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Volumn 288, Issue 34, 2013, Pages 24936-24947

The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: A proposal for an evolutionary driving force

(21)  Bocedi, Alessio a   Fabrini, Raffaele a   Farrotti, Andrea a   Stella, Lorenzo a   Ketterman, Albert J b   Pedersen, Jens Z c   Allocati, Nerino d   Lau, Peter C K e   Grosse, Stephan e   Eltis, Lindsay D f   Ruzzini, Antonio f   Edwards, Thomas E g,h   Morici, Laura a   Grosso, Erica Del a   Guidoni, Leonardo i,j   Bovi, Daniele i   Bello, Mario Lo c   Federici, Giorgio k   Parker, Michael W l,m   Board, Philip G n   more..


Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; MAMMALS; NETWORK SECURITY; NITRIC OXIDE; PEPTIDES; TOXICITY;

EID: 84883184902     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.476135     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong, R. N. (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
  • 4
    • 21644475953 scopus 로고    scopus 로고
    • Analysis of the glutathione S-transferase (GST) gene family
    • Nebert, D. W., and Vasiliou, V. (2004) Analysis of the glutathione S-transferase (GST) gene family. Hum. Genomics 1, 460-464
    • (2004) Hum. Genomics , vol.1 , pp. 460-464
    • Nebert, D.W.1    Vasiliou, V.2
  • 5
    • 72749095187 scopus 로고    scopus 로고
    • Glutathione transferases are structural and functional outliers in the thioredoxin fold
    • Atkinson, H. J., and Babbitt, P. C. (2009) Glutathione Transferases are structural and functional outliers in the thioredoxin fold. Biochemistry 48, 11108-11116
    • (2009) Biochemistry , vol.48 , pp. 11108-11116
    • Atkinson, H.J.1    Babbitt, P.C.2
  • 6
    • 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. (2001) Structure, function and evolution of glutathione transferases. Implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360, 1-16
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 7
    • 77953752629 scopus 로고    scopus 로고
    • What part of NO don't you understand? Some answers to the cardinal questions in nitric oxide biology
    • Hill, B. G., Dranka, B. P., Bailey, S. M., Lancaster, J. R., Jr., and Darley-Usmar, V. M. (2010) What part of NO don't you understand? Some answers to the cardinal questions in nitric oxide biology. J. Biol. Chem. 285, 19699-19704
    • (2010) J. Biol. Chem. , vol.285 , pp. 19699-19704
    • Hill, B.G.1    Dranka, B.P.2    Bailey, S.M.3    Lancaster Jr., J.R.4    Darley-Usmar, V.M.5
  • 8
    • 0034098690 scopus 로고    scopus 로고
    • The physiological activity and in vivo distribution of dinitrosyl dithiolato iron complex
    • Ueno, T., and Yoshimura, T. (2000) The physiological activity and in vivo distribution of dinitrosyl dithiolato iron complex. Jpn. J. Pharmacol. 82, 95-101
    • (2000) Jpn. J. Pharmacol. , vol.82 , pp. 95-101
    • Ueno, T.1    Yoshimura, T.2
  • 10
    • 0342940743 scopus 로고    scopus 로고
    • Dinitrosyl-dithiol-iron complexes, nitric oxide (NO) carriers in vivo, as potent inhibitors of human glutathione reductase and glutathione S-transferase
    • Keese, M. A., Böse, M., Mülsch, A., Schirmer, R. H., and Becker, K. (1997) Dinitrosyl-dithiol-iron complexes, nitric oxide (NO) carriers in vivo, as potent inhibitors of human glutathione reductase and glutathione S-transferase. Biochem. Pharmacol. 54, 1307-1313
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 1307-1313
    • Keese, M.A.1    Böse, M.2    Mülsch, A.3    Schirmer, R.H.4    Becker, K.5
  • 12
    • 0142242187 scopus 로고    scopus 로고
    • The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily. Suggestion for an evolutionary pressure in the direction of the storage of nitric oxide
    • De Maria, F., Pedersen, J. Z., Caccuri, A. M., Antonini, G., Turella, P., Stella, L., Lo Bello, M., Federici, G., and Ricci, G. (2003) The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily. Suggestion for an evolutionary pressure in the direction of the storage of nitric oxide. J. Biol. Chem. 278, 42283-42293
    • (2003) J. Biol. Chem. , vol.278 , pp. 42283-42293
    • De Maria, F.1    Pedersen, J.Z.2    Caccuri, A.M.3    Antonini, G.4    Turella, P.5    Stella, L.6    Lo Bello, M.7    Federici, G.8    Ricci, G.9
  • 13
    • 0142211239 scopus 로고    scopus 로고
    • Glutathione transferase superfamily behaves like storage proteins for dinitrosyl-diglutathionyliron complex in heterogeneous systems
    • Turella, P., Pedersen, J. Z., Caccuri, A. M., De Maria, F., Mastroberardino, P., Lo Bello, M., Federici, G., and Ricci, G. (2003) Glutathione transferase superfamily behaves like storage proteins for dinitrosyl-diglutathionyliron complex in heterogeneous systems. J. Biol. Chem. 278, 42294-42299
    • (2003) J. Biol. Chem. , vol.278 , pp. 42294-42299
    • Turella, P.1    Pedersen, J.Z.2    Caccuri, A.M.3    De Maria, F.4    Mastroberardino, P.5    Lo Bello, M.6    Federici, G.7    Ricci, G.8
  • 15
    • 1342288076 scopus 로고    scopus 로고
    • Functional polymorphism of human glutathione transferase A2
    • Tetlow, N., and Board, P. G. (2004) Functional polymorphism of human glutathione transferase A2. Pharmacogenetics 14, 111-116
    • (2004) Pharmacogenetics , vol.14 , pp. 111-116
    • Tetlow, N.1    Board, P.G.2
  • 16
    • 6944243913 scopus 로고    scopus 로고
    • Functional polymorphism of human glutathione transferase A3. Effects on xenobiotic metabolism and steroid biosynthesis
    • Tetlow, N., Coggan, M., Casarotto, M. G., and Board, P. G. (2004) Functional polymorphism of human glutathione transferase A3. Effects on xenobiotic metabolism and steroid biosynthesis. Pharmacogenetics 14, 657-663
    • (2004) Pharmacogenetics , vol.14 , pp. 657-663
    • Tetlow, N.1    Coggan, M.2    Casarotto, M.G.3    Board, P.G.4
  • 17
    • 16644371110 scopus 로고    scopus 로고
    • Crystallization of the major cytosolic glutathione S-transferase from Onchocerca volvulus
    • Höppner, J., Perbandt, M., Betzel, Ch., Walter, R. D., and Liebau, E. (2004) Crystallization of the major cytosolic glutathione S-transferase from Onchocerca volvulus. Acta Crystallogr. D 60, 1496-1497
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1496-1497
    • Höppner, J.1    Perbandt, M.2    Betzel, Ch.3    Walter, R.D.4    Liebau, E.5
  • 19
    • 0035985070 scopus 로고    scopus 로고
    • Glutathione S-transferase of the malarial parasite Plasmodium falciparum. Characterization of a potential drug target
    • Harwaldt, P., Rahlfs, S., and Becker, K. (2002) Glutathione S-transferase of the malarial parasite Plasmodium falciparum. Characterization of a potential drug target. Biol. Chem. 383, 821-830
    • (2002) Biol. Chem. , vol.383 , pp. 821-830
    • Harwaldt, P.1    Rahlfs, S.2    Becker, K.3
  • 21
    • 0035937120 scopus 로고    scopus 로고
    • Human glutathione transferase T2-2 discloses some evolutionary strategies for optimization of substrate binding to the active site of glutathione transferases
    • Caccuri, A. M., Antonini, G., Board, P. G., Flanagan, J., Parker, M. W., Paolesse, R., Turella, P., Federici, G., Lo Bello, M., and Ricci, G. (2001) Human glutathione transferase T2-2 discloses some evolutionary strategies for optimization of substrate binding to the active site of glutathione transferases. J. Biol. Chem. 276, 5427-5431
    • (2001) J. Biol. Chem. , vol.276 , pp. 5427-5431
    • Caccuri, A.M.1    Antonini, G.2    Board, P.G.3    Flanagan, J.4    Parker, M.W.5    Paolesse, R.6    Turella, P.7    Federici, G.8    Lo Bello, M.9    Ricci, G.10
  • 22
    • 0020724324 scopus 로고
    • Purification and characterization of corn glutathione S-transferase
    • Mozer, T. J., Tiemeier, D. C., and Jaworski, E. G. (1983) Purification and characterization of corn glutathione S-transferase. Biochemistry 22, 1068-1072
    • (1983) Biochemistry , vol.22 , pp. 1068-1072
    • Mozer, T.J.1    Tiemeier, D.C.2    Jaworski, E.G.3
  • 23
    • 0034053786 scopus 로고    scopus 로고
    • Polymorphism-and species-dependent inactivation of glutathione transferase ξ by dichloroacetate
    • Tzeng, H. F., Blackburn, A. C., Board, P. G., and Anders, M. W. (2000) Polymorphism-and species-dependent inactivation of glutathione transferase ξ by dichloroacetate. Chem. Res. Toxicol. 13, 231-236
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 231-236
    • Tzeng, H.F.1    Blackburn, A.C.2    Board, P.G.3    Anders, M.W.4
  • 24
    • 0034778978 scopus 로고    scopus 로고
    • The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B
    • Oakley, A. J., Harnnoi, T., Udomsinprasert, R., Jirajaroenrat, K., Ketterman, A. J., and Wilce, M. C. (2001) The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B. Protein Sci. 10, 2176-2185
    • (2001) Protein Sci. , vol.10 , pp. 2176-2185
    • Oakley, A.J.1    Harnnoi, T.2    Udomsinprasert, R.3    Jirajaroenrat, K.4    Ketterman, A.J.5    Wilce, M.C.6
  • 25
    • 77953416164 scopus 로고    scopus 로고
    • Structural contributions of delta class glutathione transferase active-site residues to catalysis
    • Wongsantichon, J., Robinson, R. C., and Ketterman, A. J. (2010) Structural contributions of delta class glutathione transferase active-site residues to catalysis. Biochem. J. 428, 25-32
    • (2010) Biochem. J. , vol.428 , pp. 25-32
    • Wongsantichon, J.1    Robinson, R.C.2    Ketterman, A.J.3
  • 28
    • 33744991789 scopus 로고    scopus 로고
    • A glutathione S-transferase catalyzes the dehalogenation of inhibitory metabolites of polychlorinated biphenyls
    • Fortin, P. D., Horsman, G. P., Yang, H. M., and Eltis, L. D. (2006) A glutathione S-transferase catalyzes the dehalogenation of inhibitory metabolites of polychlorinated biphenyls. J. Bacteriol. 188, 4424-4430
    • (2006) J. Bacteriol. , vol.188 , pp. 4424-4430
    • Fortin, P.D.1    Horsman, G.P.2    Yang, H.M.3    Eltis, L.D.4
  • 29
    • 0032211764 scopus 로고    scopus 로고
    • Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi
    • Favaloro, B., Tamburro, A., Angelucci, S., Luca, A. D., Melino, S., di Ilio, C., and Rotilio, D. (1998) Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi. Biochem. J. 335, 573-579
    • (1998) Biochem. J. , vol.335 , pp. 573-579
    • Favaloro, B.1    Tamburro, A.2    Angelucci, S.3    Luca, A.D.4    Melino, S.5    Di Ilio, C.6    Rotilio, D.7
  • 32
    • 0029853099 scopus 로고    scopus 로고
    • Mutagenesis of the active site of the human theta-class glutathione transferase GSTT2-2. Catalysis with different substrates involves different residues
    • Tan, K. L., Chelvanayagam, G., Parker, M. W., and Board, P. G. (1996) Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2. Catalysis with different substrates involves different residues. Biochem. J. 319, 315-321
    • (1996) Biochem. J. , vol.319 , pp. 315-321
    • Tan, K.L.1    Chelvanayagam, G.2    Parker, M.W.3    Board, P.G.4
  • 34
    • 40549133470 scopus 로고    scopus 로고
    • Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site
    • Allocati, N., Federici, L., Masulli, M., Favaloro, B., and Di Ilio, C. (2008) Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site. Proteins 71, 16-23
    • (2008) Proteins , vol.71 , pp. 16-23
    • Allocati, N.1    Federici, L.2    Masulli, M.3    Favaloro, B.4    Di Ilio, C.5
  • 35
    • 10644250257 scopus 로고
    • Inhomogeneous electron gas
    • Hohenberg, P., and Kohn, W. (1964) Inhomogeneous electron gas. Phys. Rev. B 136, 864-871
    • (1964) Phys. Rev. B , vol.136 , pp. 864-871
    • Hohenberg, P.1    Kohn, W.2
  • 36
    • 0042113153 scopus 로고
    • Self-consistent equations including exchange and correlations effects
    • Kohn, W., and Sham, L. J. (1965) Self-consistent equations including exchange and correlations effects. Phys. Rev. 140, 1133-1138
    • (1965) Phys. Rev. , vol.140 , pp. 1133-1138
    • Kohn, W.1    Sham, L.J.2
  • 37
    • 0001379854 scopus 로고
    • Broken symmetry analysis of spin coupling in iron-sulfur clusters
    • Noodleman, L., Case, D. A., and Aizman, A. (1988) Broken symmetry analysis of spin coupling in iron-sulfur clusters. J. Am. Chem. Soc. 110, 1001-1005
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1001-1005
    • Noodleman, L.1    Case, D.A.2    Aizman, A.3
  • 38
    • 84859061927 scopus 로고    scopus 로고
    • The ORCA program system
    • Neese, F. (2012) The ORCA program system. WIREs Comput. Mol. Sci. 2, 73-78
    • (2012) WIREs Comput. Mol. Sci. , vol.2 , pp. 73-78
    • Neese, F.1
  • 39
    • 0042226541 scopus 로고    scopus 로고
    • Approximate second order convergence for spin unrestricted wavefunctions
    • Neese, F. (2000) Approximate Second Order Convergence for Spin Unrestricted Wavefunctions. Chem. Phys. Lett. 325, 93-98
    • (2000) Chem. Phys. Lett. , vol.325 , pp. 93-98
    • Neese, F.1
  • 40
    • 77949871593 scopus 로고    scopus 로고
    • The unusual electronic structure of dinitrosyl iron complexes
    • Ye, S., and Neese, F. (2010) The unusual electronic structure of dinitrosyl iron complexes. J. Am. Chem. Soc. 132, 3646-3647
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3646-3647
    • Ye, S.1    Neese, F.2
  • 41
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian Genetic Algorithm and empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) Automated docking using a Lamarckian Genetic Algorithm and empirical binding free energy function. J. Comput. Chem. 19, 1639-1662
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 43
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity. A rapid access to atomic charges
    • Gasteiger, J., and Marsili, M. (1980) Iterative partial equalization of orbital electronegativity. A rapid access to atomic charges. Tetrahedron 36, 3219-3228
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 44
    • 84986468608 scopus 로고
    • An approach to computing electrostatic charge for molecules
    • Singh, U. C., and Kollman, P. A. (1984) An approach to computing electrostatic charge for molecules. J. Comp. Chem. 5, 129-145
    • (1984) J. Comp. Chem. , vol.5 , pp. 129-145
    • Singh, U.C.1    Kollman, P.A.2
  • 46
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR. An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) PDB2PQR. An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-667
    • (2004) Nucleic Acids Res. , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 47
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff, D., Sharp, K. A., and Honig, B. (1994) Accurate calculation of hydration free energies using macroscopic solvent models. J. Phys. Chem. 98, 1978-1988
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 50
    • 0032478199 scopus 로고    scopus 로고
    • Proton release upon glutathione binding to glutathione transferase P1-1. Kinetic analysis of a multistep glutathione binding process
    • Caccuri, A. M., Lo Bello, M., Nuccetelli, M., Nicotra, M., Rossi, P., Antonini, G., Federici, G., and Ricci, G. (1998) Proton release upon glutathione binding to glutathione transferase P1-1. Kinetic analysis of a multistep glutathione binding process. Biochemistry 37, 3028-3034
    • (1998) Biochemistry , vol.37 , pp. 3028-3034
    • Caccuri, A.M.1    Lo Bello, M.2    Nuccetelli, M.3    Nicotra, M.4    Rossi, P.5    Antonini, G.6    Federici, G.7    Ricci, G.8
  • 52
    • 0027365971 scopus 로고
    • Isozyme specificity of novel glutathione-S-transferase inhibitors
    • Flatgaard, J. E., Bauer, K. E., and Kauvar, L. M. (1993) Isozyme specificity of novel glutathione-S-transferase inhibitors. Cancer Chemother. Pharmacol. 33, 63-70
    • (1993) Cancer Chemother. Pharmacol. , vol.33 , pp. 63-70
    • Flatgaard, J.E.1    Bauer, K.E.2    Kauvar, L.M.3
  • 54
    • 30144434095 scopus 로고    scopus 로고
    • Phylogenies of glutathione transferase families
    • Pearson, W. R. (2005) Phylogenies of glutathione transferase families. Methods Enzymol. 401, 186-204
    • (2005) Methods Enzymol. , vol.401 , pp. 186-204
    • Pearson, W.R.1
  • 55
    • 28244459618 scopus 로고    scopus 로고
    • Nitric oxide scavenging by red blood cells as a function of hematocrit and oxygenation
    • Azarov, I., Huang, K. T., Basu, S., Gladwin, M. T., Hogg, N., and Kim-Shapiro, D. B. (2005) Nitric oxide scavenging by red blood cells as a function of hematocrit and oxygenation. J. Biol. Chem. 280, 39024-39032
    • (2005) J. Biol. Chem. , vol.280 , pp. 39024-39032
    • Azarov, I.1    Huang, K.T.2    Basu, S.3    Gladwin, M.T.4    Hogg, N.5    Kim-Shapiro, D.B.6
  • 57
    • 0033013895 scopus 로고    scopus 로고
    • Induction of the SOS DNA repair response in Escherichia coli by nitric oxide donating agents. Dinitrosyl iron complexes with thiol-containing ligands and S-nitrosothiols
    • Lobysheva, I. I., Stupakova, M. V., Mikoyan, V. D., Vasilieva, S. V., and Vanin, A. F. (1999) Induction of the SOS DNA repair response in Escherichia coli by nitric oxide donating agents. Dinitrosyl iron complexes with thiol-containing ligands and S-nitrosothiols. FEBS Lett. 454, 177-180
    • (1999) FEBS Lett. , vol.454 , pp. 177-180
    • Lobysheva, I.I.1    Stupakova, M.V.2    Mikoyan, V.D.3    Vasilieva, S.V.4    Vanin, A.F.5
  • 58
    • 64149092801 scopus 로고    scopus 로고
    • Redox control of the DNA damageinducible protein DinG helicase activity via its iron-sulfur cluster
    • Ren, B., Duan, X., and Ding, H. (2009) Redox control of the DNA damageinducible protein DinG helicase activity via its iron-sulfur cluster. J. Biol. Chem. 284, 4829-4835
    • (2009) J. Biol. Chem. , vol.284 , pp. 4829-4835
    • Ren, B.1    Duan, X.2    Ding, H.3
  • 59
    • 0035176067 scopus 로고    scopus 로고
    • The xeroderma pigmentosum groupD(XPD) gene. One gene, two functions, three diseases
    • Lehmann, A. R. (2001) The Xeroderma pigmentosum groupD(XPD) gene. One gene, two functions, three diseases. Genes Dev. 15, 15-23
    • (2001) Genes Dev. , vol.15 , pp. 15-23
    • Lehmann, A.R.1
  • 61
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities. Insights into the cancer and aging phenotypes from XPD mutations
    • Fan, L., Fuss, J. O., Cheng, Q. J., Arvai, A. S., Hammel, M., Roberts, V. A., Cooper, P. K., and Tainer, J. A. (2008) XPD helicase structures and activities. Insights into the cancer and aging phenotypes from XPD mutations. Cell 133, 789-800
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5    Roberts, V.A.6    Cooper, P.K.7    Tainer, J.A.8
  • 62
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and Fanc J have essential iron-sulfur domains
    • Rudolf, J., Makrantoni, V., Ingledew, W. J., Stark, M. J., and White, M. F. (2006) The DNA repair helicases XPD and Fanc J have essential iron-sulfur domains. Mol. Cell 23, 801-808
    • (2006) Mol. Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.4    White, M.F.5
  • 63
    • 0030474953 scopus 로고    scopus 로고
    • Mutagenesis associated with nitric oxide production intransgenic SJL mice
    • Gal, A., and Wogan, G. N. (1996) Mutagenesis associated with nitric oxide production intransgenic SJL mice. Proc. Natl. Acad. Sci. U.S.A. 93, 15102-15107
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 15102-15107
    • Gal, A.1    Wogan, G.N.2
  • 64
    • 0036679174 scopus 로고    scopus 로고
    • Nitric oxide-induced genotoxicity, mitochondrial damage, and apoptosis in human lymphoblastoid cells expressing wild-type and mutant p53
    • Li, C. Q., Trudel, L. J., and Wogan, G. N. (2002) Nitric oxide-induced genotoxicity, mitochondrial damage, and apoptosis in human lymphoblastoid cells expressing wild-type and mutant p53. Proc. Natl. Acad. Sci. U.S.A. 99, 10364-10369
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10364-10369
    • Li, C.Q.1    Trudel, L.J.2    Wogan, G.N.3


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