{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T05:28:48Z","timestamp":1791264528093,"version":"4.1.0"},"reference-count":39,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bone"],"published-print":{"date-parts":[[2009,2]]},"DOI":"10.1016\/j.bone.2008.08.130","type":"journal-article","created":{"date-parts":[[2008,9,20]],"date-time":"2008-09-20T04:59:44Z","timestamp":1221886784000},"page":"199-207","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":135,"title":["Bone density, strength, and formation in adult cathepsin K (\u2212\/\u2212) mice"],"prefix":"10.1016","volume":"44","author":[{"given":"B.","family":"Pennypacker","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M.","family":"Shea","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Q.","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P.","family":"Masarachia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P.","family":"Saftig","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Rodan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G.","family":"Rodan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D.","family":"Kimmel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bone.2008.08.130_bib1","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/S0167-4838(99)00263-0","article-title":"Lysosomal cysteine proteases: more than scavengers","volume":"1477","author":"Turk","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bone.2008.08.130_bib2","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":"Bromme","year":"1996","journal-title":"J. Biol. Chem"},{"key":"10.1016\/j.bone.2008.08.130_bib3","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1358\/dnp.2004.17.1.829022","article-title":"The role of cathepsin K in normal bone resorption","volume":"17","author":"Troen","year":"2004","journal-title":"Drug News Perspect."},{"key":"10.1016\/j.bone.2008.08.130_bib4","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1515\/bchm3.1995.376.6.379","article-title":"Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution","volume":"376","author":"Bromme","year":"1995","journal-title":"Biol. Chem. Hoppe-Seyler"},{"key":"10.1016\/j.bone.2008.08.130_bib5","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/0006-291X(84)90560-6","article-title":"In vivo and in vitro evidence for the involvement of cysteine proteases in bone resorption","volume":"125","author":"Delaisse","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bone.2008.08.130_bib6","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1359\/jbmr.1998.13.9.1420","article-title":"Cysteine proteases and matrix metalloproteinases play distinct roles in the subosteoclastic resorption zone","volume":"13","author":"Everts","year":"1998","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib7","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1002\/jcb.240560116","article-title":"Inhibition of bone resorption by selective inactivators of cysteine proteinases","volume":"56","author":"Hill","year":"1994","journal-title":"J. Cell Biochem."},{"key":"10.1016\/j.bone.2008.08.130_bib8","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/0006-291X(91)91796-F","article-title":"Selective inhibition of cysteine proteinases by Z-Phe-AlaCH2D suppress digestion of collagen by fibroblasts and osteoclasts","volume":"178","author":"Van Noorden","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bone.2008.08.130_bib9","doi-asserted-by":"crossref","first-page":"12511","DOI":"10.1074\/jbc.271.21.12511","article-title":"Cathepsin K, but cathepsins B, L, or S, is abundantly expressed in human osteoclasts","volume":"271","author":"Drake","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bone.2008.08.130_bib10","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.1359\/jbmr.1997.12.9.1396","article-title":"Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo","volume":"12","author":"Votta","year":"1997","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib11","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.bone.2008.08.130_bib12","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1101\/gr.6.11.1050","article-title":"A nonsense mutation in the cathepsin K gene observed in a family with pycnodysostosis","volume":"6","author":"Johnson","year":"1996","journal-title":"Genome. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib13","doi-asserted-by":"crossref","first-page":"1649","DOI":"10.1359\/jbmr.1999.14.10.1649","article-title":"Mutations of CTSK result in pycnodysostosis via a reduction in cathepsin K protein","volume":"14","author":"Ho","year":"1999","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib14","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.bone.2008.08.130_bib15","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.bone.2008.08.130_bib16","doi-asserted-by":"crossref","first-page":"13453","DOI":"10.1073\/pnas.95.23.13453","article-title":"Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin K deficient mice","volume":"95","author":"Saftig","year":"1998","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bone.2008.08.130_bib17","doi-asserted-by":"crossref","first-page":"1654","DOI":"10.1359\/jbmr.1999.14.10.1654","article-title":"Cathepsin, K knockout mice develop osteopetrosis due to a deficit in matrix degradation but not demineralization","volume":"14","author":"Gowen","year":"1999","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib18","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.bone.2004.09.020","article-title":"Impaired bone resorption in cathepsin K-deficient mice is partially compensated for by enhanced osteoclastogenesis and increased expression of other proteases via an increased RANKL\/OPG ratio","volume":"36","author":"Kiviranta","year":"2005","journal-title":"Bone"},{"issue":"6","key":"10.1016\/j.bone.2008.08.130_bib19","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1359\/jbmr.060313","article-title":"Mice lacking cathepsin K maintain bone remodeling but develop bone fragility despite high bone mass","volume":"21","author":"Li","year":"2006","journal-title":"J. Bone Miner. Res."},{"issue":"4","key":"10.1016\/j.bone.2008.08.130_bib20","doi-asserted-by":"crossref","first-page":"1538","DOI":"10.1210\/jc.2003-031055","article-title":"Decrease bone turnover and deterioration of bone structure in two cases of pycnodysostosis","volume":"89","author":"Fratzl-Zelman","year":"2004","journal-title":"J. Clin. Endocrinol. Metab."},{"issue":"S1","key":"10.1016\/j.bone.2008.08.130_bib21","first-page":"S378","article-title":"Knockout of Cathepsin K in adult mice does not result in bone fragility","volume":"22","author":"Hoffman","year":"2007","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib22","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1002\/jbmr.5650020617","article-title":"Bone histomorphometry: standardization of nomenclature, symbols, and units","volume":"2","author":"Parfitt","year":"1987","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib23","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/8756-3282(93)90081-K","article-title":"Basic biomechanical measurements of bone: a tutorial","volume":"14","author":"Turner","year":"1993","journal-title":"Bone"},{"key":"10.1016\/j.bone.2008.08.130_bib24","series-title":"W.G. Statistical Methods","author":"Snedecor","year":"1989"},{"key":"10.1016\/j.bone.2008.08.130_bib25","series-title":"SAS\/STAT User's Guide","first-page":"1467","year":"1999"},{"key":"10.1016\/j.bone.2008.08.130_bib26","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1016\/S0021-9258(17)42227-7","article-title":"Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts","volume":"269","author":"Tezuka","year":"1994","journal-title":"J. Biol. Chem"},{"key":"10.1016\/j.bone.2008.08.130_bib27","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1006\/bbrc.1995.1013","article-title":"Molecular cloning of human cDNA for cathepsin K: novel cysteine protease predominantly expressed in bone","volume":"206","author":"Inaoka","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bone.2008.08.130_bib28","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/0014-5793(96)00907-6","article-title":"Mouse cathepsin K: cDNA cloning and predominant expression of the gene in osteoclasts, and in some hypertrophying chondrocytes during mouse development","volume":"393","author":"Rantakokko","year":"1996","journal-title":"FEBS Lett."},{"issue":"2","key":"10.1016\/j.bone.2008.08.130_bib29","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S8756-3282(99)00160-X","article-title":"Cloning and expression of rhesus monkey cathepsin K","volume":"25","author":"Guay","year":"1999","journal-title":"Bone"},{"key":"10.1016\/j.bone.2008.08.130_bib30","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/S8756-3282(98)00138-0","article-title":"Study of immunoelectronmicroscopic localization of cathepsin K in osteoclasts and other bone cells in the mouse femur","volume":"23","author":"Yamaza","year":"1998","journal-title":"Bone"},{"issue":"5","key":"10.1016\/j.bone.2008.08.130_bib31","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/S8756-3282(02)00675-0","article-title":"A potent small molecule, nonpeptide inhibitor of cathepsin K (SB 331750) prevents bone matrix resorption in the ovariectomized rat","volume":"30","author":"Lark","year":"2002","journal-title":"Bone"},{"issue":"10","key":"10.1016\/j.bone.2008.08.130_bib32","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1359\/jbmr.2001.16.10.1739","article-title":"Potent and selective inhibition of human cathepsin K leads to inhibition of bone resorption in vivo in a nonhuman primate","volume":"16","author":"Stroup","year":"2001","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib33","doi-asserted-by":"crossref","first-page":"1985","DOI":"10.1016\/j.bmcl.2005.12.071","article-title":"Identification of a potent and selective non-basic cathepsin K inhibitor","volume":"16","author":"Li","year":"2006","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bone.2008.08.130_bib34","doi-asserted-by":"crossref","first-page":"407","DOI":"10.2174\/1566524023362401","article-title":"Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease","volume":"2","author":"Motyckova","year":"2002","journal-title":"Curr. Mol. Med."},{"issue":"Suppl. 1","key":"10.1016\/j.bone.2008.08.130_bib35","first-page":"S46","article-title":"AAE581, a novel cathepsin K inhibitor, protects against ovariectomy-induced bone loss in non-human primates, in part by stimulation of periosteal bone formation","volume":"20","author":"Jerome","year":"2005","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2008.08.130_bib36","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/j.bone.2007.01.010","article-title":"Changes in micro-CT 3D bone parameters reflect effects of a potent cathepsin K inhibitor (SB-553484) on bone resorption and cortical bone formation in ovariectomized mice","volume":"40","author":"Xiang","year":"2007","journal-title":"Bone"},{"issue":"4","key":"10.1016\/j.bone.2008.08.130_bib37","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1159\/000144767","article-title":"Age-related changes in cellular population of growth plate of normal mouse","volume":"97","author":"Silbermann","year":"1977","journal-title":"Acta. Anat."},{"key":"10.1016\/j.bone.2008.08.130_bib38","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1002\/(SICI)1097-0185(199609)246:1<39::AID-AR5>3.0.CO;2-A","article-title":"Trabecular and endocortical bone surfaces in the rat: modeling or remodeling?","volume":"245","author":"Erben","year":"1996","journal-title":"Anat. Rec."},{"key":"10.1016\/j.bone.2008.08.130_bib39","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/8756-3282(89)90142-7","article-title":"Structural and histomorphometric studies of iliac crest trabecular and cortical bone in autosomal dominant osteopetrosis: a study of two radiological types","volume":"10","author":"Bollerslev","year":"1989","journal-title":"Bone"}],"container-title":["Bone"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S8756328208007667?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S8756328208007667?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,11]],"date-time":"2025-09-11T17:34:51Z","timestamp":1757612091000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S8756328208007667"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,2]]},"references-count":39,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2009,2]]}},"alternative-id":["S8756328208007667"],"URL":"https:\/\/doi.org\/10.1016\/j.bone.2008.08.130","relation":{},"ISSN":["8756-3282"],"issn-type":[{"value":"8756-3282","type":"print"}],"subject":[],"published":{"date-parts":[[2009,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Bone density, strength, and formation in adult cathepsin K (\u2212\/\u2212) mice","name":"articletitle","label":"Article Title"},{"value":"Bone","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bone.2008.08.130","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2008 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}