메뉴 건너뛰기




Volumn 274, Issue 1, 1997, Pages 84-100

The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution

Author keywords

Detoxification; Enzyme mechanism; Glutathione S transferases; Inhibitor complexes; X ray crystallography

Indexed keywords

ENZYME INHIBITOR; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GLYCINE DERIVATIVE; HYDROXYL GROUP; PHENYL GROUP; S HEXYLGLUTATHIONE; THIOL GROUP; WATER;

EID: 0141648082     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1364     Document Type: Article
Times cited : (160)

References (60)
  • 2
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A. T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 5
    • 0029645124 scopus 로고
    • Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate
    • Cameron A. D., Sinning I., L'Hermite G., Olin B., Board P. G., Mannervik B., Jones T. A. Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure. 5:1995;717-727.
    • (1995) Structure , vol.5 , pp. 717-727
    • Cameron, A.D.1    Sinning, I.2    L'Hermite, G.3    Olin, B.4    Board, P.G.5    Mannervik, B.6    Jones, T.A.7
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;750-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 750-763
  • 8
    • 0025228968 scopus 로고
    • The role of glutathione and glutathione transferases in chemical carcinogenesis
    • Coles B., Ketterer B. The role of glutathione and glutathione transferases in chemical carcinogenesis. CRC Crit. Rev. Biochem. Mol. Biol. 25:1990;47-70.
    • (1990) CRC Crit. Rev. Biochem. Mol. Biol. , vol.25 , pp. 47-70
    • Coles, B.1    Ketterer, B.2
  • 9
    • 0028079744 scopus 로고
    • Refined crystal structure of porcine class pi glutathione S-transferase (pGST P1-1) at 2.1 Å resolution
    • Dirr H., Reinemer P., Huber R. Refined crystal structure of porcine class pi glutathione S-transferase (pGST P1-1) at 2.1 Å resolution. J. Mol. Biol. 243:1994a;72-92.
    • (1994) J. Mol. Biol. , vol.243 , pp. 72-92
    • Dirr, H.1    Reinemer, P.2    Huber, R.3
  • 10
    • 0028224013 scopus 로고
    • X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function
    • Dirr H., Reinemer P., Huber R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. Eur. J. Biochem. 220:1994b;645-661.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 645-661
    • Dirr, H.1    Reinemer, P.2    Huber, R.3
  • 11
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray structure refinement
    • Engh R. A., Huber R. Accurate bond and angle parameters for X-ray structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 12
    • 0028218792 scopus 로고
    • Molecular structure at 1.8 Å of mouse liver class pi glutathione S-transferase complexed with S -(p -nitrobenzyl)glutathione and other inhibitors
    • García-Sáez I., Párraga A., Phillips M. F., Mantle T. J., Coll M. Molecular structure at 1.8 Å of mouse liver class pi glutathione S-transferase complexed with S -(p -nitrobenzyl)glutathione and other inhibitors. J. Mol. Biol. 237:1994;298-314.
    • (1994) J. Mol. Biol. , vol.237 , pp. 298-314
    • García-Sáez, I.1    Párraga, A.2    Phillips, M.F.3    Mantle, T.J.4    Coll, M.5
  • 13
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J. D., Pulford D. J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30:1995;445-600.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 14
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF: A program to identify and analyze structural motifs in proteins
    • Hutchinson E. G., Thornton J. M. PROMOTIF: a program to identify and analyze structural motifs in proteins. Protein Sci. 5:1996;212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 15
    • 0026460365 scopus 로고
    • The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution
    • Ji X., Zhang P., Armstrong R. N., Gilliland G. L. The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution. Biochemistry. 31:1992;10169-10184.
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 16
    • 0029064985 scopus 로고
    • Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S -crystallins of cephalopods
    • Ji X., von Rosenvinge E. C., Johnson W. W., Tomarev S. I., Piatigorsky J., Armstrong R. N., Gilliland G. L. Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S -crystallins of cephalopods. Biochemistry. 34:1995;5317-5328.
    • (1995) Biochemistry , vol.34 , pp. 5317-5328
    • Ji, X.1    Von Rosenvinge, E.C.2    Johnson, W.W.3    Tomarev, S.I.4    Piatigorsky, J.5    Armstrong, R.N.6    Gilliland, G.L.7
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J.-Y., Cowan S. W., Kjeldgaard M. Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 19
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt G. Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallog. sect. D. 52:1996;842-857.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 842-857
    • Kleywegt, G.1
  • 20
    • 0002700643 scopus 로고
    • Halloween . masks and bones
    • Warrington: EPSRCDaresbury Laboratory
    • Kleywegt G., Jones T. A. Halloween . masks and bones. From First Map to Final Model. 1994a;EPSRCDaresbury Laboratory, Warrington.
    • (1994) From First Map to Final Model
    • Kleywegt, G.1    Jones, T.A.2
  • 21
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt G. J., Jones T. A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallog. sect. D. 50:1994b;178-185.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 22
    • 0031010027 scopus 로고    scopus 로고
    • Ligand based protein alignment and isozyme specificity of glutathione S-transferase inhibitors
    • Koehler R. T., Villar H. O., Bauer K. E., Higgins D. L. Ligand based protein alignment and isozyme specificity of glutathione S-transferase inhibitors. Proteins: Struct. Funct. Genet. 28:1997;202-216.
    • (1997) Proteins: Struct. Funct. Genet. , vol.28 , pp. 202-216
    • Koehler, R.T.1    Villar, H.O.2    Bauer, K.E.3    Higgins, D.L.4
  • 23
    • 0026736592 scopus 로고
    • Participation of the phenolic hydroxyl group of Tyr-8 in the catalytic mechanism of human glutathione transferase P1-1
    • Kolm R. H., Sroga G. E., Mannervik B. Participation of the phenolic hydroxyl group of Tyr-8 in the catalytic mechanism of human glutathione transferase P1-1. Biochem. J. 285:1992;537-540.
    • (1992) Biochem. J. , vol.285 , pp. 537-540
    • Kolm, R.H.1    Sroga, G.E.2    Mannervik, B.3
  • 24
    • 0026529977 scopus 로고
    • Tyrosine-7 is an essential residue for the catalytic activity of human class pi glutathione S-transferase: Chemical modification and site-directed mutagenesis studies
    • Kong K.-H., Nishida M., Inoue H., Takahashi K. Tyrosine-7 is an essential residue for the catalytic activity of human class pi glutathione S-transferase: chemical modification and site-directed mutagenesis studies. Biochem. Biophys. Res. Commun. 182:1992;1122-1129.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1122-1129
    • Kong, K.-H.1    Nishida, M.2    Inoue, H.3    Takahashi, K.4
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., McArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;282-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 282-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 0028593398 scopus 로고
    • Three-dimensional structure of Schistoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV
    • Lim K., Ho J. X., Keeling K., Gilliland G. L., Ji X., Rüker F., Carter D. C. Three-dimensional structure of Schistoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci. 3:1994;2233-2244.
    • (1994) Protein Sci. , vol.3 , pp. 2233-2244
    • Lim, K.1    Ho, J.X.2    Keeling, K.3    Gilliland, G.L.4    Ji, X.5    Rüker, F.6    Carter, D.C.7
  • 29
    • 0028842236 scopus 로고
    • Site-directed mutagenesis of human glutathione transferase P1-1. Spectral, kinetic, and structural properties of Cys-47 and Lys-54 mutants
    • Lo Bello M., Battistoni A., Mazzetti A. P., Board P. G., Muramatsu M., Federici G., Ricci G. Site-directed mutagenesis of human glutathione transferase P1-1. Spectral, kinetic, and structural properties of Cys-47 and Lys-54 mutants. J. Biol. Chem. 270:1995;1249-1253.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1249-1253
    • Lo Bello, M.1    Battistoni, A.2    Mazzetti, A.P.3    Board, P.G.4    Muramatsu, M.5    Federici, G.6    Ricci, G.7
  • 30
    • 0030923311 scopus 로고    scopus 로고
    • Multifunctional role of Tyr108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies of the Y108F mutant enzyme
    • Lo Bello M., Oakley A. J., Battistoni A., Mazzetti A. P., Nuccetelli M., Mazzarese G., Rossjohn J., Parker M. W., Ricci G. Multifunctional role of Tyr108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies of the Y108F mutant enzyme. Biochemistry. 36:1997;6207-6217.
    • (1997) Biochemistry , vol.36 , pp. 6207-6217
    • Lo Bello, M.1    Oakley, A.J.2    Battistoni, A.3    Mazzetti, A.P.4    Nuccetelli, M.5    Mazzarese, G.6    Rossjohn, J.7    Parker, M.W.8    Ricci, G.9
  • 32
    • 0024269217 scopus 로고
    • Glutathione transferases: Structure and catalytic activity
    • Mannervik B., Danielson U. H. Glutathione transferases: structure and catalytic activity. CRC Crit. Rev. Biochem. 23:1988;283-337.
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 33
    • 0000107746 scopus 로고
    • Identification of three classes of cytosolic glutathione transferase common to several mammalian species: Correlation between structural data and enzymatic properties
    • Mannervik B., Ålin P., Guthenberg C., Jensson H., Tahir M. K., Warholm M., Jornvall H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc. Natl Acad. Sci. USA. 82:1985;7202-7206.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 7202-7206
    • Mannervik, B.1    Ålin, P.2    Guthenberg, C.3    Jensson, H.4    Tahir, M.K.5    Warholm, M.6    Jornvall, H.7
  • 34
    • 0026753498 scopus 로고
    • Structural studies on human glutathione S-transferase pi. Substitution mutations to determine amino acids necessary for binding glutathione
    • Manoharan T. H., Gulick A. M., Puchalski R. B., Servais A. L., Fahl W. E. Structural studies on human glutathione S-transferase pi. Substitution mutations to determine amino acids necessary for binding glutathione. J Biol. Chem. 267:1992a;18940-18945.
    • (1992) J Biol. Chem. , vol.267 , pp. 18940-18945
    • Manoharan, T.H.1    Gulick, A.M.2    Puchalski, R.B.3    Servais, A.L.4    Fahl, W.E.5
  • 35
    • 0026652120 scopus 로고
    • Mutational substitution of residues implicated by crystal structure in binding the substrate glutathione to human glutathione S-transferase π
    • Manoharan T. H., Gulick A. M., Reinemer P., Dirr H. W., Huber R., Fahl W. E. Mutational substitution of residues implicated by crystal structure in binding the substrate glutathione to human glutathione S-transferase π J. Mol. Biol. 226:1992b;319-322.
    • (1992) J. Mol. Biol. , vol.226 , pp. 319-322
    • Manoharan, T.H.1    Gulick, A.M.2    Reinemer, P.3    Dirr, H.W.4    Huber, R.5    Fahl, W.E.6
  • 37
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel
    • McTigue M. A., Williams D. R., Tainer J. A. Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J. Mol. Biol. 246:1995;21-27.
    • (1995) J. Mol. Biol. , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 38
    • 0028871969 scopus 로고
    • Characterization of rat spleen prostaglandin H D-isomerase as a sigma-class GSH transferase
    • Meyer D. J., Thomas M. Characterization of rat spleen prostaglandin H D-isomerase as a sigma-class GSH transferase. Biochem. J. 311:1995;739-742.
    • (1995) Biochem. J. , vol.311 , pp. 739-742
    • Meyer, D.J.1    Thomas, M.2
  • 41
    • 0010512352 scopus 로고
    • Comparison of glutathione S-transferase levels in predicting the efficacy of a novel alkylating agent
    • Montali J. A., Wheatley J. B., Schmidt D. E. Comparison of glutathione S-transferase levels in predicting the efficacy of a novel alkylating agent. Cellular Pharmacol. 2:1995;241-247.
    • (1995) Cellular Pharmacol. , vol.2 , pp. 241-247
    • Montali, J.A.1    Wheatley, J.B.2    Schmidt, D.E.3
  • 42
    • 0030065613 scopus 로고    scopus 로고
    • Isozyme-specific glutathione S-transferase inhibitors potentiate drug sensitivity in cultured human cell lines
    • Morgan A. S., Ciaccio P. J., Tew K. D., Kauvar L. M. Isozyme-specific glutathione S-transferase inhibitors potentiate drug sensitivity in cultured human cell lines. Cancer Chemother. Pharmacol. 37:1996;363-370.
    • (1996) Cancer Chemother. Pharmacol. , vol.37 , pp. 363-370
    • Morgan, A.S.1    Ciaccio, P.J.2    Tew, K.D.3    Kauvar, L.M.4
  • 43
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 44
    • 0026061555 scopus 로고
    • Inactivation of human placenta glutathione S-transferase by SH/SS exchange reaction with biological disulfides
    • Nishihara T., Maeda H., Okamoto K., Oshida T., Mizoguchi T., Terada T. Inactivation of human placenta glutathione S-transferase by SH/SS exchange reaction with biological disulfides. Biochem. Biophys. Res. Commun. 174:1991;580-585.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 580-585
    • Nishihara, T.1    Maeda, H.2    Okamoto, K.3    Oshida, T.4    Mizoguchi, T.5    Terada, T.6
  • 45
    • 0031017331 scopus 로고    scopus 로고
    • The three-dimensional structure for the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate
    • Oakley A. J., Rossjohn J., Lo Bello M., Caccuri A. M., Federici G., Parker M. W. The three-dimensional structure for the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate. Biochemistry. 36:1997;576-585.
    • (1997) Biochemistry , vol.36 , pp. 576-585
    • Oakley, A.J.1    Rossjohn, J.2    Lo Bello, M.3    Caccuri, A.M.4    Federici, G.5    Parker, M.W.6
  • 46
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington: SERC Daresbury Laboratory
    • Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Data Collection and Processing. 1993;SERC Daresbury Laboratory, Warrington.
    • (1993) Data Collection and Processing
    • Otwinowski, Z.1
  • 47
    • 0025369904 scopus 로고
    • Crystallization of glutathione S-transferase from human placenta
    • Parker M. W., Lo Bello M., Federici G. Crystallization of glutathione S-transferase from human placenta. J. Mol. Biol. 213:1990;221-222.
    • (1990) J. Mol. Biol. , vol.213 , pp. 221-222
    • Parker, M.W.1    Lo Bello, M.2    Federici, G.3
  • 48
    • 0028244183 scopus 로고
    • Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity
    • Raghunathan S., Chandross R. J., Kretsinger R. H., Allison T. J., Penington C. J., Rule G. S. Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. J. Mol. Biol. 238:1994;815-832.
    • (1994) J. Mol. Biol. , vol.238 , pp. 815-832
    • Raghunathan, S.1    Chandross, R.J.2    Kretsinger, R.H.3    Allison, T.J.4    Penington, C.J.5    Rule, G.S.6
  • 49
    • 0025816448 scopus 로고
    • The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution
    • Reinemer P., Dirr H. W., Ladenstein R., Schäffer J., Gallay O., Huber R. The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J. 10:1991;1997-2005.
    • (1991) EMBO J. , vol.10 , pp. 1997-2005
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Schäffer, J.4    Gallay, O.5    Huber, R.6
  • 50
    • 0026722795 scopus 로고
    • Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution
    • Reinemer P., Dirr H. W., Ladenstein R., Huber R., Lo Bello M., Federici G., Parker M. W. Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. J. Mol. Biol. 227:1992;214-226.
    • (1992) J. Mol. Biol. , vol.227 , pp. 214-226
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Huber, R.4    Lo Bello, M.5    Federici, G.6    Parker, M.W.7
  • 51
    • 0028809193 scopus 로고
    • Site directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperativity in glutathione transferase P1-1
    • Ricci G., Lo Bello M., Caccuri A. M., Pastore A., Nuccetelli M., Parker M. W., Federici G. Site directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperativity in glutathione transferase P1-1. J. Biol. Chem. 270:1995;1243-1248.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1243-1248
    • Ricci, G.1    Lo Bello, M.2    Caccuri, A.M.3    Pastore, A.4    Nuccetelli, M.5    Parker, M.W.6    Federici, G.7
  • 52
    • 0030018850 scopus 로고    scopus 로고
    • Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 flexibility in the catalytic mechanism
    • Ricci G., Caccuri A. M., Lo Bello M., Rosato N., Mei G., Nicotra M., Chiessi E., Mazzetti A. P., Federici G. Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 flexibility in the catalytic mechanism. J. Biol. Chem. 271:1996;16187-16192.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16187-16192
    • Ricci, G.1    Caccuri, A.M.2    Lo Bello, M.3    Rosato, N.4    Mei, G.5    Nicotra, M.6    Chiessi, E.7    Mazzetti, A.P.8    Federici, G.9
  • 53
    • 0030010730 scopus 로고    scopus 로고
    • Structurally-derived consensus pattern for theta class glutathione transferases
    • Rossjohn J., Board P. G., Parker M. W., Wilce M. C. J. Structurally-derived consensus pattern for theta class glutathione transferases. Protein Eng. 9:1996;327-332.
    • (1996) Protein Eng. , vol.9 , pp. 327-332
    • Rossjohn, J.1    Board, P.G.2    Parker, M.W.3    Wilce, M.C.J.4
  • 55
    • 0025948242 scopus 로고
    • Role of cysteine residues in the activity of rat glutathione transferase P (7-7): Elucidation by oligonucleotide site-directed mutagenesis
    • Tamai K., Shen H. X., Tsuchida S., Hatayama I., Satoh K., Yasui A., Oikawa A., Sato A. Role of cysteine residues in the activity of rat glutathione transferase P (7-7): elucidation by oligonucleotide site-directed mutagenesis. Biochem. Biophys. Res. Commun. 179:1991;790-797.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 790-797
    • Tamai, K.1    Shen, H.X.2    Tsuchida, S.3    Hatayama, I.4    Satoh, K.5    Yasui, A.6    Oikawa, A.7    Sato, A.8
  • 56
    • 0026639653 scopus 로고
    • Glutathione transferases and cancer. CRC Crit. Rev
    • Tsuchida S., Sato K. Glutathione transferases and cancer. CRC Crit. Rev. Biochem. Mol. Biol. 27:1992;337-384.
    • (1992) Biochem. Mol. Biol. , vol.27 , pp. 337-384
    • Tsuchida, S.1    Sato, K.2
  • 57
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace A. C., Laskowski R. A., Thornton J. M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8:1995;127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 58
    • 0025093198 scopus 로고
    • Glutathione S-transferases: Role in alkylating agent resistance and possible target for modulation chemotherapy: A review
    • Waxman D. J. Glutathione S-transferases: role in alkylating agent resistance and possible target for modulation chemotherapy: a review. Cancer Res. 50:1990;6449-6454.
    • (1990) Cancer Res. , vol.50 , pp. 6449-6454
    • Waxman, D.J.1
  • 59
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce M. C. J., Parker M. W. Structure and function of glutathione S-transferases. Biochim. Biophys. Acta. 1994;1-18.
    • (1994) Biochim. Biophys. Acta , pp. 1-18
    • Wilce, M.C.J.1    Parker, M.W.2
  • 60


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.