메뉴 건너뛰기




Volumn 84, Issue 3, 1999, Pages 327-332

New approaches to rational drug design

Author keywords

Co solvents; MIF, migration inhibitory factor; Nonaqueous solvents; Organic solvents; Protein crystallography; SAR, structure activity relationship; Structural genomics

Indexed keywords

CHYMOTRYPSIN; DIHYDROFOLATE REDUCTASE; DIHYDROFOLIC ACID; ISOMERASE; MACROPHAGE MIGRATION INHIBITION FACTOR; METHOTREXATE; SUBTILISIN;

EID: 0032763627     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0163-7258(99)00039-X     Document Type: Review
Times cited : (21)

References (40)
  • 2
    • 0030723768 scopus 로고    scopus 로고
    • Oligomerization of a 45 kilodalton fragment from diphtheria toxin at pH 5.0 to a molecule of 20-24 subunits
    • Bell C.E., Poon P.H., Schumaker V.N., Eisenberg D. Oligomerization of a 45 kilodalton fragment from diphtheria toxin at pH 5.0 to a molecule of 20-24 subunits. Biochemistry. 36:1997;15201-15207.
    • (1997) Biochemistry , vol.36 , pp. 15201-15207
    • Bell, C.E.1    Poon, P.H.2    Schumaker, V.N.3    Eisenberg, D.4
  • 3
    • 0022397324 scopus 로고
    • Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration
    • Blewitt M.G., Chung L.A., London E. Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration. Biochemistry. 24:1985;5458-5464.
    • (1985) Biochemistry , vol.24 , pp. 5458-5464
    • Blewitt, M.G.1    Chung, L.A.2    London, E.3
  • 4
    • 0028023726 scopus 로고
    • Structure of the influenza hemagglutinin at the pH of membrane fusion
    • Bullough P.A., Hughson F.M., Skebel J.J., Wiley D.C. Structure of the influenza hemagglutinin at the pH of membrane fusion. Nature. 371:1994;37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skebel, J.J.3    Wiley, D.C.4
  • 5
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr C.M., Chaudhry C., Kim P.S. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc Natl Acad Sci USA. 94:1997;14306-14313.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 6
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • Genome sequence of the nematode C. elegans. a platform for investigating biology Science. 282:1998;2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 7
    • 0344158368 scopus 로고    scopus 로고
    • Enzyme structure in non-native environments. In R. L. Ornstein (Ed.)
    • Farber G.K. Enzyme structure in non-native environments. In R. L. Ornstein (Ed.). Improving Enzyme Catalysis. in press.(New York: Elsevier):1999.
    • (1999) Improving Enzyme Catalysis
    • Farber, G.K.1
  • 9
    • 0030724017 scopus 로고    scopus 로고
    • Assigning folds to the proteins encoded by the genome of Mycoplasma genitalium
    • Fisher D., Eisenberg D. Assigning folds to the proteins encoded by the genome of Mycoplasma genitalium. Proc Natl Acad Sci USA. 94:1997;11929-11934.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11929-11934
    • Fisher, D.1    Eisenberg, D.2
  • 11
    • 0028304966 scopus 로고
    • X-ray crystal structure of cross-linked subtilisin carlsberg in water vs. acetonitrile
    • Fitzpatrick P.A., Ringe D., Klibanov A.M. X-ray crystal structure of cross-linked subtilisin carlsberg in water vs. acetonitrile. Biochem Biophys Res Commun. 198:1994;675-681.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 675-681
    • Fitzpatrick, P.A.1    Ringe, D.2    Klibanov, A.M.3
  • 12
    • 0030708525 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins
    • Hajduk P.J., Meadows R.P., Feski S.W. Discovering high-affinity ligands for proteins. Science. 278:1997;497-499.
    • (1997) Science , vol.278 , pp. 497-499
    • Hajduk, P.J.1    Meadows, R.P.2    Feski, S.W.3
  • 13
    • 0028315470 scopus 로고
    • The methotrexate story: A paradigm of cancer chemotherapeutic agents
    • Huennekens F.M. The methotrexate story. a paradigm of cancer chemotherapeutic agents Adv Enzyme Regul. 34:1994;397-419.
    • (1994) Adv Enzyme Regul , vol.34 , pp. 397-419
    • Huennekens, F.M.1
  • 14
    • 0025866660 scopus 로고
    • Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: Indication of a conformational change in the central helix
    • Ikura M., Kay L.E., Krinks M., Bax A. Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase. indication of a conformational change in the central helix Biochemistry. 30:1991;5498-5504.
    • (1991) Biochemistry , vol.30 , pp. 5498-5504
    • Ikura, M.1    Kay, L.E.2    Krinks, M.3    Bax, A.4
  • 15
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks W.P. On the attribution and additivity of binding energies. Proc Natl Acad Sci USA. 78:1981;4046-4050.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 16
    • 0029796290 scopus 로고    scopus 로고
    • Comparison of experimental and computational functional group mapping of an RNase A structure: Implications for computer-aided drug design
    • Joseph-McCarthy D., Federov A.A., Almo S.C. Comparison of experimental and computational functional group mapping of an RNase A structure. implications for computer-aided drug design Protein Eng. 9:1996;773-780.
    • (1996) Protein Eng , vol.9 , pp. 773-780
    • Joseph-Mccarthy, D.1    Federov, A.A.2    Almo, S.C.3
  • 17
    • 0030766287 scopus 로고    scopus 로고
    • Folding with a two-stroke motor
    • Lorimer G. Folding with a two-stroke motor. Nature. 388:1997;720-723.
    • (1997) Nature , vol.388 , pp. 720-723
    • Lorimer, G.1
  • 18
    • 0032502262 scopus 로고    scopus 로고
    • Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction
    • Lukas C.M., Rubin H., Christianson D.W. Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction. Biochemistry. 37:1998;3297-3304.
    • (1998) Biochemistry , vol.37 , pp. 3297-3304
    • Lukas, C.M.1    Rubin, H.2    Christianson, D.W.3
  • 20
    • 0032512732 scopus 로고    scopus 로고
    • Taking a structured approach to understanding proteins
    • Pennisi E. Taking a structured approach to understanding proteins. Science. 279:1998;978-979.
    • (1998) Science , vol.279 , pp. 978-979
    • Pennisi, E.1
  • 21
    • 0029911948 scopus 로고    scopus 로고
    • For medicinal purposes
    • Petsko G.A. For medicinal purposes. Nature. 384(suppl.):1996;7-9.
    • (1996) Nature , vol.384 , Issue.SUPPL. , pp. 7-9
    • Petsko, G.A.1
  • 22
    • 0029137828 scopus 로고
    • The structure and evolution of alpha/beta barrel proteins
    • Reardon D., Farber G.K. The structure and evolution of alpha/beta barrel proteins. FASEB J. 9:1995;497-503.
    • (1995) FASEB J , vol.9 , pp. 497-503
    • Reardon, D.1    Farber, G.K.2
  • 23
    • 0028985318 scopus 로고
    • Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: Mechanistic implications
    • Reyes V.M., Sawaya M.R., Brown K.A., Kraut J. Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate. mechanistic implications Biochemistry. 34:1995;2710-2723.
    • (1995) Biochemistry , vol.34 , pp. 2710-2723
    • Reyes, V.M.1    Sawaya, M.R.2    Brown, K.A.3    Kraut, J.4
  • 24
    • 0029584688 scopus 로고
    • What makes a binding site a binding site?
    • Ringe D. What makes a binding site a binding site? Curr Opin Struct Biol. 5:1995;825-829.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 825-829
    • Ringe, D.1
  • 25
    • 0022555901 scopus 로고
    • Study of protein dynamics by X-ray diffraction
    • Ringe D., Petsko G.A. Study of protein dynamics by X-ray diffraction. Methods Enzymol. 131:1986;389-433.
    • (1986) Methods Enzymol , vol.131 , pp. 389-433
    • Ringe, D.1    Petsko, G.A.2
  • 26
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya M.R., Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase. crystallographic evidence Biochemistry. 36:1997;586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 27
    • 0030970824 scopus 로고    scopus 로고
    • The crystal structure of subtilisin carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile
    • Schmitke J.L., Stern L.J., Klibanov A.M. The crystal structure of subtilisin carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile. Proc Natl Acad Sci USA. 94:1997;4250-4255.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4250-4255
    • Schmitke, J.L.1    Stern, L.J.2    Klibanov, A.M.3
  • 28
    • 0014198467 scopus 로고
    • Binding of cyclopropane to sperm whale myoglobin
    • Schoenborn B.P. Binding of cyclopropane to sperm whale myoglobin. Nature. 214:1967;1120-1122.
    • (1967) Nature , vol.214 , pp. 1120-1122
    • Schoenborn, B.P.1
  • 29
    • 0013842370 scopus 로고
    • Binding of xenon to sperm whale myoglobin
    • Schoenborn B.P., Watson H.C., Kendrew J.C. Binding of xenon to sperm whale myoglobin. Nature. 207:1965;28-30.
    • (1965) Nature , vol.207 , pp. 28-30
    • Schoenborn, B.P.1    Watson, H.C.2    Kendrew, J.C.3
  • 30
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker S.B., Hajduk P.J., Meadows R.P., Fesik S.W. Discovering high-affinity ligands for proteins. SAR by NMR Science. 274:1996;1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 31
    • 0029895838 scopus 로고    scopus 로고
    • Crystal structure at 2.6 Å resolution of human macrophage migration inhibitory factor
    • Sun H.-W., Bernhagen J., Bucala R., Lolis E. Crystal structure at 2.6 Å resolution of human macrophage migration inhibitory factor. Proc Natl Acad Sci USA. 93:1996;5191-5196.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5191-5196
    • Sun, H.-W.1    Bernhagen, J.2    Bucala, R.3    Lolis, E.4
  • 32
    • 0032127485 scopus 로고    scopus 로고
    • Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor
    • Swope M., Sun H.-W., Blake P.R., Lolis E. Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor. EMBO J. 17:1998;3534-3541.
    • (1998) EMBO J , vol.17 , pp. 3534-3541
    • Swope, M.1    Sun, H.-W.2    Blake, P.R.3    Lolis, E.4
  • 33
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a met-myoglobin-xenon complex solved to 1.9 Å resolution
    • Tilton R.F., Kuntz I.D., Petsko G.A. Cavities in proteins. structure of a met-myoglobin-xenon complex solved to 1.9 Å resolution Biochemistry. 23:1984;2849-2857.
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton, R.F.1    Kuntz, I.D.2    Petsko, G.A.3
  • 34
    • 0032546555 scopus 로고    scopus 로고
    • X-ray studies on cross-linked lysozyme crystals in acetonitrile-water mixture
    • Wang Z., Zhu G., Huang Q., Qian M., Shao M., Jia Y., Tang Y. X-ray studies on cross-linked lysozyme crystals in acetonitrile-water mixture. Biochim Biophys Acta. 1384:1998;335-344.
    • (1998) Biochim Biophys Acta , vol.1384 , pp. 335-344
    • Wang, Z.1    Zhu, G.2    Huang, Q.3    Qian, M.4    Shao, M.5    Jia, Y.6    Tang, Y.7
  • 35
    • 0019890491 scopus 로고
    • Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson I.A., Skehel J.J., Wiley D.C. Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature. 289:1981;366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 37
    • 0028243728 scopus 로고
    • X-ray crystal structure of γ-chymotrypsin in hexane
    • Yennawar N.H., Yennawar H.P., Farber G.K. X-ray crystal structure of γ-chymotrypsin in hexane. Biochemistry. 33:1994;7326-7336.
    • (1994) Biochemistry , vol.33 , pp. 7326-7336
    • Yennawar, N.H.1    Yennawar, H.P.2    Farber, G.K.3
  • 38
    • 0029103572 scopus 로고
    • A structural explanation for enzyme memory in nonaqueous solvents
    • Yennawar H.P., Yennawar N.H., Farber G.K. A structural explanation for enzyme memory in nonaqueous solvents. J Am Chem Soc. 117:1995;577-585.
    • (1995) J Am Chem Soc , vol.117 , pp. 577-585
    • Yennawar, H.P.1    Yennawar, N.H.2    Farber, G.K.3
  • 39
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky P., Kardos J., Svingor A., Petsko G.A. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc Natl Acad Sci USA. 95:1998;7406-7411.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.A.4
  • 40
    • 0032407760 scopus 로고    scopus 로고
    • X-ray studies on two forms of bovine β-trypsin in neat cyclohexane
    • Zhu G., Huang Q., Wang Z., Qian M., Jia Y., Tang Y. X-ray studies on two forms of bovine β-trypsin in neat cyclohexane. Biochim Biophys Acta. 1429:1998;142-150.
    • (1998) Biochim Biophys Acta , vol.1429 , pp. 142-150
    • Zhu, G.1    Huang, Q.2    Wang, Z.3    Qian, M.4    Jia, Y.5    Tang, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.