메뉴 건너뛰기




Volumn 20, Issue 2, 2010, Pages 168-179

In silico studies of blood coagulation proteins: from mosaic proteases to nonenzymatic cofactor inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

2 [4 [(1 ACETIMIDOYL 3 PYRROLIDINYL)OXY]PHENYL] 3 (7 AMIDINO 2 NAPHTHYL)PROPIONIC ACID; 3 (5 AMIDINO 2 HYDROXYPHENYL) 1 [5 (2,6 DIMETHYL 1 PIPERIDINYL)PENTYL] 2(1H) QUINOXALINONE; ANTIVITAMIN K; APIXABAN; BLOOD CLOTTING FACTOR; BLOOD CLOTTING FACTOR 10A INHIBITOR; BLOOD CLOTTING FACTOR 5A; OTAMIXABAN; PROTEINASE; RAZAXABAN; RIVAROXABAN; RPR 208815; UNCLASSIFIED DRUG;

EID: 77951290766     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2009.12.016     Document Type: Review
Times cited : (11)

References (78)
  • 1
    • 0037320734 scopus 로고    scopus 로고
    • Introduction to thrombosis proficient and cost-effective approaches to thrombosis
    • v
    • Bick R.L. Introduction to thrombosis proficient and cost-effective approaches to thrombosis. Hematol Oncol Clin North Am 2003, 17:1-8. v.
    • (2003) Hematol Oncol Clin North Am , vol.17 , pp. 1-8
    • Bick, R.L.1
  • 2
    • 34548698444 scopus 로고    scopus 로고
    • Coagulation factor V and thrombophilia: background and mechanisms
    • Segers K., Dahlback B., Nicolaes G.A. Coagulation factor V and thrombophilia: background and mechanisms. Thromb Haemost 2007, 98:530-542.
    • (2007) Thromb Haemost , vol.98 , pp. 530-542
    • Segers, K.1    Dahlback, B.2    Nicolaes, G.A.3
  • 3
    • 69549124116 scopus 로고    scopus 로고
    • Cancer-associated thrombosis
    • Sood S.L. Cancer-associated thrombosis. Curr Opin Hematol 2009, 16:378-385.
    • (2009) Curr Opin Hematol , vol.16 , pp. 378-385
    • Sood, S.L.1
  • 4
    • 47249084343 scopus 로고    scopus 로고
    • Advances in understanding pathogenic mechanisms of thrombophilic disorders
    • Dahlback B. Advances in understanding pathogenic mechanisms of thrombophilic disorders. Blood 2008, 112:19-27.
    • (2008) Blood , vol.112 , pp. 19-27
    • Dahlback, B.1
  • 5
    • 50449098285 scopus 로고    scopus 로고
    • Mechanisms of thrombus formation
    • Furie B., Furie B.C. Mechanisms of thrombus formation. N Engl J Med 2008, 359:938-949.
    • (2008) N Engl J Med , vol.359 , pp. 938-949
    • Furie, B.1    Furie, B.C.2
  • 6
    • 20444427991 scopus 로고    scopus 로고
    • The anticoagulant protein C pathway
    • Dahlback B., Villoutreix B.O. The anticoagulant protein C pathway. FEBS Lett 2005, 579:3310-3316.
    • (2005) FEBS Lett , vol.579 , pp. 3310-3316
    • Dahlback, B.1    Villoutreix, B.O.2
  • 7
    • 21544447526 scopus 로고    scopus 로고
    • Regulation of blood coagulation by the protein C anticoagulant pathway: novel insights into structure-function relationships and molecular recognition
    • Dahlback B., Villoutreix B.O. Regulation of blood coagulation by the protein C anticoagulant pathway: novel insights into structure-function relationships and molecular recognition. Arterioscler Thromb Vasc Biol 2005, 25:1311-1320.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 1311-1320
    • Dahlback, B.1    Villoutreix, B.O.2
  • 8
    • 0036263043 scopus 로고    scopus 로고
    • Structural bioinformatics: methods, concepts and applications to blood coagulation proteins
    • Villoutreix B.O. Structural bioinformatics: methods, concepts and applications to blood coagulation proteins. Curr Protein Pept Sci 2002, 3:341-364.
    • (2002) Curr Protein Pept Sci , vol.3 , pp. 341-364
    • Villoutreix, B.O.1
  • 9
    • 67649518035 scopus 로고    scopus 로고
    • Homology modeling in drug discovery: current trends and applications
    • Cavasotto C.N., Phatak S.S. Homology modeling in drug discovery: current trends and applications. Drug Discov Today 2009, 14:676-683.
    • (2009) Drug Discov Today , vol.14 , pp. 676-683
    • Cavasotto, C.N.1    Phatak, S.S.2
  • 10
    • 64549115839 scopus 로고    scopus 로고
    • Protein structure prediction: when is it useful?
    • Zhang Y. Protein structure prediction: when is it useful?. Curr Opin Struct Biol 2009, 19:145-155.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 145-155
    • Zhang, Y.1
  • 11
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., Nicholls A. Classical electrostatics in biology and chemistry. Science 1995, 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 12
    • 0041510360 scopus 로고    scopus 로고
    • Structural genomics: computational methods for structure analysis
    • Goldsmith-Fischman S., Honig B. Structural genomics: computational methods for structure analysis. Protein Sci 2003, 12:1813-1821.
    • (2003) Protein Sci , vol.12 , pp. 1813-1821
    • Goldsmith-Fischman, S.1    Honig, B.2
  • 13
    • 60049083996 scopus 로고    scopus 로고
    • Comparative atomistic and coarse-grained study of water: What do we lose by coarse-graining?
    • Wang H., Junghans C., Kremer K. Comparative atomistic and coarse-grained study of water: What do we lose by coarse-graining?. Eur Phys J E Soft Matter 2009, 28:221-229.
    • (2009) Eur Phys J E Soft Matter , vol.28 , pp. 221-229
    • Wang, H.1    Junghans, C.2    Kremer, K.3
  • 14
    • 42549156124 scopus 로고    scopus 로고
    • Exploring energy landscapes of protein folding and aggregation
    • Mousseau N., Derreumaux P. Exploring energy landscapes of protein folding and aggregation. Front Biosci 2008, 13:4495-4516.
    • (2008) Front Biosci , vol.13 , pp. 4495-4516
    • Mousseau, N.1    Derreumaux, P.2
  • 15
    • 18744371588 scopus 로고    scopus 로고
    • Molecular dynamics and protein function
    • Karplus M., Kuriyan J. Molecular dynamics and protein function. Proc Natl Acad Sci U S A 2005, 102:6679-6685.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6679-6685
    • Karplus, M.1    Kuriyan, J.2
  • 16
    • 33749506205 scopus 로고    scopus 로고
    • Methods for the prediction of protein-ligand binding sites for structure-based drug design and virtual ligand screening
    • Laurie A.T., Jackson R.M. Methods for the prediction of protein-ligand binding sites for structure-based drug design and virtual ligand screening. Curr Protein Pept Sci 2006, 7:395-406.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 395-406
    • Laurie, A.T.1    Jackson, R.M.2
  • 17
    • 55649090573 scopus 로고    scopus 로고
    • Identification of hot-spot residues in protein-protein interactions by computational docking
    • Grosdidier S., Fernandez-Recio J. Identification of hot-spot residues in protein-protein interactions by computational docking. BMC Bioinformatics 2008, 9:447.
    • (2008) BMC Bioinformatics , vol.9 , pp. 447
    • Grosdidier, S.1    Fernandez-Recio, J.2
  • 18
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells J.A., McClendon C.L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 2007, 450:1001-1009.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 20
    • 33645961330 scopus 로고    scopus 로고
    • Flexible protein-protein docking
    • Bonvin A.M. Flexible protein-protein docking. Curr Opin Struct Biol 2006, 16:194-200.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 194-200
    • Bonvin, A.M.1
  • 21
    • 33846094031 scopus 로고    scopus 로고
    • Computational identification of inhibitors of protein-protein interactions
    • Zhong S., Macias A.T., MacKerell A.D. Computational identification of inhibitors of protein-protein interactions. Curr Top Med Chem 2007, 7:63-82.
    • (2007) Curr Top Med Chem , vol.7 , pp. 63-82
    • Zhong, S.1    Macias, A.T.2    MacKerell, A.D.3
  • 23
    • 41949102408 scopus 로고    scopus 로고
    • Predicting 3D structures of protein-protein complexes
    • Vakser I.A., Kundrotas P. Predicting 3D structures of protein-protein complexes. Curr Pharm Biotechnol 2008, 9:57-66.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 57-66
    • Vakser, I.A.1    Kundrotas, P.2
  • 24
    • 61349117968 scopus 로고    scopus 로고
    • The importance of discerning shape in molecular pharmacology
    • Kortagere S., Krasowski M.D., Ekins S. The importance of discerning shape in molecular pharmacology. Trends Pharmacol Sci 2009, 30:138-147.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 138-147
    • Kortagere, S.1    Krasowski, M.D.2    Ekins, S.3
  • 25
    • 64549106038 scopus 로고    scopus 로고
    • Convergence and combination of methods in protein-protein docking
    • Vajda S., Kozakov D. Convergence and combination of methods in protein-protein docking. Curr Opin Struct Biol 2009, 19:164-170.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 164-170
    • Vajda, S.1    Kozakov, D.2
  • 26
    • 41949132916 scopus 로고    scopus 로고
    • Flexible ligand docking to multiple receptor conformations: a practical alternative
    • Totrov M., Abagyan R. Flexible ligand docking to multiple receptor conformations: a practical alternative. Curr Opin Struct Biol 2008, 18:178-184.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 178-184
    • Totrov, M.1    Abagyan, R.2
  • 28
    • 51349130207 scopus 로고    scopus 로고
    • Building a chemical space based on fragment descriptors
    • Baskin I., Varnek A. Building a chemical space based on fragment descriptors. Comb Chem High Throughput Screen 2008, 11:661-668.
    • (2008) Comb Chem High Throughput Screen , vol.11 , pp. 661-668
    • Baskin, I.1    Varnek, A.2
  • 29
    • 33749513381 scopus 로고    scopus 로고
    • Receptor-based computational screening of compound databases: the main docking-scoring engines
    • Sperandio O., Miteva M.A., Delfaud F., Villoutreix B.O. Receptor-based computational screening of compound databases: the main docking-scoring engines. Curr Protein Pept Sci 2006, 7:369-393.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 369-393
    • Sperandio, O.1    Miteva, M.A.2    Delfaud, F.3    Villoutreix, B.O.4
  • 30
    • 33750701141 scopus 로고    scopus 로고
    • On scaffolds and hopping in medicinal chemistry
    • Brown N., Jacoby E. On scaffolds and hopping in medicinal chemistry. Mini Rev Med Chem 2006, 6:1217-1229.
    • (2006) Mini Rev Med Chem , vol.6 , pp. 1217-1229
    • Brown, N.1    Jacoby, E.2
  • 31
    • 33845780212 scopus 로고    scopus 로고
    • Basic overview of chemoinformatics
    • Engel T. Basic overview of chemoinformatics. J Chem Inf Model 2006, 46:2267-2277.
    • (2006) J Chem Inf Model , vol.46 , pp. 2267-2277
    • Engel, T.1
  • 32
    • 69249149274 scopus 로고    scopus 로고
    • Drug-like property concepts in pharmaceutical design
    • Di L., Kerns E.H., Carter G.T. Drug-like property concepts in pharmaceutical design. Curr Pharm Des 2009, 15:2184-2194.
    • (2009) Curr Pharm Des , vol.15 , pp. 2184-2194
    • Di, L.1    Kerns, E.H.2    Carter, G.T.3
  • 33
    • 70449528780 scopus 로고    scopus 로고
    • In silico toxicology for the pharmaceutical sciences
    • Valerio L.G. In silico toxicology for the pharmaceutical sciences. Toxicol Appl Pharmacol 2009, 241:356-370.
    • (2009) Toxicol Appl Pharmacol , vol.241 , pp. 356-370
    • Valerio, L.G.1
  • 34
    • 29244445116 scopus 로고    scopus 로고
    • Post-translational modifications in proteins involved in blood coagulation
    • Hansson K., Stenflo J. Post-translational modifications in proteins involved in blood coagulation. J Thromb Haemost 2005, 3:2633-2648.
    • (2005) J Thromb Haemost , vol.3 , pp. 2633-2648
    • Hansson, K.1    Stenflo, J.2
  • 35
    • 0037079573 scopus 로고    scopus 로고
    • Predicted solution structure of zymogen human coagulation FVII
    • Perera L., Darden T.A., Pedersen L.G. Predicted solution structure of zymogen human coagulation FVII. J Comput Chem 2002, 23:35-47.
    • (2002) J Comput Chem , vol.23 , pp. 35-47
    • Perera, L.1    Darden, T.A.2    Pedersen, L.G.3
  • 37
    • 0036192859 scopus 로고    scopus 로고
    • Structure and dynamics of zymogen human blood coagulation factor X
    • Venkateswarlu D., Perera L., Darden T., Pedersen L.G. Structure and dynamics of zymogen human blood coagulation factor X. Biophys J 2002, 82:1190-1206.
    • (2002) Biophys J , vol.82 , pp. 1190-1206
    • Venkateswarlu, D.1    Perera, L.2    Darden, T.3    Pedersen, L.G.4
  • 39
    • 0035968239 scopus 로고    scopus 로고
    • Structural and energetic characteristics of the heparin-binding site in antithrombotic protein C
    • Friedrich U., Blom A.M., Dahlback B., Villoutreix B.O. Structural and energetic characteristics of the heparin-binding site in antithrombotic protein C. J Biol Chem 2001, 276:24122-24128.
    • (2001) J Biol Chem , vol.276 , pp. 24122-24128
    • Friedrich, U.1    Blom, A.M.2    Dahlback, B.3    Villoutreix, B.O.4
  • 41
    • 0036263042 scopus 로고    scopus 로고
    • New insights into binding interfaces of coagulation factors V and VIII and their homologues lessons from high resolution crystal structures
    • Fuentes-Prior P., Fujikawa K., Pratt K.P. New insights into binding interfaces of coagulation factors V and VIII and their homologues lessons from high resolution crystal structures. Curr Protein Pept Sci 2002, 3:313-339.
    • (2002) Curr Protein Pept Sci , vol.3 , pp. 313-339
    • Fuentes-Prior, P.1    Fujikawa, K.2    Pratt, K.P.3
  • 42
    • 25444438704 scopus 로고    scopus 로고
    • Completed three-dimensional model of human coagulation factor Va. Molecular dynamics simulations and structural analyses
    • Orban T., Kalafatis M., Gogonea V. Completed three-dimensional model of human coagulation factor Va. Molecular dynamics simulations and structural analyses. Biochemistry 2005, 44:13082-13090.
    • (2005) Biochemistry , vol.44 , pp. 13082-13090
    • Orban, T.1    Kalafatis, M.2    Gogonea, V.3
  • 44
    • 33646060435 scopus 로고    scopus 로고
    • Proposed structural models of the prothrombinase (FXa-FVa) complex
    • Autin L., Steen M., Dahlback B., Villoutreix B.O. Proposed structural models of the prothrombinase (FXa-FVa) complex. Proteins 2006, 63:440-450.
    • (2006) Proteins , vol.63 , pp. 440-450
    • Autin, L.1    Steen, M.2    Dahlback, B.3    Villoutreix, B.O.4
  • 46
    • 41449117525 scopus 로고    scopus 로고
    • Crystal structure of human factor VIII: implications for the formation of the factor IXa-factor VIIIa complex
    • Ngo J.C., Huang M., Roth D.A., Furie B.C., Furie B. Crystal structure of human factor VIII: implications for the formation of the factor IXa-factor VIIIa complex. Structure 2008, 16:597-606.
    • (2008) Structure , vol.16 , pp. 597-606
    • Ngo, J.C.1    Huang, M.2    Roth, D.A.3    Furie, B.C.4    Furie, B.5
  • 49
    • 33745603727 scopus 로고    scopus 로고
    • Interactions of the C2 domain of human factor V with a model membrane
    • Mollica L., Fraternali F., Musco G. Interactions of the C2 domain of human factor V with a model membrane. Proteins 2006, 64:363-375.
    • (2006) Proteins , vol.64 , pp. 363-375
    • Mollica, L.1    Fraternali, F.2    Musco, G.3
  • 50
    • 33947720248 scopus 로고    scopus 로고
    • A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation
    • Olsen O.H., Rand K.D., Ostergaard H., Persson E. A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation. Protein Sci 2007, 16:671-682.
    • (2007) Protein Sci , vol.16 , pp. 671-682
    • Olsen, O.H.1    Rand, K.D.2    Ostergaard, H.3    Persson, E.4
  • 51
  • 52
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins: themes, variations, and therapeutic strategies
    • Gooptu B., Lomas D.A. Conformational pathology of the serpins: themes, variations, and therapeutic strategies. Annu Rev Biochem 2009, 78:147-176.
    • (2009) Annu Rev Biochem , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 53
    • 34547126694 scopus 로고    scopus 로고
    • Novel therapeutic strategies for the treatment of protein-misfolding diseases
    • Rochet J.C. Novel therapeutic strategies for the treatment of protein-misfolding diseases. Expert Rev Mol Med 2007, 9:1-34.
    • (2007) Expert Rev Mol Med , vol.9 , pp. 1-34
    • Rochet, J.C.1
  • 54
    • 0030062157 scopus 로고    scopus 로고
    • The biostructural pathology of the serpins: critical function of sheet opening mechanism
    • Carrell R.W., Stein P.E. The biostructural pathology of the serpins: critical function of sheet opening mechanism. Biol Chem Hoppe Seyler 1996, 377:1-17.
    • (1996) Biol Chem Hoppe Seyler , vol.377 , pp. 1-17
    • Carrell, R.W.1    Stein, P.E.2
  • 56
    • 57749176194 scopus 로고    scopus 로고
    • Modeling of factor XIII activation peptide (28-41) V34L mutant bound to thrombin
    • Nair D.G., Sunilkumar P.N., Sadasivan C. Modeling of factor XIII activation peptide (28-41) V34L mutant bound to thrombin. J Biomol Struct Dyn 2008, 26:387-394.
    • (2008) J Biomol Struct Dyn , vol.26 , pp. 387-394
    • Nair, D.G.1    Sunilkumar, P.N.2    Sadasivan, C.3
  • 57
    • 77951274153 scopus 로고    scopus 로고
    • Computer applications to prediction of protein-protein interactions and rational drug design
    • Grosdidier S., Totrov M., Fernandez-Recio J. Computer applications to prediction of protein-protein interactions and rational drug design. Adv Appl Bioinform Chem 2009, 2:101-123.
    • (2009) Adv Appl Bioinform Chem , vol.2 , pp. 101-123
    • Grosdidier, S.1    Totrov, M.2    Fernandez-Recio, J.3
  • 58
  • 59
    • 33846160915 scopus 로고    scopus 로고
    • Recent advances in serine protease inhibitors as anticoagulant agents
    • Prezelj A., Anderluh P.S., Peternel L., Urleb U. Recent advances in serine protease inhibitors as anticoagulant agents. Curr Pharm Des 2007, 13:287-312.
    • (2007) Curr Pharm Des , vol.13 , pp. 287-312
    • Prezelj, A.1    Anderluh, P.S.2    Peternel, L.3    Urleb, U.4
  • 60
    • 33947104111 scopus 로고    scopus 로고
    • Beyond heparin and warfarin: the new generation of anticoagulants
    • Weitz J.I., Linkins L.A. Beyond heparin and warfarin: the new generation of anticoagulants. Expert Opin Investig Drugs 2007, 16:271-282.
    • (2007) Expert Opin Investig Drugs , vol.16 , pp. 271-282
    • Weitz, J.I.1    Linkins, L.A.2
  • 61
    • 67849126841 scopus 로고    scopus 로고
    • Managing bleeding in anticoagulated patients with a focus on novel therapeutic agents
    • Crowther M.A., Warkentin T.E. Managing bleeding in anticoagulated patients with a focus on novel therapeutic agents. J Thromb Haemost 2009, 7(Suppl 1):107-110.
    • (2009) J Thromb Haemost , vol.7 , Issue.1 SUPPL , pp. 107-110
    • Crowther, M.A.1    Warkentin, T.E.2
  • 62
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: successes, failures and future prospects
    • Turk B. Targeting proteases: successes, failures and future prospects. Nat Rev Drug Discov 2006, 5:785-799.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 785-799
    • Turk, B.1
  • 63
    • 62249162857 scopus 로고    scopus 로고
    • Novel anticoagulants and the future of anticoagulation
    • Garcia D. Novel anticoagulants and the future of anticoagulation. Thromb Res 2009, 123(Suppl 4):S50-S55.
    • (2009) Thromb Res , vol.123 , Issue.4 SUPPL
    • Garcia, D.1
  • 64
    • 54949094382 scopus 로고    scopus 로고
    • Recent research developments in the direct inhibition of coagulation proteinases-inhibitors of the initiation phase
    • Henry B.L., Desai U.R. Recent research developments in the direct inhibition of coagulation proteinases-inhibitors of the initiation phase. Cardiovasc Hematol Agents Med Chem 2008, 6:323-336.
    • (2008) Cardiovasc Hematol Agents Med Chem , vol.6 , pp. 323-336
    • Henry, B.L.1    Desai, U.R.2
  • 66
    • 34249310268 scopus 로고    scopus 로고
    • Oral, direct factor Xa inhibitors in development for the prevention and treatment of thromboembolic diseases
    • Turpie A.G. Oral, direct factor Xa inhibitors in development for the prevention and treatment of thromboembolic diseases. Arterioscler Thromb Vasc Biol 2007, 27:1238-1247.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 1238-1247
    • Turpie, A.G.1
  • 67
    • 0346022974 scopus 로고    scopus 로고
    • Understanding protein-ligand interactions: the price of protein flexibility
    • Rauh D., Klebe G., Stubbs M.T. Understanding protein-ligand interactions: the price of protein flexibility. J Mol Biol 2004, 335:1325-1341.
    • (2004) J Mol Biol , vol.335 , pp. 1325-1341
    • Rauh, D.1    Klebe, G.2    Stubbs, M.T.3
  • 69
    • 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., Orwat M.J., Koch S., Rossi K.A., Alexander R.S., Smallwood A., Wong P.C., Rendina A.R., Luettgen J.M., Knabb R.M., 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 2007, 50:5339-5356.
    • (2007) J Med Chem , vol.50 , pp. 5339-5356
    • Pinto, D.J.1    Orwat, M.J.2    Koch, S.3    Rossi, K.A.4    Alexander, R.S.5    Smallwood, A.6    Wong, P.C.7    Rendina, A.R.8    Luettgen, J.M.9    Knabb, R.M.10
  • 70
    • 20144374942 scopus 로고    scopus 로고
    • Discovery of 1-(3′-aminobenzisoxazol-5′-yl)-3-trifluoromethyl-N-[2-fluoro-4-[(2′-dimethylaminomethyl)imidazol-1-yl]phenyl]-1H-pyrazole-5-carboxyamide hydrochloride (razaxaban), a highly potent, selective, and orally bioavailable factor Xa inhibitor
    • Quan M.L., Lam P.Y., Han Q., Pinto D.J., He M.Y., Li R., Ellis C.D., Clark C.G., Teleha C.A., Sun J.H., et al. Discovery of 1-(3′-aminobenzisoxazol-5′-yl)-3-trifluoromethyl-N-[2-fluoro-4-[(2′-dimethylaminomethyl)imidazol-1-yl]phenyl]-1H-pyrazole-5-carboxyamide hydrochloride (razaxaban), a highly potent, selective, and orally bioavailable factor Xa inhibitor. J Med Chem 2005, 48:1729-1744.
    • (2005) J Med Chem , vol.48 , pp. 1729-1744
    • Quan, M.L.1    Lam, P.Y.2    Han, Q.3    Pinto, D.J.4    He, M.Y.5    Li, R.6    Ellis, C.D.7    Clark, C.G.8    Teleha, C.A.9    Sun, J.H.10
  • 71
    • 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., Straub A., Pohlmann J., Lampe T., Pernerstorfer J., Schlemmer K.H., Reinemer P., Perzborn E. 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 2005, 48:5900-5908.
    • (2005) J Med Chem , vol.48 , pp. 5900-5908
    • Roehrig, S.1    Straub, A.2    Pohlmann, J.3    Lampe, T.4    Pernerstorfer, J.5    Schlemmer, K.H.6    Reinemer, P.7    Perzborn, E.8
  • 72
    • 13844319727 scopus 로고    scopus 로고
    • Pharmacophore identification, in silico screening, and virtual library design for inhibitors of the human factor Xa
    • Krovat E.M., Fruhwirth K.H., Langer T. Pharmacophore identification, in silico screening, and virtual library design for inhibitors of the human factor Xa. J Chem Inf Model 2005, 45:146-159.
    • (2005) J Chem Inf Model , vol.45 , pp. 146-159
    • Krovat, E.M.1    Fruhwirth, K.H.2    Langer, T.3
  • 73
    • 17144398395 scopus 로고    scopus 로고
    • Anchor-GRIND: filling the gap between standard 3D QSAR and the GRid-INdependent descriptors
    • Fontaine F., Pastor M., Zamora I., Sanz F. Anchor-GRIND: filling the gap between standard 3D QSAR and the GRid-INdependent descriptors. J Med Chem 2005, 48:2687-2694.
    • (2005) J Med Chem , vol.48 , pp. 2687-2694
    • Fontaine, F.1    Pastor, M.2    Zamora, I.3    Sanz, F.4
  • 76
    • 0842304437 scopus 로고    scopus 로고
    • Virtual screening with flexible docking and COMBINE-based models. Application to a series of factor Xa inhibitors
    • Murcia M., Ortiz A.R. Virtual screening with flexible docking and COMBINE-based models. Application to a series of factor Xa inhibitors. J Med Chem 2004, 47:805-820.
    • (2004) J Med Chem , vol.47 , pp. 805-820
    • Murcia, M.1    Ortiz, A.R.2
  • 77
    • 18344364519 scopus 로고    scopus 로고
    • Structural requirements for factor Xa inhibition by 3-oxybenzamides with neutral P1 substituents: combining X-ray crystallography, 3D-QSAR, and tailored scoring functions
    • Matter H., Will D.W., Nazare M., Schreuder H., Laux V., Wehner V. Structural requirements for factor Xa inhibition by 3-oxybenzamides with neutral P1 substituents: combining X-ray crystallography, 3D-QSAR, and tailored scoring functions. J Med Chem 2005, 48:3290-3312.
    • (2005) J Med Chem , vol.48 , pp. 3290-3312
    • Matter, H.1    Will, D.W.2    Nazare, M.3    Schreuder, H.4    Laux, V.5    Wehner, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.