{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,9]],"date-time":"2026-06-09T05:13:22Z","timestamp":1780982002323,"version":"3.54.1"},"reference-count":56,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,4,23]],"date-time":"2024-04-23T00:00:00Z","timestamp":1713830400000},"content-version":"am","delay-in-days":358,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["G1781"],"award-info":[{"award-number":["G1781"]}],"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":["R01 EY010101"],"award-info":[{"award-number":["R01 EY010101"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic & Medicinal Chemistry"],"published-print":{"date-parts":[[2023,5]]},"DOI":"10.1016\/j.bmc.2023.117289","type":"journal-article","created":{"date-parts":[[2023,4,17]],"date-time":"2023-04-17T20:48:01Z","timestamp":1681764481000},"page":"117289","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Identification of small molecule inhibitors against MMP-14 via High-Throughput screening"],"prefix":"10.1016","volume":"85","author":[{"given":"Hyun","family":"Lee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8851-0720","authenticated-orcid":false,"given":"Isoo","family":"Youn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robel","family":"Demissie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tasneem M.","family":"Vaid","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chun-Tao","family":"Che","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dimitri T.","family":"Azar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2561-8187","authenticated-orcid":false,"given":"Kyu-Yeon","family":"Han","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bmc.2023.117289_b0005","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1038\/nrd2092","article-title":"Targeting proteases: successes, failures and future prospects","volume":"5","author":"Turk","year":"2006","journal-title":"Nature Reviews. Drug Discovery"},{"key":"10.1016\/j.bmc.2023.117289_b0010","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1183\/09031936.00146510","article-title":"Biological role of matrix metalloproteinases: a critical balance","volume":"38","author":"L\u00f6ffek","year":"2011","journal-title":"The European Respiratory Journal"},{"key":"10.1016\/j.bmc.2023.117289_b0015","doi-asserted-by":"crossref","first-page":"177","DOI":"10.3109\/14756366.2016.1161620","article-title":"Matrix metalloproteinases (MMPs), the main extracellular matrix (ECM) enzymes in collagen degradation, as a target for anticancer drugs","volume":"31","author":"Jab\u0142o\u0144ska-Trypu\u0107","year":"2016","journal-title":"Journal of Enzyme Inhibition and Medicinal Chemistry"},{"key":"10.1016\/j.bmc.2023.117289_b0020","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.cardiores.2005.12.002","article-title":"Structure and function of matrix metalloproteinases and TIMPs","volume":"69","author":"Nagase","year":"2006","journal-title":"Cardiovascular Research"},{"key":"10.1016\/j.bmc.2023.117289_b0025","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1023\/B:JCAM.0000005765.13637.38","article-title":"Modeling of enzyme-substrate complexes for the metalloproteases MMP-3, ADAM-9 and ADAM-10","volume":"17","author":"Manzetti","year":"2003","journal-title":"Journal of Computer-Aided Molecular Design"},{"key":"10.1016\/j.bmc.2023.117289_b0030","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1007\/s00726-010-0689-x","article-title":"Physiology and pathophysiology of matrix metalloproteases","volume":"41","author":"Klein","year":"2011","journal-title":"Amino Acids"},{"key":"10.1016\/j.bmc.2023.117289_b0035","doi-asserted-by":"crossref","first-page":"e15781","DOI":"10.1371\/journal.pone.0015781","article-title":"A self-propagating matrix metalloprotease-9 (MMP-9) dependent cycle of chronic neutrophilic inflammation","volume":"6","author":"Xu","year":"2011","journal-title":"PLoS One1"},{"key":"10.1016\/j.bmc.2023.117289_b0040","first-page":"4136","article-title":"Expression of MMP-9 in different degrees of chronic hepatitis B and its correlation with inflammation","volume":"16","author":"Li","year":"2018","journal-title":"Experimental and Therapeutic Medicine"},{"key":"10.1016\/j.bmc.2023.117289_b0045","first-page":"1701","article-title":"Modulation of matrix metalloproteinase activity by EDTA prevents posterior capsular opacification","volume":"18","author":"Hazra","year":"2012","journal-title":"Molecular Vision"},{"key":"10.1016\/j.bmc.2023.117289_b0050","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.joen.2011.09.005","article-title":"Inhibition of endogenous dentin matrix metalloproteinases by ethylenediaminetetraacetic acid","volume":"38","author":"Thompson","year":"2012","journal-title":"Journal of Endodontia"},{"key":"10.1016\/j.bmc.2023.117289_b0055","doi-asserted-by":"crossref","first-page":"2387","DOI":"10.1126\/science.1067100","article-title":"Matrix metalloproteinase inhibitors and cancer: trials and tribulations","volume":"295","author":"Coussens","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.bmc.2023.117289_b0060","doi-asserted-by":"crossref","first-page":"32659","DOI":"10.1038\/srep32659","article-title":"Matrix metalloproteinase inhibitor, doxycycline and progression of calcific aortic valve disease in hyperlipidemic mice","volume":"6","author":"Jung","year":"2016","journal-title":"Science Reports"},{"key":"10.1016\/j.bmc.2023.117289_b0065","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1111\/jcmm.13962","article-title":"EDTA\/gelatin zymography method to identify C1s versus activated MMP-9 in plasma and immune complexes of patients with systemic lupus erythematosus","volume":"23","author":"Ugarte-Berzal","year":"2019","journal-title":"Journal of Cellular and Molecular Medicine"},{"key":"10.1016\/j.bmc.2023.117289_b0070","doi-asserted-by":"crossref","first-page":"2807259","DOI":"10.1155\/2020\/2807259","article-title":"Effect of Subantimicrobial Dose Doxycycline Treatment on Gingival Crevicular Fluid Levels of MMP-9 and MMP-13 in Periodontitis Stage 2, Grade B in Subjects with Type 2 Diabetes Mellitus","volume":"2020","author":"Attia","year":"2020","journal-title":"Journal of Immunology Research"},{"key":"10.1016\/j.bmc.2023.117289_b0075","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/s13569-020-00128-6","article-title":"The anti-neoplastic effect of doxycycline in osteosarcoma as a metalloproteinase (MMP) inhibitor: a systematic review","volume":"10","author":"Hadjimichael","year":"2020","journal-title":"Clin Sarcoma Res."},{"key":"10.1016\/j.bmc.2023.117289_b0080","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1080\/15376520500194734","article-title":"Changes in Activities of MMP in Alcohol and Thermally Oxidized Sunflower Oil-Induced Liver Damage: NAC Antioxidant Therapy","volume":"16","author":"Penumathsa","year":"2006","journal-title":"Toxicology Mechanisms and Methods"},{"key":"10.1016\/j.bmc.2023.117289_b0085","doi-asserted-by":"crossref","first-page":"14230","DOI":"10.3390\/molecules171214230","article-title":"Peptide-based selective inhibitors of matrix metalloproteinase-mediated activities","volume":"17","author":"Ndinguri","year":"2012","journal-title":"Molecules"},{"key":"10.1016\/j.bmc.2023.117289_b0090","doi-asserted-by":"crossref","first-page":"e80","DOI":"10.1038\/oncsis.2013.44","article-title":"A monoclonal antibody interferes with TIMP-2 binding and incapacitates the MMP-2-activating function of multifunctional, pro-tumorigenic MMP-14\/MT1-MMP","volume":"2","author":"Shiryaev","year":"2013","journal-title":"Oncogenesis."},{"key":"10.1016\/j.bmc.2023.117289_b0095","doi-asserted-by":"crossref","first-page":"1517","DOI":"10.1158\/0008-5472.CAN-08-3255","article-title":"Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis","volume":"69","author":"Devy","year":"2009","journal-title":"Cancer Research"},{"key":"10.1016\/j.bmc.2023.117289_b0100","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1126\/science.8278810","article-title":"Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor","volume":"263","author":"Lovejoy","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.bmc.2023.117289_b0105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.pmbts.2017.02.005","article-title":"Biochemical and Biological Attributes of Matrix Metalloproteinases","volume":"147","author":"Cui","year":"2017","journal-title":"Progress in Molecular Biology and Translational Science"},{"key":"10.1016\/j.bmc.2023.117289_b0110","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/bs.pmbts.2017.04.003","article-title":"Matrix Metalloproteinase Inhibitors as Investigational and Therapeutic Tools in Unrestrained Tissue Remodeling and Pathological Disorders","volume":"148","author":"Liu","year":"2017","journal-title":"Progress in Molecular Biology and Translational Science"},{"key":"10.1016\/j.bmc.2023.117289_b0115","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1016\/j.bmc.2007.01.011","article-title":"Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs","volume":"15","author":"Verma","year":"2007","journal-title":"Bioorganic & Medicinal Chemistry"},{"key":"10.1016\/j.bmc.2023.117289_b0120","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.drudis.2019.07.013","article-title":"Understanding the variability of the S1' pocket to improve matrix metalloproteinase inhibitor selectivity profiles","volume":"25","author":"Gimeno","year":"2020","journal-title":"Drug Discovery Today"},{"key":"10.1016\/j.bmc.2023.117289_b0125","doi-asserted-by":"crossref","DOI":"10.3390\/cells9051076","article-title":"Structure and Function of Human Matrix Metalloproteinases","volume":"9","author":"Laronha","year":"2020","journal-title":"Cells."},{"key":"10.1016\/j.bmc.2023.117289_b0130","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1016\/j.survophthal.2017.12.008","article-title":"Angiogenesis and lymphangiogenesis in corneal transplantation-A review","volume":"63","author":"Zhong","year":"2018","journal-title":"Survey of Ophthalmology"},{"key":"10.1016\/j.bmc.2023.117289_b0135","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.3389\/fimmu.2019.01278","article-title":"Mechanisms of Action of Novel Drugs Targeting Angiogenesis-Promoting Matrix Metalloproteinases","volume":"10","author":"Fields","year":"2019","journal-title":"Frontiers in Immunology"},{"key":"10.1016\/j.bmc.2023.117289_b0140","doi-asserted-by":"crossref","DOI":"10.3390\/ph12020077","article-title":"The Expanding Role of MT1-MMP in Cancer Progression","volume":"12","author":"Knapinska","year":"2019","journal-title":"Pharmaceuticals."},{"key":"10.1016\/j.bmc.2023.117289_b0145","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1172\/JCI135239","article-title":"How the matrix metalloproteinase MMP14 contributes to the progression of colorectal cancer","volume":"130","author":"Claesson-Welsh","year":"2020","journal-title":"The Journal of Clinical Investigation"},{"key":"10.1016\/j.bmc.2023.117289_b0150","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.lfs.2019.05.038","article-title":"MMP targeting in the battle for vision: Recent developments and future prospects in the treatment of diabetic retinopathy","volume":"229","author":"Drankowska","year":"2019","journal-title":"Life Sciences"},{"key":"10.1016\/j.bmc.2023.117289_b0155","doi-asserted-by":"crossref","first-page":"9423907","DOI":"10.1155\/2019\/9423907","article-title":"The Role of Matrix Metalloproteinases in the Epithelial-Mesenchymal Transition of Hepatocellular Carcinoma","volume":"2019","author":"Scheau","year":"2019","journal-title":"Analytical Cellular Pathology"},{"key":"10.1016\/j.bmc.2023.117289_b0160","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.semcancer.2019.08.003","article-title":"Epithelial-to-mesenchymal transition and invadopodia markers in breast cancer: Lumican a key regulator","volume":"62","author":"Karamanou","year":"2020","journal-title":"Seminars in Cancer Biology"},{"key":"10.1016\/j.bmc.2023.117289_b0165","doi-asserted-by":"crossref","DOI":"10.3390\/cells10030687","article-title":"Cell-Matrix Interactions in the Eye: From Cornea to Choroid","volume":"10","author":"Pouw","year":"2021","journal-title":"Cells."},{"key":"10.1016\/j.bmc.2023.117289_b0170","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1186\/s12885-020-07150-3","article-title":"Tumoral and stromal expression of MMP-2, MMP-9, MMP-14, TIMP-1, TIMP-2, and VEGF-A in cervical cancer patient survival: a competing risk analysis","volume":"20","author":"Azevedo Martins","year":"2020","journal-title":"BMC Cancer"},{"key":"10.1016\/j.bmc.2023.117289_b0175","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1016\/j.devcel.2012.04.014","article-title":"MT1-MMP inactivates ADAM9 to regulate FGFR2 signaling and calvarial osteogenesis","volume":"22","author":"Chan","year":"2012","journal-title":"Developmental Cell"},{"key":"10.1016\/j.bmc.2023.117289_b0180","doi-asserted-by":"crossref","first-page":"4052","DOI":"10.1073\/pnas.060037197","article-title":"Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I","volume":"97","author":"Zhou","year":"2000","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"key":"10.1016\/j.bmc.2023.117289_b0185","doi-asserted-by":"crossref","first-page":"3313","DOI":"10.1167\/iovs.16-19420","article-title":"Proangiogenic Interactions of Vascular Endothelial MMP14 With VEGF Receptor 1 in VEGFA-Mediated Corneal Angiogenesis","volume":"57","author":"Han","year":"2016","journal-title":"Investigative Ophthalmology & Visual Science"},{"key":"10.1016\/j.bmc.2023.117289_b0190","doi-asserted-by":"crossref","first-page":"5450","DOI":"10.1167\/iovs.14-16248","article-title":"MMP14 Cleavage of VEGFR1 in the Cornea Leads to a VEGF-Trap Antiangiogenic Effect","volume":"56","author":"Han","year":"2015","journal-title":"Investigative Ophthalmology & Visual Science"},{"key":"10.1016\/j.bmc.2023.117289_b0195","doi-asserted-by":"crossref","first-page":"2321","DOI":"10.1167\/iovs.18-26277","article-title":"MMP14-Containing Exosomes Cleave VEGFR1 and Promote VEGFA-Induced Migration and Proliferation of Vascular Endothelial Cells","volume":"60","author":"Han","year":"2019","journal-title":"Investigative Ophthalmology & Visual Science"},{"key":"10.1016\/j.bmc.2023.117289_b0200","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1056\/NEJMoa032691","article-title":"Bevacizumab plus irinotecan, fluorouracil, and leucovorin for metastatic colorectal cancer","volume":"350","author":"Hurwitz","year":"2004","journal-title":"The New England Journal of Medicine"},{"key":"10.1016\/j.bmc.2023.117289_b0205","doi-asserted-by":"crossref","unstructured":"Hiratsuka S, Minowa O, Kuno J, Noda T, Shibuya M. Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice. Proceedings of the National Academy of Sciences. 1998;95(16): 9349-9354.","DOI":"10.1073\/pnas.95.16.9349"},{"key":"10.1016\/j.bmc.2023.117289_b0210","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1080\/10739680802095964","article-title":"Systems biology of vascular endothelial growth factors","volume":"15","author":"Gabhann","year":"2008","journal-title":"Microcirculation"},{"key":"10.1016\/j.bmc.2023.117289_b0215","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1177\/108705719900400206","article-title":"A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays","volume":"4","author":"Zhang","year":"1999","journal-title":"Journal of Biomolecular Screening"},{"key":"10.1016\/j.bmc.2023.117289_b0220","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.ab.2005.05.001","article-title":"Sensitivity enhancement of surface plasmon resonance biosensing of small molecules","volume":"343","author":"Mitchell","year":"2005","journal-title":"Analytical Biochemistry"},{"key":"10.1016\/j.bmc.2023.117289_b0225","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/nrd1468","article-title":"Drug repositioning: identifying and developing new uses for existing drugs","volume":"3","author":"Ashburn","year":"2004","journal-title":"Nature Reviews. Drug Discovery"},{"key":"10.1016\/j.bmc.2023.117289_b0230","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1016\/j.drudis.2015.05.001","article-title":"Drug repositioning and repurposing: terminology and definitions in literature","volume":"20","author":"Langedijk","year":"2015","journal-title":"Drug Discovery Today"},{"key":"10.1016\/j.bmc.2023.117289_b0235","first-page":"365","article-title":"Recent studies of antioxidant quinoline derivatives","volume":"13","author":"Orhan Puskullu","year":"2013","journal-title":"Mini Reviews in Medicinal Chemistry"},{"key":"10.1016\/j.bmc.2023.117289_b0240","doi-asserted-by":"crossref","first-page":"3795","DOI":"10.1021\/ic0494051","article-title":"Clioquinol, a drug for Alzheimer's disease specifically interfering with brain metal metabolism: structural characterization of its zinc(II) and copper(II) complexes","volume":"43","author":"Di Vaira","year":"2004","journal-title":"Inorganic Chemistry"},{"key":"10.1016\/j.bmc.2023.117289_b0245","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1002\/jcc.540150503","article-title":"Icm - a New Method for Protein Modeling and Design - Applications to Docking and Structure Prediction from the Distorted Native Conformation","volume":"15","author":"Abagyan","year":"1994","journal-title":"Journal of Computational Chemistry"},{"key":"10.1016\/j.bmc.2023.117289_b0250","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.bmc.2013.11.041","article-title":"Identification of novel drug scaffolds for inhibition of SARS-CoV 3-Chymotrypsin-like protease using virtual and high-throughput screenings","volume":"22","author":"Lee","year":"2014","journal-title":"Bioorganic & Medicinal Chemistry"},{"key":"10.1016\/j.bmc.2023.117289_b0255","doi-asserted-by":"crossref","first-page":"6177","DOI":"10.1021\/jm051256o","article-title":"Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes","volume":"49","author":"Friesner","year":"2006","journal-title":"Journal of Medicinal Chemistry"},{"key":"10.1016\/j.bmc.2023.117289_b0260","doi-asserted-by":"crossref","first-page":"5238","DOI":"10.1093\/emboj\/17.17.5238","article-title":"Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor","volume":"17","author":"Fernandez-Catalan","year":"1998","journal-title":"The EMBO Journal"},{"key":"10.1016\/j.bmc.2023.117289_b0265","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s10822-013-9644-8","article-title":"Protein and ligand preparation: parameters, protocols, and influence on virtual screening enrichments","volume":"27","author":"Sastry","year":"2013","journal-title":"Journal of Computer-Aided Molecular Design"},{"key":"10.1016\/j.bmc.2023.117289_b0270","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1021\/ja00214a001","article-title":"The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin","volume":"110","author":"Jorgensen","year":"1988","journal-title":"Journal of the American Chemical Society"},{"key":"10.1016\/j.bmc.2023.117289_b0275","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1021\/ci800324m","article-title":"Identifying and characterizing binding sites and assessing druggability","volume":"49","author":"Halgren","year":"2009","journal-title":"Journal of Chemical Information and Modeling"},{"key":"10.1016\/j.bmc.2023.117289_b0280","doi-asserted-by":"crossref","first-page":"9220","DOI":"10.1021\/jm500734a","article-title":"Importance of purity evaluation and the potential of quantitative 1H NMR as a purity assay: miniperspective","volume":"57","author":"Pauli","year":"2014","journal-title":"Journal of Medicinal Chemistry"}],"container-title":["Bioorganic & Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089623001372?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089623001372?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T08:29:58Z","timestamp":1778574598000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968089623001372"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,5]]},"references-count":56,"alternative-id":["S0968089623001372"],"URL":"https:\/\/doi.org\/10.1016\/j.bmc.2023.117289","relation":{},"ISSN":["0968-0896"],"issn-type":[{"value":"0968-0896","type":"print"}],"subject":[],"published":{"date-parts":[[2023,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Identification of small molecule inhibitors against MMP-14 via High-Throughput screening","name":"articletitle","label":"Article Title"},{"value":"Bioorganic & Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bmc.2023.117289","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"117289"}}