{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T07:00:53Z","timestamp":1785135653294,"version":"3.55.0"},"reference-count":45,"publisher":"Informa UK Limited","issue":"1","license":[{"start":{"date-parts":[[2026,7,26]],"date-time":"2026-07-26T00:00:00Z","timestamp":1785024000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,7,26]],"date-time":"2026-07-26T00:00:00Z","timestamp":1785024000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/doi.org\/10.1080\/policies-text-data-mining"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["U2202213"],"award-info":[{"award-number":["U2202213"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.tandfonline.com"],"crossmark-restriction":true},"short-container-title":["Journal of Enzyme Inhibition and Medicinal Chemistry"],"published-print":{"date-parts":[[2026,12,31]]},"DOI":"10.1080\/14756366.2026.2704785","type":"journal-article","created":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T06:19:52Z","timestamp":1785133192000},"update-policy":"https:\/\/doi.org\/10.1080\/tandf_crossmark_01","source":"Crossref","is-referenced-by-count":0,"title":["Exploration of tropocollagen unwinding by cathepsin K dimer with chondroitin 4-sulphate through microsecond timescale molecular dynamics"],"prefix":"10.1080","volume":"41","author":[{"given":"Mengyi","family":"Shan","sequence":"first","affiliation":[{"name":"School of Pharmaceutical Sciences, The First Affiliated Hospital of Zhejiang Chinese Medical University","place":["Hangzhou, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yue","family":"Wu","sequence":"additional","affiliation":[{"name":"School of Pharmaceutical Sciences, The First Affiliated Hospital of Zhejiang Chinese Medical University","place":["Hangzhou, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chen","family":"Jiang","sequence":"additional","affiliation":[{"name":"School of Pharmaceutical Sciences, The First Affiliated Hospital of Zhejiang Chinese Medical University","place":["Hangzhou, China"]},{"name":"QuanMin RenZheng (HangZhou) Technology Co., Ltd","place":["Hangzhou, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Chen","sequence":"additional","affiliation":[{"name":"School of Pharmaceutical Sciences, The First Affiliated Hospital of Zhejiang Chinese Medical University","place":["Hangzhou, China"]},{"name":"College of Pharmaceutical Sciences, Zhejiang University","place":["Hangzhou, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gang","family":"Cheng","sequence":"additional","affiliation":[{"name":"School of Pharmaceutical Sciences, The First Affiliated Hospital of Zhejiang Chinese Medical University","place":["Hangzhou, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lu-Ping","family":"Qin","sequence":"additional","affiliation":[{"name":"School of Pharmaceutical Sciences, The First Affiliated Hospital of Zhejiang Chinese Medical University","place":["Hangzhou, China"]},{"name":"Zhejiang Key Laboratory of Chinese Medicine Modernization, Zhejiang Chinese Medical University","place":["Hangzhou, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"301","published-online":{"date-parts":[[2026,7,26]]},"reference":[{"key":"e_1_3_3_2_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/20.17.4629"},{"key":"e_1_3_3_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.21.12517"},{"key":"e_1_3_3_4_1","doi-asserted-by":"publisher","DOI":"10.1110\/ps.8.2.283"},{"issue":"3","key":"e_1_3_3_5_1","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1021\/bi9822271","article-title":"The crystal structure of human procathepsin K","volume":"38","author":"LaLonde JM","year":"1999","unstructured":"LaLonde JM, Zhao B, Janson CA, D\u2019Alessio KJ, McQueney MS, Orsini MJ, Debouck CM, Smith WW. The crystal structure of human procathepsin K. Biochem J. 1999;38(3):862\u2013869.","journal-title":"Biochem J"},{"key":"e_1_3_3_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2008.07.038"},{"key":"e_1_3_3_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.jmedchem.9b00683"},{"key":"e_1_3_3_8_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0710588105"},{"key":"e_1_3_3_9_1","doi-asserted-by":"publisher","DOI":"10.1006\/jsbi.1998.3977"},{"issue":"3","key":"e_1_3_3_10_1","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 W","year":"1998","unstructured":"Kafienah W, Br\u00f6mme D, Buttle DJ, Croucher LJ, Hollander AP. Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem J. 1998;331 (Pt 3)(Pt 3)Pt 3), :727\u2013732.","journal-title":"Biochem J"},{"issue":"32","key":"e_1_3_3_11_1","doi-asserted-by":"crossref","first-page":"28669","DOI":"10.1074\/jbc.M204004200","article-title":"Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate","volume":"277","author":"Li Z","year":"2002","unstructured":"Li Z, Hou WS, Escalante-Torres CR, Gelb BD, Bromme D. Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J Biol Chem. 2002;277(32):28669\u201328676.","journal-title":"J Biol Chem"},{"key":"e_1_3_3_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.mattod.2014.01.019"},{"key":"e_1_3_3_13_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1414126111"},{"issue":"48","key":"e_1_3_3_14_1","doi-asserted-by":"crossref","first-page":"34871","DOI":"10.1074\/jbc.M113.510008","article-title":"Elastin degradation by cathepsin V requires two exosites","volume":"288","author":"Du X","year":"2013","unstructured":"Du X, Chen NL, Wong A, Craik CS, Br\u00f6mme D. Elastin degradation by cathepsin V requires two exosites. J Biol Chem. 2013;288(48):34871\u201334881.","journal-title":"J Biol Chem"},{"key":"e_1_3_3_15_1","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20140809"},{"key":"e_1_3_3_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biochi.2007.08.011"},{"key":"e_1_3_3_17_1","doi-asserted-by":"publisher","DOI":"10.1080\/13543776.2022.2040480"},{"issue":"3","key":"e_1_3_3_18_1","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 TM","year":"2012","unstructured":"R\u00fcnger TM, Adami S, Benhamou C-L, Czerwi\u0144ski E, Farrerons J, Kendler DL, Mindeholm L, Realdi G, Roux C, Smith V. Morphea-like skin reactions in patients treated with the cathepsin K inhibitor balicatib. J Am Acad Dermatol. 2012;66(3):e89\u2013e96.","journal-title":"J Am Acad Dermatol"},{"key":"e_1_3_3_19_1","doi-asserted-by":"publisher","DOI":"10.1111\/bcp.13869"},{"key":"e_1_3_3_20_1","doi-asserted-by":"publisher","DOI":"10.2210\/pdb3ah9\/pdb"},{"key":"e_1_3_3_21_1","doi-asserted-by":"publisher","DOI":"10.2210\/pdb7CWK\/pdb"},{"key":"e_1_3_3_22_1","doi-asserted-by":"publisher","DOI":"10.2210\/pdb3C9E\/pdb"},{"key":"e_1_3_3_23_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4939-7000-1_26"},{"key":"e_1_3_3_24_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.21.13955"},{"key":"e_1_3_3_25_1","doi-asserted-by":"publisher","DOI":"10.1109\/SC.2006.54"},{"key":"e_1_3_3_26_1","doi-asserted-by":"publisher","DOI":"10.1063\/1.445869"},{"key":"e_1_3_3_27_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.jctc.1c00302"},{"key":"e_1_3_3_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmgm.2009.01.006"},{"key":"e_1_3_3_29_1","doi-asserted-by":"publisher","DOI":"10.1007\/s11030-023-10608-8"},{"key":"e_1_3_3_30_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcc.20291"},{"issue":"12","key":"e_1_3_3_31_1","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1038\/s41589-024-01670-w","article-title":"Engineering miniature IscB nickase for robust base editing with broad targeting range","volume":"20","author":"Han L","year":"2024","unstructured":"Han L, Hu Y, Mo Q, Yang H, Gu F, Bai F, Sun Y, Ma H. Engineering miniature IscB nickase for robust base editing with broad targeting range. Nat Chem Biol. 2024;20(12):1629\u20131639.","journal-title":"Nat Chem Biol"},{"key":"e_1_3_3_32_1","doi-asserted-by":"publisher","DOI":"10.1111\/febs.13499"},{"issue":"2","key":"e_1_3_3_33_1","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1016\/0003-9861(73)90539-0","article-title":"Hydroxyproline content determines the denaturation temperature of chick tendon collagen","volume":"158","author":"Rosenbloom J","year":"1973","unstructured":"Rosenbloom J, Harsch M, Jimenez S. Hydroxyproline content determines the denaturation temperature of chick tendon collagen. Arch Biochem Biophys. 1973;158(2):478\u2013484.","journal-title":"Arch Biochem Biophys"},{"key":"e_1_3_3_34_1","doi-asserted-by":"crossref","first-page":"126325","DOI":"10.1016\/j.molliq.2024.126325","article-title":"Investigating the effect of water on collagen triple helix stability","volume":"415","author":"Balupuri A","year":"2024","unstructured":"Balupuri A, Son D-H, Sook Kang N. Investigating the effect of water on collagen triple helix stability. J Mol Liq. 2024;415:126325.","journal-title":"J Mol Liq"},{"issue":"23","key":"e_1_3_3_35_1","doi-asserted-by":"crossref","first-page":"4901","DOI":"10.1021\/acs.jpcb.9b03078","article-title":"Structure and Dynamics of Collagen Hydration Water from Molecular Dynamics Simulations: Implications of Temperature and Pressure","volume":"123","author":"Madhavi WAM","year":"2019","unstructured":"Madhavi WAM, Weerasinghe S, Fullerton GD, Momot KI. Structure and Dynamics of Collagen Hydration Water from Molecular Dynamics Simulations: Implications of Temperature and Pressure. J Phys Chem B. 2019;123(23):4901\u20134914.","journal-title":"J Phys Chem B"},{"issue":"15","key":"e_1_3_3_36_1","doi-asserted-by":"crossref","first-page":"5937","DOI":"10.1021\/jacs.1c01512","article-title":"Influence of lipidation on the folding and stability of collagen triple helices\u2014an experimental and theoretical study","volume":"143","author":"Egli J","year":"2021","unstructured":"Egli J, Esposito C, M\u00fcri M, Riniker S, Wennemers H. Influence of lipidation on the folding and stability of collagen triple helices\u2014an experimental and theoretical study. J Am Chem Soc. 2021;143(15):5937\u20135942.","journal-title":"J Am Chem Soc"},{"issue":"36","key":"e_1_3_3_37_1","doi-asserted-by":"crossref","first-page":"7754","DOI":"10.1021\/acs.jpcb.9b05006","article-title":"Unraveling the Role of Hydroxyproline in Maintaining the Thermal Stability of the Collagen Triple Helix Structure Using Simulation","volume":"123","author":"Xu S","year":"2019","unstructured":"Xu S, Gu M, Wu K, Li G. Unraveling the Role of Hydroxyproline in Maintaining the Thermal Stability of the Collagen Triple Helix Structure Using Simulation. J Phys Chem B. 2019;123(36):7754\u20137763.","journal-title":"J Phys Chem B"},{"issue":"42","key":"e_1_3_3_38_1","doi-asserted-by":"crossref","first-page":"12567","DOI":"10.1039\/D2SC03666E","article-title":"Terminal repeats impact collagen triple-helix stability through hydrogen bonding","volume":"13","author":"Qi Y","year":"2022","unstructured":"Qi Y, Zhou D, Kessler JL, Qiu R, Yu SM, Li G, Qin Z, Li Y. Terminal repeats impact collagen triple-helix stability through hydrogen bonding. Chem Sci. 2022;13(42):12567\u201312576.","journal-title":"Chem Sci"},{"key":"e_1_3_3_39_1","doi-asserted-by":"publisher","DOI":"10.1517\/13543780902832661"},{"key":"e_1_3_3_40_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.phymed.2025.156720"},{"key":"e_1_3_3_41_1","doi-asserted-by":"publisher","DOI":"10.1111\/bph.14133"},{"issue":"11","key":"e_1_3_3_42_1","doi-asserted-by":"crossref","first-page":"8988","DOI":"10.1074\/jbc.M110.126706","article-title":"Structure-Activity Analysis of Cathepsin K\/Chondroitin 4-Sulfate Interactions","volume":"286","author":"Cherney MM","year":"2011","unstructured":"Cherney MM, Lecaille F, Kienitz M, Nallaseth FS, Li Z, James MNG, Br\u00f6mme D. Structure-Activity Analysis of Cathepsin K\/Chondroitin 4-Sulfate Interactions. J Biol Chem. 2011;286(11):8988\u20138998.","journal-title":"J Biol Chem"},{"key":"e_1_3_3_43_1","doi-asserted-by":"publisher","DOI":"10.1002\/anie.200802019"},{"key":"e_1_3_3_44_1","doi-asserted-by":"publisher","DOI":"10.1021\/jp709896w"},{"issue":"4","key":"e_1_3_3_45_1","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/0022-2836(91)90528-E","article-title":"Suggestions for \u201csafe\u201d residue substitutions in site-directed mutagenesis","volume":"217","author":"Bordo D","year":"1991","unstructured":"Bordo D, Argos P. Suggestions for \u201csafe\u201d residue substitutions in site-directed mutagenesis. J Mol Biol. 1991;217(4):721\u2013729.","journal-title":"J Mol Biol"},{"issue":"1","key":"e_1_3_3_46_1","doi-asserted-by":"crossref","first-page":"2529","DOI":"10.1038\/s41467-022-30338-z","article-title":"Identification of oleoylethanolamide as an endogenous ligand for HIF-3\u03b1","volume":"13","author":"Diao X","year":"2022","unstructured":"Diao X, Ye F, Zhang M, Ren X, Tian X, Lu J, Sun X, Hou Z, Chen X, Li F, et al. Identification of oleoylethanolamide as an endogenous ligand for HIF-3\u03b1. Nat Commun. 2022;13(1):2529.","journal-title":"Nat Commun"}],"container-title":["Journal of Enzyme Inhibition and Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.tandfonline.com\/doi\/pdf\/10.1080\/14756366.2026.2704785","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.tandfonline.com\/doi\/full-xml\/10.1080\/14756366.2026.2704785","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.tandfonline.com\/doi\/pdf\/10.1080\/14756366.2026.2704785","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T06:19:55Z","timestamp":1785133195000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.tandfonline.com\/doi\/full\/10.1080\/14756366.2026.2704785"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,26]]},"references-count":45,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2026,12,31]]}},"alternative-id":["10.1080\/14756366.2026.2704785"],"URL":"https:\/\/doi.org\/10.1080\/14756366.2026.2704785","relation":{},"ISSN":["1475-6366","1475-6374"],"issn-type":[{"value":"1475-6366","type":"print"},{"value":"1475-6374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,26]]},"assertion":[{"value":"The publishing and review policy for this title is described in its Aims & Scope.","order":1,"name":"peerreview_statement","label":"Peer Review Statement"},{"value":"http:\/\/www.tandfonline.com\/action\/journalInformation?show=aimsScope&journalCode=ienz20","URL":"http:\/\/www.tandfonline.com\/action\/journalInformation?show=aimsScope&journalCode=ienz20","order":2,"name":"aims_and_scope_url","label":"Aim & Scope"},{"value":"2026-05-07","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-06-18","order":1,"name":"revised","label":"Revised","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-07-10","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-07-26","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"2704785"}}