메뉴 건너뛰기




Volumn 7, Issue 4, 2012, Pages

Differential scanning fluorometry signatures as indicators of enzyme inhibitor mode of action: Case study of glutathione s-transferase

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; GLUTATHIONE; GLUTATHIONE CONJUGATE; GLUTATHIONE S TRANSFERASE INHIBITOR; GLUTATHIONE TRANSFERASE; UNCLASSIFIED DRUG; BIOMIMETIC MATERIAL; ISOENZYME;

EID: 84860472604     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036219     Document Type: Article
Times cited : (29)

References (52)
  • 1
    • 27244440118 scopus 로고    scopus 로고
    • Affinity assays for decrypting protein targets of unknown function
    • Todd MCMD, Nelen MI, (2005) Affinity assays for decrypting protein targets of unknown function. Drug Discovery Today: Technologies 2: 267-273.
    • (2005) Drug Discovery Today: Technologies , vol.2 , pp. 267-273
    • Todd, M.C.M.D.1    Nelen, M.I.2
  • 2
    • 33749850046 scopus 로고    scopus 로고
    • Universal screening methods and applications of ThermoFluor
    • Cummings MD, Farnum MA, Nelen MI, (2006) Universal screening methods and applications of ThermoFluor. J Biomol Screen 11: 854-863.
    • (2006) J Biomol Screen , vol.11 , pp. 854-863
    • Cummings, M.D.1    Farnum, M.A.2    Nelen, M.I.3
  • 4
    • 0030726361 scopus 로고    scopus 로고
    • pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far- and near-UV CD spectroscopy, and ANS fluorescence
    • Poklar N, Lah J, Salobir M, Macek P, Vesnaver G, (1997) pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far- and near-UV CD spectroscopy, and ANS fluorescence. Biochemistry 36: 14345-14352.
    • (1997) Biochemistry , vol.36 , pp. 14345-14352
    • Poklar, N.1    Lah, J.2    Salobir, M.3    Macek, P.4    Vesnaver, G.5
  • 5
    • 33750470057 scopus 로고    scopus 로고
    • Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
    • Vedadi M, Niesen FH, Allali-Hassani A, Fedorov OY, Finerty PJ Jr, et al. (2006) Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc Natl Acad Sci U S A 103: 15835-15840.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15835-15840
    • Vedadi, M.1    Niesen, F.H.2    Allali-Hassani, A.3    Fedorov, O.Y.4    Finerty Jr., P.J.5
  • 6
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, Hallberg BM, Detitta GT, Dekker N, Nordlund P, (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem 357: 289-298.
    • (2006) Anal Biochem , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 7
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M, (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2: 2212-2221.
    • (2007) Nat Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 8
    • 77958601308 scopus 로고    scopus 로고
    • Affinity-based screening techniques: their impact and benefit to increase the number of high quality leads
    • Bergsdorf C, Ottl J, (2010) Affinity-based screening techniques: their impact and benefit to increase the number of high quality leads. Expert Opinion in Drug Discovery 5: 1095-1107.
    • (2010) Expert Opinion in Drug Discovery , vol.5 , pp. 1095-1107
    • Bergsdorf, C.1    Ottl, J.2
  • 9
    • 20144384268 scopus 로고    scopus 로고
    • Decrypting the biochemical function of an essential gene from Streptococcus pneumoniae using ThermoFluor technology
    • Carver TE, Bordeau B, Cummings MD, Petrella EC, Pucci MJ, et al. (2005) Decrypting the biochemical function of an essential gene from Streptococcus pneumoniae using ThermoFluor technology. J Biol Chem 280: 11704-11712.
    • (2005) J Biol Chem , vol.280 , pp. 11704-11712
    • Carver, T.E.1    Bordeau, B.2    Cummings, M.D.3    Petrella, E.C.4    Pucci, M.J.5
  • 10
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo MC, Aulabaugh A, Jin G, Cowling R, Bard J, et al. (2004) Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal Biochem 332: 153-159.
    • (2004) Anal Biochem , vol.332 , pp. 153-159
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5
  • 11
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor
    • Matulis D, Kranz JK, Salemme FR, Todd MJ, (2005) Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry 44: 5258-5266.
    • (2005) Biochemistry , vol.44 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 12
    • 28144464847 scopus 로고    scopus 로고
    • Structural basis of inhibitor specificity of the human protooncogene proviral insertion site in moloney murine leukemia virus (PIM-1) kinase
    • Bullock AN, Debreczeni JE, Fedorov OY, Nelson A, Marsden BD, et al. (2005) Structural basis of inhibitor specificity of the human protooncogene proviral insertion site in moloney murine leukemia virus (PIM-1) kinase. J Med Chem 48: 7604-7614.
    • (2005) J Med Chem , vol.48 , pp. 7604-7614
    • Bullock, A.N.1    Debreczeni, J.E.2    Fedorov, O.Y.3    Nelson, A.4    Marsden, B.D.5
  • 13
    • 67649644363 scopus 로고    scopus 로고
    • Measurement of nanomolar dissociation constants by titration calorimetry and thermal shift assay - radicicol binding to Hsp90 and ethoxzolamide binding to CAII
    • Zubriene A, Matuliene J, Baranauskiene L, Jachno J, Torresan J, et al. (2009) Measurement of nanomolar dissociation constants by titration calorimetry and thermal shift assay- radicicol binding to Hsp90 and ethoxzolamide binding to CAII. Int J Mol Sci 10: 2662-2680.
    • (2009) Int J Mol Sci , vol.10 , pp. 2662-2680
    • Zubriene, A.1    Matuliene, J.2    Baranauskiene, L.3    Jachno, J.4    Torresan, J.5
  • 15
    • 78249266924 scopus 로고    scopus 로고
    • High-affinity inhibitors of human NAD-dependent 15-hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and structure-activity relationships
    • Niesen FH, Schultz L, Jadhav A, Bhatia C, Guo K, et al. High-affinity inhibitors of human NAD-dependent 15-hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and structure-activity relationships. PLoS One 5: e13719.
    • PLoS One , vol.5
    • Niesen, F.H.1    Schultz, L.2    Jadhav, A.3    Bhatia, C.4    Guo, K.5
  • 18
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong RN, (1997) Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 10: 2-18.
    • (1997) Chem Res Toxicol , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 20
    • 0030963692 scopus 로고    scopus 로고
    • Expression of a Schistosoma mansoni 28-kilodalton glutathione S-transferase in the livers of transgenic mice and its effect on parasite infection
    • Xu X, Lemaire C, Grzych JM, Pierce RJ, Raccurt M, et al. (1997) Expression of a Schistosoma mansoni 28-kilodalton glutathione S-transferase in the livers of transgenic mice and its effect on parasite infection. Infect Immun 65: 3867-3874.
    • (1997) Infect Immun , vol.65 , pp. 3867-3874
    • Xu, X.1    Lemaire, C.2    Grzych, J.M.3    Pierce, R.J.4    Raccurt, M.5
  • 21
    • 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 MA, Williams DR, Tainer JA, (1995) 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: 21-27.
    • (1995) J Mol Biol , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 22
    • 0343852701 scopus 로고    scopus 로고
    • Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag
    • Kaplan W, Husler P, Klump H, Erhardt J, Sluis-Cremer N, et al. (1997) Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag. Protein Sci 6: 399-406.
    • (1997) Protein Sci , vol.6 , pp. 399-406
    • Kaplan, W.1    Husler, P.2    Klump, H.3    Erhardt, J.4    Sluis-Cremer, N.5
  • 23
    • 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 AD, Sinning I, L'Hermite G, Olin B, Board PG, et al. (1995) 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 3: 717-727.
    • (1995) Structure , vol.3 , pp. 717-727
    • Cameron, A.D.1    Sinning, I.2    L'Hermite, G.3    Olin, B.4    Board, P.G.5
  • 24
    • 0036719369 scopus 로고    scopus 로고
    • 1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site
    • Le Trong I, Stenkamp RE, Ibarra C, Atkins WM, Adman ET, (2002) 1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site. Proteins 48: 618-627.
    • (2002) Proteins , vol.48 , pp. 618-627
    • Le Trong, I.1    Stenkamp, R.E.2    Ibarra, C.3    Atkins, W.M.4    Adman, E.T.5
  • 25
    • 33644549065 scopus 로고    scopus 로고
    • X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site
    • Rufer AC, Thiebach L, Baer K, Klein HW, Hennig M, (2005) X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site. Acta Crystallogr Sect F Struct Biol Cryst Commun 61: 263-265.
    • (2005) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.61 , pp. 263-265
    • Rufer, A.C.1    Thiebach, L.2    Baer, K.3    Klein, H.W.4    Hennig, M.5
  • 26
    • 24944535773 scopus 로고    scopus 로고
    • Crystal structure of non-fused glutathione S-transferase from Schistosoma japonicum in complex with glutathione
    • Kursula I, Heape AM, Kursula P, (2005) Crystal structure of non-fused glutathione S-transferase from Schistosoma japonicum in complex with glutathione. Protein Pept Lett 12: 709-712.
    • (2005) Protein Pept Lett , vol.12 , pp. 709-712
    • Kursula, I.1    Heape, A.M.2    Kursula, P.3
  • 27
    • 0037375585 scopus 로고    scopus 로고
    • Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum
    • Cardoso RM, Daniels DS, Bruns CM, Tainer JA, (2003) Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum. Proteins 51: 137-146.
    • (2003) Proteins , vol.51 , pp. 137-146
    • Cardoso, R.M.1    Daniels, D.S.2    Bruns, C.M.3    Tainer, J.A.4
  • 28
    • 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 AJ, Rossjohn J, Lo Bello M, Caccuri AM, Federici G, et al. (1997) 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: 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
  • 29
    • 0026722795 scopus 로고
    • Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution
    • Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, et al. (1992) Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol 227: 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
  • 30
    • 21144440291 scopus 로고    scopus 로고
    • The chemistry and biology of inhibitors and pro-drugs targeted to glutathione S-transferases
    • Mahajan S, Atkins WM, (2005) The chemistry and biology of inhibitors and pro-drugs targeted to glutathione S-transferases. Cell Mol Life Sci 62: 1221-1233.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1221-1233
    • Mahajan, S.1    Atkins, W.M.2
  • 32
    • 0033038758 scopus 로고    scopus 로고
    • Concise review of the glutathione S-transferases and their significance to toxicology
    • Eaton DL, Bammler TK, (1999) Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol Sci 49: 156-164.
    • (1999) Toxicol Sci , vol.49 , pp. 156-164
    • Eaton, D.L.1    Bammler, T.K.2
  • 33
    • 0033609951 scopus 로고    scopus 로고
    • The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site)
    • Oakley AJ, Lo Bello M, Nuccetelli M, Mazzetti AP, Parker MW, (1999) The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site). J Mol Biol 291: 913-926.
    • (1999) J Mol Biol , vol.291 , pp. 913-926
    • Oakley, A.J.1    Lo Bello, M.2    Nuccetelli, M.3    Mazzetti, A.P.4    Parker, M.W.5
  • 34
    • 0035877779 scopus 로고    scopus 로고
    • Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus
    • Wang T, Arifoglu P, Ronai Z, Tew KD, (2001) Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus. J Biol Chem 276: 20999-21003.
    • (2001) J Biol Chem , vol.276 , pp. 20999-21003
    • Wang, T.1    Arifoglu, P.2    Ronai, Z.3    Tew, K.D.4
  • 35
    • 77955713764 scopus 로고    scopus 로고
    • Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death
    • Laborde E, Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death Cell Death Differ 17: 1373-1380.
    • Cell Death Differ , vol.17 , pp. 1373-1380
    • Laborde, E.1
  • 36
    • 0035918227 scopus 로고    scopus 로고
    • Glutathione S-transferase mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1
    • Cho SG, Lee YH, Park HS, Ryoo K, Kang KW, et al. (2001) Glutathione S-transferase mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1. J Biol Chem 276: 12749-12755.
    • (2001) J Biol Chem , vol.276 , pp. 12749-12755
    • Cho, S.G.1    Lee, Y.H.2    Park, H.S.3    Ryoo, K.4    Kang, K.W.5
  • 37
    • 0026049559 scopus 로고
    • The inhibition of glutathione S-transferases: mechanisms, toxic consequences and therapeutic benefits
    • van Bladeren PJ, van Ommen B, (1991) The inhibition of glutathione S-transferases: mechanisms, toxic consequences and therapeutic benefits. Pharmacol Ther 51: 35-46.
    • (1991) Pharmacol Ther , vol.51 , pp. 35-46
    • van Bladeren, P.J.1    van Ommen, B.2
  • 38
    • 0041316988 scopus 로고    scopus 로고
    • Novel class of bivalent glutathione S-transferase inhibitors
    • Lyon RP, Hill JJ, Atkins WM, (2003) Novel class of bivalent glutathione S-transferase inhibitors. Biochemistry 42: 10418-10428.
    • (2003) Biochemistry , vol.42 , pp. 10418-10428
    • Lyon, R.P.1    Hill, J.J.2    Atkins, W.M.3
  • 40
    • 22544436117 scopus 로고    scopus 로고
    • 7-Nitro-2,1,3-benzoxadiazole derivatives, a new class of suicide inhibitors for glutathione S-transferases. Mechanism of action of potential anticancer drugs
    • Ricci G, De Maria F, Antonini G, Turella P, Bullo A, et al. (2005) 7-Nitro-2,1,3-benzoxadiazole derivatives, a new class of suicide inhibitors for glutathione S-transferases. Mechanism of action of potential anticancer drugs. J Biol Chem 280: 26397-26405.
    • (2005) J Biol Chem , vol.280 , pp. 26397-26405
    • Ricci, G.1    De Maria, F.2    Antonini, G.3    Turella, P.4    Bullo, A.5
  • 41
    • 0034625367 scopus 로고    scopus 로고
    • The catalytic Tyr-9 of glutathione S-transferase A1-1 controls the dynamics of the C terminus
    • Nieslanik BS, Atkins WM, (2000) The catalytic Tyr-9 of glutathione S-transferase A1-1 controls the dynamics of the C terminus. J Biol Chem 275: 17447-17451.
    • (2000) J Biol Chem , vol.275 , pp. 17447-17451
    • Nieslanik, B.S.1    Atkins, W.M.2
  • 44
    • 0016821982 scopus 로고
    • Purification and Characterization of Two Glutathione S-Aryltransferase Activities from Rat Liver
    • Askelof P, Guthenberg C, Jakobson I, Mannervik B, (1975) Purification and Characterization of Two Glutathione S-Aryltransferase Activities from Rat Liver. Biochem J 147: 513-522.
    • (1975) Biochem J , vol.147 , pp. 513-522
    • Askelof, P.1    Guthenberg, C.2    Jakobson, I.3    Mannervik, B.4
  • 45
    • 33646501425 scopus 로고    scopus 로고
    • Kinetic study on the irreversible thermal denaturation of Schistosoma japonicum glutathione S-transferase
    • Quesada-Soriano I, Garcia-Maroto F, Garcia-Fuentes L, (2006) Kinetic study on the irreversible thermal denaturation of Schistosoma japonicum glutathione S-transferase. Biochim Biophys Acta 1764: 979-984.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 979-984
    • Quesada-Soriano, I.1    Garcia-Maroto, F.2    Garcia-Fuentes, L.3
  • 46
    • 0030581299 scopus 로고    scopus 로고
    • Effect of glutathione, glutathione sulphonate and S-hexylglutathione on the conformational stability of class pi glutathione S-transferase
    • Erhardt J, Dirr H, (1996) Effect of glutathione, glutathione sulphonate and S-hexylglutathione on the conformational stability of class pi glutathione S-transferase. FEBS Lett 391: 313-316.
    • (1996) FEBS Lett , vol.391 , pp. 313-316
    • Erhardt, J.1    Dirr, H.2
  • 47
    • 13444311620 scopus 로고    scopus 로고
    • Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum
    • Andujar-Sanchez M, Smith AW, Clemente-Jimenez JM, Rodriguez-Vico F, Las Heras-Vazquez FJ, et al. (2005) Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum. Biochemistry 44: 1174-1183.
    • (2005) Biochemistry , vol.44 , pp. 1174-1183
    • Andujar-Sanchez, M.1    Smith, A.W.2    Clemente-Jimenez, J.M.3    Rodriguez-Vico, F.4    Las Heras-Vazquez, F.J.5
  • 48
    • 0027451261 scopus 로고
    • Significance of an unusually low Km for glutathione in glutathione transferases of the alpha, mu and pi classes
    • Meyer DJ, (1993) Significance of an unusually low Km for glutathione in glutathione transferases of the alpha, mu and pi classes. Xenobiotica 23: 823-834.
    • (1993) Xenobiotica , vol.23 , pp. 823-834
    • Meyer, D.J.1
  • 49
    • 0027304368 scopus 로고
    • Interactions of glutathione S-transferase-pi with ethacrynic acid and its glutathione conjugate
    • Awasthi S, Srivastava SK, Ahmad F, Ahmad H, Ansari GA, (1993) Interactions of glutathione S-transferase-pi with ethacrynic acid and its glutathione conjugate. Biochim Biophys Acta 1164: 173-178.
    • (1993) Biochim Biophys Acta , vol.1164 , pp. 173-178
    • Awasthi, S.1    Srivastava, S.K.2    Ahmad, F.3    Ahmad, H.4    Ansari, G.A.5
  • 51
    • 0025743949 scopus 로고
    • Flavonoids as inhibitors of rat liver cytosolic glutathione S-transferase
    • Merlos M, Sanchez RM, Camarasa J, Adzet T, (1990) Flavonoids as inhibitors of rat liver cytosolic glutathione S-transferase. Experientia 47: 616-619.
    • (1990) Experientia , vol.47 , pp. 616-619
    • Merlos, M.1    Sanchez, R.M.2    Camarasa, J.3    Adzet, T.4
  • 52
    • 2342449282 scopus 로고    scopus 로고
    • Implications of the ligandin binding site on the binding of non-substrate ligands to Schistosoma japonicum-glutathione transferase
    • Yassin Z, Ortiz-Salmeron E, Garcia-Maroto F, Baron C, Garcia-Fuentes L, (2004) Implications of the ligandin binding site on the binding of non-substrate ligands to Schistosoma japonicum-glutathione transferase. Biochim Biophys Acta 1698: 227-237.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 227-237
    • Yassin, Z.1    Ortiz-Salmeron, E.2    Garcia-Maroto, F.3    Baron, C.4    Garcia-Fuentes, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.