메뉴 건너뛰기




Volumn 8, Issue 1, 2017, Pages

Engineered factor Xa variants retain procoagulant activity independent of direct factor Xa inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; APIXABAN; BLOOD CLOTTING FACTOR 10A; EDOXABAN; ENZYME VARIANT; PHENYLALANINE; RIVAROXABAN; SNAKE VENOM; TYROSINE; BLOOD CLOTTING FACTOR 10A INHIBITOR;

EID: 85029327965     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/s41467-017-00647-9     Document Type: Article
Times cited : (38)

References (62)
  • 1
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the Vitamin K-dependent enzyme complexes
    • Mann, K. G., Nesheim, M. E., Church, W. R., Haley, P. & Krishnaswamy, S. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood 76, 1-16 (1990).
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 3
    • 77449128728 scopus 로고    scopus 로고
    • The molecular basis of factor V and VIII procofactor activation
    • Camire, R. M. & Bos, M. H. The molecular basis of factor V and VIII procofactor activation. J. Thromb. Haemost. 7, 1951-1961 (2009).
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 1951-1961
    • Camire, R.M.1    Bos, M.H.2
  • 4
    • 0023924910 scopus 로고
    • Cofactor proteins in the assembly and expression of blood clotting enzyme complexes
    • Mann, K. G., Jenny, R. J. & Krishnaswamy, S. Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. Annu. Rev. Biochem. 57, 915-956 (1988).
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 915-956
    • Mann, K.G.1    Jenny, R.J.2    Krishnaswamy, S.3
  • 5
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom, L. Serine protease mechanism and specificity. Chem. Rev. 102, 4501-4524 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 6
    • 17644371341 scopus 로고    scopus 로고
    • Exosite-driven substrate specificity and function in coagulation
    • Krishnaswamy, S. Exosite-driven substrate specificity and function in coagulation. J. Thromb. Haemost. 3, 54-67 (2005).
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 54-67
    • Krishnaswamy, S.1
  • 7
    • 0019957643 scopus 로고
    • Computer-generated models of blood coagulation factor Xa, factor IXa, and thrombin based upon structural homology with other serine proteases
    • Furie, B. et al. Computer-generated models of blood coagulation factor Xa, factor IXa, and thrombin based upon structural homology with other serine proteases. J. Biol. Chem. 257, 3875-3882 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 3875-3882
    • Furie, B.1
  • 8
    • 0037020083 scopus 로고    scopus 로고
    • Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site
    • Camire, R. M. Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site. J. Biol. Chem. 277, 37863-37870 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 37863-37870
    • Camire, R.M.1
  • 9
    • 49649122047 scopus 로고    scopus 로고
    • The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly
    • Toso, R., Zhu, H. & Camire, R. M. The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly. J. Biol. Chem. 283, 18627-18635 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 18627-18635
    • Toso, R.1    Zhu, H.2    Camire, R.M.3
  • 10
    • 0024543984 scopus 로고
    • Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor
    • Girard, T. J. et al. Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor. Nature 338, 518-520 (1989).
    • (1989) Nature , vol.338 , pp. 518-520
    • Girard, T.J.1
  • 11
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., Read, R. J. & Carrell, R. W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926 (2000).
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 13
    • 24944536065 scopus 로고    scopus 로고
    • Discovery of the novel antithrombotic agent 5-chloro-N-({(5S)-2-oxo-3-[4-(3-oxomorpholin-4-yl)phenyl]-1,3-oxazolidin-5-yl}methyl)thiophene-2-carboxamide (BAY 59-7939): An oral, direct factor Xa inhibitor
    • Roehrig, S. et al. Discovery of the novel antithrombotic agent 5-chloro-N-({(5S)-2-oxo-3-[4-(3-oxomorpholin-4-yl)phenyl]-1,3-oxazolidin-5-yl}methyl)thiophene-2-carboxamide (BAY 59-7939): an oral, direct factor Xa inhibitor. J. Med. Chem. 48, 5900-5908 (2005).
    • (2005) J. Med. Chem. , vol.48 , pp. 5900-5908
    • Roehrig, S.1
  • 14
    • 35848929515 scopus 로고    scopus 로고
    • Discovery of 1-(4-methoxyphenyl)-7-oxo-6-(4-(2-oxopiperidin-1-yl)phenyl)-4,5,6,7-tetrahydro-1H-pyrazolo[3,4-c]pyridine-3-carboxamide (apixaban, BMS-562247), a highly potent, selective, efficacious, and orally bioavailable inhibitor of blood coagulation factor Xa
    • Pinto, D. J. et al. Discovery of 1-(4-methoxyphenyl)-7-oxo-6-(4-(2-oxopiperidin-1-yl)phenyl)-4,5,6,7-tetrahydro-1H-pyrazolo[3,4-c]pyridine-3-carboxamide (apixaban, BMS-562247), a highly potent, selective, efficacious, and orally bioavailable inhibitor of blood coagulation factor Xa. J. Med. Chem. 50, 5339-5356 (2007).
    • (2007) J. Med. Chem. , vol.50 , pp. 5339-5356
    • Pinto, D.J.1
  • 15
    • 4744376263 scopus 로고    scopus 로고
    • Synthesis and conformational analysis of a non-amidine factor Xa inhibitor that incorporates 5-methyl-4,5,6,7-tetrahydrothiazolo[5,4-c]pyridine as S4 binding element
    • Haginoya, N. et al. Synthesis and conformational analysis of a non-amidine factor Xa inhibitor that incorporates 5-methyl-4,5,6,7-tetrahydrothiazolo[5,4-c]pyridine as S4 binding element. J. Med. Chem. 47, 5167-5182 (2004).
    • (2004) J. Med. Chem. , vol.47 , pp. 5167-5182
    • Haginoya, N.1
  • 16
    • 0010333946 scopus 로고    scopus 로고
    • Coagulation factor IXa: The relaxed conformation of Tyr99 blocks substrate binding
    • Hopfner, K. P. et al. Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding. Structure 7, 989-996 (1999).
    • (1999) Structure , vol.7 , pp. 989-996
    • Hopfner, K.P.1
  • 17
    • 76249089297 scopus 로고    scopus 로고
    • Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex
    • Johnson, D. J., Langdown, J. & Huntington, J. A. Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex. Proc. Natl Acad. Sci. USA 107, 645-650 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 645-650
    • Johnson, D.J.1    Langdown, J.2    Huntington, J.A.3
  • 18
    • 79952086865 scopus 로고    scopus 로고
    • Procoagulant adaptation of a blood coagulation prothrombinase-like enzyme complex in australian elapid venom
    • Bos, M. H. & Camire, R. M. Procoagulant adaptation of a blood coagulation prothrombinase-like enzyme complex in australian elapid venom. Toxins 2, 1554-1567 (2010).
    • (2010) Toxins , vol.2 , pp. 1554-1567
    • Bos, M.H.1    Camire, R.M.2
  • 19
    • 4544363680 scopus 로고    scopus 로고
    • The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa
    • Rao, V. S., Swarup, S. & Manjunatha Kini, R. The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa. Thromb. Haemost. 92, 509-521 (2004).
    • (2004) Thromb. Haemost. , vol.92 , pp. 509-521
    • Rao, V.S.1    Swarup, S.2    Manjunatha Kini, R.3
  • 20
    • 33646780547 scopus 로고    scopus 로고
    • Molecular evolution caught in action: Gene duplication and evolution of molecular isoforms of prothrombin activators in Pseudonaja textilis (brown snake)
    • Reza, M. A., Minh Le, T. N., Swarup, S. & Manjunatha Kini, R. Molecular evolution caught in action: gene duplication and evolution of molecular isoforms of prothrombin activators in Pseudonaja textilis (brown snake). J. Thromb. Haemost. 4, 1346-1353 (2006).
    • (2006) J. Thromb. Haemost. , vol.4 , pp. 1346-1353
    • Reza, M.A.1    Minh Le, T.N.2    Swarup, S.3    Manjunatha Kini, R.4
  • 21
    • 84877737236 scopus 로고    scopus 로고
    • Population divergence in venom bioactivities of elapid snake Pseudonaja textilis: Role of procoagulant proteins in rapid rodent prey incapacitation
    • Skejic, J. & Hodgson, W. C. Population divergence in venom bioactivities of elapid snake Pseudonaja textilis: role of procoagulant proteins in rapid rodent prey incapacitation. PLoS ONE 8, e63988 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e63988
    • Skejic, J.1    Hodgson, W.C.2
  • 22
    • 84887052679 scopus 로고    scopus 로고
    • Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilis
    • Lechtenberg, B. C. et al. Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilis. Blood 122, 2777-2783 (2013).
    • (2013) Blood , vol.122 , pp. 2777-2783
    • Lechtenberg, B.C.1
  • 23
    • 2442655492 scopus 로고    scopus 로고
    • Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized
    • Toso, R. & Camire, R. M. Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized. J. Biol. Chem. 279, 21643-21650 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 21643-21650
    • Toso, R.1    Camire, R.M.2
  • 24
    • 9144269020 scopus 로고    scopus 로고
    • Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low-molecular-weight heparin
    • Olson, S. T. et al. Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low-molecular-weight heparin. Thromb. Haemost. 92, 929-939 (2004).
    • (2004) Thromb. Haemost. , vol.92 , pp. 929-939
    • Olson, S.T.1
  • 25
    • 0034447287 scopus 로고    scopus 로고
    • Heparin-binding exosite of factor Xa
    • Rezaie, A. R. Heparin-binding exosite of factor Xa. Trends Cardiovasc. Med. 10, 333-338 (2000).
    • (2000) Trends Cardiovasc. Med. , vol.10 , pp. 333-338
    • Rezaie, A.R.1
  • 26
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman, L., Smith, D. E., Arcuri, K. E. & Vlasuk, G. P. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 248, 593-596 (1990).
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 27
    • 0031566430 scopus 로고    scopus 로고
    • The second Kunitz domain of human tissue factor pathway inhibitor: Cloning, structure determination and interaction with factor Xa
    • Burgering, M. J. et al. The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa. J. Mol. Biol. 269, 395-407 (1997).
    • (1997) J. Mol. Biol. , vol.269 , pp. 395-407
    • Burgering, M.J.1
  • 28
    • 0032538320 scopus 로고    scopus 로고
    • Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa
    • Wei, A. et al. Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J. Mol. Biol. 283, 147-154 (1998).
    • (1998) J. Mol. Biol. , vol.283 , pp. 147-154
    • Wei, A.1
  • 29
    • 84909606545 scopus 로고    scopus 로고
    • Molecular dynamics characterization of five pathogenic Factor X mutants associated with decreased catalytic activity
    • Abdel-Azeim, S., Oliva, R., Chermak, E., De Cristofaro, R. & Cavallo, L. Molecular dynamics characterization of five pathogenic Factor X mutants associated with decreased catalytic activity. Biochemistry 53, 6992-7001 (2014).
    • (2014) Biochemistry , vol.53 , pp. 6992-7001
    • Abdel-Azeim, S.1    Oliva, R.2    Chermak, E.3    De Cristofaro, R.4    Cavallo, L.5
  • 30
    • 0036382902 scopus 로고    scopus 로고
    • Crystal structure of a prostate kallikrein isolated from stallion seminal plasma: A homologue of human PSA
    • Carvalho, A. L. et al. Crystal structure of a prostate kallikrein isolated from stallion seminal plasma: a homologue of human PSA. J. Mol. Biol. 322, 325-337 (2002).
    • (2002) J. Mol. Biol. , vol.322 , pp. 325-337
    • Carvalho, A.L.1
  • 31
    • 2442656636 scopus 로고    scopus 로고
    • Blarina toxin, a mammalian lethal venom from the short-tailed shrew Blarina brevicauda: Isolation and characterization
    • Kita, M. et al. Blarina toxin, a mammalian lethal venom from the short-tailed shrew Blarina brevicauda: Isolation and characterization. Proc. Natl Acad. Sci. USA 101, 7542-7547 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7542-7547
    • Kita, M.1
  • 32
    • 84917673231 scopus 로고    scopus 로고
    • Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity
    • Skala, W. et al. Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity. J. Biol. Chem. 289, 34267-34283 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 34267-34283
    • Skala, W.1
  • 33
    • 70450280583 scopus 로고    scopus 로고
    • Convergent evolution of novel protein function in shrew and lizard venom
    • Aminetzach, Y. T., Srouji, J. R., Kong, C. Y. & Hoekstra, H. E. Convergent evolution of novel protein function in shrew and lizard venom. Curr. Biol. 19, 1925-1931 (2009).
    • (2009) Curr. Biol. , vol.19 , pp. 1925-1931
    • Aminetzach, Y.T.1    Srouji, J.R.2    Kong, C.Y.3    Hoekstra, H.E.4
  • 34
    • 0242401773 scopus 로고    scopus 로고
    • Calibrated automated thrombin generation measurement in clotting plasma
    • Hemker, H. C. et al. Calibrated automated thrombin generation measurement in clotting plasma. Pathophysiol. Haemost. Thromb. 33, 4-15 (2003).
    • (2003) Pathophysiol. Haemost. Thromb. , vol.33 , pp. 4-15
    • Hemker, H.C.1
  • 35
    • 84880329348 scopus 로고    scopus 로고
    • Factor Xa activation of factor V is of paramount importance in initiating the coagulation system: Lessons from a tick salivary protein
    • Schuijt, T. J. et al. Factor Xa activation of factor V is of paramount importance in initiating the coagulation system: lessons from a tick salivary protein. Circulation 128, 254-266 (2013).
    • (2013) Circulation , vol.128 , pp. 254-266
    • Schuijt, T.J.1
  • 36
    • 84937596938 scopus 로고    scopus 로고
    • Asymmetric processing of mutant factor X Arg386Cys reveals differences between intrinsic and extrinsic pathway activation
    • Baroni, M. et al. Asymmetric processing of mutant factor X Arg386Cys reveals differences between intrinsic and extrinsic pathway activation. Biochim. Biophys. Acta 1854, 1351-1356 (2015).
    • (2015) Biochim. Biophys. Acta , vol.1854 , pp. 1351-1356
    • Baroni, M.1
  • 37
    • 35949003684 scopus 로고    scopus 로고
    • Role of the alpha-helix 163-170 in factor Xa catalytic activity
    • Levigne, S. et al. Role of the alpha-helix 163-170 in factor Xa catalytic activity. J. Biol. Chem. 282, 31569-31579 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 31569-31579
    • Levigne, S.1
  • 38
    • 84937780393 scopus 로고    scopus 로고
    • Hemostatic agents of broad applicability produced by selective tuning of factor Xa zymogenicity
    • Ivanciu, L. & Camire, R. M. Hemostatic agents of broad applicability produced by selective tuning of factor Xa zymogenicity. Blood 126, 94-102 (2015).
    • (2015) Blood , vol.126 , pp. 94-102
    • Ivanciu, L.1    Camire, R.M.2
  • 39
    • 84964599249 scopus 로고    scopus 로고
    • Molecular basis of enhanced activity in factor VIIa-trypsin variants conveys insights into tissue factor-mediated allosteric regulation of factor VIIa activity
    • Sorensen, A. B. et al. Molecular basis of enhanced activity in factor VIIa-trypsin variants conveys insights into tissue factor-mediated allosteric regulation of factor VIIa activity. J. Biol. Chem. 291, 4671-4683 (2016).
    • (2016) J. Biol. Chem. , vol.291 , pp. 4671-4683
    • Sorensen, A.B.1
  • 40
    • 79960541421 scopus 로고    scopus 로고
    • Allostery in trypsin-like proteases suggests new therapeutic strategies
    • Gohara, D. W. & Di Cera, E. Allostery in trypsin-like proteases suggests new therapeutic strategies. Trends Biotechnol. 29, 577-585 (2011).
    • (2011) Trends Biotechnol. , vol.29 , pp. 577-585
    • Gohara, D.W.1    Di Cera, E.2
  • 41
    • 84979210724 scopus 로고    scopus 로고
    • Management of bleeding with non-Vitamin K antagonist oral anticoagulants in the era of specific reversal agents
    • Ruff, C. T., Giugliano, R. P. & Antman, E. M. Management of bleeding with non-vitamin K antagonist oral anticoagulants in the era of specific reversal agents. Circulation 134, 248-261 (2016).
    • (2016) Circulation , vol.134 , pp. 248-261
    • Ruff, C.T.1    Giugliano, R.P.2    Antman, E.M.3
  • 42
    • 84878460192 scopus 로고    scopus 로고
    • A specific antidote for reversal of anticoagulation by direct and indirect inhibitors of coagulation factor Xa
    • Lu, G. et al. A specific antidote for reversal of anticoagulation by direct and indirect inhibitors of coagulation factor Xa. Nat. Med. 19, 446-451 (2013).
    • (2013) Nat. Med. , vol.19 , pp. 446-451
    • Lu, G.1
  • 43
    • 85011068507 scopus 로고    scopus 로고
    • Single-dose ciraparantag safely and completely reverses anticoagulant effects of edoxaban
    • Ansell, J. E. et al. Single-dose ciraparantag safely and completely reverses anticoagulant effects of edoxaban. Thromb. Haemost. 117, 238-245 (2016).
    • (2016) Thromb. Haemost. , vol.117 , pp. 238-245
    • Ansell, J.E.1
  • 44
    • 84979544134 scopus 로고    scopus 로고
    • A rapid pro-hemostatic approach to overcome direct oral anticoagulants
    • Thalji, N. K. et al. A rapid pro-hemostatic approach to overcome direct oral anticoagulants. Nat. Med. 22, 924-932 (2016).
    • (2016) Nat. Med. , vol.22 , pp. 924-932
    • Thalji, N.K.1
  • 45
    • 84878952383 scopus 로고    scopus 로고
    • Safety, pharmacokinetics and pharmacodynamics of multiple oral doses of apixaban, a factor Xa inhibitor, in healthy subjects
    • Frost, C. et al. Safety, pharmacokinetics and pharmacodynamics of multiple oral doses of apixaban, a factor Xa inhibitor, in healthy subjects. Br. J. Clin. Pharmacol. 76, 776-786 (2013).
    • (2013) Br. J. Clin. Pharmacol. , vol.76 , pp. 776-786
    • Frost, C.1
  • 46
    • 84905044202 scopus 로고    scopus 로고
    • Edoxaban: A focused review of its clinical pharmacology
    • Lip, G. Y. & Agnelli, G. Edoxaban: a focused review of its clinical pharmacology. Eur. Heart. J. 35, 1844-1855 (2014).
    • (2014) Eur. Heart. J. , vol.35 , pp. 1844-1855
    • Lip, G.Y.1    Agnelli, G.2
  • 47
    • 0034700266 scopus 로고    scopus 로고
    • Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide
    • Camire, R. M., Larson, P. J., Stafford, D. W. & High, K. A. Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide. Biochemistry 39, 14322-14329 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14322-14329
    • Camire, R.M.1    Larson, P.J.2    Stafford, D.W.3    High, K.A.4
  • 48
    • 0020633335 scopus 로고
    • The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles
    • Higgins, D. L. & Mann, K. G. The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles. J. Biol. Chem. 258, 6503-6508 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 6503-6508
    • Higgins, D.L.1    Mann, K.G.2
  • 49
    • 84907884991 scopus 로고    scopus 로고
    • Cirrhosis patients have a coagulopathy that is associated with decreased clot formation capacity
    • Kleinegris, M. C. et al. Cirrhosis patients have a coagulopathy that is associated with decreased clot formation capacity. J. Thromb. Haemost. 12, 1647-1657 (2014).
    • (2014) J. Thromb. Haemost. , vol.12 , pp. 1647-1657
    • Kleinegris, M.C.1
  • 50
    • 0032492690 scopus 로고    scopus 로고
    • Structure/function analyses of recombinant variants of human factor Xa: Factor Xa incorporation into prothrombinase on the thrombin-activated platelet surface is not mimicked by synthetic phospholipid vesicles
    • Larson, P. J. et al. Structure/function analyses of recombinant variants of human factor Xa: factor Xa incorporation into prothrombinase on the thrombin-activated platelet surface is not mimicked by synthetic phospholipid vesicles. Biochemistry 37, 5029-5038 (1998).
    • (1998) Biochemistry , vol.37 , pp. 5029-5038
    • Larson, P.J.1
  • 51
    • 70149107327 scopus 로고    scopus 로고
    • Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations
    • Bos, M. H. et al. Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations. Blood 114, 686-692 (2009).
    • (2009) Blood , vol.114 , pp. 686-692
    • Bos, M.H.1
  • 52
    • 0027498670 scopus 로고
    • Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin
    • Olson, S. T., Bjork, I. & Shore, J. D. Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol. 222, 525-559 (1993).
    • (1993) Methods Enzymol. , vol.222 , pp. 525-559
    • Olson, S.T.1    Bjork, I.2    Shore, J.D.3
  • 53
    • 84946416234 scopus 로고    scopus 로고
    • GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers
    • Abraham, M. J. et al. GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX 1-2, 19-25 (2015).
    • (2015) SoftwareX , vol.1-2 , pp. 19-25
    • Abraham, M.J.1
  • 54
    • 62449330667 scopus 로고    scopus 로고
    • Empirical scoring functions for advanced protein-ligand docking with PLANTS
    • Korb, O., Stutzle, T. & Exner, T. E. Empirical scoring functions for advanced protein-ligand docking with PLANTS. J. Chem. Inf. Model. 49, 84-96 (2009).
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 84-96
    • Korb, O.1    Stutzle, T.2    Exner, T.E.3
  • 55
    • 79959713919 scopus 로고    scopus 로고
    • Definition and testing of the GROMOS force-field versions 54A7 and 54B7
    • Schmid, N. et al. Definition and testing of the GROMOS force-field versions 54A7 and 54B7. Eur. Biophys. J. 40, 843-856 (2011).
    • (2011) Eur. Biophys. J. , vol.40 , pp. 843-856
    • Schmid, N.1
  • 57
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G., Donadio, D. & Parrinello, M. Canonical sampling through velocity rescaling. J. Chem. Phys. 126, 01410 (2007).
    • (2007) J. Chem. Phys. , vol.126 , pp. 01410
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 59
  • 60
    • 84888294449 scopus 로고    scopus 로고
    • A flexible algorithm for calculating pair interactions on SIMD architectures
    • Pall, S. & Hess, B. A flexible algorithm for calculating pair interactions on SIMD architectures. Comput. Phys. Commun. 184, 2641-2650 (2013).
    • (2013) Comput. Phys. Commun. , vol.184 , pp. 2641-2650
    • Pall, S.1    Hess, B.2
  • 62
    • 0030008810 scopus 로고    scopus 로고
    • Kinetics of blood coagulation factor Xaalpha autoproteolytic conversion to factor Xabeta. Effect on inhibition by antithrombin, prothrombinase assembly, and enzyme activity
    • Pryzdial, E. L. & Kessler, G. E. Kinetics of blood coagulation factor Xaalpha autoproteolytic conversion to factor Xabeta. Effect on inhibition by antithrombin, prothrombinase assembly, and enzyme activity. J. Biol. Chem. 271, 16621-16626 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 16621-16626
    • Pryzdial, E.L.1    Kessler, G.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.