메뉴 건너뛰기




Volumn 380, Issue 1, 2008, Pages 131-144

The Anti-cancer Drug Chlorambucil as a Substrate for the Human Polymorphic Enzyme Glutathione Transferase P1-1: Kinetic Properties and Crystallographic Characterisation of Allelic Variants

Author keywords

anti cancer drugs; detoxification; glutathione transferases; polymorphisms; X ray crystallography

Indexed keywords

CHLORAMBUCIL; ENZYME VARIANT; GLUTATHIONE; GLUTATHIONE TRANSFERASE P1;

EID: 44649175626     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.04.066     Document Type: Article
Times cited : (51)

References (54)
  • 1
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan D., Meade G., Foley V.M., and Dowd C.A. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360 (2001) 1-16
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 3
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce M.C., and Parker M.W. Structure and function of glutathione S-transferases. Biochim. Biophys. Acta 1205 (1994) 1-18
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.1    Parker, M.W.2
  • 4
    • 0029089249 scopus 로고
    • Glutathione S transferase Pi is a powerful indicator in chemotherapy of human lung squamous-cell carcinoma
    • Inoue T., Ishida T., Sugio K., Maehara Y., and Sugimachi K. Glutathione S transferase Pi is a powerful indicator in chemotherapy of human lung squamous-cell carcinoma. Respiration 62 (1995) 223-227
    • (1995) Respiration , vol.62 , pp. 223-227
    • Inoue, T.1    Ishida, T.2    Sugio, K.3    Maehara, Y.4    Sugimachi, K.5
  • 5
    • 0024490605 scopus 로고
    • Glutathione transferases as markers of preneoplasia and neoplasia
    • Sato K. Glutathione transferases as markers of preneoplasia and neoplasia. Adv. Cancer Res. 52 (1989) 205-255
    • (1989) Adv. Cancer Res. , vol.52 , pp. 205-255
    • Sato, K.1
  • 6
    • 0342903296 scopus 로고    scopus 로고
    • P-glycoprotein, glutathione and glutathione S-transferase increase in a colon carcinoma cell line by colchicine
    • Ruiz-Gomez M.J., Souviron A., Martinez-Morillo M., and Gil L. P-glycoprotein, glutathione and glutathione S-transferase increase in a colon carcinoma cell line by colchicine. J. Physiol. Biochem. 56 (2000) 307-312
    • (2000) J. Physiol. Biochem. , vol.56 , pp. 307-312
    • Ruiz-Gomez, M.J.1    Souviron, A.2    Martinez-Morillo, M.3    Gil, L.4
  • 7
    • 0027250219 scopus 로고
    • Glutathione S-transferase expression in benign and malignant ovarian tumours
    • Green J.A., Robertson L.J., and Clark A.H. Glutathione S-transferase expression in benign and malignant ovarian tumours. Br. J. Cancer 68 (1993) 235-239
    • (1993) Br. J. Cancer , vol.68 , pp. 235-239
    • Green, J.A.1    Robertson, L.J.2    Clark, A.H.3
  • 8
    • 0027245815 scopus 로고
    • Immunohistochemical detection of P-glycoprotein and GSTP1-1 in testis cancer
    • Katagiri A., Tomita Y., Nishiyama T., Kimura M., and Sato S. Immunohistochemical detection of P-glycoprotein and GSTP1-1 in testis cancer. Br. J. Cancer 68 (1993) 125-129
    • (1993) Br. J. Cancer , vol.68 , pp. 125-129
    • Katagiri, A.1    Tomita, Y.2    Nishiyama, T.3    Kimura, M.4    Sato, S.5
  • 9
    • 0029143232 scopus 로고
    • Characterization of a human bladder cancer cell line selected for resistance to BMY 25067, a novel analogue of mitomycin C
    • Singh S.V., Xu B.H., Gupta V., Emerson E.O., Zaren H.A., and Jani J.P. Characterization of a human bladder cancer cell line selected for resistance to BMY 25067, a novel analogue of mitomycin C. Cancer Lett. 95 (1995) 49-56
    • (1995) Cancer Lett. , vol.95 , pp. 49-56
    • Singh, S.V.1    Xu, B.H.2    Gupta, V.3    Emerson, E.O.4    Zaren, H.A.5    Jani, J.P.6
  • 10
    • 0028370564 scopus 로고
    • Increase in placental glutathione S-transferase in human oral epithelial dysplastic lesions and squamous cell carcinomas
    • Zhang L., Xiao Y., and Priddy R. Increase in placental glutathione S-transferase in human oral epithelial dysplastic lesions and squamous cell carcinomas. J. Oral Pathol. Med. 23 (1994) 75-79
    • (1994) J. Oral Pathol. Med. , vol.23 , pp. 75-79
    • Zhang, L.1    Xiao, Y.2    Priddy, R.3
  • 11
    • 0028373157 scopus 로고
    • Glutathione S-transferase expression in renal cell carcinoma: a new marker of differentiation
    • Grignon D.J., Abdel-Malak M., Mertens W.C., Sakr W.A., and Shepherd R.R. Glutathione S-transferase expression in renal cell carcinoma: a new marker of differentiation. Mod. Pathol. 7 (1994) 186-189
    • (1994) Mod. Pathol. , vol.7 , pp. 186-189
    • Grignon, D.J.1    Abdel-Malak, M.2    Mertens, W.C.3    Sakr, W.A.4    Shepherd, R.R.5
  • 12
    • 15944389432 scopus 로고    scopus 로고
    • Glutathione S-transferase-pi expression is downregulated in patients with Barrett's esophagus and esophageal adenocarcinoma
    • Brabender J., Lord R.V., Wickramasinghe K., Metzger R., Schneider P.M., Park J.M., et al. Glutathione S-transferase-pi expression is downregulated in patients with Barrett's esophagus and esophageal adenocarcinoma. J. Gastrointest. Surg. 6 (2002) 359-367
    • (2002) J. Gastrointest. Surg. , vol.6 , pp. 359-367
    • Brabender, J.1    Lord, R.V.2    Wickramasinghe, K.3    Metzger, R.4    Schneider, P.M.5    Park, J.M.6
  • 13
    • 0028068239 scopus 로고
    • Expression of glutathione S-transferase-pi and sensitivity of human gastric cancer cells to cisplatin
    • Okuyama T., Maehara Y., Endo K., Baba H., Adachi Y., Kuwano M., and Sugimachi K. Expression of glutathione S-transferase-pi and sensitivity of human gastric cancer cells to cisplatin. Cancer 74 (1994) 1230-1236
    • (1994) Cancer , vol.74 , pp. 1230-1236
    • Okuyama, T.1    Maehara, Y.2    Endo, K.3    Baba, H.4    Adachi, Y.5    Kuwano, M.6    Sugimachi, K.7
  • 15
    • 0028809193 scopus 로고
    • Site-directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperatively in glutathione transferase P1-1
    • Ricci G., Lo Bello M., Caccurri A.M., Pastore A., Nuccetelli M., Parker M.W., and Federici G. Site-directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperatively 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    Caccurri, A.M.3    Pastore, A.4    Nuccetelli, M.5    Parker, M.W.6    Federici, G.7
  • 16
    • 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., and 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
  • 17
    • 29644440152 scopus 로고    scopus 로고
    • Nitrosylation of human glutathione transferase P1-1 with dinitrosyl diglutathionyl iron complex in vitro and in vivo
    • Cesareo E., Parker L.J., Pedersen J.Z., Nuccetelli M., Mazzetti A.P., Pastore A., et al. Nitrosylation of human glutathione transferase P1-1 with dinitrosyl diglutathionyl iron complex in vitro and in vivo. J. Biol. Chem. 280 (2005) 42172-42180
    • (2005) J. Biol. Chem. , vol.280 , pp. 42172-42180
    • Cesareo, E.1    Parker, L.J.2    Pedersen, J.Z.3    Nuccetelli, M.4    Mazzetti, A.P.5    Pastore, A.6
  • 18
    • 0033516580 scopus 로고    scopus 로고
    • Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding
    • Caccuri A.M., Antonini G., Ascenzi P., Nicotra M., Nuccetelli M., Mazzetti A.P., et al. Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding. J. Biol. Chem. 274 (1999) 19276-19280
    • (1999) J. Biol. Chem. , vol.274 , pp. 19276-19280
    • Caccuri, A.M.1    Antonini, G.2    Ascenzi, P.3    Nicotra, M.4    Nuccetelli, M.5    Mazzetti, A.P.6
  • 19
    • 0030923311 scopus 로고    scopus 로고
    • Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme
    • Lo Bello M., Oakley A.J., Battistoni A., Mazzetti A.P., Nuccetelli M., Mazzarese G., et al. Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on 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
  • 20
    • 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., et al. 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
  • 21
    • 0030057817 scopus 로고    scopus 로고
    • Structural flexibility modulates the activity of human glutathione transferase P1-1. Influence of a poor co-substrate on dynamics and kinetics of human glutathione transferase
    • Caccuri A.M., Ascenzi P., Antonini G., Parker M.W., Oakley A.J., Chiessi E., et al. Structural flexibility modulates the activity of human glutathione transferase P1-1. Influence of a poor co-substrate on dynamics and kinetics of human glutathione transferase. J. Biol. Chem. 271 (1996) 16193-16198
    • (1996) J. Biol. Chem. , vol.271 , pp. 16193-16198
    • Caccuri, A.M.1    Ascenzi, P.2    Antonini, G.3    Parker, M.W.4    Oakley, A.J.5    Chiessi, E.6
  • 22
    • 0025255437 scopus 로고
    • Primary and secondary structural analyses of glutathione S-transferase pi from human placenta
    • Ahmad H., Wilson D.E., Fritz R.R., Singh S.V., Medh R.D., Nagle G.T., et al. Primary and secondary structural analyses of glutathione S-transferase pi from human placenta. Arch. Biochem. Biophys. 278 (1990) 398-408
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 398-408
    • Ahmad, H.1    Wilson, D.E.2    Fritz, R.R.3    Singh, S.V.4    Medh, R.D.5    Nagle, G.T.6
  • 23
    • 0030899372 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins
    • Ali-Osman F., Akande O., Antoun G., Mao J.X., and Buolamwini J. Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins. J. Biol. Chem. 272 (1997) 10004-10012
    • (1997) J. Biol. Chem. , vol.272 , pp. 10004-10012
    • Ali-Osman, F.1    Akande, O.2    Antoun, G.3    Mao, J.X.4    Buolamwini, J.5
  • 25
    • 0031558238 scopus 로고    scopus 로고
    • Inhibitors of glutathione S-transferases as therapeutic agents
    • Tew K.D., Dutta S., and Schultz M. Inhibitors of glutathione S-transferases as therapeutic agents. Adv. Drug Deliv. Rev. 26 (1997) 91-104
    • (1997) Adv. Drug Deliv. Rev. , vol.26 , pp. 91-104
    • Tew, K.D.1    Dutta, S.2    Schultz, M.3
  • 26
    • 0025039054 scopus 로고
    • Chronic lymphocytic leukemia: new insights into biology and therapy
    • Foon K.A., Rai K.R., and Gale R.P. Chronic lymphocytic leukemia: new insights into biology and therapy. Ann. Intern. Med. 113 (1990) 525-539
    • (1990) Ann. Intern. Med. , vol.113 , pp. 525-539
    • Foon, K.A.1    Rai, K.R.2    Gale, R.P.3
  • 27
    • 0025123477 scopus 로고
    • The spontaneous and glutathione S-transferase-mediated reaction of chlorambucil with glutathione
    • Ciaccio P.J., Tew K.D., and LaCreta F.P. The spontaneous and glutathione S-transferase-mediated reaction of chlorambucil with glutathione. Cancer Commun. 2 (1990) 279-285
    • (1990) Cancer Commun. , vol.2 , pp. 279-285
    • Ciaccio, P.J.1    Tew, K.D.2    LaCreta, F.P.3
  • 29
    • 0033567422 scopus 로고    scopus 로고
    • Characterization of a chlorambucil-resistant human ovarian carcinoma cell line overexpressing glutathione S-transferase m
    • Horton J.K., Roy G., Piper J.T., van Houten B., Awasthi Y.C., Mitra S., et al. Characterization of a chlorambucil-resistant human ovarian carcinoma cell line overexpressing glutathione S-transferase m. Biochem. Pharmacol. 58 (1999) 693-702
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 693-702
    • Horton, J.K.1    Roy, G.2    Piper, J.T.3    van Houten, B.4    Awasthi, Y.C.5    Mitra, S.6
  • 30
    • 0141648082 scopus 로고    scopus 로고
    • The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution
    • Oakley A.J., Lo Bello M., Battistoni A., Ricci G., Rossjohn J., Villar H.O., and Parker M.W. The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution. J. Mol. Biol. 274 (1997) 84-100
    • (1997) J. Mol. Biol. , vol.274 , pp. 84-100
    • Oakley, A.J.1    Lo Bello, M.2    Battistoni, A.3    Ricci, G.4    Rossjohn, J.5    Villar, H.O.6    Parker, M.W.7
  • 31
    • 0029783044 scopus 로고    scopus 로고
    • Cross-linking of human placenta pi class glutathione S-transferase dimer by chlorambucil
    • Hathout Y., Ellis T., Fabris D., and Fenselau C. Cross-linking of human placenta pi class glutathione S-transferase dimer by chlorambucil. Chem. Res. Toxicol. 9 (1996) 1044-1049
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 1044-1049
    • Hathout, Y.1    Ellis, T.2    Fabris, D.3    Fenselau, C.4
  • 32
    • 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., and 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
  • 33
    • 0031017331 scopus 로고    scopus 로고
    • The three-dimensional structure of 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., and Parker M.W. The three-dimensional structure of 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
  • 34
    • 0028088048 scopus 로고
    • Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties
    • Zimniak P., Nanduri B., Pikula S., Bandorowicz-Pikula J., Singhal S.S., Srivastava S.K., et al. Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties. Eur. J. Biochem. 224 (1994) 893-899
    • (1994) Eur. J. Biochem. , vol.224 , pp. 893-899
    • Zimniak, P.1    Nanduri, B.2    Pikula, S.3    Bandorowicz-Pikula, J.4    Singhal, S.S.5    Srivastava, S.K.6
  • 35
    • 0032496408 scopus 로고    scopus 로고
    • Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105
    • Johansson A.S., Stenberg G., Widersten M., and Mannervik B. Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105. J. Mol. Biol. 278 (1998) 687-698
    • (1998) J. Mol. Biol. , vol.278 , pp. 687-698
    • Johansson, A.S.1    Stenberg, G.2    Widersten, M.3    Mannervik, B.4
  • 36
    • 0344352500 scopus 로고    scopus 로고
    • The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two different modes
    • Oakley A.J., Lo Bello M., Mazzetti A.P., Federici G., and Parker M.W. The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two different modes. FEBS Lett. 419 (1997) 32-36
    • (1997) FEBS Lett. , vol.419 , pp. 32-36
    • Oakley, A.J.1    Lo Bello, M.2    Mazzetti, A.P.3    Federici, G.4    Parker, M.W.5
  • 37
    • 0030748102 scopus 로고    scopus 로고
    • Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase
    • Ji X., Tordova M., O'Donnell R., Parsons J.F., Hayden J.B., Gilliland G.L., and Zimniak P. Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochemistry 36 (1997) 9690-9702
    • (1997) Biochemistry , vol.36 , pp. 9690-9702
    • Ji, X.1    Tordova, M.2    O'Donnell, R.3    Parsons, J.F.4    Hayden, J.B.5    Gilliland, G.L.6    Zimniak, P.7
  • 38
    • 0033543218 scopus 로고    scopus 로고
    • Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1
    • Ji X., Blaszczyk J., Xiao B., O'Donnell R., Hu X., Herzog C., et al. Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1. Biochemistry 38 (1999) 10231-10238
    • (1999) Biochemistry , vol.38 , pp. 10231-10238
    • Ji, X.1    Blaszczyk, J.2    Xiao, B.3    O'Donnell, R.4    Hu, X.5    Herzog, C.6
  • 39
    • 0031577576 scopus 로고    scopus 로고
    • Activity of four allelic forms of glutathione S-transferase hGSTP1-1 for diol epoxides of polycyclic aromatic hydrocarbons
    • Hu X., Xia H., Srivastava S.K., Herzog C., Awasthi Y.C., Ji X., et al. Activity of four allelic forms of glutathione S-transferase hGSTP1-1 for diol epoxides of polycyclic aromatic hydrocarbons. Biochem. Biophys. Res. Commun. 238 (1997) 397-402
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 397-402
    • Hu, X.1    Xia, H.2    Srivastava, S.K.3    Herzog, C.4    Awasthi, Y.C.5    Ji, X.6
  • 41
    • 0021687639 scopus 로고
    • Different base/base mismatches are corrected with different efficiencies by the methyl-directed DNA mismatch-repair system of E. coli
    • Kramer B., Kramer W., and Fritz M.J. Different base/base mismatches are corrected with different efficiencies by the methyl-directed DNA mismatch-repair system of E. coli. Cell 38 (1984) 879-887
    • (1984) Cell , vol.38 , pp. 879-887
    • Kramer, B.1    Kramer, W.2    Fritz, M.J.3
  • 42
    • 0017669854 scopus 로고
    • Purification of glutathione S-transferase from human liver by affinity chromatography
    • Simon P.C., and Vander Jagt D.L. Purification of glutathione S-transferase from human liver by affinity chromatography. Anal. Biochem. 82 (1977) 334-341
    • (1977) Anal. Biochem. , vol.82 , pp. 334-341
    • Simon, P.C.1    Vander Jagt, D.L.2
  • 44
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.T., and Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.T.2    Jakoby, W.B.3
  • 45
    • 0028262418 scopus 로고
    • Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole
    • Ricci G., Caccuri A.M., Lo Bello M., Pastore A., Piemonte F., and Federici G. Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Anal. Biochem. 218 (1994) 463-465
    • (1994) Anal. Biochem. , vol.218 , pp. 463-465
    • Ricci, G.1    Caccuri, A.M.2    Lo Bello, M.3    Pastore, A.4    Piemonte, F.5    Federici, G.6
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in the oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in the oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 0033119386 scopus 로고    scopus 로고
    • Software for handling macromolecular envelopes
    • Kleywegt G.J., and Jones T.A. Software for handling macromolecular envelopes. Acta Crystallogr. D 55 (1999) 941-944
    • (1999) Acta Crystallogr. D , vol.55 , pp. 941-944
    • Kleywegt, G.J.1    Jones, T.A.2
  • 50
    • 0030498233 scopus 로고    scopus 로고
    • xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets
    • Kleywegt G.J., and Jones T.A. xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets. Acta Crystallogr. D 52 (1996) 826-828
    • (1996) Acta Crystallogr. D , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 51
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 52
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 54


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.