article-title":"Interstitial collagenase is a Brownian rachet driven by proteolysis of collagen","volume":"306","author":"Saffarian","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0140","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0079-6603(08)60249-4","article-title":"Collagen genes: mutations affecting collagen structure and expression","volume":"47","author":"Cole","year":"1994","journal-title":"Prog. Nucleic Acid Res. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0145","doi-asserted-by":"crossref","first-page":"19781","DOI":"10.1074\/jbc.R109.013219","article-title":"Structural insights into the interactions between platelet receptors and fibrillar collagen","volume":"284","author":"Herr","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0150","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1146\/annurev.biochem.77.032207.120833","article-title":"Collagen structure and stability","volume":"78","author":"Shoulders","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0155","series-title":"Cell Biology of Extracellular Matrix","first-page":"7","article-title":"Collagen","author":"Linsenmayer","year":"1991"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0160","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1146\/annurev.bi.64.070195.002155","article-title":"Collagens: molecular biology, diseases, and potentials for therapy","volume":"64","author":"Prockop","year":"1995","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0165","series-title":"Post-translational Modifications of Proteins","first-page":"1","article-title":"Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins","author":"Kivirikko","year":"1992"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0170","doi-asserted-by":"crossref","first-page":"36158","DOI":"10.1074\/jbc.M006203200","article-title":"Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity","volume":"275","author":"Heikkinen","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0175","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/j.matbio.2007.01.002","article-title":"Lysyl hydroxylase 2 is a specific telopeptide hydroxylase, while all three isoenzymes hydroxylate collagenous sequences","volume":"26","author":"Takaluoma","year":"2007","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0180","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1128\/MCB.02085-07","article-title":"Core glycosylation of collagen is initiated by two \u03b2(1-O)galactosyltransferases","volume":"29","author":"Schegg","year":"2009","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0185","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1111\/j.1432-1033.1978.tb12641.x","article-title":"The role of cis-trans isomerization of peptide bonds in the coil <=> triple helix conversion of collagen","volume":"90","author":"B\u00e4chinger","year":"1978","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0190","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1111\/j.1432-1033.1980.tb04610.x","article-title":"Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen","volume":"106","author":"B\u00e4chinger","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0195","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/S0959-440X(99)80016-5","article-title":"Folding of peptide models of collagen and misfolding in disease","volume":"9","author":"Baum","year":"1999","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0200","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1073\/pnas.042707899","article-title":"Unstable molecules form stable tissues","volume":"99","author":"Persikov","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0205","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0001029","article-title":"Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm","volume":"2","author":"Makareeva","year":"2007","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0210","doi-asserted-by":"crossref","first-page":"6810","DOI":"10.1074\/jbc.M111.280248","article-title":"Direct in vitro and in vivo evidence for interaction between Hsp47 protein and collagen triple helix","volume":"287","author":"Ono","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0215","doi-asserted-by":"crossref","first-page":"13243","DOI":"10.1073\/pnas.1208072109","article-title":"Molecular basis for the action of the collagen-specific chaperone Hsp47\/SERPINH1 and its structure-specific client recognition","volume":"109","author":"Widmer","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0220","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.2174\/138161209788682433","article-title":"A review of the ADAMTS family, pharmaceutical targets of the future","volume":"15","author":"Tortorella","year":"2009","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0225","doi-asserted-by":"crossref","first-page":"5127","DOI":"10.1073\/pnas.93.10.5127","article-title":"The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1","volume":"93","author":"Li","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0230","doi-asserted-by":"crossref","first-page":"3231","DOI":"10.1021\/bi992312o","article-title":"Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, cicular dichroism, binding to procollagen type I, and computer modeling","volume":"39","author":"Sieron","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0235","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.bbamcr.2017.04.015_bb0240","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3160001","article-title":"Collagen fibril formation","volume":"316","author":"Kadler","year":"1996","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0245","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/0003-2697(81)90204-9","article-title":"Proteolytic enzymes as probes for the triple-helical conformation of procollagen","volume":"110","author":"Bruckner","year":"1981","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0250","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1016\/S0021-9258(20)71207-X","article-title":"Degradation of monomeric and fibrillar type III collagens by human skin collagenase","volume":"260","author":"Welgus","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0255","doi-asserted-by":"crossref","first-page":"38302","DOI":"10.1074\/jbc.M606004200","article-title":"The roles of substrate thermal stability and P2 and P1\u2032 subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity","volume":"281","author":"Minond","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0260","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1016\/j.matbio.2009.04.009","article-title":"Matrix metalloproteinase-1 cleavage site recognition and binding in full-length human type III collagen","volume":"28","author":"Williams","year":"2009","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0265","doi-asserted-by":"crossref","first-page":"1544","DOI":"10.1074\/jbc.271.3.1544","article-title":"Biochemical characterization of human collagenase-3","volume":"271","author":"Kn\u00e4uper","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0270","doi-asserted-by":"crossref","first-page":"16411","DOI":"10.1016\/S0021-9258(17)36252-X","article-title":"Cleavage of bovine skin type III collagen by proteolytic enzymes","volume":"260","author":"Birkedal-Hansen","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0275","doi-asserted-by":"crossref","first-page":"9516","DOI":"10.1016\/S0021-9258(19)68793-4","article-title":"Human skin fibroblast collagenase: assessment of activation energy and deuterium isotope effect with collagenous substrates","volume":"256","author":"Welgus","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0280","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/S0022-5193(05)80157-2","article-title":"A model for interstitial collagen catabolism by mammalian collagenases","volume":"153","author":"Fields","year":"1991","journal-title":"J. Theor. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0285","doi-asserted-by":"crossref","first-page":"16766","DOI":"10.1016\/S0021-9258(19)89457-7","article-title":"Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas","volume":"269","author":"Freije","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0290","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1172\/JCI118475","article-title":"Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage","volume":"97","author":"Mitchell","year":"1996","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0295","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1091\/mbc.7.10.1471","article-title":"Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development","volume":"7","author":"Stolow","year":"1996","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0300","doi-asserted-by":"crossref","first-page":"17893","DOI":"10.1074\/jbc.273.28.17893","article-title":"Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts","volume":"273","author":"Yang","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0305","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.biochi.2004.12.009","article-title":"Collagenases in cancer","volume":"87","author":"Ala-aho","year":"2005","journal-title":"Biochimie"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0310","doi-asserted-by":"crossref","first-page":"8785","DOI":"10.1074\/jbc.R113.451211","article-title":"Interstitial collagen catabolism","volume":"288","author":"Fields","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0315","doi-asserted-by":"crossref","first-page":"10048","DOI":"10.1016\/S0021-9258(18)61073-7","article-title":"The collagen substrate specificity of human neutrophil collagenase","volume":"262","author":"Hasty","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0320","doi-asserted-by":"crossref","first-page":"5872","DOI":"10.1074\/jbc.270.11.5872","article-title":"Matrix metalloproteinase-2 is an interstitial collagenase","volume":"270","author":"Aimes","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0325","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/S0945-053X(98)90110-X","article-title":"New collagenolytic enzymes\/cascade identified at the pannus-hard tissue junction in rheumatoid arthritis: destruction from above","volume":"17","author":"Konttinen","year":"1998","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0330","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/S0014-5793(01)02723-5","article-title":"Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain","volume":"503","author":"Patterson","year":"2001","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0335","doi-asserted-by":"crossref","first-page":"4662","DOI":"10.1016\/S0021-9258(19)69486-X","article-title":"Purification and properties of a gelatin-specific neutral protease from human skin","volume":"256","author":"Seltzer","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0340","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0024029","article-title":"Diffusion of MMPs on the surface of collagen fibrils: the mobile cell surface - collagen substratum interface","volume":"6","author":"Collier","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0345","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1111\/j.1742-4658.2007.05669.x","article-title":"Activity of matrix metalloproteinase-9 against native collagen types I and III","volume":"274","author":"Bigg","year":"2007","journal-title":"FEBS J."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0350","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1006\/bbrc.1994.1931","article-title":"A 92kDa gelatinase (MMP-9) cleavage site in native type V collagen","volume":"202","author":"Niyibizi","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0355","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1006\/abbi.1998.0662","article-title":"The fibronectin-like domain is required for the type V and XI collagenolytic activity of gelatinase B","volume":"354","author":"O'Farrell","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0360","doi-asserted-by":"crossref","first-page":"27964","DOI":"10.1074\/jbc.M003936200","article-title":"Identification of structural elements important for matrix metalloproteinase type V collagenolytic activity as revealed by chimeric enzymes","volume":"275","author":"O'Farrell","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0365","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1083\/jcb.149.6.1309","article-title":"Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3","volume":"149","author":"Hotary","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0370","doi-asserted-by":"crossref","first-page":"2446","DOI":"10.1074\/jbc.272.4.2446","article-title":"Membrane type I matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules","volume":"272","author":"Ohuchi","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0375","doi-asserted-by":"crossref","first-page":"8440","DOI":"10.1074\/jbc.M109128200","article-title":"Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase","volume":"277","author":"Lehti","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0380","doi-asserted-by":"crossref","first-page":"5390","DOI":"10.1091\/mbc.e06-08-0740","article-title":"Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP","volume":"17","author":"Itoh","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0385","doi-asserted-by":"crossref","first-page":"3221","DOI":"10.1091\/mbc.e08-01-0016","article-title":"Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase","volume":"19","author":"Li","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0390","doi-asserted-by":"crossref","first-page":"23001","DOI":"10.1074\/jbc.M109.002808","article-title":"Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion","volume":"284","author":"Sabeh","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0395","doi-asserted-by":"crossref","first-page":"29511","DOI":"10.1038\/srep29511","article-title":"Bilayer membrane modulation of membrane type 1 matrix metalloproteinase (MT1-MMP) structure and proteolytic activity","volume":"6","author":"Cerofolini","year":"2016","journal-title":"Nat. Sci. Rep."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0400","doi-asserted-by":"crossref","first-page":"39005","DOI":"10.1074\/jbc.M206874200","article-title":"Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain","volume":"277","author":"Tam","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0405","doi-asserted-by":"crossref","first-page":"7587","DOI":"10.1074\/jbc.M110.178434","article-title":"The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions","volume":"286","author":"Tochowicz","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0410","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1046\/j.1432-1327.1999.00459.x","article-title":"Characterization of a truncated recombinant form of human membrane type 3 matrix metalloproteinase","volume":"262","author":"Shimada","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0415","doi-asserted-by":"crossref","first-page":"38765","DOI":"10.1074\/jbc.M306618200","article-title":"Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis","volume":"278","author":"Jiang","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0420","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0028325","article-title":"Membrane-type-3 matrix metalloproteinase (MT3-MMP) functions as a matrix composition-dependent effector of melanoma cell invasion","volume":"6","author":"Tatti","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0425","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.ydbio.2007.10.017","article-title":"Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis","volume":"313","author":"Shi","year":"2008","journal-title":"Dev. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0430","doi-asserted-by":"crossref","first-page":"21960","DOI":"10.1074\/jbc.M007997200","article-title":"Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin\/MT6-MMP\/MMP-25 in neutrophils","volume":"276","author":"Kang","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0435","doi-asserted-by":"crossref","first-page":"16076","DOI":"10.1074\/jbc.M110.107094","article-title":"Biochemical characterization of the cellular glycosylphosphatidylinositol-linked membrane type-6 matrix metalloproteinase","volume":"285","author":"Radichev","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0440","doi-asserted-by":"crossref","first-page":"13382","DOI":"10.1074\/jbc.M111.314179","article-title":"Biochemical characterization and N-terminomics analysis of leukolysin, the membrane-type 6 matrix metalloprotease (MMP25)","volume":"287","author":"Starr","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0445","series-title":"Peptides 2012 (Proceedings of the Thirty-Second European Peptide Symposium)","first-page":"102","article-title":"Production and characterization of matrix metalloproteinases implicated in multiple sclerosis","author":"Amar","year":"2012"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0450","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/j.bbapap.2009.11.014","article-title":"MMP-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type I and type III","volume":"1804","author":"Taddese","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0455","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1006\/prep.2000.1376","article-title":"Cloning, expression, purification, and characterization of rat MMP-12","volume":"21","author":"Fu","year":"2001","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0460","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1242\/jcs.99.4.789","article-title":"Binding of latent and high Mr forms of stromelysin to collagen is mediated by the C-terminal domain","volume":"99","author":"Allan","year":"1991","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0465","doi-asserted-by":"crossref","first-page":"9612","DOI":"10.1016\/S0021-9258(19)50134-X","article-title":"The role of the C-terminal domain in collagenase and stromelysin specificity","volume":"267","author":"Murphy","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0470","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1038\/sj.emboj.7600318","article-title":"Collagenase unwinds triple helical collagen prior to peptide bond hydrolysis","volume":"23","author":"Chung","year":"2004","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0475","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1016\/j.str.2007.07.019","article-title":"Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9\/gelatinase B","volume":"15","author":"Rosenblum","year":"2007","journal-title":"Structure"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0480","doi-asserted-by":"crossref","first-page":"7011","DOI":"10.1021\/ja710491y","article-title":"Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12","volume":"130","author":"Bertini","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0485","doi-asserted-by":"crossref","first-page":"12821","DOI":"10.1074\/jbc.M809627200","article-title":"Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1)","volume":"284","author":"Bertini","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0490","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0011043","article-title":"Direct visualization of protease action on collagen triple helical structure","volume":"5","author":"Rosenblum","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0495","doi-asserted-by":"crossref","first-page":"27378","DOI":"10.1074\/jbc.M201367200","article-title":"Unexpected crucial role of residue 272 in substrate specificity of fibroblast collagenase","volume":"277","author":"Tsukada","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0500","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1007\/s00775-012-0886-z","article-title":"The collagenolytic action of MMP-1 is regulated by the interaction between the catalytic domain and the hinge region","volume":"17","author":"Fasciglione","year":"2012","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0505","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0043751","article-title":"Detection of the heterogeneous O-glycosylation profile of MT1-MMP expressed in cancer cells by a simple MALDI-MS method","volume":"7","author":"Shuo","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0510","doi-asserted-by":"crossref","first-page":"2569","DOI":"10.1073\/pnas.90.7.2569","article-title":"Structure-function relationship of human neutrophil collagenase: identification of regions responsible for substrate specificity and general proteinase activity","volume":"90","author":"Hirose","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0515","doi-asserted-by":"crossref","first-page":"29610","DOI":"10.1074\/jbc.M004039200","article-title":"Identification of the RWTNNFREY(183\u2013191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity","volume":"275","author":"Chung","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0520","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1074\/jbc.271.4.2126","article-title":"Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts","volume":"271","author":"Br\u00f6mme","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0525","doi-asserted-by":"crossref","first-page":"32347","DOI":"10.1074\/jbc.273.48.32347","article-title":"The collagenolytic acitivity of cathepsin K is unique among mammalian proteinases","volume":"273","author":"Garnero","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0530","doi-asserted-by":"crossref","first-page":"17474","DOI":"10.1073\/pnas.1414126111","article-title":"Structural basis of collagen fiber degradation by cathepsin K","volume":"111","author":"Aguda","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0535","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1042\/bj3310727","article-title":"Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix","volume":"331","author":"Kafienah","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0540","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1038\/370061a0","article-title":"A matrix metalloproteinase expressed on the surface of invasive tumour cells","volume":"370","author":"Sato","year":"1994","journal-title":"Nature"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0545","doi-asserted-by":"crossref","first-page":"5331","DOI":"10.1074\/jbc.270.10.5331","article-title":"Mechanism of cell surface activation of 72-kDa type IV collagenase","volume":"270","author":"Strongin","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0550","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1002\/(SICI)1521-1878(199911)21:11<940::AID-BIES6>3.0.CO;2-J","article-title":"Membrane associated matrix metalloproteinases in metastasis","volume":"21","author":"Ellerbroek","year":"1999","journal-title":"BioEssays"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0555","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1083\/jcb.153.5.893","article-title":"Membrane-type 1 matrix metallproteinase cleaves CD44 and promotes cell migration","volume":"153","author":"Kajita","year":"2001","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0560","doi-asserted-by":"crossref","first-page":"9749","DOI":"10.1074\/jbc.M110269200","article-title":"Processing of integrin alpha(v) subunit by membrane type 1 matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase","volume":"277","author":"Deryugina","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0565","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.bbapap.2004.08.001","article-title":"A proteomic approach to identify substrates of matrix metalloproteinase-14 in human plasma","volume":"1702","author":"Hwang","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0570","doi-asserted-by":"crossref","first-page":"6917","DOI":"10.1073\/pnas.0305862101","article-title":"Membrane protease proteomics: isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates","volume":"101","author":"Tam","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0575","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1093\/jb\/mvi009","article-title":"Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation","volume":"137","author":"Aoki","year":"2005","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0580","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1074\/jbc.M411824200","article-title":"Membrane-type matrix metalloproteinase-1 (MT1-MMP) is a processing enzyme for human laminin gamma 2 chain","volume":"280","author":"Koshikawa","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0585","doi-asserted-by":"crossref","first-page":"37576","DOI":"10.1074\/jbc.M606993200","article-title":"Membrane type 1 matrix metalloproteinase (MT1-MMP\/MMP-14) cleaves and releases a 22-kDa extracellular matrix metalloproteinase inducer (EMMPRIN) fragment from tumor cells","volume":"281","author":"Egawa","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0590","doi-asserted-by":"crossref","first-page":"1381","DOI":"10.1016\/j.yexcr.2006.01.008","article-title":"Membrane-type 1 matrix metalloproteinase modulates focal adhesion stability and cell migration","volume":"312","author":"Takino","year":"2006","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0595","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1080\/15216540600962818","article-title":"MT1-MMP: a key regulator of cell migration in tissue","volume":"58","author":"Itoh","year":"2006","journal-title":"IUBMB Life"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0600","doi-asserted-by":"crossref","first-page":"4896","DOI":"10.1128\/MCB.01775-07","article-title":"Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding","volume":"28","author":"Butler","year":"2008","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0605","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.bbamcr.2009.04.009","article-title":"Proteolytic and non-proteolytic roles of membrane type-1 matrix metalloproteinase in malignancy","volume":"1803","author":"Strongin","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0610","doi-asserted-by":"crossref","first-page":"3346","DOI":"10.4049\/jimmunol.0903789","article-title":"The membrane type matrix metalloproteinase MMP14 mediates constitutive shedding of MHC class I chain-related molecule A independent of A disintegrin and metalloproteinases","volume":"184","author":"Liu","year":"2010","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0615","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1021\/bi901994d","article-title":"Degradation of soluble and fibrillar amyloid beta-protein by matrix metalloproteinase (MT1-MMP) in vitro","volume":"49","author":"Liao","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0620","doi-asserted-by":"crossref","first-page":"416","DOI":"10.3390\/cancers6010416","article-title":"Monitoring and inhibiting MT1-MMP during cancer initiation and progression","volume":"6","author":"Pahwa","year":"2014","journal-title":"Cancer"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0625","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.phrs.2016.05.019","article-title":"The membrane tethered matrix metalloproteinase MT1-MMP at the forefront of melanoma cell invasion and metastasis","volume":"111","author":"Thakur","year":"2016","journal-title":"Pharmacol. Res."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0630","doi-asserted-by":"crossref","first-page":"147","DOI":"10.4161\/cc.6.2.3706","article-title":"Proteolysis-driven oncogenesis","volume":"6","author":"Golubkov","year":"2007","journal-title":"Cell Cycle"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0635","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.1016\/j.bbrc.2013.12.103","article-title":"Centrosomal BRCA2 is a target protein of membrane type-1 matrix metalloproteinase (MT1-MMP)","volume":"443","author":"Wali","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0640","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1083\/jcb.121.5.1165","article-title":"Fibronectin binding site in type I collagen regulates fibronectin fibril formation","volume":"121","author":"Dzamba","year":"1993","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0645","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1016\/0006-291X(92)91834-D","article-title":"Affinity of integrins for damaged extracellular matrix: alphavbeta3 binds to denatured collagen type I through RGD sites","volume":"182","author":"Davis","year":"1992","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0650","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1006\/bbrc.1993.1827","article-title":"Adhesion of mouse hepatocytes to type I collagen: role of supramolecular forms and effect of proteolytic degradation","volume":"194","author":"Berman","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0655","doi-asserted-by":"crossref","first-page":"8856","DOI":"10.1073\/pnas.91.19.8856","article-title":"Integrin alphavbeta3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen","volume":"91","author":"Montgomery","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0660","doi-asserted-by":"crossref","first-page":"10884","DOI":"10.1073\/pnas.1519676113","article-title":"Distinct biological events generated by ECM proteolysis by two homologous collagenases","volume":"113","author":"Solomonov","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0665","doi-asserted-by":"crossref","first-page":"4812","DOI":"10.1091\/mbc.e06-06-0486","article-title":"A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis","volume":"17","author":"Lee","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0670","doi-asserted-by":"crossref","first-page":"6309","DOI":"10.1128\/MCB.00291-07","article-title":"Complementary roles of intracellular and pericellular collagen degradation pathways in vivo","volume":"27","author":"Wagenaar-Miller","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0675","doi-asserted-by":"crossref","first-page":"27037","DOI":"10.1074\/jbc.M701088200","article-title":"Extracellular collagenases and the endocytic receptor, urokinase plasminogen activator receptor-associated protein\/Endo180, cooperate in fibroblast-mediated collagen degradation","volume":"282","author":"Madsen","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0680","doi-asserted-by":"crossref","first-page":"26996","DOI":"10.1074\/jbc.M110.208033","article-title":"The non-phagocytic route of collagen uptake: a distinct degradation pathway","volume":"286","author":"Madsen","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0685","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1042\/BST0350704","article-title":"Phagocytosis of collagen by fibroblasts and invasive cancer cells in mediated by MT1-MMP","volume":"35","author":"Lee","year":"2007","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0690","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0092-8674(00)80064-1","article-title":"MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover","volume":"99","author":"Holmbeck","year":"1999","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0695","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/nrm2125","article-title":"Matrix metalloproteinases and the regulation of tissue remodelling","volume":"8","author":"Page-McCaw","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0700","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.ajhg.2012.07.022","article-title":"Mutation of membrane type-1 metalloproteinase, MT1-MMP, causes the multicentric osteolysis and arthritis disease Winchester syndrome","volume":"91","author":"Evans","year":"2012","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0705","doi-asserted-by":"crossref","first-page":"5883","DOI":"10.1242\/dev.01461","article-title":"Altered endochondral bone development in matrix metalloproteinase 13-deficient mice","volume":"131","author":"Stickens","year":"2004","journal-title":"Development"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0710","first-page":"OC40","article-title":"Matrix metalloproteinase 13 (MMP13) mutation causes spondyloepimetaphyseal dysplasia (SEMD), Missouri variant","volume":"5","author":"Kennedy","year":"2003","journal-title":"Endocr. Abstr."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0715","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1002\/ajmg.a.30881","article-title":"Novel amino acid substitution in the Y-position of collagen type II causes spondyloepimetaphyseal dysplasia congenita","volume":"137A","author":"Sulko","year":"2005","journal-title":"Am. J. Med. Genet. A"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0720","doi-asserted-by":"crossref","first-page":"8580","DOI":"10.1021\/acs.jpcb.6b02573","article-title":"Identification of an electrostatic ruler motif for sequence-specific binding of collagenase to collagen","volume":"120","author":"Subramanian","year":"2016","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0725","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1016\/j.jmb.2005.07.019","article-title":"Guilty by association: some collagen II mutants alter the formation of ECM as a result of atypical interaction with fibronectin","volume":"352","author":"Ito","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0730","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.09345","article-title":"Matrix metalloproteinase 14 is required for fibrous tissue expansion","volume":"4","author":"Taylor","year":"2015","journal-title":"eLife"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0735","doi-asserted-by":"crossref","first-page":"5888","DOI":"10.1073\/pnas.87.15.5888","article-title":"Generation of collagenase-resistant collagen by site-directed mutagenesis of murine pro \u03b11(I) collagen gene","volume":"87","author":"Wu","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0740","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0934-8832(11)80001-6","article-title":"Susceptibility of type I collagen containing mutated \u03b11(I) chains to cleavage by human neutrophil collagenase","volume":"13","author":"Hasty","year":"1993","journal-title":"Matrix"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0745","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S0092-8674(03)00513-0","article-title":"Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix","volume":"114","author":"Hotary","year":"2003","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0750","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1083\/jcb.130.1.227","article-title":"A targeted mutation at the known collagenase cleavage site in mouse type I collagen impairs tissue remodeling","volume":"130","author":"Liu","year":"1995","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0755","doi-asserted-by":"crossref","first-page":"28509","DOI":"10.1074\/jbc.271.45.28509","article-title":"Different collagenase gene products have different roles in degradation of type I collagen","volume":"271","author":"Krane","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0760","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1006\/bbrc.1996.5924","article-title":"The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides","volume":"230","author":"Lemaitre","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0765","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1073\/pnas.032307099","article-title":"Type I collagen is thermally unstable at body temperature","volume":"99","author":"Leikina","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0770","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1172\/JCI10158","article-title":"Osteocyte and osteoblast apoptosis and excessive bone deposition accompany failure of collagenase cleavage of collagen","volume":"106","author":"Zhao","year":"2000","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0775","first-page":"5467","article-title":"Effect of tissue inhibitor of the matrix metalloproteinases-2 expression on the growth and spontaneous metastasis of a human melanoma cell line","volume":"54","author":"Montgomery","year":"1994","journal-title":"Cancer Res."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0780","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1172\/JCI5481","article-title":"Bone resorption induced by parathyroid hormone is strikingly diminished in collagenase-resistant mutant mice","volume":"103","author":"Zhao","year":"1999","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0785","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1096\/fj.02-0494fje","article-title":"Mutation in collagen-1 that confers resistance to the action of collagenase results in failure of recovery from CCl4-induced liver fibrosis, persistence of activated hepatic stellate cells, and diminished hepatocyte regeneration","volume":"17","author":"Issa","year":"2003","journal-title":"FASEB J."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0790","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1046\/j.1523-1747.2003.12019.x","article-title":"Severely impaired wound healing in the collagenase-resistant mouse","volume":"120","author":"Beare","year":"2003","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0795","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.1083\/jcb.137.6.1445","article-title":"The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix","volume":"137","author":"Pilcher","year":"1997","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0800","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.matbio.2015.03.002","article-title":"Matrix remodeling by MMPs during wound repair","volume":"44-46","author":"Rohani","year":"2015","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0805","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.bbamcr.2017.04.015_bb0810","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1126\/science.273.5279.1236","article-title":"Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency","volume":"273","author":"Gelb","year":"1996","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0815","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/BF02557674","article-title":"Phagocytosis of bone collagen by osteoclasts in two cases of pycnodysostosis","volume":"37","author":"Everts","year":"1985","journal-title":"Calcif. Tissue Int."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0820","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1007\/s00223-002-2092-4","article-title":"Cathepsin K deficiency in pycnodysostosis results in accumulation of non-digested phagocytosed collagen in fibroblasts","volume":"73","author":"Everts","year":"2003","journal-title":"Calcif. Tissue Int."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0825","doi-asserted-by":"crossref","first-page":"e89","DOI":"10.1016\/j.jaad.2010.11.033","article-title":"Morphea-like skin reactions in patients treated with the cathepsin K inhibitor balicatib","volume":"66","author":"R\u00fcnger","year":"2012","journal-title":"J. Am. Acad. Dermatol."},{"issue":"2","key":"10.1016\/j.bbamcr.2017.04.015_bb0830","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1038\/scientificamerican0292-54","article-title":"Cancer cell invasion and metastasis","volume":"266","author":"Liotta","year":"1992","journal-title":"Sci. Am."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0835","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1177\/10454411930040020401","article-title":"Matrix metalloproteinases: a review","volume":"4","author":"Birkedal-Hansen","year":"1993","journal-title":"Crit. Rev. Oral Biol. Med."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0840","series-title":"Zinc Metalloproteases In Health and Disease","first-page":"153","article-title":"Matrix metalloproteinases","author":"Nagase","year":"1996"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0845","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1093\/jnci\/89.17.1260","article-title":"Changing views of the role of matrix metalloproteinases in metastasis","volume":"89","author":"Chambers","year":"1997","journal-title":"J. Natl. Cancer Inst."},{"issue":"Suppl","key":"10.1016\/j.bbamcr.2017.04.015_bb0850","doi-asserted-by":"crossref","first-page":"S42","DOI":"10.1007\/s002800051097","article-title":"Matrix metalloproteinases and metastasis","volume":"43","author":"Kleiner","year":"1999","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0855","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1200\/JCO.2000.18.5.1135","article-title":"Matrix metalloproteinases: biologic activity and clinical implications","volume":"18","author":"Nelson","year":"2000","journal-title":"J. Clin. Oncol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0860","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/S0378-5173(83)90103-5","article-title":"A sensitive assay for collagenolytic activity using tritiated collagen","volume":"70","author":"Labrosse","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0865","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1146\/annurev.cellbio.24.110707.175315","article-title":"Navigating ECM barriers at the invasive front: the cancer cell-stroma interface","volume":"25","author":"Rowe","year":"2009","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0870","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.bbamcr.2009.04.011","article-title":"Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity","volume":"1803","author":"Gingras","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0875","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.semcdb.2007.06.008","article-title":"Membrane type 1-matrix metalloproteinase: substrate diversity in pericellular proteolysis","volume":"19","author":"Barbolina","year":"2008","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0880","doi-asserted-by":"crossref","first-page":"3274","DOI":"10.1038\/sj.onc.1210982","article-title":"MT1-MMP is required for efficient tumor dissemination in experimental metastatic disease","volume":"27","author":"Szabova","year":"2007","journal-title":"Oncogene"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0885","doi-asserted-by":"crossref","first-page":"33167","DOI":"10.1074\/jbc.M111.256644","article-title":"Inhibition of matrix metalloproteinase-14 (MMP-14)-mediated cancer cell migration","volume":"286","author":"Zarrabi","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0890","doi-asserted-by":"crossref","first-page":"4558","DOI":"10.1242\/jcs.050724","article-title":"MT1-MMP- and Cdc42-dependent signaling co-regulate cell invasion and tunnel formation in 3D collagen matrices","volume":"122","author":"Fisher","year":"2009","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0895","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1038\/ncb1616","article-title":"Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion","volume":"9","author":"Wolf","year":"2007","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0900","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1002\/jcb.10257","article-title":"MT1-MMP, but not secreted MMPs, influences the migration of human microvascular endothelial cells in 3-dimensional collagen gels","volume":"86","author":"Koike","year":"2002","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0905","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1186\/1471-2407-6-52","article-title":"Fibroblast-derived MT1-MMP promotes tumor progression in vitro and in vivo","volume":"6","author":"Zhang","year":"2006","journal-title":"BMC Cancer"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0910","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1083\/jcb.200408028","article-title":"Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP","volume":"167","author":"Sabeh","year":"2004","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0915","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1083\/jcb.200807195","article-title":"Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited","volume":"185","author":"Sabeh","year":"2009","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0920","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1016\/j.bbrc.2010.05.059","article-title":"MT1-MMP promotes cell growth and ERK activation through c-Src and paxillin in three-dimensional collagen matrix","volume":"396","author":"Takino","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0925","series-title":"The Tumor Microenvironment","first-page":"477","article-title":"Collagen in cancer","author":"Lauer","year":"2010"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0930","doi-asserted-by":"crossref","first-page":"24330","DOI":"10.1074\/jbc.M112.356303","article-title":"Matrix metalloproteinase-1a promotes tumorigenesis and metastasis","volume":"287","author":"Foley","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0935","doi-asserted-by":"crossref","first-page":"4366","DOI":"10.1158\/0008-5472.CAN-09-4057","article-title":"Carcinomas contain a matrix metalloproteinase-resistant isoform of type I collagen exerting selective support to invasion","volume":"70","author":"Makareeva","year":"2010","journal-title":"Cancer Res."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0940","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/S0174-173X(84)80036-9","article-title":"Action of mammalian collagenases on type-I trimer collagen","volume":"4","author":"Narayanan","year":"1984","journal-title":"Coll. Relat. Res."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0945","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/j.ccr.2009.11.013","article-title":"A stiff blow from the stroma: collagen crosslinking drives tumor progression","volume":"16","author":"Ng","year":"2009","journal-title":"Cancer Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0950","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1039\/c5ib00040h","article-title":"Human breast cancer invasion and aggression correlates with ECM stiffening and immune cell infiltration","volume":"7","author":"Acerbi","year":"2015","journal-title":"Integr. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0955","doi-asserted-by":"crossref","first-page":"1294","DOI":"10.1158\/1541-7786.MCR-11-0023","article-title":"MT1-MMP cooperates with Kras(G12D) to promote pancreatic fibrosis through increased TGF-\u03b2 signaling","volume":"9","author":"Krantz","year":"2011","journal-title":"Mol. Cancer Res."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0960","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1101\/gad.14.2.163","article-title":"Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-b and promotes tumor invasion and angiogenesis","volume":"14","author":"Yu","year":"2000","journal-title":"Genes Dev."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0965","doi-asserted-by":"crossref","first-page":"44061","DOI":"10.1074\/jbc.M207205200","article-title":"Matrix metalloproteinase-dependent activation of latent transforming growth factor-beta controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis","volume":"277","author":"Karsdal","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0970","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.cell.2010.03.015","article-title":"Matrix metalloproteinases: regulators of the tumor microenvironment","volume":"141","author":"Kessenbrock","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0975","doi-asserted-by":"crossref","first-page":"618","DOI":"10.2174\/1568009616666160216125634","article-title":"MT1-MMP activation of TGF-\u03b2\u00a0\u00ae signaling enables intercellular activation of an epithelial-mesenchymal transition program in cancer","volume":"16","author":"Nguyen","year":"2016","journal-title":"Curr. Cancer Drug Targets"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0980","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1016\/j.cell.2009.10.027","article-title":"Matrix crosslinking forces tumor progression by enhancing integrin signaling","volume":"139","author":"Levental","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0985","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/S0945-053X(00)00078-0","article-title":"Mechanisms involved in cartilage proteoglycan catabolism","volume":"19","author":"Caterson","year":"2000","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0990","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1006\/scdb.2000.0243","article-title":"Cartilage proteoglycans","volume":"12","author":"Knudson","year":"2001","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb0995","doi-asserted-by":"crossref","first-page":"45539","DOI":"10.1074\/jbc.M303737200","article-title":"Aggrecan protects cartilage collagen from proteolytic cleavage","volume":"278","author":"Pratta","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1000","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1042\/BJ20040424","article-title":"The ADAMTS metalloproteinases","volume":"386","author":"Porter","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1005","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1172\/JCI10564","article-title":"Postnatal expression in hyaline cartilage of constitutively active human collagenase-3 (MMP-13) induces osteoarthritis in mice","volume":"107","author":"Neuhold","year":"2001","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1010","doi-asserted-by":"crossref","first-page":"3081","DOI":"10.2741\/2034","article-title":"The role of collagenolytic matrix metalloproteinases in the loss of articular cartilage in osteoarthritis","volume":"11","author":"Smith","year":"2006","journal-title":"Front. Biosci."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1015","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1016\/S1063-4584(03)00170-5","article-title":"Impairment of the collagenase-3 endocytotic receptor system in cells from patients with osteoarthritis","volume":"11","author":"Walling","year":"2003","journal-title":"Osteoarthr. Cartil."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1020","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.matbio.2016.03.007","article-title":"MMP-13 is constitutively produced in human chondrocytes and co-endocytosed with ADAMTS-5 and TIMP-3 by the endocytic receptor LRP1","volume":"56","author":"Yamamoto","year":"2016","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1025","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.aott.2015.11.003","article-title":"Serum and knee synovial fluid matrix metalloproteinase-13 and tumor necrosis factor-alpha levels in patients with late-stage osteoarthritis","volume":"50","author":"\u00d6zler","year":"2016","journal-title":"Acta Orthop. Traumatol. Turc."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1030","doi-asserted-by":"crossref","first-page":"2008","DOI":"10.1002\/art.24629","article-title":"A new class of potent matrix metalloproteinase 13 inhibitors for potential treatment of osteoarthritis: evidence of histologic and clinical efficacy without musculoskeletal toxicity in rat models","volume":"60","author":"Baragi","year":"2009","journal-title":"Arthritis Rheum."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1035","doi-asserted-by":"crossref","first-page":"27781","DOI":"10.1074\/jbc.M703286200","article-title":"Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects","volume":"282","author":"Johnson","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1040","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1515\/hsz-2013-0134","article-title":"Cathepsin K: a unique collagenolytic cysteine peptidase","volume":"394","author":"Novinec","year":"2013","journal-title":"Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1045","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1185\/03007990802115796","article-title":"Osteoporosis management: impact of fracture type on cost and quality of life in patients at risk for fracture I","volume":"24","author":"Boonen","year":"2008","journal-title":"Curr. Med. Res. Opin."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1050","doi-asserted-by":"crossref","first-page":"825","DOI":"10.7150\/ijms.5180","article-title":"Immune regulation of osteoclast function in postmenopausal osteoporosis: a critical interdisciplinary perspective","volume":"9","author":"Zhao","year":"2012","journal-title":"Int. J. Med. Sci."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1055","first-page":"802","article-title":"Osteoimmunology: from mice to humans","volume":"5","author":"D'Amelio","year":"2016","journal-title":"BoneKey Rep."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1060","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.bone.2003.09.001","article-title":"Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia","volume":"34","author":"Nakamura","year":"2004","journal-title":"Bone"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1065","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1002\/(SICI)1097-4644(19980901)70:3<391::AID-JCB12>3.0.CO;2-O","article-title":"Intermittent administration of parathyroid hormone (1\u201334) stimulates matrix metalloproteinase-9 (MMP-9) expression in rat long bone","volume":"70","author":"McClelland","year":"1998","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1070","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1007\/s10735-004-6206-3","article-title":"Effects of 17 beta-estradiol on the expression of interstitial collagenases-8 and -13 (MMP-8 and MMP-13) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in ovariectomized rat osteoblastic cells","volume":"35","author":"Li","year":"2004","journal-title":"J. Mol. Histol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1075","doi-asserted-by":"crossref","first-page":"R63","DOI":"10.1186\/ar2434","article-title":"Cartilage degradation is fully reversible in the presence of aggrecanase but not matrix metalloproteinase activity","volume":"10","author":"Karsdal","year":"2008","journal-title":"Arthritis Res. Ther."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1080","doi-asserted-by":"crossref","first-page":"23291","DOI":"10.1074\/jbc.M115.644310","article-title":"Changes in structural-mechanical properties and degradability of collagen during aging-associated modifications","volume":"290","author":"Panwar","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1085","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1084\/jem.20050607","article-title":"MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells","volume":"202","author":"Filippov","year":"2005","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1090","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1159\/000446703","article-title":"Multidimensional contribution of matrix metalloproteinases to atherosclerotic plaque vulnerability: multiple mechanisms of inhibition to promote stability","volume":"53","author":"Ruddy","year":"2016","journal-title":"J. Vasc. Res."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1095","doi-asserted-by":"crossref","first-page":"1645","DOI":"10.1161\/CIRCULATIONAHA.109.912774","article-title":"Circulating biomarkers of collagen metabolism in cardiac diseases","volume":"121","author":"L\u00f3pez","year":"2010","journal-title":"Circulation"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1100","doi-asserted-by":"crossref","first-page":"H1656","DOI":"10.1152\/ajpheart.00141.2011","article-title":"Direct regulation of membrane type-1 matrix metalloproteinase following myocardial infarction causes changes in survival, cardiac function and remodeling","volume":"301","author":"Zavadzkas","year":"2011","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1105","doi-asserted-by":"crossref","first-page":"1863","DOI":"10.1016\/j.ajpath.2012.01.022","article-title":"MT1-MMP-dependent remodeling of cardiac extracellular matrix structure and function following myocardial infarction","volume":"180","author":"Koenig","year":"2012","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1110","doi-asserted-by":"crossref","first-page":"1364","DOI":"10.1016\/j.jacc.2015.07.035","article-title":"A novel collagen matricryptin reduces left ventricular dilation post-myocardial infarction by promoting scar formation and angiogenesis","volume":"66","author":"Lindsey","year":"2015","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1115","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.yjmcc.2016.10.005","article-title":"Early matrix metalloproteinase-9 inhibition post-myocardial infarction worsens cardiac dysfunction by delaying inflammation resolution","volume":"100","author":"Iyer","year":"2016","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1120","doi-asserted-by":"crossref","first-page":"L709","DOI":"10.1152\/ajplung.00418.2012","article-title":"Always cleave up your mess: targeting collagen degradation to treat tissue fibrosis","volume":"304","author":"McKleroy","year":"2013","journal-title":"Am. J. Physiol. Lung Cell. Mol. Physiol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1125","doi-asserted-by":"crossref","first-page":"3277","DOI":"10.1111\/j.1742-4658.2011.08244.x","article-title":"Matrix metalloproteinase proteolysis of the mycobacterial HSP65 protein as a potential source of immunogenic peptides in human tuberculosis","volume":"278","author":"Shiryaev","year":"2011","journal-title":"FEBS J."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1130","doi-asserted-by":"crossref","first-page":"882","DOI":"10.4049\/jimmunol.1403110","article-title":"Membrane type 1 matrix metalloproteinase regulates monocyte migration and collagen destruction in tuberculosis","volume":"195","author":"Sathyamoorthy","year":"2015","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1135","doi-asserted-by":"crossref","first-page":"1827","DOI":"10.1172\/JCI45666","article-title":"MMP-1 drives immunopathology in human tuberculosis and transgenic mice","volume":"121","author":"Elkington","year":"2011","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1140","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1038\/nri2432","article-title":"Two ways to survive infection: what resistance and tolerance can teach us about treating infectious diseases","volume":"8","author":"Schneider","year":"2008","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1145","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1126\/science.1214935","article-title":"Disease tolerance as a defense strategy","volume":"335","author":"Medzhitov","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1150","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/j.chom.2016.09.005","article-title":"Extracellular matrix proteolysis by MT1-MMP contributes to influenza-related tissue damage and mortality","volume":"20","author":"Talmi-Frank","year":"2016","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1155","doi-asserted-by":"crossref","first-page":"5987","DOI":"10.1038\/srep05987","article-title":"Introduction of correlative light and airSEM\u2122 microscopy imaging for tissue research under ambient conditions","volume":"4","author":"Solomonov","year":"2014","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1160","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.str.2014.10.012","article-title":"Inhibition mechanism of membrane metalloprotease by an exosite-swiveling conformational antibody","volume":"23","author":"Udi","year":"2015","journal-title":"Structure"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1165","series-title":"Guidebook to the Extracellular Matrix, Anchor, and Adhesion Proteins","first-page":"380","article-title":"Collagens: overview of the family","author":"Olsen","year":"1999"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1170","doi-asserted-by":"crossref","first-page":"4223","DOI":"10.1074\/jbc.M110709200","article-title":"Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen","volume":"277","author":"Di Lullo","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1175","doi-asserted-by":"crossref","first-page":"4273","DOI":"10.1073\/pnas.070050097","article-title":"Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine","volume":"97","author":"Beck","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1180","doi-asserted-by":"crossref","first-page":"1981","DOI":"10.1074\/jbc.M113.513408","article-title":"The role of collagen charge clusters in the regulation of matrix metalloproteinase activity","volume":"289","author":"Lauer","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1185","doi-asserted-by":"crossref","first-page":"616","DOI":"10.3109\/1354750X.2011.620628","article-title":"A novel marker for assessment of liver matrix remodeling: an enzyme-linked immunosorbent assay (ELISA) detecting a MMP generated type I collagen neo-epitope (C1M)","volume":"16","author":"Leeming","year":"2011","journal-title":"Biomarkers"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1190","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.ebiom.2015.04.017","article-title":"Matrix metalloproteinase mediated type I collagen degradation \u2014 an independent risk factor for mortality in women","volume":"2","author":"Dragsb\u00e6k","year":"2015","journal-title":"EBioMedicine"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1195","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1038\/nrd2308","article-title":"Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases","volume":"6","author":"Hu","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1200","doi-asserted-by":"crossref","first-page":"5662","DOI":"10.4049\/jimmunol.180.8.5662","article-title":"A novel proteolytic cascade generates an extracellular matrix-derived chemoattractant in chronic neutrophilic inflammation","volume":"180","author":"Gaggar","year":"2008","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1205","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.jneuroim.2009.09.020","article-title":"Neutrophils contain prolyl endopeptidase and generate the chemotactic peptide, PGP, from collagen","volume":"217","author":"O'Reilly","year":"2009","journal-title":"J. Neuroimmunol."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1210","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1038\/nm1361","article-title":"A novel peptide CXCR ligand derived from extracellular matrix degradation during airway inflammation","volume":"12","author":"Weathington","year":"2006","journal-title":"Nat. Med."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1215","doi-asserted-by":"crossref","first-page":"11534","DOI":"10.1016\/S0021-9258(18)33794-3","article-title":"The gelatinolytic activity of human skin fibroblast collagenase","volume":"257","author":"Welgus","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1220","doi-asserted-by":"crossref","first-page":"15411","DOI":"10.1021\/bi060849d","article-title":"Matrix metalloproteinase-1 takes advantage of the induced fit mechanism to cleave the triple-helical type I collagen molecule","volume":"45","author":"O'Farrell","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1225","doi-asserted-by":"crossref","first-page":"18657","DOI":"10.1074\/jbc.M000283200","article-title":"Cleavage of bovine collagen I by neutrophil collagenase MMP-8. Effect of pH on the catalytic properties as compared to synthetic substrates","volume":"275","author":"Marini","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1230","doi-asserted-by":"crossref","first-page":"9511","DOI":"10.1016\/S0021-9258(19)68792-2","article-title":"The collagen substrate specificity of human skin fibroblast collagenase","volume":"256","author":"Welgus","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2017.04.015_bb1235","doi-asserted-by":"crossref","first-page":"22988","DOI":"10.1074\/jbc.M112.348979","article-title":"Defining requirements for collagenase cleavage in collagen type III using a bacterial collagen system","volume":"287","author":"Yu","year":"2012","journal-title":"J. Biol. Chem."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S016748891730109X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S016748891730109X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,7,27]],"date-time":"2022-07-27T19:01:05Z","timestamp":1658948465000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S016748891730109X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,11]]},"references-count":247,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2017,11]]}},"alternative-id":["S016748891730109X"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamcr.2017.04.015","relation":{},"ISSN":["0167-4889"],"issn-type":[{"value":"0167-4889","type":"print"}],"subject":[],"published":{"date-parts":[[2017,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Matrix metalloproteinase collagenolysis in health and disease","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Cell Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamcr.2017.04.015","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier B.V.","name":"copyright","label":"Copyright"}]}}