메뉴 건너뛰기




Volumn , Issue , 2008, Pages 605-634

Protein Crystallography and Drug Discovery

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77956304898     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374194-3.00030-5     Document Type: Chapter
Times cited : (5)

References (191)
  • 3
    • 33745161050 scopus 로고    scopus 로고
    • Structural biology and drug discovery
    • Scapin G. Structural biology and drug discovery. Curr. Pharm. Design, 2006, 12:2087-2097.
    • (2006) Curr. Pharm. Design, , vol.12 , pp. 2087-2097
    • Scapin, G.1
  • 4
    • 32544452857 scopus 로고    scopus 로고
    • A critical appraisal of structure-based drug design
    • Tintelnot-Blomley M., Lewis R.A. A critical appraisal of structure-based drug design. IDrugs, 2006, 9:114-118.
    • (2006) IDrugs, , vol.9 , pp. 114-118
    • Tintelnot-Blomley, M.1    Lewis, R.A.2
  • 5
    • 6444234760 scopus 로고    scopus 로고
    • A guide to drug discovery: the role of the medicinal chemist in drug discovery - then and now
    • Lombardino J.G., Lowe J.A. A guide to drug discovery: the role of the medicinal chemist in drug discovery - then and now. Nat. Rev. Drug Discov. 2004, 3:853-862.
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 853-862
    • Lombardino, J.G.1    Lowe, J.A.2
  • 6
    • 22544461068 scopus 로고    scopus 로고
    • Recent applications of protein crystallography and structure-guided drug design
    • Williams S.P., Kuyper L.F., Pearce K.H. Recent applications of protein crystallography and structure-guided drug design. Curr. Opin. Chem. Biol. 2005, 9:371-380.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 371-380
    • Williams, S.P.1    Kuyper, L.F.2    Pearce, K.H.3
  • 7
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell T.L., Jhoti H., Abell C. High-throughput crystallography for lead discovery in drug design. Nat. Rev. Drug Discov. 2002, 1:45-54.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 8
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: strategic advances and lessons learned
    • Hajduk P.J., Greer J. A decade of fragment-based drug design: strategic advances and lessons learned. Nat. Rev. Drug Discov. 2006, 6:211-219.
    • (2006) Nat. Rev. Drug Discov. , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 10
    • 33751290908 scopus 로고    scopus 로고
    • Structural genomics for membrane proteins
    • Lundström K. Structural genomics for membrane proteins. Cell. Mol. Life Sci. 2006, 63:2597-2607.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2597-2607
    • Lundström, K.1
  • 12
    • 36949066642 scopus 로고
    • Structure of haemoglobin-3-dimensional fourier synthesis at 5.5-A resolution, obtained by X-ray analysis
    • Perutz M.F., Rossmann M.G., Cullis A.F., Muirhead H., Will G., North A.C.T. Structure of haemoglobin-3-dimensional fourier synthesis at 5.5-A resolution, obtained by X-ray analysis. Nature, 1960, 185:416-422.
    • (1960) Nature, , vol.185 , pp. 416-422
    • Perutz, M.F.1    Rossmann, M.G.2    Cullis, A.F.3    Muirhead, H.4    Will, G.5    North, A.C.T.6
  • 13
    • 0026122183 scopus 로고
    • A brief history of protein crystal growth
    • McPherson A. A brief history of protein crystal growth. J. Cryst. Growth, 1991, 110:1-10.
    • (1991) J. Cryst. Growth, , vol.110 , pp. 1-10
    • McPherson, A.1
  • 14
    • 0000474342 scopus 로고
    • Evidence for 2-chain helix in crystalline structure of sodium deoxyribonucleate
    • Franklin R.E., Gosling R.G. Evidence for 2-chain helix in crystalline structure of sodium deoxyribonucleate. Nature, 1953, 172:156-157.
    • (1953) Nature, , vol.172 , pp. 156-157
    • Franklin, R.E.1    Gosling, R.G.2
  • 15
    • 36949070206 scopus 로고
    • Helical structure of crystalline deoxypentose nucleic acid
    • Wilkins M.H.F., Seeds W.E., Stokes A.R., Wilson H.R. Helical structure of crystalline deoxypentose nucleic acid. Nature, 1953, 172:759-762.
    • (1953) Nature, , vol.172 , pp. 759-762
    • Wilkins, M.H.F.1    Seeds, W.E.2    Stokes, A.R.3    Wilson, H.R.4
  • 16
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids - a structure for deoxyribose nucleic acid
    • Watson J.D., Crick F.H.C. Molecular structure of nucleic acids - a structure for deoxyribose nucleic acid. Nature, 1953, 171:737-738.
    • (1953) Nature, , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 19
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3A ring; resolution
    • Deisenhofer J., Epp O., Miki K., Huber R., Michel H. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3Å resolution. Nature, 1985, 318:618-624.
    • (1985) Nature, , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 20
    • 0028114231 scopus 로고
    • Structure at 2.8 A ring; resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G., Lutter R., Walker J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature, 1994, 370:621-628.
    • (1994) Nature, , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 21
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A ring; resolution
    • Löwe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science, 1995, 268:533-539.
    • (1995) Science, , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 23
    • 0034704217 scopus 로고    scopus 로고
    • The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit
    • Brodersen D.E., Clemons W.M., Carter A.P., Morgan-Warren R.J., Wimberly B.T., Ramakrishnan V. The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit. Cell, 2000, 103:1143-1154.
    • (2000) Cell, , vol.103 , pp. 1143-1154
    • Brodersen, D.E.1    Clemons, W.M.2    Carter, A.P.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 24
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science, 2000, 289:905-920.
    • (2000) Science, , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 25
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A. The structural basis of ribosome activity in peptide bond synthesis. Science, 2000, 289:920-930.
    • (2000) Science, , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 27
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A ring; resolution
    • Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 Å resolution. Science, 2001, 292:1876-1882.
    • (2001) Science, , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 29
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature, 2002, 417:515-522.
    • (2002) Nature, , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 30
    • 0038198865 scopus 로고    scopus 로고
    • High-throughput crystallography to enhance drug discovery
    • Sharff A., Jhoti H. High-throughput crystallography to enhance drug discovery. Curr. Opin. Chem. Biol. 2003, 7:340-345.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 340-345
    • Sharff, A.1    Jhoti, H.2
  • 31
    • 16644368493 scopus 로고    scopus 로고
    • APRV - a program for automated data processing, refinement and visualization
    • Kroemer M., Dreyer M.K., Wendt K.U. APRV - a program for automated data processing, refinement and visualization. Acta Cryst. D 2004, 60:1679-1682.
    • (2004) Acta Cryst. D , vol.60 , pp. 1679-1682
    • Kroemer, M.1    Dreyer, M.K.2    Wendt, K.U.3
  • 34
    • 0036913881 scopus 로고    scopus 로고
    • Veni, vidi, vici - atomic resolution unraveling the mysteries of protein function
    • Schmidt A., Lamzin V.S. Veni, vidi, vici - atomic resolution unraveling the mysteries of protein function. Curr. Opin. Struct. Biol. 2002, 12:698-703.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 698-703
    • Schmidt, A.1    Lamzin, V.S.2
  • 35
    • 4644359235 scopus 로고    scopus 로고
    • Protein crystallography at subatomic resolution
    • Petrova T., Podjarny A. Protein crystallography at subatomic resolution. Rep. Prog. Phys. 2004, 67:1565-1605.
    • (2004) Rep. Prog. Phys. , vol.67 , pp. 1565-1605
    • Petrova, T.1    Podjarny, A.2
  • 39
    • 0017578611 scopus 로고
    • Design of specific inhibitors of angiotensin-converting enzyme - new class of orally active antihypertensive agents
    • Ondetti M.A., Cushman D.W. Design of specific inhibitors of angiotensin-converting enzyme - new class of orally active antihypertensive agents. Science 1977, 196:441-444.
    • (1977) Science , vol.196 , pp. 441-444
    • Ondetti, M.A.1    Cushman, D.W.2
  • 40
    • 3042732126 scopus 로고    scopus 로고
    • Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme
    • Natesh R., Schwager S.L.U., Evans H.R., Sturrock E.D., Acharya K.R. Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme. Biochemistry, 2004, 43:8718-8724.
    • (2004) Biochemistry, , vol.43 , pp. 8718-8724
    • Natesh, R.1    Schwager, S.L.U.2    Evans, H.R.3    Sturrock, E.D.4    Acharya, K.R.5
  • 41
    • 34248221658 scopus 로고    scopus 로고
    • The structure of testis angiotensin-converting enzyme in complex with the C domain-specific inhibitor RXPA380
    • Corradi H.R., Chitapi I., Sewell B.T., Georgiadis D., Dive V., Sturrock E.D., Acharya K.R. The structure of testis angiotensin-converting enzyme in complex with the C domain-specific inhibitor RXPA380. Biochemistry, 2007, 46:5473-5478.
    • (2007) Biochemistry, , vol.46 , pp. 5473-5478
    • Corradi, H.R.1    Chitapi, I.2    Sewell, B.T.3    Georgiadis, D.4    Dive, V.5    Sturrock, E.D.6    Acharya, K.R.7
  • 42
    • 0024218271 scopus 로고
    • Refined structure of human carbonic anhydrase II at 2.0 A ring; resolution
    • Eriksson A.E., Jones T.A., Liljas A. Refined structure of human carbonic anhydrase II at 2.0 Å resolution. Proteins, 1988, 4:274-282.
    • (1988) Proteins, , vol.4 , pp. 274-282
    • Eriksson, A.E.1    Jones, T.A.2    Liljas, A.3
  • 44
    • 3442883664 scopus 로고    scopus 로고
    • Carbonic anhydrases: current state of the art, therapeutic applications and future prospects
    • Pastorekova S., Parkkila S., Pastorek J., Supuran C.T. Carbonic anhydrases: current state of the art, therapeutic applications and future prospects. J. Enzyme Inhib. Med. Chem. 2004, 19:199-229.
    • (2004) J. Enzyme Inhib. Med. Chem. , vol.19 , pp. 199-229
    • Pastorekova, S.1    Parkkila, S.2    Pastorek, J.3    Supuran, C.T.4
  • 45
    • 0030772018 scopus 로고    scopus 로고
    • Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine
    • Briganti F., Mangani S., Orioli P., Scozzafava A., Vernaglione G., Supuran C.T. Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine. Biochemistry, 1997, 36:10384-10392.
    • (1997) Biochemistry, , vol.36 , pp. 10384-10392
    • Briganti, F.1    Mangani, S.2    Orioli, P.3    Scozzafava, A.4    Vernaglione, G.5    Supuran, C.T.6
  • 46
    • 0030875781 scopus 로고    scopus 로고
    • 'Flu' and structure-based drug design
    • Wade R.C. 'Flu' and structure-based drug design. Structure, 1997, 5:1139-1145.
    • (1997) Structure, , vol.5 , pp. 1139-1145
    • Wade, R.C.1
  • 47
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A ring; resolution
    • Varghese J.N., Laver W.G., Colman P.M. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature, 1983, 303:35-40.
    • (1983) Nature, , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 48
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman P.M., Varghese J.N., Laver W.G. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature, 1983, 303:41-44.
    • (1983) Nature, , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 49
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford P.J. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 1985, 28:849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 51
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • Kim C.U., Lew W., Williams M.A., Liu H., Zhang L., Swaminathan S., Bishofberger N., Chen M.S., Mendel D.B., Tai C.Y., Laver W.G., Stevens R.C. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J. Am. Chem. Soc. 1997, 119:681-690.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3    Liu, H.4    Zhang, L.5    Swaminathan, S.6    Bishofberger, N.7    Chen, M.S.8    Mendel, D.B.9    Tai, C.Y.10    Laver, W.G.11    Stevens, R.C.12
  • 52
    • 4644248792 scopus 로고    scopus 로고
    • Recent advances in the design of matrix metalloprotease inhibitors
    • Matter H., Schudok M. Recent advances in the design of matrix metalloprotease inhibitors. Curr. Opin. Drug Discov. Dev. 2004, 7:513-535.
    • (2004) Curr. Opin. Drug Discov. Dev. , vol.7 , pp. 513-535
    • Matter, H.1    Schudok, M.2
  • 53
    • 1842431419 scopus 로고    scopus 로고
    • High-throughput structural biology in drug discovery: protein kinases
    • Stout T.J., Foster P.G., Matthews D.J. High-throughput structural biology in drug discovery: protein kinases. Curr. Pharm. Design, 2004, 10:1069-1082.
    • (2004) Curr. Pharm. Design, , vol.10 , pp. 1069-1082
    • Stout, T.J.1    Foster, P.G.2    Matthews, D.J.3
  • 54
    • 33646161254 scopus 로고    scopus 로고
    • Structure- and fragment-based approaches to protease inhibition
    • Johnson S.L., Pellecchia M. Structure- and fragment-based approaches to protease inhibition. Curr. Top. Med. Chem. 2006, 6:317-329.
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 317-329
    • Johnson, S.L.1    Pellecchia, M.2
  • 55
    • 33746349572 scopus 로고    scopus 로고
    • Targeting cancer: the challenges and successes of structure-based drug design against the human purinome
    • Knapp M., Bellamacina C., Murray J.M., Bussiere D.E. Targeting cancer: the challenges and successes of structure-based drug design against the human purinome. Curr. Top. Med. Chem. 2006, 6:1129-1159.
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 1129-1159
    • Knapp, M.1    Bellamacina, C.2    Murray, J.M.3    Bussiere, D.E.4
  • 56
    • 33646052849 scopus 로고    scopus 로고
    • Structure-based discovery and optimization of potential cancer therapeutics targeting the cell cycle
    • Thomas M.P., McInnes C. Structure-based discovery and optimization of potential cancer therapeutics targeting the cell cycle. IDrugs, 2006, 9:273-278.
    • (2006) IDrugs, , vol.9 , pp. 273-278
    • Thomas, M.P.1    McInnes, C.2
  • 57
    • 33947301761 scopus 로고    scopus 로고
    • Structure-based drug design of new leads for phosphatase research
    • Combs A.P. Structure-based drug design of new leads for phosphatase research. IDrugs, 2006, 10:112-115.
    • (2006) IDrugs, , vol.10 , pp. 112-115
    • Combs, A.P.1
  • 58
    • 0036176766 scopus 로고    scopus 로고
    • Rational approach to AIDS drug design through structural biology
    • Wlodawer A. Rational approach to AIDS drug design through structural biology. Annu. Rev. Med. 2002, 53:595-614.
    • (2002) Annu. Rev. Med. , vol.53 , pp. 595-614
    • Wlodawer, A.1
  • 59
    • 0348227698 scopus 로고    scopus 로고
    • The impact of structure-guided drug design on clinical agents
    • Dec
    • Hardy L.W., Malikayil A. The impact of structure-guided drug design on clinical agents. Curr. Drug Discov. 2003, (Dec):15-20.
    • (2003) Curr. Drug Discov. , pp. 15-20
    • Hardy, L.W.1    Malikayil, A.2
  • 61
    • 0020002135 scopus 로고
    • Enzymes of the renin-angiotensin system and their inhibitors
    • Ondetti M.A., Cushman D.W. Enzymes of the renin-angiotensin system and their inhibitors. Annu. Rev. Biochem. 1982, 51:283-308.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 283-308
    • Ondetti, M.A.1    Cushman, D.W.2
  • 62
    • 0023191215 scopus 로고
    • On the rational design of renin inhibitors: X-ray studies of aspartic proteinases complexed with transition-state analogues
    • Blundell T.L., Cooper J., Foundling S.I., Jones D.M., Atrash B., Szelke M. On the rational design of renin inhibitors: X-ray studies of aspartic proteinases complexed with transition-state analogues. Biochemistry, 1987, 26:5585-5590.
    • (1987) Biochemistry, , vol.26 , pp. 5585-5590
    • Blundell, T.L.1    Cooper, J.2    Foundling, S.I.3    Jones, D.M.4    Atrash, B.5    Szelke, M.6
  • 63
    • 0025360877 scopus 로고
    • Renin inhibitors
    • Greenlee W.J. Renin inhibitors. Med. Res. Rev. 1990, 10:173-236.
    • (1990) Med. Res. Rev. , vol.10 , pp. 173-236
    • Greenlee, W.J.1
  • 66
    • 0026323860 scopus 로고    scopus 로고
    • The crystal structures of recombinant glycosylated human renin alone and in complex with a transition-state analog inhibitor
    • Rahuel J., Priestle J.P., Grütter M.G. The crystal structures of recombinant glycosylated human renin alone and in complex with a transition-state analog inhibitor. J. Struct. Biol. 1996, 107:227-236.
    • (1996) J. Struct. Biol. , vol.107 , pp. 227-236
    • Rahuel, J.1    Priestle, J.P.2    Grütter, M.G.3
  • 67
    • 0001334658 scopus 로고    scopus 로고
    • Design principles for orally bioavailable drugs.
    • Navia M.A., Chaturvedi P.R. Design principles for orally bioavailable drugs. Drug Discov. Today, 1996, 1:179-189.
    • (1996) Drug Discov. Today, , vol.1 , pp. 179-189
    • Navia, M.A.1    Chaturvedi, P.R.2
  • 71
    • 34848869297 scopus 로고    scopus 로고
    • Structural modification of the P2' position of 2,7-dialkyl substituted 5(S)-amino-4(S)-hydroxy-8-phenyl-octanecarboxamides: the discovery of aliskiren, a potent non-peptide human renin inhibitor active after once daily dosing in marmosets
    • 4832-4844.
    • Maibaum J., Stutz S., Göschke R., Rigollier P., Yamaguchi Y., Cumin F., Rahuel J., Baum H.-P., Cohen N.-C., Schnell C.R., Fuhrer W., Gruetter M.G., Schilling W., Wood J.M. Structural modification of the P2' position of 2,7-dialkyl substituted 5(S)-amino-4(S)-hydroxy-8-phenyl-octanecarboxamides: the discovery of aliskiren, a potent non-peptide human renin inhibitor active after once daily dosing in marmosets. J. Med. Chem. 2007, 50. 4832-4844.
    • (2007) J. Med. Chem. , vol.50
    • Maibaum, J.1    Stutz, S.2    Göschke, R.3    Rigollier, P.4    Yamaguchi, Y.5    Cumin, F.6    Rahuel, J.7    Baum, H.-P.8    Cohen, N.-C.9    Schnell, C.R.10    Fuhrer, W.11    Gruetter, M.G.12    Schilling, W.13    Wood, J.M.14
  • 73
    • 0031026055 scopus 로고    scopus 로고
    • Potent and selective inhibitors of the Abl-kinase: phenylaminopyrimidine (PAP) derivatives
    • Zimmermann J., Buchdunger E., Mett H., Meyer T., Lydon N.B. Potent and selective inhibitors of the Abl-kinase: phenylaminopyrimidine (PAP) derivatives. Bioorg. Med. Chem. Lett. 1997, 7:187-192.
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 187-192
    • Zimmermann, J.1    Buchdunger, E.2    Mett, H.3    Meyer, T.4    Lydon, N.B.5
  • 75
    • 0036591874 scopus 로고    scopus 로고
    • Structural biology in drug design: selective protein kinase inhibitors
    • Scapin G. Structural biology in drug design: selective protein kinase inhibitors. Drug Discov. Today, 2002, 7:601-611.
    • (2002) Drug Discov. Today, , vol.7 , pp. 601-611
    • Scapin, G.1
  • 76
    • 1642323740 scopus 로고    scopus 로고
    • Protein kinase inhibitors: insights into drug design from structure
    • Noble M.E.M., Endicott J.A., Johnson L.N. Protein kinase inhibitors: insights into drug design from structure. Science, 2004, 303:1800-1805.
    • (2004) Science, , vol.303 , pp. 1800-1805
    • Noble, M.E.M.1    Endicott, J.A.2    Johnson, L.N.3
  • 77
    • 33751272653 scopus 로고    scopus 로고
    • Structural biology of protein tyrosine kinases
    • Cowan-Jacob S.W. Structural biology of protein tyrosine kinases. Cell. Mol. Life Sci. 2006, 63:2608-2625.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2608-2625
    • Cowan-Jacob, S.W.1
  • 79
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • Nagar B., Bommann W.G., Pellicena P., Schindler T., Veach D.R., Miller W.T., Clarkson B., Kuriyan J. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). Cancer Res. 2002, 62:4236-4243.
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bommann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6    Clarkson, B.7    Kuriyan, J.8
  • 84
    • 33745058125 scopus 로고    scopus 로고
    • Molecular interactions between the highly selective pan-Bcr-Abl inhibitor, AMN107, and the tyrosine kinase domain of Abl
    • Manley P.W., Cowan-Jacob S.W., Fendrich G., Metan J. Molecular interactions between the highly selective pan-Bcr-Abl inhibitor, AMN107, and the tyrosine kinase domain of Abl. Blood, 2005, 106:940a.
    • (2005) Blood, , vol.106
    • Manley, P.W.1    Cowan-Jacob, S.W.2    Fendrich, G.3    Metan, J.4
  • 87
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B. Solvent content of protein crystals. J. Mol. Biol. 1968, 33:491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.1
  • 90
    • 1642404661 scopus 로고    scopus 로고
    • Which strategy for a protein crystallization project?
    • Kundrot C.E. Which strategy for a protein crystallization project?. Cell. Mol. Life Sci. 2004, 61:525-536.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 525-536
    • Kundrot, C.E.1
  • 92
    • 4344698577 scopus 로고    scopus 로고
    • The use of recombinant methods and molecular engineering in protein crystallization
    • Derewenda Z.S. The use of recombinant methods and molecular engineering in protein crystallization. Methods, 2004, 34:354-363.
    • (2004) Methods, , vol.34 , pp. 354-363
    • Derewenda, Z.S.1
  • 94
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 1999, 293:321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 95
    • 4344579363 scopus 로고    scopus 로고
    • A pedestrian guide to membrane protein crystallization
    • Wiener M.C. A pedestrian guide to membrane protein crystallization. Methods, 2004, 34:364-372.
    • (2004) Methods, , vol.34 , pp. 364-372
    • Wiener, M.C.1
  • 96
    • 34248577308 scopus 로고    scopus 로고
    • The neurobiologist's guide to structural biology: a primer on why macromolecular structure matters and how to evaluate structural data
    • Minor D.L. The neurobiologist's guide to structural biology: a primer on why macromolecular structure matters and how to evaluate structural data. Neuron, 2007, 54:511-533.
    • (2007) Neuron, , vol.54 , pp. 511-533
    • Minor, D.L.1
  • 97
    • 33751000441 scopus 로고    scopus 로고
    • Searching for silver bullets: an alternative strategy for crystallizing macromolecules
    • McPherson A., Cudney B. Searching for silver bullets: an alternative strategy for crystallizing macromolecules. J. Struct. Biol. 2006, 156:387-406.
    • (2006) J. Struct. Biol. , vol.156 , pp. 387-406
    • McPherson, A.1    Cudney, B.2
  • 98
    • 35448950408 scopus 로고    scopus 로고
    • Improved expression of kinases in Baculovirus-infected insect cells upon addition of specific kinase inhibitors to the culture helpful for structural studies
    • 56, 167-176.
    • Strauss A., Fendrich G., Horisberger M.A., Liebetanz J., Meyhack B., Schlaeppi J.-M., Schmitz R. Improved expression of kinases in Baculovirus-infected insect cells upon addition of specific kinase inhibitors to the culture helpful for structural studies. Protein Expr. Purif. 2007, 56, 167-176.
    • (2007) Protein Expr. Purif.
    • Strauss, A.1    Fendrich, G.2    Horisberger, M.A.3    Liebetanz, J.4    Meyhack, B.5    Schlaeppi, J.-M.6    Schmitz, R.7
  • 100
    • 0001083794 scopus 로고    scopus 로고
    • A gentle vapor-diffusion technique for cross-linking of protein crystals for cryocrystallography
    • Lusty C. A gentle vapor-diffusion technique for cross-linking of protein crystals for cryocrystallography. J. Appl. Cryst. 1999, 32:106-112.
    • (1999) J. Appl. Cryst. , vol.32 , pp. 106-112
    • Lusty, C.1
  • 101
    • 33644877757 scopus 로고    scopus 로고
    • Cryocooling and radiation damage in macromolecular crystallography
    • Garman E.F., Owen R.L. Cryocooling and radiation damage in macromolecular crystallography. Acta Cryst. D, 2006, 62:32-47.
    • (2006) Acta Cryst. D, , vol.62 , pp. 32-47
    • Garman, E.F.1    Owen, R.L.2
  • 103
    • 0033772589 scopus 로고    scopus 로고
    • Advances in multiple wavelength anomalous diffraction crystallography
    • Ealick S.E. Advances in multiple wavelength anomalous diffraction crystallography. Curr. Opin. Chem. Biol. 2000, 4:495-499.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 495-499
    • Ealick, S.E.1
  • 104
    • 0035094743 scopus 로고    scopus 로고
    • Entering a new phase: using solvent halide ions in protein structure determination
    • Dauter Z., Dauter M. Entering a new phase: using solvent halide ions in protein structure determination. Structure, 2001, 9:21-26.
    • (2001) Structure, , vol.9 , pp. 21-26
    • Dauter, Z.1    Dauter, M.2
  • 105
    • 0345373838 scopus 로고    scopus 로고
    • In-house measurement of the sulfur anomalous signal and its use for phasing
    • Debreczeni J.É., Bunkóczi G., Ma Q., Blaser H., Sheldrick G.M. In-house measurement of the sulfur anomalous signal and its use for phasing. Acta Cryst. D, 2003, 59:688-696.
    • (2003) Acta Cryst. D, , vol.59 , pp. 688-696
    • Debreczeni, J.1    Bunkóczi, G.2    Ma, Q.3    Blaser, H.4    Sheldrick, G.M.5
  • 107
    • 0026597444 scopus 로고
    • Value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T., Free R. Value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 1992, 355:472-475.
    • (1992) Nature, , vol.355 , pp. 472-475
    • Brünger, A.T.1    Free, R.2
  • 108
    • 0027458493 scopus 로고
    • Active-centre torsion-angle strain revealed in 1.6 A ring;-resolution structure of histidine-containing phosphocarrier protein
    • Jia Z., Vandonselaar M., Quail J.W., Delbaere L.T.J. Active-centre torsion-angle strain revealed in 1.6 Å-resolution structure of histidine-containing phosphocarrier protein. Nature, 1993, 361:94-97.
    • (1993) Nature, , vol.361 , pp. 94-97
    • Jia, Z.1    Vandonselaar, M.2    Quail, J.W.3    Delbaere, L.T.J.4
  • 109
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family
    • Chevrier B., Schalk C., D'Orchymont H., Rondeau J.-M., Moras D., Tarnus C. Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure, 1994, 2:283-291.
    • (1994) Structure, , vol.2 , pp. 283-291
    • Chevrier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau, J.-M.4    Moras, D.5    Tarnus, C.6
  • 110
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 1993, 26:283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 111
    • 0038336897 scopus 로고    scopus 로고
    • Application and limitations of X-ray crystallographic data in structure-based ligand and drug design
    • Davis A.M., Teague S.J., Kleywegt G.J. Application and limitations of X-ray crystallographic data in structure-based ligand and drug design. Angew. Chem. Int. Ed. 2003, 42:2718-2736.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 2718-2736
    • Davis, A.M.1    Teague, S.J.2    Kleywegt, G.J.3
  • 112
    • 2342525085 scopus 로고    scopus 로고
    • Heterogeneity and inaccuracy in protein structures solved by X-ray crystallography
    • DePristo M.A., de Bakker P.I.W., Blundell T.L. Heterogeneity and inaccuracy in protein structures solved by X-ray crystallography. Structure, 2004, 12:831-838.
    • (2004) Structure, , vol.12 , pp. 831-838
    • DePristo, M.A.1    de Bakker, P.I.W.2    Blundell, T.L.3
  • 113
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague S. Implications of protein flexibility for drug discovery. Nat. Rev. Drug Discov. 2003, 2:527-541.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 527-541
    • Teague, S.1
  • 114
    • 33846448786 scopus 로고    scopus 로고
    • Crystallographic refinement of ligand complexes
    • Kleywegt G.J. Crystallographic refinement of ligand complexes. Acta Cryst. D 2007, 63:94-100.
    • (2007) Acta Cryst. D , vol.63 , pp. 94-100
    • Kleywegt, G.J.1
  • 115
    • 1642382166 scopus 로고    scopus 로고
    • Protein NMR in biomedical research
    • Jahnke W., Widmer H. Protein NMR in biomedical research. Cell. Mol. Life Sci. 2004, 61:580-599.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 580-599
    • Jahnke, W.1    Widmer, H.2
  • 116
    • 33846419564 scopus 로고    scopus 로고
    • The use of biophysical methods increases success in obtaining liganded crystal structures
    • Chung. C.-W. The use of biophysical methods increases success in obtaining liganded crystal structures. Acta Cryst. 2007, D63, 62-71.
    • (2007) Acta Cryst. , vol.D63 , pp. 62-71
    • Chung, C.-W.1
  • 120
    • 22544486576 scopus 로고    scopus 로고
    • Protein function prediction using local 3D templates
    • Laskowski R.A., Watson J.D., Thornton J.M. Protein function prediction using local 3D templates. J. Mol. Biol. 2005, 351:614-626.
    • (2005) J. Mol. Biol. , vol.351 , pp. 614-626
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 121
    • 28844492648 scopus 로고    scopus 로고
    • Protein surface analysis for function annotation in high-throughput structural genomics pipeline
    • Binkowski T.A., Joachimiak A., Liang J. Protein surface analysis for function annotation in high-throughput structural genomics pipeline. Protein Sci. 2005, 14:2972-2981.
    • (2005) Protein Sci. , vol.14 , pp. 2972-2981
    • Binkowski, T.A.1    Joachimiak, A.2    Liang, J.3
  • 122
    • 19544389524 scopus 로고    scopus 로고
    • Real spherical harmonic expansion coefficients as 3D shape descriptors for protein binding pocket and ligand comparisons
    • Morris R.J., Najmanovich R.J., Kahraman A., Thornton J.M. Real spherical harmonic expansion coefficients as 3D shape descriptors for protein binding pocket and ligand comparisons. Bioinformatics, 2005, 21:2347-2355.
    • (2005) Bioinformatics, , vol.21 , pp. 2347-2355
    • Morris, R.J.1    Najmanovich, R.J.2    Kahraman, A.3    Thornton, J.M.4
  • 124
    • 33846438657 scopus 로고    scopus 로고
    • Computational analyses of the surface properties of protein-protein interfaces
    • Gruber J., Zawaira A., Saunders R., Barrett C.P., Noble M.E.M. Computational analyses of the surface properties of protein-protein interfaces. Acta Cryst. D, 2007, 63:50-57.
    • (2007) Acta Cryst. D, , vol.63 , pp. 50-57
    • Gruber, J.1    Zawaira, A.2    Saunders, R.3    Barrett, C.P.4    Noble, M.E.M.5
  • 126
    • 33748189789 scopus 로고    scopus 로고
    • Peptide deformylase is a potential target for anti-Helicobacter pylori drugs: Reverse docking, enzymatic assay, and X-ray crystallography validation
    • Cai J.H., Han C., Hu T.C., Zhang J., Wu D.L., Wang F.D., Liu Y.Q., Ding J.P., Chen K.X., Yue J.M., Shen X., Jiang H.L. Peptide deformylase is a potential target for anti-Helicobacter pylori drugs: Reverse docking, enzymatic assay, and X-ray crystallography validation. Protein Sci. 2006, 15:2071-2081.
    • (2006) Protein Sci. , vol.15 , pp. 2071-2081
    • Cai, J.H.1    Han, C.2    Hu, T.C.3    Zhang, J.4    Wu, D.L.5    Wang, F.D.6    Liu, Y.Q.7    Ding, J.P.8    Chen, K.X.9    Yue, J.M.10    Shen, X.11    Jiang, H.L.12
  • 127
    • 20444369842 scopus 로고    scopus 로고
    • Rapid computational identification of the targets of protein kinase inhibitors
    • Rockey W.M., Elcock A.H. Rapid computational identification of the targets of protein kinase inhibitors. J. Med. Chem. 2005, 48:4138-4152.
    • (2005) J. Med. Chem. , vol.48 , pp. 4138-4152
    • Rockey, W.M.1    Elcock, A.H.2
  • 129
    • 33846676987 scopus 로고    scopus 로고
    • Chemical genetics: where genetics and pharmacology meet
    • Knight Z.A., Shokat K.M. Chemical genetics: where genetics and pharmacology meet. Cell, 2007, 128:425-430.
    • (2007) Cell, , vol.128 , pp. 425-430
    • Knight, Z.A.1    Shokat, K.M.2
  • 131
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski C.A., Lombardo F., Dominy B.W., Feeney P.J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliver. Rev. 1997, 23:3-25.
    • (1997) Adv. Drug Deliver. Rev. , vol.23 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 132
    • 33847401924 scopus 로고    scopus 로고
    • High-throughput electronic biology: mining information for drug discovery
    • Loging W., Harland L., Williams-Jones B. High-throughput electronic biology: mining information for drug discovery. Nat. Rev. Drug Discov. 2007, 6:220-230.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 220-230
    • Loging, W.1    Harland, L.2    Williams-Jones, B.3
  • 134
    • 9944263528 scopus 로고    scopus 로고
    • Searching for new allosteric sites in enzymes
    • Hardy J.A., Wells J.A. Searching for new allosteric sites in enzymes. Curr. Opin. Struct. Biol. 2004, 14:706-715.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 706-715
    • Hardy, J.A.1    Wells, J.A.2
  • 135
    • 33750610998 scopus 로고    scopus 로고
    • Drug targeting protein-protein interactions
    • Chène P. Drug targeting protein-protein interactions. ChemMedChem 2006, 1:400-411.
    • (2006) ChemMedChem , vol.1 , pp. 400-411
    • Chène, P.1
  • 140
    • 34248997450 scopus 로고    scopus 로고
    • De novo parallel design, synthesis and evaluation of inhibitors against the reverse transcriptase of human immunodeficiency virus type-1 and drug resistant variants
    • Herschhorn A., Lerman L., Weitman M., Gleenberg I.O., Nudelman A., Hizi A. De novo parallel design, synthesis and evaluation of inhibitors against the reverse transcriptase of human immunodeficiency virus type-1 and drug resistant variants. J. Med. Chem. 2007, 50:2370-2384.
    • (2007) J. Med. Chem. , vol.50 , pp. 2370-2384
    • Herschhorn, A.1    Lerman, L.2    Weitman, M.3    Gleenberg, I.O.4    Nudelman, A.5    Hizi, A.6
  • 141
    • 11144323163 scopus 로고    scopus 로고
    • Virtual screening of chemical libraries
    • Shoichet B.K. Virtual screening of chemical libraries. Nature, 2004, 432:862-865.
    • (2004) Nature, , vol.432 , pp. 862-865
    • Shoichet, B.K.1
  • 142
    • 33745199815 scopus 로고    scopus 로고
    • Virtual ligand screening: strategies, perspectives and limitations
    • Klebe G. Virtual ligand screening: strategies, perspectives and limitations. Drug Discov. Today. 2006, 11:580-594.
    • (2006) Drug Discov. Today. , vol.11 , pp. 580-594
    • Klebe, G.1
  • 143
    • 34447275949 scopus 로고    scopus 로고
    • Ligand docking and structure-based virtual screening in drug discovery
    • Cavasotto C.N., Orry A.J.W. Ligand docking and structure-based virtual screening in drug discovery. Curr. Topics Med. Chem. 2007, 7:1006-1014.
    • (2007) Curr. Topics Med. Chem. , vol.7 , pp. 1006-1014
    • Cavasotto, C.N.1    Orry, A.J.W.2
  • 144
    • 3242884966 scopus 로고    scopus 로고
    • High-throughput docking as a source of novel drug leads
    • Alvarez J.C. High-throughput docking as a source of novel drug leads. Curr. Opin. Chem. Biol. 2004, 8:365-370.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 365-370
    • Alvarez, J.C.1
  • 145
    • 3342933156 scopus 로고    scopus 로고
    • Target-biased scoring approaches and expert systems in structure-based virtual screening
    • Jansen J.M., Martin E.J. Target-biased scoring approaches and expert systems in structure-based virtual screening. Curr. Opin. Chem. Biol. 2004, 8:359-364.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 359-364
    • Jansen, J.M.1    Martin, E.J.2
  • 146
  • 148
    • 0036076470 scopus 로고    scopus 로고
    • Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta;-lactamase
    • Powers R.A., Morandi F., Shoichet B.K. Structure-based discovery of a novel, noncovalent inhibitor of AmpC β-lactamase. Structure, 2002, 10:1013-1023.
    • (2002) Structure, , vol.10 , pp. 1013-1023
    • Powers, R.A.1    Morandi, F.2    Shoichet, B.K.3
  • 149
    • 0037493019 scopus 로고    scopus 로고
    • Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough
    • Soelaiman S., Wei B.Q., Bergson P., Lee Y.-S., Shen Y., Mrksich M., Shoichet B.K., Tang W.-J. Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J. Biol. Chem. 2003, 278:25990-25997.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25990-25997
    • Soelaiman, S.1    Wei, B.Q.2    Bergson, P.3    Lee, Y.-S.4    Shen, Y.5    Mrksich, M.6    Shoichet, B.K.7    Tang, W.-J.8
  • 150
    • 0345269288 scopus 로고    scopus 로고
    • Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis
    • Brenk R., Naerum L., Grädler U., Gerber H.-D., Garcia G.A., Reuter K., Stubbs M.T., Klebe G. Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis. J. Med. Chem. 2003, 46:1133-1143.
    • (2003) J. Med. Chem. , vol.46 , pp. 1133-1143
    • Brenk, R.1    Naerum, L.2    Grädler, U.3    Gerber, H.-D.4    Garcia, G.A.5    Reuter, K.6    Stubbs, M.T.7    Klebe, G.8
  • 153
    • 2542631937 scopus 로고    scopus 로고
    • Virtual screening for inhibitors of human aldose reductase
    • Kraemer O., Hazemann I., Podjarny A.D., Klebe G. Virtual screening for inhibitors of human aldose reductase. Proteins, 2004, 55:814-823.
    • (2004) Proteins, , vol.55 , pp. 814-823
    • Kraemer, O.1    Hazemann, I.2    Podjarny, A.D.3    Klebe, G.4
  • 155
    • 0035324944 scopus 로고    scopus 로고
    • Molecular complexity and its impact on the probability of finding leads for drug discovery
    • Hann M.M., Leach A.R., Harper G. Molecular complexity and its impact on the probability of finding leads for drug discovery. J. Chem. Inf. Comput. Sci. 2001, 41:856-864.
    • (2001) J. Chem. Inf. Comput. Sci. , vol.41 , pp. 856-864
    • Hann, M.M.1    Leach, A.R.2    Harper, G.3
  • 156
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: a useful metric for lead selection
    • Hopkins A.L., Groom C.R., Alex A. Ligand efficiency: a useful metric for lead selection. Drug Discov. Today, 2004, 9:430-431.
    • (2004) Drug Discov. Today, , vol.9 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 157
    • 34447548576 scopus 로고    scopus 로고
    • Ligand efficiency indices for effective drug discovery
    • Abad-Zapatero C. Ligand efficiency indices for effective drug discovery. Expert Opin. Drug Discov. 2007, 2:469-488.
    • (2007) Expert Opin. Drug Discov. , vol.2 , pp. 469-488
    • Abad-Zapatero, C.1
  • 159
    • 0141726877 scopus 로고    scopus 로고
    • A quot;rule of three quot; for fragment-based lead discovery?
    • Congreve M., Carr R., Murray C., Jhoti H. A "rule of three" for fragment-based lead discovery?. Drug Discov. Today, 2003, 8:876-877.
    • (2003) Drug Discov. Today, , vol.8 , pp. 876-877
    • Congreve, M.1    Carr, R.2    Murray, C.3    Jhoti, H.4
  • 160
    • 0024745871 scopus 로고
    • The price of lost freedom: entropy of bimolecular complex formation
    • Finkelstein A.V., Janin J. The price of lost freedom: entropy of bimolecular complex formation. Protein Eng. 1989, 3:1-3.
    • (1989) Protein Eng. , vol.3 , pp. 1-3
    • Finkelstein, A.V.1    Janin, J.2
  • 161
    • 0036821028 scopus 로고    scopus 로고
    • The consequences of translational and rotational entropy lost by small molecules on binding to proteins
    • Murray C.W., Verdonk M.L. The consequences of translational and rotational entropy lost by small molecules on binding to proteins. J. Comput. Aided Mol. Des. 2002, 16:741-753.
    • (2002) J. Comput. Aided Mol. Des. , vol.16 , pp. 741-753
    • Murray, C.W.1    Verdonk, M.L.2
  • 162
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: strategic advances and lessons learned
    • Hajduk P.J., Greer J. A decade of fragment-based drug design: strategic advances and lessons learned. Nat. Rev. Drug Discov. 2007, 6:211-219.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 164
    • 84882508543 scopus 로고    scopus 로고
    • Fragment-based Approaches in Drug Discovery. Methods and Principles in Medicinal Chemistry (Jahnke, W.; Erlanson, D. A., Eds.), Vol. 34. Wiley-VCH, weinheim, Germany 2006.
  • 165
    • 0034629461 scopus 로고    scopus 로고
    • Re-engineering of human urokinase provides a system for structure-based drug design at high resolution and reveals a novel structural subsite
    • Nienaber V., Wang J., Davidson D., Henkin J. Re-engineering of human urokinase provides a system for structure-based drug design at high resolution and reveals a novel structural subsite. J. Biol. Chem. 2000, 275:7239-7248.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7239-7248
    • Nienaber, V.1    Wang, J.2    Davidson, D.3    Henkin, J.4
  • 170
    • 27344436962 scopus 로고    scopus 로고
    • Measurements of binding thermodynamics in drug discovery
    • Holdgate G.A., Ward W.H.J. Measurements of binding thermodynamics in drug discovery. Drug Discov. Today, 2005, 10:1543-1550.
    • (2005) Drug Discov. Today, , vol.10 , pp. 1543-1550
    • Holdgate, G.A.1    Ward, W.H.J.2
  • 171
    • 84952944528 scopus 로고    scopus 로고
    • Quot;Hot spot quot; analysis of protein-binding sites as a prerequisite for structure-based virtual screening and lead optimization
    • Brenk R., Klebe G. quot;Hot spot" analysis of protein-binding sites as a prerequisite for structure-based virtual screening and lead optimization. Meth. Prin. Med. Chem. 2006, 32:171-192.
    • (2006) Meth. Prin. Med. Chem. , vol.32 , pp. 171-192
    • Brenk, R.1    Klebe, G.2
  • 172
    • 33746885488 scopus 로고    scopus 로고
    • Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods
    • Ciulli A., Williams G., Smith A.G., Blundell T.L., Abell C. Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods. J. Med. Chem. 2006, 49:4992-5000.
    • (2006) J. Med. Chem. , vol.49 , pp. 4992-5000
    • Ciulli, A.1    Williams, G.2    Smith, A.G.3    Blundell, T.L.4    Abell, C.5
  • 173
    • 0033668689 scopus 로고    scopus 로고
    • Predicting binding modes, binding affinities and quot;hot spots quot; for protein-ligand complexes using a knowledge-based scoring function
    • Gohlke H., Hendlich M., Klebe G. Predicting binding modes, binding affinities and "hot spots" for protein-ligand complexes using a knowledge-based scoring function. Perspect. Drug Discov. Des. 2000, 20:115-144.
    • (2000) Perspect. Drug Discov. Des. , vol.20 , pp. 115-144
    • Gohlke, H.1    Hendlich, M.2    Klebe, G.3
  • 174
    • 0035970295 scopus 로고    scopus 로고
    • Superstar: improved knowledge-based interaction fields for protein binding sites
    • Verdonk M.L., Cole J.C., Watson P., Gillet V., Willett P. Superstar: improved knowledge-based interaction fields for protein binding sites. J. Mol. Biol. 2001, 307:841-859.
    • (2001) J. Mol. Biol. , vol.307 , pp. 841-859
    • Verdonk, M.L.1    Cole, J.C.2    Watson, P.3    Gillet, V.4    Willett, P.5
  • 176
    • 2342586724 scopus 로고    scopus 로고
    • Conformational analysis of drug-like molecules bound to proteins: an extensive study of ligand reorganization upon binding
    • Perola E., Charifson P.S. Conformational analysis of drug-like molecules bound to proteins: an extensive study of ligand reorganization upon binding. J. Med. Chem. 2004, 47:2499-2510.
    • (2004) J. Med. Chem. , vol.47 , pp. 2499-2510
    • Perola, E.1    Charifson, P.S.2
  • 177
    • 0028846226 scopus 로고
    • Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme
    • Kim E.E., Baker C.T., Dwyer M.D., Murcko M.A., Rao B.G., Tung R.D., Navia M.A. Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme. J. Am. Chem. Soc. 1995, 117:1181-1182.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1181-1182
    • Kim, E.E.1    Baker, C.T.2    Dwyer, M.D.3    Murcko, M.A.4    Rao, B.G.5    Tung, R.D.6    Navia, M.A.7
  • 178
    • 0028297112 scopus 로고
    • Application of the three-dimensional structures of protein target molecules in structure-based drug design
    • Greer J., Erickson J.W., Baldwin J.J., Varney M.D. Application of the three-dimensional structures of protein target molecules in structure-based drug design. J. Med. Chem. 1994, 37:1035-1054.
    • (1994) J. Med. Chem. , vol.37 , pp. 1035-1054
    • Greer, J.1    Erickson, J.W.2    Baldwin, J.J.3    Varney, M.D.4
  • 181
    • 0036078615 scopus 로고    scopus 로고
    • Overcoming drug resistance in HIV-1 chemotherapy: the binding thermodynamics of Amprenavir and TMC-126 to wild-type and drug resistant mutants of the HIV-1 protease
    • Ohtaka H., Velázquez-Campoy A., Xie D., Freire E. Overcoming drug resistance in HIV-1 chemotherapy: the binding thermodynamics of Amprenavir and TMC-126 to wild-type and drug resistant mutants of the HIV-1 protease. Protein Science 2002, 11:1908-1916.
    • (2002) Protein Science , vol.11 , pp. 1908-1916
    • Ohtaka, H.1    Velázquez-Campoy, A.2    Xie, D.3    Freire, E.4
  • 182
    • 0034333415 scopus 로고    scopus 로고
    • Structure-based drug design of non-nucleoside inhibitors for wild-type and drug resistant HIV reverse transcriptase
    • Mao C., Sudbeck E.A., Ventakatachalam T.K., Uckun F.M. Structure-based drug design of non-nucleoside inhibitors for wild-type and drug resistant HIV reverse transcriptase. Biochem. Pharmacol. 2000, 60:1251-1265.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1251-1265
    • Mao, C.1    Sudbeck, E.A.2    Ventakatachalam, T.K.3    Uckun, F.M.4
  • 184
    • 0034093758 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors: enthalpic versus entropic optimization of the binding affinity
    • Velazquez-Campoy A., Todd M.J., Freire E. HIV-1 protease inhibitors: enthalpic versus entropic optimization of the binding affinity. Biochemistry, 2000, 39:2201-2207.
    • (2000) Biochemistry, , vol.39 , pp. 2201-2207
    • Velazquez-Campoy, A.1    Todd, M.J.2    Freire, E.3
  • 186
    • 2442647742 scopus 로고    scopus 로고
    • BREED: generating novel inhibitors through hybridization of known ligands. Application to CDK2, P38, and HIV protease
    • Pierce A.C., Rao G., Bemis G.W. BREED: generating novel inhibitors through hybridization of known ligands. Application to CDK2, P38, and HIV protease. J. Med. Chem. 2004, 47:2768-2775.
    • (2004) J. Med. Chem. , vol.47 , pp. 2768-2775
    • Pierce, A.C.1    Rao, G.2    Bemis, G.W.3
  • 188
    • 0347129832 scopus 로고    scopus 로고
    • A highly potent non-nucleoside adenosine deaminase inhibitor: efficient drug discovery by intentional lead hydridization
    • Terasaka T., Kinoshita T., Kuno M., Nakanishi I. A highly potent non-nucleoside adenosine deaminase inhibitor: efficient drug discovery by intentional lead hydridization. J. Am. Chem. Soc. 2004, 126:34-35.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 34-35
    • Terasaka, T.1    Kinoshita, T.2    Kuno, M.3    Nakanishi, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.