{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,31]],"date-time":"2026-10-31T12:44:48Z","timestamp":1793450688107,"version":"4.5.0"},"reference-count":0,"publisher":"Walter de Gruyter GmbH","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biological Chemistry"],"published-print":{"date-parts":[[2013,9,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Cathepsin K has emerged as a promising target for the treatment of osteoporosis in recent years. Initially identified as a papain-like cysteine peptidase expressed in high levels in osteoclasts, the important role of this enzyme in bone metabolism was highlighted by the finding that mutations in the\n                    <jats:italic>CTSK<\/jats:italic>\n                    gene cause the rare recessive disorder pycnodysostosis, which is characterized by severe bone anomalies. At the molecular level, the physiological role of cathepsin K is reflected by its unique cleavage pattern of type I collagen molecules, which is fundamentally different from that of other endogenous collagenases. Several cathepsin K inhibitors have been developed to reduce the excessive bone matrix degradation associated with osteoporosis, with the frontrunner odanacatib about to successfully conclude Phase 3 clinical trials. Apart from osteoclasts, cathepsin K is expressed in different cell types throughout the body and is involved in processes of adipogenesis, thyroxine liberation and peptide hormone regulation. Elevated activity of cathepsin K has been associated with arthritis, atherosclerosis, obesity, schizophrenia, and tumor metastasis. Accordingly, its activity is tightly regulated\n                    <jats:italic>via<\/jats:italic>\n                    multiple mechanisms, including competitive inhibition by endogenous macromolecular inhibitors and allosteric regulation by glycosaminoglycans. This review provides a state-of-the-art description of the activity of cathepsin K at the molecular level, its biological functions and the mechanisms involved in its regulation.\n                  <\/jats:p>","DOI":"10.1515\/hsz-2013-0134","type":"journal-article","created":{"date-parts":[[2013,8,1]],"date-time":"2013-08-01T16:10:58Z","timestamp":1375373458000},"page":"1163-1179","source":"Crossref","is-referenced-by-count":125,"title":["Cathepsin K: a unique collagenolytic cysteine peptidase"],"prefix":"10.1515","volume":"394","author":[{"given":"Marko","family":"Novinec","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, SI-1000 Ljubljana, Slovenia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brigita","family":"Lenar\u010di\u010d","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","published-online":{"date-parts":[[2013,4,27]]},"container-title":["bchm"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.degruyter.com\/view\/j\/bchm.2013.394.issue-9\/hsz-2013-0134\/hsz-2013-0134.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/hsz-2013-0134\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/hsz-2013-0134\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,14]],"date-time":"2022-03-14T11:21:05Z","timestamp":1647256865000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/hsz-2013-0134\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,4,27]]},"references-count":0,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2013,6,4]]},"published-print":{"date-parts":[[2013,9,1]]}},"alternative-id":["10.1515\/hsz-2013-0134"],"URL":"https:\/\/doi.org\/10.1515\/hsz-2013-0134","relation":{},"ISSN":["1437-4315","1431-6730"],"issn-type":[{"value":"1437-4315","type":"electronic"},{"value":"1431-6730","type":"print"}],"subject":[],"published":{"date-parts":[[2013,4,27]]}}}