Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation

Search Page

Filters

My NCBI Filters

Results by year

Table representation of search results timeline featuring number of search results per year.

Year Number of Results
2004 1
2005 3
2006 2
2009 1
2010 1
2015 1
2017 1
2018 1
2020 1
2022 2
2024 0

Text availability

Article attribute

Article type

Publication date

Search Results

13 results

Results by year

Filters applied: . Clear all
Page 1
Crystal structures of the FXIa catalytic domain in complex with ecotin mutants reveal substrate-like interactions.
Jin L, Pandey P, Babine RE, Gorga JC, Seidl KJ, Gelfand E, Weaver DT, Abdel-Meguid SS, Strickler JE. Jin L, et al. J Biol Chem. 2005 Feb 11;280(6):4704-12. doi: 10.1074/jbc.M411309200. Epub 2004 Nov 15. J Biol Chem. 2005. PMID: 15545266 Free article.
The presence of ecotin not only assisted in the crystallization of the enzyme but also revealed unique structural features in the active site of FXIa. Subsequently, the sequence from P5 to P2' in ecotin was mutated to the FXIa substrate sequence, and the structures …
The presence of ecotin not only assisted in the crystallization of the enzyme but also revealed unique structural features in the active sit …
Identification of an anticoagulant peptide that inhibits both fXIa and fVIIa/tissue factor from the blood-feeding nematode Ancylostoma caninum.
Li D, He Q, Kang T, Yin H, Jin X, Li H, Gan W, Yang C, Hu J, Wu Y, Peng L. Li D, et al. Biochem Biophys Res Commun. 2010 Feb 5;392(2):155-9. doi: 10.1016/j.bbrc.2009.12.177. Epub 2010 Jan 7. Biochem Biophys Res Commun. 2010. PMID: 20059979
Factor VIIa-tissue factor complex (fVIIa/TF) and factor XIa (fXIa) play important roles in the initiation and amplification of coagulation, respectively. ...This is the first report on an anticoagulant that can inhibit both fXIa and fVIIa/TF. This anticoagulant pept …
Factor VIIa-tissue factor complex (fVIIa/TF) and factor XIa (fXIa) play important roles in the initiation and amplification of coagul …
SHR2285, the first selectively oral FXIa inhibitor in China: Safety, tolerability, pharmacokinetics and pharmacodynamics combined with aspirin, clopidogrel or ticagrelor.
Ma T, Dong Y, Huang L, Yang Y, Geng Y, Fei F, Xie P, Zhao Y, Lin H, Yang Z, Jin Y, Ju X, Sun R, Li J. Ma T, et al. Front Pharmacol. 2022 Oct 19;13:1027627. doi: 10.3389/fphar.2022.1027627. eCollection 2022. Front Pharmacol. 2022. PMID: 36339534 Free PMC article.
Purpose: To evaluate the safety, tolerability, pharmacokinetics and pharmacodynamics of SHR2285, the first oral coagulation factor XIa (FXIa) inhibitor developed in China in combination with aspirin, clopidogrel or ticagrelor in healthy subjects. ...Conclusion: These data …
Purpose: To evaluate the safety, tolerability, pharmacokinetics and pharmacodynamics of SHR2285, the first oral coagulation factor XIa (F …
The Antithrombotic Effect of Recombinant Neorudin on Thrombi.
Liu YB, Zhang L, Zhou XC, Zhou Y, Liu Y, Zheng C, Xu X, Geng PP, Hao CH, Zhao ZY, Wu CT, Jin JD. Liu YB, et al. Drug Des Devel Ther. 2022 Jun 2;16:1667-1678. doi: 10.2147/DDDT.S353088. eCollection 2022. Drug Des Devel Ther. 2022. PMID: 35677424 Free PMC article.
INTRODUCTION: Recombinant neorudin (EPR-hirudin, EH) was developed through the addition of an EPR (Glu-Pro-Arg) peptide to the amino terminus of hirudin, which can be recognized and cut by coagulation factors XIa (FXIa) and/or Xa (FXa). In this study, the low-bleeding anti …
INTRODUCTION: Recombinant neorudin (EPR-hirudin, EH) was developed through the addition of an EPR (Glu-Pro-Arg) peptide to the amino terminu …
Effect of Hemodilution In Vitro with Hydroxyethyl Starch on Hemostasis.
Jin S, Yu G, Hou R, Shen B, Jiang H. Jin S, et al. Med Sci Monit. 2017 May 8;23:2189-2197. doi: 10.12659/msm.901588. Med Sci Monit. 2017. PMID: 28481865 Free PMC article.
CONCLUSIONS By reducing FVIII activity and platelet PS expression, HES interfered with PS combining to FXIa, FVIIIa, and FVa, which affected the acceleration and explosion stage of thrombin. ...
CONCLUSIONS By reducing FVIII activity and platelet PS expression, HES interfered with PS combining to FXIa, FVIIIa, and FVa, which a …
Design, synthesis, and biological evaluation of peptidomimetic inhibitors of factor XIa as novel anticoagulants.
Lin J, Deng H, Jin L, Pandey P, Quinn J, Cantin S, Rynkiewicz MJ, Gorga JC, Bibbins F, Celatka CA, Nagafuji P, Bannister TD, Meyers HV, Babine RE, Hayward NJ, Weaver D, Benjamin H, Stassen F, Abdel-Meguid SS, Strickler JE. Lin J, et al. J Med Chem. 2006 Dec 28;49(26):7781-91. doi: 10.1021/jm060978s. J Med Chem. 2006. PMID: 17181160
To investigate the potential of FXIa inhibitors as safe anticoagulants, a series of potent, selective peptidomimetic inhibitors of FXIa were designed and synthesized. Some of these inhibitors showed low nanomolar FXIa inhibitory activity with >1000-fold FX …
To investigate the potential of FXIa inhibitors as safe anticoagulants, a series of potent, selective peptidomimetic inhibitors of …
Phenotypic and Genotypic Analysis of a Hereditary Antithrombin Deficiency Pedigree Due to a Novel SERPINC1 Mutation (p.Met281Thr).
Liu S, Luo S, Yang L, Wang M, Jin Y, Li X, Xu Q. Liu S, et al. Hamostaseologie. 2020 Dec;40(5):687-690. doi: 10.1055/a-1145-4224. Epub 2020 May 25. Hamostaseologie. 2020. PMID: 32450575
As a protease inhibitor belonging to the serpin superfamily, AT is able to inactivate thrombin and inhibit activated coagulation factors IX, X, XI, and XII (FIXa, FXa, FXIa, and FXIIa).1 Moreover, it has been found that AT can inhibit activated FVII (FVIIa) by accelerating …
As a protease inhibitor belonging to the serpin superfamily, AT is able to inactivate thrombin and inhibit activated coagulation factors IX, …
An anticoagulant peptide from the human hookworm, Ancylostoma duodenale that inhibits coagulation factors Xa and XIa.
Gan W, Deng L, Yang C, He Q, Hu J, Yin H, Jin X, Lu C, Wu Y, Peng L. Gan W, et al. FEBS Lett. 2009 Jun 18;583(12):1976-80. doi: 10.1016/j.febslet.2009.05.009. Epub 2009 May 14. FEBS Lett. 2009. PMID: 19446556 Free article.
AduNAP4 is extremely efficient at prolonging the activated partial thromboplastin time, and is an inhibitor of both fXa (K(i)=7.34+/-1.74 nM) and fXIa (K(i)=42.45+/-3.25 nM). No fXIa inhibitor has previously been described from other blood-feeding animals. Our resul …
AduNAP4 is extremely efficient at prolonging the activated partial thromboplastin time, and is an inhibitor of both fXa (K(i)=7.34+/-1.74 nM …
Structural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2.
Navaneetham D, Jin L, Pandey P, Strickler JE, Babine RE, Abdel-Meguid SS, Walsh PN. Navaneetham D, et al. J Biol Chem. 2005 Oct 28;280(43):36165-75. doi: 10.1074/jbc.M504990200. Epub 2005 Aug 6. J Biol Chem. 2005. PMID: 16085935 Free article.
Factor XIa (FXIa) is a serine protease important for initiating the intrinsic pathway of blood coagulation. ...To determine the contributions of residues within PN2KPI to its inhibitory activity, selected point mutations in PN2KPI loop 1 11TGPCRAMISR20 and loop 2 34FYGGC38 …
Factor XIa (FXIa) is a serine protease important for initiating the intrinsic pathway of blood coagulation. ...To determine the contr …
Evaluating prodrug characteristics of a novel anticoagulant fusion protein neorudin, a prodrug targeting release of hirudin variant 2-Lys47 at the thrombosis site, by means of in vitro pharmacokinetics.
Dong X, Gu R, Zhu X, Gan H, Liu J, Jin J, Meng Z, Dou G. Dong X, et al. Eur J Pharm Sci. 2018 Aug 30;121:166-177. doi: 10.1016/j.ejps.2018.05.025. Epub 2018 May 23. Eur J Pharm Sci. 2018. PMID: 29802897
Recombinant neorudin (EPR-hirudin, EH), a low-bleeding anticoagulant fusion protein, is an inactive prodrug designed to be converted to the active metabolite, hirudin variant 2-Lys47 (HV2), locally at the thrombus site by FXa and/or FXIa, following activation of the coagul …
Recombinant neorudin (EPR-hirudin, EH), a low-bleeding anticoagulant fusion protein, is an inactive prodrug designed to be converted to the …
13 results