메뉴 건너뛰기




Volumn 58, Issue 6, 2015, Pages 2799-2808

Discovery of novel P1 groups for coagulation factor VIIa inhibition using fragment-based screening

Author keywords

[No Author keywords available]

Indexed keywords

ARYL HALIDE DERIVATIVE; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING FACTOR 7A INHIBITOR; HETEROCYCLE DERIVATIVE; LACTAM; UNCLASSIFIED DRUG; HALOGEN; HETEROCYCLIC COMPOUND; SERINE PROTEINASE INHIBITOR;

EID: 84925935684     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm501982k     Document Type: Article
Times cited : (18)

References (76)
  • 2
    • 80052413972 scopus 로고    scopus 로고
    • Bleeding risk and reversal strategies for old and new anticoagulants and antiplatelet agents
    • Levi, M.; Eerenberg, E.; Kamphuisen, P. W. Bleeding risk and reversal strategies for old and new anticoagulants and antiplatelet agents Thromb. Haemostasis 2011, 9 (9) 1705-1712
    • (2011) Thromb. Haemostasis , vol.9 , Issue.9 , pp. 1705-1712
    • Levi, M.1    Eerenberg, E.2    Kamphuisen, P.W.3
  • 3
    • 0041829444 scopus 로고    scopus 로고
    • Oral ximelagatran for secondary prophylaxis after myocardial infarction: The ESTEEM randomised controlled trial
    • Wallentin, L.; Wilcox, R. G.; Weaver, W. D.; Emanuelsson, H.; Goodvin, A.; Nystrom, P.; Bylock, A. Oral ximelagatran for secondary prophylaxis after myocardial infarction: the ESTEEM randomised controlled trial Lancet 2003, 362 (9386) 789-797
    • (2003) Lancet , vol.362 , Issue.9386 , pp. 789-797
    • Wallentin, L.1    Wilcox, R.G.2    Weaver, W.D.3    Emanuelsson, H.4    Goodvin, A.5    Nystrom, P.6    Bylock, A.7
  • 7
    • 77955458657 scopus 로고    scopus 로고
    • BMS-593214, an active site-directed factor VIIa inhibitor: Enzyme kinetics, antithrombotic and antihaemostatic studies
    • Wong, P. C.; Luettgen, J. M.; Rendina, A. R.; Kettner, C. A.; Xin, B.; Knabb, R. M.; Wexler, R.; Priestley, E. S. BMS-593214, an active site-directed factor VIIa inhibitor: Enzyme kinetics, antithrombotic and antihaemostatic studies Thromb. Haemostasis 2010, 104 (2) 261-269
    • (2010) Thromb. Haemostasis , vol.104 , Issue.2 , pp. 261-269
    • Wong, P.C.1    Luettgen, J.M.2    Rendina, A.R.3    Kettner, C.A.4    Xin, B.5    Knabb, R.M.6    Wexler, R.7    Priestley, E.S.8
  • 8
    • 4444282406 scopus 로고    scopus 로고
    • Inhibitors of tissue factor•factor VIIa for anticoagulant therapy
    • Lazarus, R. A.; Olivero, A. G.; Eigenbrot, C.; Kirchhofer, D. Inhibitors of tissue factor•factor VIIa for anticoagulant therapy Curr. Med. Chem. 2004, 11, 2275-2290
    • (2004) Curr. Med. Chem. , vol.11 , pp. 2275-2290
    • Lazarus, R.A.1    Olivero, A.G.2    Eigenbrot, C.3    Kirchhofer, D.4
  • 9
    • 0041932150 scopus 로고    scopus 로고
    • Pharmacological interruption of acute thrombus formation with minimal hemorrhagic complications by a small molecule tissue factor/factor VIIa inhibitor: Comparison to factor Xa and thrombin inhibition in a nonhuman primate thrombosis model
    • Suleymanov, O. D.; Szalony, J. A.; Salyers, A. K.; Lachance, R. M.; Parlow, J. J.; South, M. S.; Wood, R. S.; Nicholson, N. S. Pharmacological interruption of acute thrombus formation with minimal hemorrhagic complications by a small molecule tissue factor/factor VIIa inhibitor: Comparison to factor Xa and thrombin inhibition in a nonhuman primate thrombosis model J. Pharmacol. Exp. Ther. 2003, 306, 1115-1121
    • (2003) J. Pharmacol. Exp. Ther. , vol.306 , pp. 1115-1121
    • Suleymanov, O.D.1    Szalony, J.A.2    Salyers, A.K.3    Lachance, R.M.4    Parlow, J.J.5    South, M.S.6    Wood, R.S.7    Nicholson, N.S.8
  • 10
    • 10744220161 scopus 로고    scopus 로고
    • Administration of a small molecule tissue factor/factor VIIa inhibitor in a non-human primate thrombosis model of venous thrombosis: Effects on thrombus formation and bleeding time
    • Szalony, J. A.; Suleymanov, O. D.; Salyers, A. K.; Panzer-Knodle, S. G.; Blom, J. D.; LaChance, R. M.; Case, B. L.; Parlow, J. J.; South, M. S.; Wood, R. S.; Nicholson, N. S. Administration of a small molecule tissue factor/factor VIIa inhibitor in a non-human primate thrombosis model of venous thrombosis: Effects on thrombus formation and bleeding time Thromb Res. 2003, 112, 167-174
    • (2003) Thromb Res. , vol.112 , pp. 167-174
    • Szalony, J.A.1    Suleymanov, O.D.2    Salyers, A.K.3    Panzer-Knodle, S.G.4    Blom, J.D.5    Lachance, R.M.6    Case, B.L.7    Parlow, J.J.8    South, M.S.9    Wood, R.S.10    Nicholson, N.S.11
  • 11
    • 0347418242 scopus 로고    scopus 로고
    • Assessment of bleeding propensity in non-human primates by combination of selective tissue factor/VIIa inhibition and aspirin compared to warfarin and aspirin treatment
    • Salyers, A. K.; Szalony, J. A.; Suleymanov, O. D.; Parlow, J. J.; Wood, R. S.; South, M. S.; Nicholson, N. S. Assessment of bleeding propensity in non-human primates by combination of selective tissue factor/VIIa inhibition and aspirin compared to warfarin and aspirin treatment Pharmacology 2004, 70, 100-106
    • (2004) Pharmacology , vol.70 , pp. 100-106
    • Salyers, A.K.1    Szalony, J.A.2    Suleymanov, O.D.3    Parlow, J.J.4    Wood, R.S.5    South, M.S.6    Nicholson, N.S.7
  • 12
    • 0037541104 scopus 로고    scopus 로고
    • Pharmacological intervention at disparate sites in the coagulation cascade: Comparison of anti-thrombotic efficacy vs bleeding propensity in a rat model of acute arterial thrombosis
    • Szalony, J. A.; Taite, B. B.; Girard, T. J.; Nicholson, N. S.; LaChance, R. M. Pharmacological intervention at disparate sites in the coagulation cascade: comparison of anti-thrombotic efficacy vs bleeding propensity in a rat model of acute arterial thrombosis J. Thromb. Thrombolysis 2002, 14 (2) 113-121
    • (2002) J. Thromb. Thrombolysis , vol.14 , Issue.2 , pp. 113-121
    • Szalony, J.A.1    Taite, B.B.2    Girard, T.J.3    Nicholson, N.S.4    Lachance, R.M.5
  • 14
    • 0031649079 scopus 로고    scopus 로고
    • Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa
    • Ruf, W.; Dickinson, C. D. Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa Trends Cardiovasc. Med. 1998, 8 (8) 350-356
    • (1998) Trends Cardiovasc. Med. , vol.8 , Issue.8 , pp. 350-356
    • Ruf, W.1    Dickinson, C.D.2
  • 16
    • 79959569996 scopus 로고    scopus 로고
    • Allosteric activation of coagulation factor VIIa
    • Persson, E.; Olsen, O. H. Allosteric activation of coagulation factor VIIa Front. Biosci., Landmark Ed. 2011, 16, 3156-3163
    • (2011) Front. Biosci., Landmark Ed. , vol.16 , pp. 3156-3163
    • Persson, E.1    Olsen, O.H.2
  • 17
    • 0842283889 scopus 로고    scopus 로고
    • Similar molecular interactions of factor VII and factor VIIa with the tissue factor region that allosterically regulates enzyme activity
    • Kelley, R. F.; Yang, J.; Eigenbrot, C.; Moran, P.; Peek, M.; Lipari, M. T.; Kirchhofer, D. Similar molecular interactions of factor VII and factor VIIa with the tissue factor region that allosterically regulates enzyme activity Biochemistry 2004, 43 (5) 1223-1229
    • (2004) Biochemistry , vol.43 , Issue.5 , pp. 1223-1229
    • Kelley, R.F.1    Yang, J.2    Eigenbrot, C.3    Moran, P.4    Peek, M.5    Lipari, M.T.6    Kirchhofer, D.7
  • 18
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I.; Berger, A. On the size of the active site in proteases. I. Papain Biochem. Biophys. Res. Commun. 1967, 27 (2) 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , Issue.2 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 19
    • 84969528333 scopus 로고    scopus 로고
    • Principles of enzyme-inhibitor design
    • Banner, D. W. Principles of enzyme-inhibitor design Methods Princ. Med. Chem. 2003, 19, 163-185
    • (2003) Methods Princ. Med. Chem. , vol.19 , pp. 163-185
    • Banner, D.W.1
  • 20
    • 84925932488 scopus 로고    scopus 로고
    • Although the structure of the Michaelis factor VIIa/substrate complex is unknown, the subsites S1′, S1, S2, etc. binding P1′, P1, P2, etc. substrate amino acids can be inferred from crystallographic structures of factor VIIa bound with peptide-like structures. See, for example, the crystallographic structures of several tripeptide mimetics bound to factor VIIa, PDBID 1W0Y, 1W2K, 1W7X, 1W8B, 1WQV, 1WSS, 1WTG, 1WUN, and 1WV7, as well as BPTI bound to factor VIIa (PDBID 1FAK)
    • Although the structure of the Michaelis factor VIIa/substrate complex is unknown, the subsites S1′, S1, S2, etc. binding P1′, P1, P2, etc. substrate amino acids can be inferred from crystallographic structures of factor VIIa bound with peptide-like structures. See, for example, the crystallographic structures of several tripeptide mimetics bound to factor VIIa, PDBID 1W0Y, 1W2K, 1W7X, 1W8B, 1WQV, 1WSS, 1WTG, 1WUN, and 1WV7, as well as BPTI bound to factor VIIa (PDBID 1FAK).
  • 27
    • 0027761152 scopus 로고
    • A genetic selection elucidates structural determinants of arginine versus lysine specificity in trypsin
    • Perona, J. J.; Evnin, L. B.; Craik, C. S. A genetic selection elucidates structural determinants of arginine versus lysine specificity in trypsin Gene 1993, 137 (1) 121-126
    • (1993) Gene , vol.137 , Issue.1 , pp. 121-126
    • Perona, J.J.1    Evnin, L.B.2    Craik, C.S.3
  • 29
    • 84925932487 scopus 로고    scopus 로고
    • Discovery of pyrazole based geminally substituted p4 groups as potent, selective, and orally bioavailable inhibitors of blood coagulation factor xa
    • American Chemical Society: Washington, DC, MEDI-436
    • Orwat, M. J.; Rossi, K. A.; Luettgen, J.; Knabb, R. M.; He, K.; Wexler, R. R.; Lam, P. Y. S.; Pinto, D. J. Discovery of pyrazole based geminally substituted p4 groups as potent, selective, and orally bioavailable inhibitors of blood coagulation factor xa. Abstracts of Papers, 238th ACS National Meeting; American Chemical Society: Washington, DC, 2009; MEDI-436.
    • (2009) Abstracts of Papers, 238th ACS National Meeting
    • Orwat, M.J.1    Rossi, K.A.2    Luettgen, J.3    Knabb, R.M.4    He, K.5    Wexler, R.R.6    Lam, P.Y.S.7    Pinto, D.J.8
  • 30
    • 47149111206 scopus 로고    scopus 로고
    • Achieving structural diversity using the perpendicular conformation of alpha-substituted phenylcyclopropanes to mimic the bioactive conformation of ortho-substituted biphenyl P4 moieties: Discovery of novel, highly potent inhibitors of Factor Xa
    • Qiao, J. X.; Cheney, D. L.; Alexander, R. S.; Smallwood, A. M.; King, S. R.; He, K.; Rendina, A. R.; Luettgen, J. M.; Knabb, R. M.; Wexler, R. R.; Lam, P. Y. S. Achieving structural diversity using the perpendicular conformation of alpha-substituted phenylcyclopropanes to mimic the bioactive conformation of ortho-substituted biphenyl P4 moieties: Discovery of novel, highly potent inhibitors of Factor Xa Bioorg. Med. Chem. Lett. 2008, 18 (14) 4118-4123
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , Issue.14 , pp. 4118-4123
    • Qiao, J.X.1    Cheney, D.L.2    Alexander, R.S.3    Smallwood, A.M.4    King, S.R.5    He, K.6    Rendina, A.R.7    Luettgen, J.M.8    Knabb, R.M.9    Wexler, R.R.10    Lam, P.Y.S.11
  • 32
    • 34547898374 scopus 로고    scopus 로고
    • Enantiopure five-membered cyclic diamine derivatives as potent and selective inhibitors of factor Xa. Improving in vitro metabolic stability via core modifications
    • Qiao, J. X.; Wang, T. C.; Wang, G. Z.; Cheney, D. L.; He, K.; Rendina, A. R.; Xin, B.; Luettgen, J. M.; Knabb, R. M.; Wexler, R. R.; Lam, P. Y. S. Enantiopure five-membered cyclic diamine derivatives as potent and selective inhibitors of factor Xa. Improving in vitro metabolic stability via core modifications Bioorg. Med. Chem. Lett. 2007, 17 (18) 5041-5048
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , Issue.18 , pp. 5041-5048
    • Qiao, J.X.1    Wang, T.C.2    Wang, G.Z.3    Cheney, D.L.4    He, K.5    Rendina, A.R.6    Xin, B.7    Luettgen, J.M.8    Knabb, R.M.9    Wexler, R.R.10    Lam, P.Y.S.11
  • 33
    • 35848929515 scopus 로고    scopus 로고
    • Discovery of 1-(4-Methoxyphenyl)-7-oxo-6-[4-(2-oxo-1-piperidinyl]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. P.; 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.; He, K.; Xin, B.; Wexler, R. R.; Lam, P. Y. S. Discovery of 1-(4-Methoxyphenyl)-7-oxo-6-[4-(2-oxo-1-piperidinyl]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 (22) 5339-5356
    • (2007) J. Med. Chem. , vol.50 , Issue.22 , pp. 5339-5356
    • Pinto, D.J.P.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    He, K.11    Xin, B.12    Wexler, R.R.13    Lam, P.Y.S.14
  • 34
    • 0037468471 scopus 로고    scopus 로고
    • Molecular structures of human factor Xa complexed with ketopiperazine inhibitors: Preference for a neutral group in the S1 pocket
    • Maignan, S.; Guilloteau, J. P.; Choi-Sledeski, Y. M.; Becker, M. R.; Ewing, W. R.; Pauls, H. W.; Spada, A. P.; Mikol, V. Molecular structures of human factor Xa complexed with ketopiperazine inhibitors: Preference for a neutral group in the S1 pocket J. Med. Chem. 2003, 46 (5) 685-690
    • (2003) J. Med. Chem. , vol.46 , Issue.5 , pp. 685-690
    • Maignan, S.1    Guilloteau, J.P.2    Choi-Sledeski, Y.M.3    Becker, M.R.4    Ewing, W.R.5    Pauls, H.W.6    Spada, A.P.7    Mikol, V.8
  • 35
    • 84864878309 scopus 로고    scopus 로고
    • Fragment-based Lead Discovery and Optimization Using X-Ray Crystallography, Computational Chemistry, and High-throughput Organic Synthesis
    • In; Wiley-VCH Verlag GmbH & Co. KGaA: Weinheim, Germany
    • Blaney, J.; Nienaber, V.; Burley, S. K., Fragment-based Lead Discovery and Optimization Using X-Ray Crystallography, Computational Chemistry, and High-throughput Organic Synthesis. In Fragment-based Approaches in Drug Discovery; Wiley-VCH Verlag GmbH & Co. KGaA: Weinheim, Germany, 2006; pp 215-248.
    • (2006) Fragment-based Approaches in Drug Discovery , pp. 215-248
    • Blaney, J.1    Nienaber, V.2    Burley, S.K.3
  • 36
    • 84925932486 scopus 로고    scopus 로고
    • Available Chemicals Directory; Accelrys, I. 5005 Wateridge Vista Drive, San Diego, CA 92121, USA
    • Available Chemicals Directory; Accelrys, I., 5005 Wateridge Vista Drive, San Diego, CA 92121, USA; accelrys.com.
  • 37
    • 84925932485 scopus 로고    scopus 로고
    • Pipeline Pilot; Accelrys, I. 5005 Wateridge Vista Drive, San Diego, CA 92121, USA
    • Pipeline Pilot; Accelrys, I., 5005 Wateridge Vista Drive, San Diego, CA 92121, USA; accelrys.com.
  • 38
    • 33845379303 scopus 로고
    • Atom pairs as molecular features in structure-activity studies: Definition and applications
    • Carhart, R. E.; Smith, D. H.; Venkataraghavan, R. Atom pairs as molecular features in structure-activity studies: definition and applications J. Chem. Inf. Comput. Sci. 1985, 25 (2) 64-73
    • (1985) J. Chem. Inf. Comput. Sci. , vol.25 , Issue.2 , pp. 64-73
    • Carhart, R.E.1    Smith, D.H.2    Venkataraghavan, R.3
  • 39
    • 33750124980 scopus 로고    scopus 로고
    • Extra Precision Glide: Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein-ligand Complexes
    • Friesner, R. A.; Murphy, R. B.; Repasky, M. P.; Frye, L. L.; Greenwood, J. R.; Halgren, T. A.; Sanschagrin, P.; Mainz, D. T. Extra Precision Glide: Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein-ligand Complexes J. Med. Chem. 2006, 49 (21) 6177-6196
    • (2006) J. Med. Chem. , vol.49 , Issue.21 , pp. 6177-6196
    • Friesner, R.A.1    Murphy, R.B.2    Repasky, M.P.3    Frye, L.L.4    Greenwood, J.R.5    Halgren, T.A.6    Sanschagrin, P.7    Mainz, D.T.8
  • 41
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A New Approach for Rapid, Accurate Docking and Scoring. 2. Enrichment Factors in Database Screening
    • Halgren, T. A.; Murphy, R. B.; Friesner, R. A.; Beard, H. S.; Frye, L. L.; Pollard, W. T.; Banks, J. L. Glide: A New Approach for Rapid, Accurate Docking and Scoring. 2. Enrichment Factors in Database Screening J. Med. Chem. 2004, 47 (7) 1750-1759
    • (2004) J. Med. Chem. , vol.47 , Issue.7 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6    Banks, J.L.7
  • 43
    • 84925947180 scopus 로고    scopus 로고
    • Toward the development of an accurate virtual screening protocol: Recent improvements in protein ensemble docking
    • American Chemical Society: Washington, DC, COMP
    • Mueller, L.; Cheney, D. L. Toward the development of an accurate virtual screening protocol: Recent improvements in protein ensemble docking. Abstracts of Papers, 230th ACS National Meeting, Washington, DC, United States, Aug. 28-Sept. 1; American Chemical Society: Washington, DC, 2005; COMP- 163.
    • (2005) Abstracts of Papers, 230th ACS National Meeting, Washington, DC, United States, Aug. 28-Sept. 1 , pp. 163
    • Mueller, L.1    Cheney, D.L.2
  • 46
    • 84925932483 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Version 1.5.0.4, Schrodinger, LLC
    • The PyMOL Molecular Graphics System, Version 1.5.0.4, Schrodinger, LLC.
  • 47
    • 84925932482 scopus 로고    scopus 로고
    • Schrodinger Release 2013-3, Maestro, version 9.6, Schrodinger, LLC, New York, NY
    • Schrodinger Release 2013-3, Maestro, version 9.6, Schrodinger, LLC, New York, NY, 2013.
    • (2013)
  • 50
    • 0034055545 scopus 로고    scopus 로고
    • Structural changes in a cryo-cooled protein crystal owing to radiation damage
    • Burmeister, W. P. Structural changes in a cryo-cooled protein crystal owing to radiation damage Acta Crystallogr., Sect. D: Biol. Crystallogr. 2000, 56 (3) 328-341
    • (2000) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.56 , Issue.3 , pp. 328-341
    • Burmeister, W.P.1
  • 52
    • 84925932480 scopus 로고    scopus 로고
    • Evaluation of several correlated electronic methods in the context of calculations common to drug design
    • American Chemical Society: Washington, DC, COMP-22
    • Cheney, D. L.; Rossi, K. A. Evaluation of several correlated electronic methods in the context of calculations common to drug design. Abstracts of Papers, 235th ACS National Meeting, New Orleans, LA, United States, April 6-10; American Chemical Society: Washington, DC, 2008; COMP-22.
    • (2008) Abstracts of Papers, 235th ACS National Meeting, New Orleans, LA, United States, April 6-10
    • Cheney, D.L.1    Rossi, K.A.2
  • 53
    • 84925932480 scopus 로고    scopus 로고
    • Comparison of DFT and MP2-based electronic models in the estimation of relative conformational and tautomeric energies and torsional potentials of drug-like moieties
    • American Chemical Society: Washington, DC, COMP-143
    • Cheney, D. L.; Rossi, K. A. Comparison of DFT and MP2-based electronic models in the estimation of relative conformational and tautomeric energies and torsional potentials of drug-like moieties. Abstracts of Papers, 235th ACS National Meeting, New Orleans, LA, United States, April 6-10; American Chemical Society: Washington, DC, 2008; COMP-143.
    • (2008) Abstracts of Papers, 235th ACS National Meeting, New Orleans, LA, United States, April 6-10
    • Cheney, D.L.1    Rossi, K.A.2
  • 55
    • 0001109389 scopus 로고
    • Stereochemistry of reaction paths at carbonyl centres
    • Burgi, H. B.; Dunitz, J. D.; Lehn, J. M.; Wipff, G. Stereochemistry of reaction paths at carbonyl centres Tetrahedron 1974, 30 (12) 1563-1572
    • (1974) Tetrahedron , vol.30 , Issue.12 , pp. 1563-1572
    • Burgi, H.B.1    Dunitz, J.D.2    Lehn, J.M.3    Wipff, G.4
  • 56
    • 84925932479 scopus 로고    scopus 로고
    • Private communication
    • Friesner, R. A. Private communication, 2004.
    • (2004)
    • Friesner, R.A.1
  • 58
    • 84874582783 scopus 로고    scopus 로고
    • Intimate Interactions with Carbonyl Groups: Dipole-Dipole or n
    • Kamer, K. J.; Choudhary, A.; Raines, R. T. Intimate Interactions with Carbonyl Groups: Dipole-Dipole or n J. Org. Chem. 2013, 78 (5) 2099-2103
    • (2013) J. Org. Chem. , vol.78 , Issue.5 , pp. 2099-2103
    • Kamer, K.J.1    Choudhary, A.2    Raines, R.T.3
  • 59
    • 0033455572 scopus 로고    scopus 로고
    • Carbonyl-carbonyl interactions stabilize the partially allowed Ramachandran conformations of asparagine and aspartic acid
    • Deane, C. M.; Allen, F. H.; Taylor, R.; Blundell, T. L. Carbonyl-carbonyl interactions stabilize the partially allowed Ramachandran conformations of asparagine and aspartic acid Protein Eng. 1999, 12 (12) 1025-1028
    • (1999) Protein Eng. , vol.12 , Issue.12 , pp. 1025-1028
    • Deane, C.M.1    Allen, F.H.2    Taylor, R.3    Blundell, T.L.4
  • 62
    • 3242739976 scopus 로고    scopus 로고
    • PAMPA - A drug absorption in vitro model 11. Matching the in vivo unstirred water layer thickness by individual-well stirring in microtitre plates
    • Avdeef, A.; Nielsen, P. E.; Tsinman, O. PAMPA - a drug absorption in vitro model 11. Matching the in vivo unstirred water layer thickness by individual-well stirring in microtitre plates Eur. J. Pharm. Sci. 2004, 22 (5) 365-374
    • (2004) Eur. J. Pharm. Sci. , vol.22 , Issue.5 , pp. 365-374
    • Avdeef, A.1    Nielsen, P.E.2    Tsinman, O.3
  • 64
    • 84903545297 scopus 로고    scopus 로고
    • Ensemble generation and the influence of protein flexibility on geometric tunnel prediction in cytochrome P450 enzymes
    • Kingsley, L. J.; Lill, M. A. Ensemble generation and the influence of protein flexibility on geometric tunnel prediction in cytochrome P450 enzymes PloS One 2014, 9 (6 e99408
    • (2014) PloS One , vol.9 , Issue.6 , pp. 99408
    • Kingsley, L.J.1    Lill, M.A.2
  • 65
    • 84904976112 scopus 로고    scopus 로고
    • Ensemble-Based Docking Using Biased Molecular Dynamics
    • Campbell, A. J.; Lamb, M. L.; Joseph-McCarthy, D. Ensemble-Based Docking Using Biased Molecular Dynamics J. Chem. Inf. Model. 2014, 54 (7) 2127-2138
    • (2014) J. Chem. Inf. Model. , vol.54 , Issue.7 , pp. 2127-2138
    • Campbell, A.J.1    Lamb, M.L.2    Joseph-Mccarthy, D.3
  • 66
    • 0027022713 scopus 로고
    • Expression and purification of a soluble tissue factor fusion protein with an epitope for an unusual calcium-dependent antibody
    • Rezaie, A. R.; Fiore, M. M.; Neuenschwander, P. F.; Esmon, C. T.; Morrissey, J. H. Expression and purification of a soluble tissue factor fusion protein with an epitope for an unusual calcium-dependent antibody Protein Expression Purif. 1992, 3 (6) 453-460
    • (1992) Protein Expression Purif. , vol.3 , Issue.6 , pp. 453-460
    • Rezaie, A.R.1    Fiore, M.M.2    Neuenschwander, P.F.3    Esmon, C.T.4    Morrissey, J.H.5
  • 67
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy
    • Mayer, M.; Meyer, B. Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy Angew. Chem., Int. Ed. 1999, 38 (12) 1784-1788
    • (1999) Angew. Chem., Int. Ed. , vol.38 , Issue.12 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 69
    • 84925932477 scopus 로고    scopus 로고
    • CNX; Accelrys, I. 5005 Wateridge Vista Drive, San Diego, CA 92121, USA
    • CNX; Accelrys, I., 5005 Wateridge Vista Drive, San Diego, CA 92121, USA; accelrys.com.
  • 70
    • 84925932476 scopus 로고    scopus 로고
    • Quanta; Accelrys, I. 5005 Wateridge Vista Drive, San Diego, CA 92121, USA
    • Quanta; Accelrys, I., 5005 Wateridge Vista Drive, San Diego, CA 92121, USA; accelrys.com.
  • 73
    • 33947119575 scopus 로고    scopus 로고
    • Protonation Changes upon Ligand Binding to Trypsin and Thrombin: Structural Interpretation Based on pKa Calculations and ITC Experiments
    • Czodrowski, P.; Sotriffer, C. A.; Klebe, G. Protonation Changes upon Ligand Binding to Trypsin and Thrombin: Structural Interpretation Based on pKa Calculations and ITC Experiments J. Mol. Biol. 2007, 367 (5) 1347-1356
    • (2007) J. Mol. Biol. , vol.367 , Issue.5 , pp. 1347-1356
    • Czodrowski, P.1    Sotriffer, C.A.2    Klebe, G.3
  • 75
    • 84925932474 scopus 로고    scopus 로고
    • Prime, version 1.5112, Schrodinger, LLC, New York, NY
    • Prime, version 1.5112, Schrodinger, LLC, New York, NY, 2006.
    • (2006)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.