{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,3]],"date-time":"2026-03-03T15:29:54Z","timestamp":1772551794141,"version":"3.50.1"},"reference-count":88,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,12,16]],"date-time":"2025-12-16T00:00:00Z","timestamp":1765843200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,12,16]],"date-time":"2025-12-16T00:00:00Z","timestamp":1765843200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32260132"],"award-info":[{"award-number":["32260132"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Yunnan Provincial University Serving Key Industry Science and Technology Special Project","award":["FWCY-ZD2024009"],"award-info":[{"award-number":["FWCY-ZD2024009"]}]},{"name":"Joint Special Project for Basic Research of Local Universities in Yunnan Province","award":["202301BA070001-105"],"award-info":[{"award-number":["202301BA070001-105"]}]},{"name":"Frontier Research Team of Kunming University 2023, the National Key R&D Program of China","award":["2023YFF1305000"],"award-info":[{"award-number":["2023YFF1305000"]}]},{"name":"Yunnan International Joint Laboratory with South and Southeast Asia for the Integrated Development of Animal-Derived Anti-Thrombosis Chinese Medicine","award":["202503AP140025"],"award-info":[{"award-number":["202503AP140025"]}]},{"name":"Yunnan Ten Thousand Talents Program for Young Top Notch Talents","award":["YNWR-QNBJ-2020-122"],"award-info":[{"award-number":["YNWR-QNBJ-2020-122"]}]},{"name":"Special Project of Science-Technology Talent and Platform in Yunnan Province","award":["202105AC160042"],"award-info":[{"award-number":["202105AC160042"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Pharm Res"],"published-print":{"date-parts":[[2026,1]]},"DOI":"10.1007\/s11095-025-03989-y","type":"journal-article","created":{"date-parts":[[2025,12,16]],"date-time":"2025-12-16T22:54:26Z","timestamp":1765925666000},"page":"279-290","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Multi-Target Anticoagulant Regulation by Peptides from Medicinal Leeches: A Unique Natural Strategy against Thrombosis"],"prefix":"10.1007","volume":"43","author":[{"given":"Feng","family":"Shi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qingmei","family":"Hu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yiquan","family":"Lin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sijia","family":"Fan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xueting","family":"Cao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dezhi","family":"Yang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuanhai","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dejun","family":"Kong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kaiqing","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7509-6209","authenticated-orcid":false,"given":"Zichao","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2025,12,16]]},"reference":[{"key":"3989_CR1","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1016\/j.imr.2017.08.001","volume":"6","author":"AK Sig","year":"2017","unstructured":"Sig AK, Guney M, Uskudar Guclu A, Ozmen E. Medicinal leech therapy-an overall perspective. Integr Med Res. 2017;6:337\u201343. https:\/\/doi.org\/10.1016\/j.imr.2017.08.001.","journal-title":"Integr Med Res"},{"key":"3989_CR2","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1016\/j.ctcp.2017.12.001","volume":"31","author":"A Shakouri","year":"2018","unstructured":"Shakouri A, Adljouy N, Balkani S, Mohamadi M, Hamishehkar H, Abdolalizadeh J, Kazem Shakouri S. Effectiveness of topical gel of medical leech (Hirudo medicinalis) saliva extract on patients with knee osteoarthritis: a randomized clinical trial. Complement Ther Clin Pract. 2018;31:352\u20139. https:\/\/doi.org\/10.1016\/j.ctcp.2017.12.001.","journal-title":"Complement Ther Clin Pract"},{"key":"3989_CR3","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1016\/j.jams.2014.01.001","volume":"7","author":"KD Darestani","year":"2014","unstructured":"Darestani KD, Mirghazanfari SM, Moghaddam KG, Hejazi S. Leech therapy for linear lncisional skin-wound healing in rats. J Acupunct Meridian Stud. 2014;7:194\u2013201. https:\/\/doi.org\/10.1016\/j.jams.2014.01.001.","journal-title":"J Acupunct Meridian Stud"},{"key":"3989_CR4","doi-asserted-by":"publisher","first-page":"1090e","DOI":"10.1097\/PRS.0000000000009096","volume":"149","author":"JP Shtraks","year":"2022","unstructured":"Shtraks JP, Peng GL, Nassif PS. Utilization of leech therapy after rhinoplasty. Plast Reconstr Surg. 2022;149:1090e\u20135e. https:\/\/doi.org\/10.1097\/PRS.0000000000009096.","journal-title":"Plast Reconstr Surg"},{"key":"3989_CR5","doi-asserted-by":"publisher","first-page":"e335","DOI":"10.1097\/SCS.0000000000007111","volume":"32","author":"JE Cohn","year":"2021","unstructured":"Cohn JE, Othman S, Evarts M, Papajohn P, Mattioni J, Zwillenberg S. Leech therapy for complex facial lacerations. J Craniofac Surg. 2021;32:e335\u20137. https:\/\/doi.org\/10.1097\/SCS.0000000000007111.","journal-title":"J Craniofac Surg"},{"key":"3989_CR6","doi-asserted-by":"publisher","DOI":"10.1016\/j.jep.2020.112723","volume":"254","author":"B Hu","year":"2020","unstructured":"Hu B, Xu L, Li Y, Bai X, Xing M, Cao Q, Liang H, Song S, Ji A. A peptide inhibitor of macrophage migration in atherosclerosis purified from the leech Whitmania pigra. J Ethnopharmacol. 2020;254: 112723. https:\/\/doi.org\/10.1016\/j.jep.2020.112723.","journal-title":"J Ethnopharmacol"},{"key":"3989_CR7","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1007\/s11239-020-02337-8","volume":"52","author":"P Li","year":"2021","unstructured":"Li P, Lin B, Tang P, Ye Y, Wu Z, Gui S, Zhan Y, Yang W, Lin B. Aqueous extract of Whitmania pigra whitman ameliorates ferric chloride-induced venous thrombosis in rats via antioxidation. J Thromb Thrombolysis. 2021;52:59\u201368. https:\/\/doi.org\/10.1007\/s11239-020-02337-8.","journal-title":"J Thromb Thrombolysis"},{"key":"3989_CR8","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1016\/j.jss.2019.07.094","volume":"245","author":"X Yao","year":"2020","unstructured":"Yao X, Liu H, Li P, Chen W, Guan S, Chen Y, Wu Y-N, Lin B. Aqueous extract of Whitmania pigra whitman alleviates thrombus burden via sirtuin 1\/NF-\u03baB pathway. J Surg Res. 2020;245:441\u201352. https:\/\/doi.org\/10.1016\/j.jss.2019.07.094.","journal-title":"J Surg Res"},{"key":"3989_CR9","doi-asserted-by":"publisher","first-page":"301","DOI":"10.5551\/jat.36558","volume":"24","author":"S Li","year":"2017","unstructured":"Li S, Cheng L, An D, Song S, Liang H, Chu F, Ji A. Whitmania pigra whitman extracts inhibit lipopolysaccharide induced rat vascular smooth muscle cells migration and their adhesion ability to THP-1 and RAW 264.7 cells. J Atheroscler Thromb. 2017;24:301\u201311. https:\/\/doi.org\/10.5551\/jat.36558.","journal-title":"J Atheroscler Thromb"},{"key":"3989_CR10","doi-asserted-by":"publisher","unstructured":"Zhong WL, Ma YN, Ye JH, Fan XY, Shen HJ, Yuan R, Zhang YX, Liu ZY, Du SY, Li PY. Comparison of protein and polypeptide components and antithrombotic activity in vitro of three preparations containing hirudo. Chin J Exp Tradit Med Formulae. 2024;1\u201311. https:\/\/doi.org\/10.13422\/j.cnki.syfjx.20251067.","DOI":"10.13422\/j.cnki.syfjx.20251067"},{"key":"3989_CR11","doi-asserted-by":"publisher","first-page":"1281","DOI":"10.3760\/j.issn.1673-4777.2024.09.001","volume":"19","author":"JL Zhang","year":"2024","unstructured":"Zhang JL, Li CQ, Bao QH. Clinical study of huoxue tongmai tablets combined with alteplase in the treatment of acutr myocardial infarction. Chin Med. 2024;19:1281\u20134. https:\/\/doi.org\/10.3760\/j.issn.1673-4777.2024.09.001.","journal-title":"Chin Med"},{"key":"3989_CR12","doi-asserted-by":"publisher","first-page":"120","DOI":"10.19528\/j.issn.1003-3548.2022.03.047","volume":"42","author":"Y Zhang","year":"2022","unstructured":"Zhang Y. The effect of brain xinkang capsules combined with alteplase on inflammatory factors and brain oxygen metabolism in patients with acute cerebral infarction. Clin Med. 2022;42:120\u20132. https:\/\/doi.org\/10.19528\/j.issn.1003-3548.2022.03.047.","journal-title":"Clin Med"},{"key":"3989_CR13","doi-asserted-by":"publisher","first-page":"701","DOI":"10.19803\/j.1672-8629.2021.08.01","volume":"18","author":"HJ Geng","year":"2021","unstructured":"Geng HJ, Wang Y, Zhang YY, Xie YM, Chen RB, Gai GZ, Zhang WL. Real-world study on use of maixuekang capsules combined with western medicines in treating coronary heart disease. Chin J Pharmacovigil. 2021;18:701\u20134. https:\/\/doi.org\/10.19803\/j.1672-8629.2021.08.01.","journal-title":"Chin J Pharmacovigil"},{"key":"3989_CR14","unstructured":"Cardiovascular diseases (n.d.). https:\/\/www.who.int\/zh\/news-room\/fact-sheets\/detail\/cardiovascular-diseases-(cvd). Accessed March 7, 2025)."},{"key":"3989_CR15","doi-asserted-by":"publisher","first-page":"885","DOI":"10.1055\/s-0031-1297367","volume":"37","author":"W Lijfering","year":"2011","unstructured":"Lijfering W, Flinterman L, Vandenbroucke J, Rosendaal F, Cannegieter S. Relationship between venous and arterial thrombosis: a review of the literature from a causal perspective. Semin Thromb Hemost. 2011;37:885\u201396. https:\/\/doi.org\/10.1055\/s-0031-1297367.","journal-title":"Semin Thromb Hemost"},{"key":"3989_CR16","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1007\/978-1-0716-3175-1_22","volume":"2663","author":"CL Dean","year":"2023","unstructured":"Dean CL. An overview of heparin monitoring with the anti-xa assay. Methods Mol Biol. 2023;2663:343\u201353. https:\/\/doi.org\/10.1007\/978-1-0716-3175-1_22.","journal-title":"Methods Mol Biol"},{"key":"3989_CR17","doi-asserted-by":"publisher","DOI":"10.1001\/jamanetworkopen.2024.3786","volume":"7","author":"E Larsen","year":"2024","unstructured":"Larsen E, Nilius H, Studt J, Tsakiris DA, Greinacher A, Mendez A, Schmidt A, Wuillemin WA, Gerber B, Vishnu P, Graf L, Kremer Hovinga JA, Goetze JP, Bakchoul T, Nagler M. Accuracy of diagnosing heparin-induced thrombocytopenia. JAMA Netw Open. 2024;7: e243786. https:\/\/doi.org\/10.1001\/jamanetworkopen.2024.3786.","journal-title":"JAMA Netw Open"},{"key":"3989_CR18","doi-asserted-by":"publisher","first-page":"13","DOI":"10.2174\/0113892002290846240228061506","volume":"25","author":"S Hazra","year":"2024","unstructured":"Hazra S, Singh PA, Bajwa N. Safety issues of herb-warfarin interactions. Curr Drug Metab. 2024;25:13\u201327. https:\/\/doi.org\/10.2174\/0113892002290846240228061506.","journal-title":"Curr Drug Metab"},{"key":"3989_CR19","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1007\/s10928-021-09783-8","volume":"49","author":"M Bontempi","year":"2022","unstructured":"Bontempi M. Semi-empirical anticoagulation model (SAM): INR monitoring during warfarin therapy. J Pharmacokinet Pharmacodyn. 2022;49:271\u201382. https:\/\/doi.org\/10.1007\/s10928-021-09783-8.","journal-title":"J Pharmacokinet Pharmacodyn"},{"key":"3989_CR20","doi-asserted-by":"publisher","DOI":"10.1016\/j.phymed.2024.155479","volume":"128","author":"L Xue","year":"2024","unstructured":"Xue L, Singla RK, He S, Arrasate S, Gonz\u00e1lez-D\u00edaz H, Miao L, Shen B. Warfarin\u2013a natural anticoagulant: a review of research trends for precision medication. Phytomedicine. 2024;128: 155479. https:\/\/doi.org\/10.1016\/j.phymed.2024.155479.","journal-title":"Phytomedicine"},{"key":"3989_CR21","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1146\/annurev-pharmtox-032823-122811","volume":"64","author":"RH Olie","year":"2024","unstructured":"Olie RH, Winckers K, Rocca B, Ten Cate H. Oral anticoagulants beyond warfarin. Annu Rev Pharmacol Toxicol. 2024;64:551\u201375. https:\/\/doi.org\/10.1146\/annurev-pharmtox-032823-122811.","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"3989_CR22","doi-asserted-by":"publisher","first-page":"3355","DOI":"10.1016\/j.jtha.2024.08.011","volume":"22","author":"SNJ Laan","year":"2024","unstructured":"Laan SNJ, Lenderink BG, Eikenboom JCJ, Bierings R. Endothelial colony-forming cells in the spotlight: insights into the pathophysiology of von willebrand disease and rare bleeding disorders. J Thromb Haemost. 2024;22:3355\u201365. https:\/\/doi.org\/10.1016\/j.jtha.2024.08.011.","journal-title":"J Thromb Haemost"},{"key":"3989_CR23","doi-asserted-by":"publisher","first-page":"294","DOI":"10.1097\/MOH.0000000000000832","volume":"31","author":"L Huang","year":"2024","unstructured":"Huang L, Shao B. New insights of glycoprotein Ib-IX-V complex organization and glycoprotein Ib\u03b1 in platelet biogenesis. Curr Opin Hematol. 2024;31:294\u2013301. https:\/\/doi.org\/10.1097\/MOH.0000000000000832.","journal-title":"Curr Opin Hematol"},{"key":"3989_CR24","doi-asserted-by":"publisher","unstructured":"Tuna R, Yi W, Crespo Cruz E, Romero J, Ren Y, Guan J, Li Y, Deng Y, Bluestein D, Liu ZL, Sheriff J. Platelet biorheology and mechanobiology in thrombosis: In silico perspectives. Prepr Org. 2024;1\u201317. https:\/\/doi.org\/10.20944\/preprints202402.0799.v1.","DOI":"10.20944\/preprints202402.0799.v1"},{"key":"3989_CR25","doi-asserted-by":"publisher","first-page":"1071","DOI":"10.1182\/blood-2010-01-264507","volume":"117","author":"RD Starke","year":"2011","unstructured":"Starke RD, Ferraro F, Paschalaki KE, Dryden NH, McKinnon TAJ, Sutton RE, Payne EM, Haskard DO, Hughes AD, Cutler DF, Laffan MA, Randi AM. Endothelial von willebrand factor regulates angiogenesis. Blood. 2011;117:1071\u201380. https:\/\/doi.org\/10.1182\/blood-2010-01-264507.","journal-title":"Blood"},{"key":"3989_CR26","doi-asserted-by":"publisher","first-page":"2174","DOI":"10.1182\/blood.2023023277","volume":"144","author":"PJ Lenting","year":"2024","unstructured":"Lenting PJ, Denis CV, Christophe OD. How unique structural adaptations support and coordinate the complex function of von willebrand factor. Blood. 2024;144:2174\u201384. https:\/\/doi.org\/10.1182\/blood.2023023277.","journal-title":"Blood"},{"key":"3989_CR27","doi-asserted-by":"publisher","DOI":"10.1063\/1.5007313","volume":"148","author":"S Posch","year":"2018","unstructured":"Posch S, Obser T, K\u00f6nig G, Schneppenheim R, Tamp\u00e9 R, Hinterdorfer P. Interaction of von willebrand factor domains with collagen investigated by single molecule force spectroscopy. J Chem Phys. 2018;148: 123310. https:\/\/doi.org\/10.1063\/1.5007313.","journal-title":"J Chem Phys"},{"key":"3989_CR28","doi-asserted-by":"publisher","first-page":"10511","DOI":"10.1038\/s41598-021-89799-9","volume":"11","author":"J Chung","year":"2021","unstructured":"Chung J, Jeong D, Kim G, Go S, Song J, Moon E, Huh YH, Kim D. Super-resolution imaging of platelet-activation process and its quantitative analysis. Sci Rep. 2021;11:10511. https:\/\/doi.org\/10.1038\/s41598-021-89799-9.","journal-title":"Sci Rep"},{"key":"3989_CR29","doi-asserted-by":"publisher","first-page":"1607","DOI":"10.1182\/blood-2017-03-773614","volume":"130","author":"TN Durrant","year":"2017","unstructured":"Durrant TN, Van Den Bosch MT, Hers I. Integrin \u03b1IIb\u03b23 outside-in signaling. Blood. 2017;130:1607\u201319. https:\/\/doi.org\/10.1182\/blood-2017-03-773614.","journal-title":"Blood"},{"key":"3989_CR30","doi-asserted-by":"publisher","first-page":"725","DOI":"10.1038\/s41422-024-00997-2","volume":"34","author":"J Guo","year":"2024","unstructured":"Guo J, Zhou Y-L, Yang Y, Guo S, You E, Xie X, Jiang Y, Mao C, Xu HE, Zhang Y. Structural basis of tethered agonism and G protein coupling of protease-activated receptors. Cell Res. 2024;34:725\u201334. https:\/\/doi.org\/10.1038\/s41422-024-00997-2.","journal-title":"Cell Res"},{"key":"3989_CR31","doi-asserted-by":"publisher","first-page":"930","DOI":"10.1111\/jth.12168","volume":"11","author":"L Jiang","year":"2013","unstructured":"Jiang L, Xu C, Yu S, Liu P, Luo D, Zhou Q, Gao C, Hu H. A critical role of thrombin\/PAR-1 in ADP-induced platelet secretion and the second wave of aggregation. J Thromb Haemost. 2013;11:930\u201340. https:\/\/doi.org\/10.1111\/jth.12168.","journal-title":"J Thromb Haemost"},{"key":"3989_CR32","doi-asserted-by":"publisher","first-page":"879","DOI":"10.1172\/JCI6042","volume":"103","author":"ML Kahn","year":"1999","unstructured":"Kahn ML, Nakanishi-Matsui M, Shapiro MJ, Ishihara H, Coughlin SR. Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin. J Clin Invest. 1999;103:879\u201387. https:\/\/doi.org\/10.1172\/JCI6042.","journal-title":"J Clin Invest"},{"key":"3989_CR33","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1097\/00001721-199102000-00027","volume":"2","author":"R Munro","year":"1991","unstructured":"Munro R, Jones CP, Sawyer RT. Calin\u2014a platelet adhesion inhibitor from the saliva of the medicinal leech. Blood Coagul Fibrinolysis. 1991;2:179\u201384. https:\/\/doi.org\/10.1097\/00001721-199102000-00027.","journal-title":"Blood Coagul Fibrinolysis"},{"key":"3989_CR34","doi-asserted-by":"publisher","first-page":"705","DOI":"10.1182\/blood.V85.3.705.bloodjournal853705","volume":"85","author":"J Harsfalvi","year":"1995","unstructured":"Harsfalvi J, Stassen J, Hoylaerts M, Van Houtte E, Sawyer R, Vermylen J, Deckmyn H. Calin from Hirudo medicinalis, an inhibitor of von willebrand factor binding to collagen under static and flow conditions. Blood. 1995;85:705\u201311. https:\/\/doi.org\/10.1182\/blood.V85.3.705.bloodjournal853705.","journal-title":"Blood"},{"key":"3989_CR35","doi-asserted-by":"publisher","first-page":"6893","DOI":"10.1016\/S0021-9258(19)50512-9","volume":"267","author":"TM Connolly","year":"1992","unstructured":"Connolly TM, Jacobs JW, Condra C. An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. I. identification, isolation, and characterization. J Biol Chem. 1992;267:6893\u20138. https:\/\/doi.org\/10.1016\/S0021-9258(19)50512-9.","journal-title":"J Biol Chem"},{"key":"3989_CR36","doi-asserted-by":"publisher","first-page":"913","DOI":"10.1016\/j.jmb.2008.06.034","volume":"381","author":"W Gronwald","year":"2008","unstructured":"Gronwald W, Bomke J, Maurer T, Domogalla B, Huber F, Schumann F, Kremer W, Fink F, Rysiok T, Frech M, Kalbitzer HR. Structure of the leech protein saratin and characterization of its binding to collagen. J Mol Biol. 2008;381:913\u201327. https:\/\/doi.org\/10.1016\/j.jmb.2008.06.034.","journal-title":"J Mol Biol"},{"key":"3989_CR37","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/j.bbrc.2016.03.117","volume":"473","author":"X Liu","year":"2016","unstructured":"Liu X, Wang C, Ding X, Liu X, Li Q, Kong Y. A novel selective inhibitor to thrombin-induced platelet aggregation purified from the leech Whitmania pigra. Biochem Biophys Res Commun. 2016;473:349\u201354. https:\/\/doi.org\/10.1016\/j.bbrc.2016.03.117.","journal-title":"Biochem Biophys Res Commun"},{"key":"3989_CR38","doi-asserted-by":"publisher","first-page":"10143","DOI":"10.1016\/S0021-9258(19)38791-5","volume":"265","author":"JL Seymour","year":"1990","unstructured":"Seymour JL, Henzel WJ, Nevins B, Stults JT, Lazarus RA. Decorsin a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora. J Biol Chem. 1990;265:10143\u20137. https:\/\/doi.org\/10.1016\/S0021-9258(19)38791-5.","journal-title":"J Biol Chem"},{"key":"3989_CR39","doi-asserted-by":"publisher","first-page":"1073","DOI":"10.1111\/j.1432-1033.1991.tb16472.x","volume":"202","author":"P Mazur","year":"1991","unstructured":"Mazur P, Henzel WJ, Seymour JL, Lazarus RA. Ornatins: potent glycoprotein IIb\u2010IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata. Eur J Biochem. 1991;202:1073\u201382. https:\/\/doi.org\/10.1111\/j.1432-1033.1991.tb16472.x.","journal-title":"Eur J Biochem"},{"key":"3989_CR40","doi-asserted-by":"publisher","first-page":"294","DOI":"10.1016\/j.jcis.2022.04.147","volume":"623","author":"A Luchini","year":"2022","unstructured":"Luchini A, Tidemand FG, Arayasecchi R, Campana M, C\u00e1rdenas M, Arleth L. Structural model of tissue factor (TF) and TF-factor vIIa complex in a lipid membrane: a combined experimental and computational study. J Colloid Interface Sci. 2022;623:294\u2013305. https:\/\/doi.org\/10.1016\/j.jcis.2022.04.147.","journal-title":"J Colloid Interface Sci"},{"key":"3989_CR41","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1042\/BJ20140130","volume":"462","author":"T Koklic","year":"2014","unstructured":"Koklic T, Majumder R, Lentz BR. Ca2+ switches the effect of PS-containing membranes on factor Xa from activating to inhibiting: implications for initiation of blood coagulation. Biochem J. 2014;462:591\u2013601. https:\/\/doi.org\/10.1042\/BJ20140130.","journal-title":"Biochem J"},{"key":"3989_CR42","doi-asserted-by":"publisher","first-page":"489","DOI":"10.1055\/a-1528-0499","volume":"41","author":"S Konrath","year":"2021","unstructured":"Konrath S, Mailer RK, Renn\u00e9 T. Mechanism, functions, and diagnostic relevance of FXII activation by foreign surfaces. Hamostaseologie. 2021;41:489\u2013501. https:\/\/doi.org\/10.1055\/a-1528-0499.","journal-title":"Hamostaseologie"},{"key":"3989_CR43","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1016\/j.jtha.2023.09.027","volume":"22","author":"BM Mohammed","year":"2024","unstructured":"Mohammed BM, Sun M, Cheng Q, Litvak M, McCrae KR, Emsley J, McCarty OJT, Gailani D. High molecular weight kininogen interactions with the homologs prekallikrein and factor XI: importance to surface-induced coagulation. J Thromb Haemost. 2024;22:225\u201337. https:\/\/doi.org\/10.1016\/j.jtha.2023.09.027.","journal-title":"J Thromb Haemost"},{"key":"3989_CR44","doi-asserted-by":"publisher","first-page":"1894","DOI":"10.1111\/j.1538-7836.2005.01365.x","volume":"3","author":"MW Mosesson","year":"2005","unstructured":"Mosesson MW. Fibrinogen and fibrin structure and functions. J Thromb Haemost. 2005;3:1894\u2013904. https:\/\/doi.org\/10.1111\/j.1538-7836.2005.01365.x.","journal-title":"J Thromb Haemost"},{"key":"3989_CR45","doi-asserted-by":"publisher","first-page":"e13","DOI":"10.1161\/ATVBAHA.117.308564","volume":"37","author":"S Kattula","year":"2017","unstructured":"Kattula S, Byrnes JR, Wolberg AS. Fibrinogen and fibrin in hemostasis and thrombosis. Arterioscler Thromb Vasc Biol. 2017;37:e13\u201321. https:\/\/doi.org\/10.1161\/ATVBAHA.117.308564.","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"3989_CR46","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.blre.2014.09.003","volume":"29","author":"JC Chapin","year":"2015","unstructured":"Chapin JC, Hajjar KA. Fibrinolysis and the control of blood coagulation. Blood Rev. 2015;29:17\u201324. https:\/\/doi.org\/10.1016\/j.blre.2014.09.003.","journal-title":"Blood Rev"},{"key":"3989_CR47","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1111\/jth.12455","volume":"12","author":"EL Hethershaw","year":"2014","unstructured":"Hethershaw EL, Cilia La Corte AL, Duval C, Ali M, Grant PJ, Ari\u00ebns RAS, Philippou H. The effect of blood coagulation factor XIII on fibrin clot structure and fibrinolysis. J Thromb Haemost. 2014;12:197\u2013205. https:\/\/doi.org\/10.1111\/jth.12455.","journal-title":"J Thromb Haemost"},{"key":"3989_CR48","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2014810118","volume":"118","author":"KJ Kearney","year":"2021","unstructured":"Kearney KJ, Butler J, Posada OM, Wilson C, Heal S, Ali M, Hardy L, Ahnstr\u00f6m J, Gailani D, Foster R, Hethershaw E, Longstaff C, Philippou H. Kallikrein directly interacts with and activates factor IX, resulting in thrombin generation and fibrin formation independent of factor XI. Proc Natl Acad Sci U S A. 2021;118: e2014810118. https:\/\/doi.org\/10.1073\/pnas.2014810118.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"3989_CR49","doi-asserted-by":"publisher","first-page":"302","DOI":"10.1055\/s-2007-1002723","volume":"15","author":"P Johnson","year":"1989","unstructured":"Johnson P, Sze P, Winant R, Payne P, Lazar J. Biochemistry and genetic engineering of hirudin. Semin Thromb Hemost. 1989;15:302\u201315. https:\/\/doi.org\/10.1055\/s-2007-1002723.","journal-title":"Semin Thromb Hemost"},{"key":"3989_CR50","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1016\/0003-9861(88)90019-7","volume":"267","author":"S Konno","year":"1988","unstructured":"Konno S, Fenton JW, Villanueva GB. Analysis of the secondary structure of hirudin and the mechanism of its interaction with thrombin. Arch Biochem Biophys. 1988;267:158\u201366. https:\/\/doi.org\/10.1016\/0003-9861(88)90019-7.","journal-title":"Arch Biochem Biophys"},{"key":"3989_CR51","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1097\/00001721-199102000-00013","volume":"2","author":"A Electricwala","year":"1991","unstructured":"Electricwala A, Sawyer RT, Jones CP, Atkinson T. Isolation of thrombin inhibitor from the leech Hirudinaria manillensis. Blood Coagul Fibrinolysis. 1991;2:83\u201390. https:\/\/doi.org\/10.1097\/00001721-199102000-00013.","journal-title":"Blood Coagul Fibrinolysis"},{"key":"3989_CR52","doi-asserted-by":"publisher","first-page":"8590","DOI":"10.1016\/S0021-9258(18)52916-1","volume":"268","author":"KH Strube","year":"1993","unstructured":"Strube KH, Kr\u00f6ger B, Bialojan S, Otte M, Dodt J. Isolation, sequence analysis, and cloning of haemadin an anticoagulant peptide from the indian leech. J Biol Chem. 1993;268:8590\u20135. https:\/\/doi.org\/10.1016\/S0021-9258(18)52916-1.","journal-title":"J Biol Chem"},{"key":"3989_CR53","doi-asserted-by":"publisher","first-page":"340","DOI":"10.1006\/prep.1999.1077","volume":"16","author":"SJ Hong","year":"1999","unstructured":"Hong SJ, Kang KW. Purification of granulin-like polypeptide from the blood-sucking leech, Hirudo nipponia. Protein Expr Purif. 1999;16:340\u20136. https:\/\/doi.org\/10.1006\/prep.1999.1077.","journal-title":"Protein Expr Purif"},{"key":"3989_CR54","doi-asserted-by":"publisher","first-page":"30774","DOI":"10.1074\/jbc.M000787200","volume":"275","author":"M Salzet","year":"2000","unstructured":"Salzet M, Chopin V, Baert J, Matias I, Malecha J. Theromin, a novel leech thrombin inhibitor. J Biol Chem. 2000;275:30774\u201380. https:\/\/doi.org\/10.1074\/jbc.M000787200.","journal-title":"J Biol Chem"},{"key":"3989_CR55","doi-asserted-by":"publisher","first-page":"16694","DOI":"10.1016\/S0021-9258(19)84761-0","volume":"264","author":"C Dunwiddie","year":"1989","unstructured":"Dunwiddie C, Thornberry NA, Bull HG, Sardana M, Friedman PA, Jacobs JW, Simpson E. Antistasin, a leech-derived inhibitor of factor Xa.Kinetic analysis of enzyme inhibition andidentification of the reactive site. J Biol Chem. 1989;264:16694\u20139. https:\/\/doi.org\/10.1016\/S0021-9258(19)84761-0.","journal-title":"J Biol Chem"},{"key":"3989_CR56","doi-asserted-by":"publisher","first-page":"1384","DOI":"10.1016\/0006-291x(90)91020-s","volume":"166","author":"DT Blankenship","year":"1990","unstructured":"Blankenship DT, Brankamp RG, Manley GD, Cardin AD. Amino acid sequence of ghilanten: anticoagulant-antimetastatic principle of the South American leech, Haementeria ghilianii. Biochem Biophys Res Commun. 1990;166:1384\u20139. https:\/\/doi.org\/10.1016\/0006-291x(90)91020-s.","journal-title":"Biochem Biophys Res Commun"},{"key":"3989_CR57","doi-asserted-by":"publisher","first-page":"1469","DOI":"10.1055\/s-0037-1614857","volume":"82","author":"F Faria","year":"1999","unstructured":"Faria F, Kelen EM, Sampaio C, Bon C, Duval N, Chudzinski-Tavassi AM. A new factor Xa inhibitor (lefaxin) from the Haementeria depressa leech. Thromb Haemost. 1999;82:1469\u201373. https:\/\/doi.org\/10.1055\/s-0037-1614857.","journal-title":"Thromb Haemost"},{"key":"3989_CR58","doi-asserted-by":"publisher","first-page":"32701","DOI":"10.1074\/jbc.M909217199","volume":"275","author":"V Chopin","year":"2000","unstructured":"Chopin V, Salzet M, Baert J, Vandenbulcke F, Sauti\u00e8re P-E, Kerckaert J-P, Malecha J. Therostasin, a novel clotting factor Xa inhibitor from the rhynchobdellid leech, Theromyzon tessulatum. J Biol Chem. 2000;275:32701\u20137. https:\/\/doi.org\/10.1074\/jbc.M909217199.","journal-title":"J Biol Chem"},{"key":"3989_CR59","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1007\/s004380050291","volume":"253","author":"L Zavalova","year":"1996","unstructured":"Zavalova L, Lukyanov S, Baskova I, Snezhkov E, Akopov S, Berezhnoy S, Bogdanova E, Barsova E, Sverdlov ED. Genes from the medicinal leech (Hirudo medicinalis ) coding for unusual enzymes that specifically cleave endo-epsilon (gamma -Glu)-Lys isopeptide bonds and help to dissolve blood clots. Mol Gen Genet. 1996;253:20\u20135. https:\/\/doi.org\/10.1007\/s004380050291.","journal-title":"Mol Gen Genet"},{"key":"3989_CR60","doi-asserted-by":"publisher","first-page":"2068","DOI":"10.3390\/cimb43030143","volume":"43","author":"P Bobrovsky","year":"2021","unstructured":"Bobrovsky P, Manuvera V, Baskova I, Nemirova S, Medvedev A, Lazarev V. Recombinant destabilase from Hirudo medicinalis is able to dissolve human blood clots in vitro. Curr Issues Mol Biol. 2021;43:2068\u201381. https:\/\/doi.org\/10.3390\/cimb43030143.","journal-title":"Curr Issues Mol Biol"},{"key":"3989_CR61","doi-asserted-by":"publisher","first-page":"797","DOI":"10.1042\/bj3240797","volume":"324","author":"S Finney","year":"1997","unstructured":"Finney S, Seale L, Sawyer RT, Wallis RB. Tridegin, a new peptidic inhibitor of factor XIIIa, from the blood-sucking leech Haementeria ghilianii. Biochem J. 1997;324:797\u2013805. https:\/\/doi.org\/10.1042\/bj3240797.","journal-title":"Biochem J"},{"key":"3989_CR62","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1046\/j.1432-1327.1998.2560297.x","volume":"256","author":"T Friedrich","year":"1998","unstructured":"Friedrich T, Kr\u00f6ger B, Koerwer W, Strube K, Meyer T, Bialojan S. An isopeptide bond splitting enzyme from Hirudo medicinalis similar to gamma-glutamyl transpeptidase. Eur J Biochem. 1998;256:297\u2013302. https:\/\/doi.org\/10.1046\/j.1432-1327.1998.2560297.x.","journal-title":"Eur J Biochem"},{"key":"3989_CR63","doi-asserted-by":"publisher","first-page":"2370","DOI":"10.1161\/ATVBAHA.120.315754","volume":"41","author":"G Alkarithi","year":"2021","unstructured":"Alkarithi G, Duval C, Shi Y, Macrae FL, Ari\u00ebns RAS. Thrombus structural composition in cardiovascular disease. Arterioscler Thromb Vasc Biol. 2021;41:2370\u201383. https:\/\/doi.org\/10.1161\/ATVBAHA.120.315754.","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"3989_CR64","doi-asserted-by":"publisher","unstructured":"Shi L, Wei CX, Sun L, Zhang GM, Zhang YR, Zhai WJ, Qi YM, Zhou RL, Meng LJ, Zhang Y. Relationship between thrombus vWF and NETs with clinical severity and peripheral blood immunocytes\u2019 indicators in patients with acute ischemic stroke. Interv Neuroradiol. 2024;15910199241258374. https:\/\/doi.org\/10.1177\/15910199241258374.","DOI":"10.1177\/15910199241258374"},{"key":"3989_CR65","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1111\/j.1538-7836.2008.03220.x","volume":"7","author":"DC Rijken","year":"2009","unstructured":"Rijken DC, Lijnen HR. New insights into the molecular mechanisms of the fibrinolytic system. J Thromb Haemost. 2009;7:4\u201313. https:\/\/doi.org\/10.1111\/j.1538-7836.2008.03220.x.","journal-title":"J Thromb Haemost"},{"key":"3989_CR66","doi-asserted-by":"publisher","first-page":"1053","DOI":"10.1097\/TA.0000000000001685","volume":"83","author":"CD Barrett","year":"2017","unstructured":"Barrett CD, Moore HB, Banerjee A, Silliman CC, Moore EE, Yaffe MB. Human neutrophil elastase mediates fibrinolysis shutdown through competitive degradation of plasminogen and generation of angiostatin. J Trauma Acute Care Surg. 2017;83:1053\u201361. https:\/\/doi.org\/10.1097\/TA.0000000000001685.","journal-title":"J Trauma Acute Care Surg"},{"key":"3989_CR67","doi-asserted-by":"publisher","first-page":"14270","DOI":"10.1096\/fj.201901363rrr","volume":"33","author":"DBD Cruz","year":"2019","unstructured":"Cruz DBD, Helms J, Aquino LR, Stiel L, Cougourdan L, Broussard C, Chafey P, Ri\u00e8s\u2010Kautt M, Meziani F, Toti F, Gaussem P, Angl\u00e9s\u2010Cano E. DNA\u2010bound elastase of neutrophil extracellular traps degrades plasminogen, reduces plasmin formation, and decreases fibrinolysis: proof of concept in septic shock plasma. FASEB J. 2019;33:14270\u201380. https:\/\/doi.org\/10.1096\/fj.201901363rrr.","journal-title":"FASEB J"},{"key":"3989_CR68","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1159\/000214088","volume":"4","author":"EMA Kelen","year":"1975","unstructured":"Kelen EMA, Rosenfeld G. Fibrinogenolytic substance (hementerin) of brazilian blood-sucking leeches (Haementeria lutzi pinto 1920). Haemostasis. 1975;4:51\u201364. https:\/\/doi.org\/10.1159\/000214088.","journal-title":"Haemostasis"},{"key":"3989_CR69","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.1515\/bchm2.1980.361.2.1841","volume":"361","author":"U Seem\u00fcller","year":"1980","unstructured":"Seem\u00fcller U, EuLrrz M, Fritz H, Strobl A. Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis. Hoppe Seylers Z Physiol Chem. 1980;361:1841\u20136.","journal-title":"Hoppe Seylers Z Physiol Chem"},{"key":"3989_CR70","doi-asserted-by":"publisher","first-page":"543","DOI":"10.1002\/prot.26750","volume":"93","author":"BZ N\u00e9meth","year":"2025","unstructured":"N\u00e9meth BZ, Kiss B, Sahin-T\u00f3th M, Magyar C, P\u00e1l G. The high-affinity chymotrypsin inhibitor eglin c poorly inhibits human chymotrypsin-like protease: Gln192 and Lys 218 are key determinants. Proteins. 2025;93:543\u201354. https:\/\/doi.org\/10.1002\/prot.26750.","journal-title":"Proteins"},{"key":"3989_CR71","doi-asserted-by":"publisher","first-page":"937","DOI":"10.1111\/j.1432-1033.1994.tb18575.x","volume":"219","author":"C S\u00f6llner","year":"1994","unstructured":"S\u00f6llner C, Mentele R, Eckerskorn C, Fritz H, Sommerhoff CP. Isolation and characterization of hirustasin, an antistasin\u2010type serine\u2010proteinase inhibitor from the medical leech Hirudo medicinalis. Eur J Biochem. 1994;219:937\u201343. https:\/\/doi.org\/10.1111\/j.1432-1033.1994.tb18575.x.","journal-title":"Eur J Biochem"},{"key":"3989_CR72","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1016\/S0969-2126(97)00183-4","volume":"5","author":"PR Mittl","year":"1997","unstructured":"Mittl PR, Marco SD, Fendrich G, Pohlig G, Heim J, Sommerhoff C, Fritz H, Priestle JP, Gr\u00fctter MG. A new structural class of serine protease inhibitors revealed by the structure of the hirustasin\u2013kallikrein complex. Structure. 1997;5:253\u201364. https:\/\/doi.org\/10.1016\/S0969-2126(97)00183-4.","journal-title":"Structure"},{"key":"3989_CR73","doi-asserted-by":"publisher","first-page":"13879","DOI":"10.1074\/jbc.270.23.13879","volume":"270","author":"H Jung","year":"1995","unstructured":"Jung H, Kim S, Ha K, Joe CO, Kang KW. Isolation and characterization of guamerin, a new human leukocyte elastase inhibitor from Hirudo nipponia. J Biol Chem. 1995;270:13879\u201384. https:\/\/doi.org\/10.1074\/jbc.270.23.13879.","journal-title":"J Biol Chem"},{"key":"3989_CR74","doi-asserted-by":"publisher","first-page":"540","DOI":"10.1016\/S1875-5364(21)60054-7","volume":"19","author":"KH Xu","year":"2021","unstructured":"Xu KH, Zhou M, Wu FL, Tang XP, Lu QM, Lai R, Long CB. Identification and characterization of a novel elastase inhibitor from Hirudinaria manillensis. Chin J Nat Med. 2021;19:540\u20134. https:\/\/doi.org\/10.1016\/S1875-5364(21)60054-7.","journal-title":"Chin J Nat Med"},{"key":"3989_CR75","doi-asserted-by":"publisher","first-page":"1169","DOI":"10.3390\/medicina59061169","volume":"59","author":"R Santoro","year":"2023","unstructured":"Santoro R, Molinari A, Leotta M, Martini T. Isolated prolongation of activated partial thromboplastin time: not just bleeding risk! Medicina (Kaunas. 2023;59:1169. https:\/\/doi.org\/10.3390\/medicina59061169.","journal-title":"Medicina (Kaunas"},{"key":"3989_CR76","doi-asserted-by":"publisher","first-page":"692","DOI":"10.1046\/j.1432-1327.1998.2540692.x","volume":"254","author":"DR Kim","year":"1998","unstructured":"Kim DR, Kang KW. Amino acid sequence of piguamerin, an antistasin-type protease inhibitor from the blood sucking leech Hirudo nipponia. Eur J Biochem. 1998;254:692\u20137. https:\/\/doi.org\/10.1046\/j.1432-1327.1998.2540692.x.","journal-title":"Eur J Biochem"},{"key":"3989_CR77","doi-asserted-by":"publisher","first-page":"2657","DOI":"10.1007\/s00726-016-2299-8","volume":"48","author":"Y Ren","year":"2016","unstructured":"Ren Y, Yang Y, Wu W, Zhang M, Wu H, Li X. Identification and characterization of novel anticoagulant peptide with thrombolytic effect and nutrient oligopeptides with high branched chain amino acid from Whitmania pigra protein. Amino Acids. 2016;48:2657\u201370. https:\/\/doi.org\/10.1007\/s00726-016-2299-8.","journal-title":"Amino Acids"},{"key":"3989_CR78","doi-asserted-by":"publisher","DOI":"10.3390\/toxins10110429","volume":"10","author":"X Tang","year":"2018","unstructured":"Tang X, Chen M, Duan Z, Mwangi J, Li P, Lai R. Isolation and characterization of poecistasin, an anti-thrombotic antistasin-type serine protease inhibitor from leech Poecilobdella manillensis. Toxins Basel. 2018;10: 429. https:\/\/doi.org\/10.3390\/toxins10110429.","journal-title":"Toxins Basel"},{"key":"3989_CR79","doi-asserted-by":"publisher","first-page":"205","DOI":"10.24272\/j.issn.2095-8137.2019.037","volume":"40","author":"R Cheng","year":"2019","unstructured":"Cheng R, Tang X, Long A-L, Mwangi J, Lai R, Sun R, Long C, Zhang Z. Purification and characterization of a novel anti-coagulant from the leech Hirudinaria manillensis. Zool Res. 2019;40:205\u201310. https:\/\/doi.org\/10.24272\/j.issn.2095-8137.2019.037.","journal-title":"Zool Res"},{"key":"3989_CR80","doi-asserted-by":"publisher","first-page":"444","DOI":"10.4103\/0973-1296.160446","volume":"11","author":"X Zheng","year":"2015","unstructured":"Zheng X, Li J, Chen Z, Liu Y, Chen K. Purification and characterization of an anticoagulant oligopeptide from Whitmania pigra Whitman. Pharmacogn Mag. 2015;11:444\u20138. https:\/\/doi.org\/10.4103\/0973-1296.160446.","journal-title":"Pharmacogn Mag"},{"key":"3989_CR81","unstructured":"Gui YL, Dong DX, Li RX. Biomimetic affinity purification and identification of a new anticoagulant protein from Hirudo nipponia. Chin J Biochem Pharm. 2008;29(3):145\u2013148."},{"key":"3989_CR82","doi-asserted-by":"publisher","first-page":"390","DOI":"10.1007\/s00436-024-08404-w","volume":"123","author":"C M\u00fcller","year":"2024","unstructured":"M\u00fcller C, Sponholz D, Tolksdorf C, Rauch BH, Kvist S. Identification and functional characterization of multiple haemadins and an oligomeric decorsin in the Asian land leech Haemadipsa interrupta. Parasitol Res. 2024;123:390. https:\/\/doi.org\/10.1007\/s00436-024-08404-w.","journal-title":"Parasitol Res"},{"key":"3989_CR83","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2024.132278","volume":"270","author":"F Zhao","year":"2024","unstructured":"Zhao F, Huang Z, He B, Liu K, Li J, Liu Z, Lin G. Comparative genomics of two Asian medicinal leeches Hirudo nipponia and Hirudo tianjinensis: with emphasis on antithrombotic genes and their corresponding proteins. Int J Biol Macromol. 2024;270: 132278. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.132278.","journal-title":"Int J Biol Macromol"},{"key":"3989_CR84","doi-asserted-by":"publisher","DOI":"10.3390\/genes14112068","volume":"14","author":"Z Liu","year":"2023","unstructured":"Liu Z, Zhao F, Huang Z, Hu Q, Meng R, Lin Y, Qi J, Lin G. Revisiting the Asian buffalo leech (Hirudinaria manillensis) genome: focus on antithrombotic genes and their corresponding proteins. Genes. 2023;14: 2068. https:\/\/doi.org\/10.3390\/genes14112068.","journal-title":"Genes"},{"key":"3989_CR85","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1186\/s12864-022-08290-5","volume":"23","author":"L Tong","year":"2022","unstructured":"Tong L, Dai S, Kong D, Yang P, Tong X, Tong X, Bi X, Su Y, Zhao Y, Liu Z. The genome of medicinal leech (Whitmania pigra) and comparative genomic study for exploration of bioactive ingredients. BMC Genomics. 2022;23:76. https:\/\/doi.org\/10.1186\/s12864-022-08290-5.","journal-title":"BMC Genomics"},{"key":"3989_CR86","doi-asserted-by":"publisher","DOI":"10.3389\/fgene.2025.1548006","volume":"16","author":"F Zhao","year":"2025","unstructured":"Zhao F, Huang Z, Tang L, Zhang W, Liu Z, Lin G. Comparative genomics of three non-hematophagous leeches (Whitmania spp.) with emphasis on antithrombotic biomolecules. Front Genet. 2025;16: 1548006. https:\/\/doi.org\/10.3389\/fgene.2025.1548006.","journal-title":"Front Genet"},{"key":"3989_CR87","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1016\/S1875-5364(19)30061-5","volume":"17","author":"S Ren","year":"2019","unstructured":"Ren S, Liu Z, Cao Y, Hua Y, Chen C, Guo W, Kong Y. A novel protease-activated receptor 1 inhibitor from the leech whitmania pigra. Chin J Nat Med. 2019;17:591\u20139. https:\/\/doi.org\/10.1016\/S1875-5364(19)30061-5.","journal-title":"Chin J Nat Med"},{"key":"3989_CR88","doi-asserted-by":"publisher","DOI":"10.3390\/genes15020164","volume":"15","author":"Z Liu","year":"2024","unstructured":"Liu Z, Zhao F, Huang Z, He B, Liu K, Shi F, Zhao Z, Lin G. A chromosome-level genome assembly of the non-hematophagous leech whitmania pigra (Whitman 1884): identification and expression analysis of antithrombotic genes. Genes. 2024;15: 164. https:\/\/doi.org\/10.3390\/genes15020164.","journal-title":"Genes"}],"container-title":["Pharmaceutical Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11095-025-03989-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11095-025-03989-y","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11095-025-03989-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T17:05:43Z","timestamp":1771347943000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11095-025-03989-y"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,16]]},"references-count":88,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2026,1]]}},"alternative-id":["3989"],"URL":"https:\/\/doi.org\/10.1007\/s11095-025-03989-y","relation":{},"ISSN":["0724-8741","1573-904X"],"issn-type":[{"value":"0724-8741","type":"print"},{"value":"1573-904X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,12,16]]},"assertion":[{"value":"26 June 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"28 November 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 December 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"All authors have no conflicts of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interest"}}]}}