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Artigo de periodico
The bicarbonate/carbon dioxide pair increases hydrogen peroxide−mediated hyperoxidation of human peroxiredoxin 1 (2019)
Truzzi, Daniela Ramos ; Coelho, Fernando Rodrigues; Paviani, Veronica; Alves, Simone Vidigal; Netto, Luis Eduardo Soares ; Augusto, Ohara
Source: Journal of Biological Chemistry. Unidades: IQ, IB
Subjects: DIÓXIDO DE CARBONO, PEROXIDASE
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ABNT
TRUZZI, Daniela Ramos et al. The bicarbonate/carbon dioxide pair increases hydrogen peroxide−mediated hyperoxidation of human peroxiredoxin 1. Journal of Biological Chemistry, v. 294, n. 38, p. 14055-14067 :+Supplementary materials (S1-19), 2019Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA119.008825. Acesso em: 27 nov. 2025.
APA
Truzzi, D. R., Coelho, F. R., Paviani, V., Alves, S. V., Netto, L. E. S., & Augusto, O. (2019). The bicarbonate/carbon dioxide pair increases hydrogen peroxide−mediated hyperoxidation of human peroxiredoxin 1. Journal of Biological Chemistry, 294( 38), 14055-14067 :+Supplementary materials (S1-19). doi:10.1074/jbc.RA119.008825
NLM
Truzzi DR, Coelho FR, Paviani V, Alves SV, Netto LES, Augusto O. The bicarbonate/carbon dioxide pair increases hydrogen peroxide−mediated hyperoxidation of human peroxiredoxin 1 [Internet]. Journal of Biological Chemistry. 2019 ; 294( 38): 14055-14067 :+Supplementary materials (S1-19).[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.RA119.008825
Vancouver
Truzzi DR, Coelho FR, Paviani V, Alves SV, Netto LES, Augusto O. The bicarbonate/carbon dioxide pair increases hydrogen peroxide−mediated hyperoxidation of human peroxiredoxin 1 [Internet]. Journal of Biological Chemistry. 2019 ; 294( 38): 14055-14067 :+Supplementary materials (S1-19).[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.RA119.008825
Artigo de periodico
Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments (2017)
Gomes, Fernando ; Palma, Flávio Romero; Barros, Mário Henrique de ; Tsuchida, Eduardo T; Turano, Helena G; Alegria, Thiago G. P; Demasi, Marilene; Netto, Luis Eduardo Soares
Source: Journal of Biological Chemistry. Unidades: ICB, IB
Subjects: BIOLOGIA MOLECULAR, BIOQUÍMICA, LEVEDURAS, SACCHAROMYCES, PROTEÍNAS
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ABNT
GOMES, Fernando et al. Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments. Journal of Biological Chemistry, v. 292, n. 41, p. 17011-17024, 2017Tradução . . Disponível em: https://doi.org/10.1074/jbc.M117.788588. Acesso em: 27 nov. 2025.
APA
Gomes, F., Palma, F. R., Barros, M. H. de, Tsuchida, E. T., Turano, H. G., Alegria, T. G. P., et al. (2017). Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments. Journal of Biological Chemistry, 292( 41), 17011-17024. doi:10.1074/jbc.M117.788588
NLM
Gomes F, Palma FR, Barros MH de, Tsuchida ET, Turano HG, Alegria TGP, Demasi M, Netto LES. Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments [Internet]. Journal of Biological Chemistry. 2017 ; 292( 41): 17011-17024.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M117.788588
Vancouver
Gomes F, Palma FR, Barros MH de, Tsuchida ET, Turano HG, Alegria TGP, Demasi M, Netto LES. Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments [Internet]. Journal of Biological Chemistry. 2017 ; 292( 41): 17011-17024.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M117.788588
Artigo de periodico
Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites (2017)
Morais, Mariana A. B ; Giuseppe, Priscila O ; Souza, Tatiana A. C. B; Castro, Helena ; Honorato, Rodrigo V; Oliveira, Paulo S. L; Netto, Luis Eduardo Soares ; Tomas, Ana M ; Murakami, Mário T
Source: Journal of Biological Chemistry. Unidade: IB
Subjects: BIOLOGIA MOLECULAR, PARASITOLOGIA, PEROXIDASE, BIOQUÍMICA, LEISHMANIA, ENZIMAS OXIRREDUTORAS
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MORAIS, Mariana A. B et al. Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites. Journal of Biological Chemistry, v. 292, n. 17, p. 7023-7039, 2017Tradução . . Disponível em: https://doi.org/10.1074/jbc.M116.762039. Acesso em: 27 nov. 2025.
APA
Morais, M. A. B., Giuseppe, P. O., Souza, T. A. C. B., Castro, H., Honorato, R. V., Oliveira, P. S. L., et al. (2017). Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites. Journal of Biological Chemistry, 292( 17), 7023-7039. doi:10.1074/jbc.M116.762039
NLM
Morais MAB, Giuseppe PO, Souza TACB, Castro H, Honorato RV, Oliveira PSL, Netto LES, Tomas AM, Murakami MT. Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites [Internet]. Journal of Biological Chemistry. 2017 ; 292( 17): 7023-7039.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M116.762039
Vancouver
Morais MAB, Giuseppe PO, Souza TACB, Castro H, Honorato RV, Oliveira PSL, Netto LES, Tomas AM, Murakami MT. Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites [Internet]. Journal of Biological Chemistry. 2017 ; 292( 17): 7023-7039.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M116.762039
Artigo de periodico
Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2 (2017)
Carvalho, Larissa Anastácio da Costa; Truzzi, Daniela Ramos ; Fallani, Thamiris S; Alves, Simone Vidigal; Toledo Junior, José Carlos; Augusto, Ohara ; Netto, Luis Eduardo Soares ; Meotti, Flavia Carla
Source: Journal of Biological Chemistry. Unidades: IB, FFCLRP, IQ
Subjects: PERÓXIDO DE HIDROGÊNIO, INFLAMAÇÃO, ÁCIDO ÚRICO, OXIDAÇÃO
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CARVALHO, Larissa Anastácio da Costa et al. Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2. Journal of Biological Chemistry, v. 292, n. 21, p. 8705-8715, 2017Tradução . . Disponível em: https://doi.org/10.1074/jbc.M116.767657. Acesso em: 27 nov. 2025.
APA
Carvalho, L. A. da C., Truzzi, D. R., Fallani, T. S., Alves, S. V., Toledo Junior, J. C., Augusto, O., et al. (2017). Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2. Journal of Biological Chemistry, 292( 21), 8705-8715. doi:10.1074/jbc.M116.767657
NLM
Carvalho LA da C, Truzzi DR, Fallani TS, Alves SV, Toledo Junior JC, Augusto O, Netto LES, Meotti FC. Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2 [Internet]. Journal of Biological Chemistry. 2017 ; 292( 21): 8705-8715.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M116.767657
Vancouver
Carvalho LA da C, Truzzi DR, Fallani TS, Alves SV, Toledo Junior JC, Augusto O, Netto LES, Meotti FC. Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2 [Internet]. Journal of Biological Chemistry. 2017 ; 292( 21): 8705-8715.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M116.767657
Artigo de periodico
How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily (2015)
Morais, Mariana A. B; Giuseppe, Priscila O; Souza, Tatiana Arruda Campos Brasil; Alegria, Thiago Gerônimo Pires; Oliveira, Marcos A; Netto, Luis Eduardo Soares ; Murakami, Mário Tyago
Source: Journal of Biological Chemistry. Unidade: IB
Subjects: PEROXIDASE, ESTRESSE OXIDATIVO, LEISHMANIA, BIOQUÍMICA CELULAR, PROTEÍNAS, CRISTALOGRAFIA, BIOLOGIA MOLECULAR
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ABNT
MORAIS, Mariana A. B et al. How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily. Journal of Biological Chemistry, v. 290, p. 8582-859, 2015Tradução . . Disponível em: https://doi.org/10.1074/jbc.M114.619205. Acesso em: 27 nov. 2025.
APA
Morais, M. A. B., Giuseppe, P. O., Souza, T. A. C. B., Alegria, T. G. P., Oliveira, M. A., Netto, L. E. S., & Murakami, M. T. (2015). How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily. Journal of Biological Chemistry, 290, 8582-859. doi:10.1074/jbc.M114.619205
NLM
Morais MAB, Giuseppe PO, Souza TACB, Alegria TGP, Oliveira MA, Netto LES, Murakami MT. How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily [Internet]. Journal of Biological Chemistry. 2015 ; 290 8582-859.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M114.619205
Vancouver
Morais MAB, Giuseppe PO, Souza TACB, Alegria TGP, Oliveira MA, Netto LES, Murakami MT. How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily [Internet]. Journal of Biological Chemistry. 2015 ; 290 8582-859.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M114.619205
Artigo de periodico
Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase (2010)
Cussiol, José Renato Rosa; Alegria, Thiago Gerônimo Pires; Szweda, Luke I; Netto, Luis Eduardo Soares
Source: Journal of Biological Chemistry. Unidade: IB
Subjects: PROTEÍNAS, ENZIMAS OXIRREDUTORAS
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ABNT
CUSSIOL, José Renato Rosa et al. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. Journal of Biological Chemistry, v. 285, n. 29, p. 21943-21950, 2010Tradução . . Disponível em: https://doi.org/10.1074/jbc.M110.117283. Acesso em: 27 nov. 2025.
APA
Cussiol, J. R. R., Alegria, T. G. P., Szweda, L. I., & Netto, L. E. S. (2010). Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. Journal of Biological Chemistry, 285( 29), 21943-21950. doi:10.1074/jbc.M110.117283
NLM
Cussiol JRR, Alegria TGP, Szweda LI, Netto LES. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase [Internet]. Journal of Biological Chemistry. 2010 ; 285( 29): 21943-21950.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M110.117283
Vancouver
Cussiol JRR, Alegria TGP, Szweda LI, Netto LES. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase [Internet]. Journal of Biological Chemistry. 2010 ; 285( 29): 21943-21950.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M110.117283
Artigo de periodico
Structural and biochemical characterization of peroxiredoxin Qβ from Xylella fastidiosa: catalytic mechanism and high reactivity (2010)
Horta, Bruno Brasil; Oliveira, Marcos Antônio de; Discola, Karen Fulan; Cussiol, José Renato Rosa; Netto, Luis Eduardo Soares
Source: Journal of Biological Chemistry. Unidade: IB
Subjects: PEROXIDASE, BACTÉRIAS FITOPATOGÊNICAS
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ABNT
HORTA, Bruno Brasil et al. Structural and biochemical characterization of peroxiredoxin Qβ from Xylella fastidiosa: catalytic mechanism and high reactivity. Journal of Biological Chemistry, v. 285, n. 21, p. 16051-16065, 2010Tradução . . Disponível em: https://doi.org/10.1074/jbc.M109.094839. Acesso em: 27 nov. 2025.
APA
Horta, B. B., Oliveira, M. A. de, Discola, K. F., Cussiol, J. R. R., & Netto, L. E. S. (2010). Structural and biochemical characterization of peroxiredoxin Qβ from Xylella fastidiosa: catalytic mechanism and high reactivity. Journal of Biological Chemistry, 285( 21), 16051-16065. doi:10.1074/jbc.M109.094839
NLM
Horta BB, Oliveira MA de, Discola KF, Cussiol JRR, Netto LES. Structural and biochemical characterization of peroxiredoxin Qβ from Xylella fastidiosa: catalytic mechanism and high reactivity [Internet]. Journal of Biological Chemistry. 2010 ; 285( 21): 16051-16065.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M109.094839
Vancouver
Horta BB, Oliveira MA de, Discola KF, Cussiol JRR, Netto LES. Structural and biochemical characterization of peroxiredoxin Qβ from Xylella fastidiosa: catalytic mechanism and high reactivity [Internet]. Journal of Biological Chemistry. 2010 ; 285( 21): 16051-16065.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1074/jbc.M109.094839
Artigo de periodico
Superoxide dismutase 1-mediated production of ethanol- and DNA-derived radicals in yeasts challenged with hydrogen peroxide: molecular insights into genome instability of peroxiredoxin-null strains (2009)
Ogusucu, Renata; Rettori, Daniel; Netto, Luis Eduardo Soares ; Augusto, Ohara
Source: Journal of Biological Chemistry. Unidades: IB, IQ
Subjects: SUPERÓXIDO DISMUTASE, PEROXIDASE, RADICAIS LIVRES
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ABNT
OGUSUCU, Renata et al. Superoxide dismutase 1-mediated production of ethanol- and DNA-derived radicals in yeasts challenged with hydrogen peroxide: molecular insights into genome instability of peroxiredoxin-null strains. Journal of Biological Chemistry, v. 284, n. 9, p. 5546-5556, 2009Tradução . . Acesso em: 27 nov. 2025.
APA
Ogusucu, R., Rettori, D., Netto, L. E. S., & Augusto, O. (2009). Superoxide dismutase 1-mediated production of ethanol- and DNA-derived radicals in yeasts challenged with hydrogen peroxide: molecular insights into genome instability of peroxiredoxin-null strains. Journal of Biological Chemistry, 284( 9), 5546-5556.
NLM
Ogusucu R, Rettori D, Netto LES, Augusto O. Superoxide dismutase 1-mediated production of ethanol- and DNA-derived radicals in yeasts challenged with hydrogen peroxide: molecular insights into genome instability of peroxiredoxin-null strains. Journal of Biological Chemistry. 2009 ; 284( 9): 5546-5556.[citado 2025 nov. 27 ]
Vancouver
Ogusucu R, Rettori D, Netto LES, Augusto O. Superoxide dismutase 1-mediated production of ethanol- and DNA-derived radicals in yeasts challenged with hydrogen peroxide: molecular insights into genome instability of peroxiredoxin-null strains. Journal of Biological Chemistry. 2009 ; 284( 9): 5546-5556.[citado 2025 nov. 27 ]
Artigo de periodico
Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and perodiredoxins cooperate in the decomposition of 'H IND.2''O IND.2' by yeast (2004)
Munhoz, Daniela Cristina; Netto, Luis Eduardo Soares
Source: Journal of Biological Chemistry. Unidade: IB
Subjects: PEROXIDASE, ENZIMAS OXIRREDUTORAS, LEVEDURAS
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ABNT
MUNHOZ, Daniela Cristina e NETTO, Luis Eduardo Soares. Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and perodiredoxins cooperate in the decomposition of 'H IND.2''O IND.2' by yeast. Journal of Biological Chemistry, v. 279, n. 34, p. 35219-35227, 2004Tradução . . Acesso em: 27 nov. 2025.
APA
Munhoz, D. C., & Netto, L. E. S. (2004). Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and perodiredoxins cooperate in the decomposition of 'H IND.2''O IND.2' by yeast. Journal of Biological Chemistry, 279( 34), 35219-35227.
NLM
Munhoz DC, Netto LES. Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and perodiredoxins cooperate in the decomposition of 'H IND.2''O IND.2' by yeast. Journal of Biological Chemistry. 2004 ; 279( 34): 35219-35227.[citado 2025 nov. 27 ]
Vancouver
Munhoz DC, Netto LES. Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and perodiredoxins cooperate in the decomposition of 'H IND.2''O IND.2' by yeast. Journal of Biological Chemistry. 2004 ; 279( 34): 35219-35227.[citado 2025 nov. 27 ]
Artigo de periodico
Organic hydroperoxide resistance gene encodes a Thiol-dependent peroxidase (2003)
Cussiol, José Renato Rosa; Alves, Simone Vidigal; Oliveira, Marco Antônio de; Netto, Luis Eduardo Soares
Source: Journal of Biological Chemistry. Unidade: IB
Subjects: ENZIMAS, BACTÉRIAS
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ABNT
CUSSIOL, José Renato Rosa et al. Organic hydroperoxide resistance gene encodes a Thiol-dependent peroxidase. Journal of Biological Chemistry, v. 278, n. 13, p. 11570-11578, 2003Tradução . . Acesso em: 27 nov. 2025.
APA
Cussiol, J. R. R., Alves, S. V., Oliveira, M. A. de, & Netto, L. E. S. (2003). Organic hydroperoxide resistance gene encodes a Thiol-dependent peroxidase. Journal of Biological Chemistry, 278( 13), 11570-11578.
NLM
Cussiol JRR, Alves SV, Oliveira MA de, Netto LES. Organic hydroperoxide resistance gene encodes a Thiol-dependent peroxidase. Journal of Biological Chemistry. 2003 ; 278( 13): 11570-11578.[citado 2025 nov. 27 ]
Vancouver
Cussiol JRR, Alves SV, Oliveira MA de, Netto LES. Organic hydroperoxide resistance gene encodes a Thiol-dependent peroxidase. Journal of Biological Chemistry. 2003 ; 278( 13): 11570-11578.[citado 2025 nov. 27 ]
Artigo de periodico
20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-Glutathionylated (2003)
Demasi, Marilene; Silva, Gustavo Monteiro; Netto, Luis Eduardo Soares
Source: Journal of Biological Chemistry. Unidade: IB
Assunto: CÉLULAS EUCARIÓTICAS
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ABNT
DEMASI, Marilene e SILVA, Gustavo Monteiro e NETTO, Luis Eduardo Soares. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-Glutathionylated. Journal of Biological Chemistry, v. 278, n. 1, p. 679-685, 2003Tradução . . Acesso em: 27 nov. 2025.
APA
Demasi, M., Silva, G. M., & Netto, L. E. S. (2003). 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-Glutathionylated. Journal of Biological Chemistry, 278( 1), 679-685.
NLM
Demasi M, Silva GM, Netto LES. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-Glutathionylated. Journal of Biological Chemistry. 2003 ; 278( 1): 679-685.[citado 2025 nov. 27 ]
Vancouver
Demasi M, Silva GM, Netto LES. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-Glutathionylated. Journal of Biological Chemistry. 2003 ; 278( 1): 679-685.[citado 2025 nov. 27 ]
Artigo de periodico
The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition (1998)
Kowaltowski, Alicia Juliana ; Netto, Luis Eduardo Soares ; Vercesi, Anibal E
Source: Journal of Biological Chemistry. Unidade: IB
Assunto: BIOLOGIA
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ABNT
KOWALTOWSKI, Alicia Juliana e NETTO, Luis Eduardo Soares e VERCESI, Anibal E. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Journal of Biological Chemistry, v. 273, n. 21, p. 12766-12769, 1998Tradução . . Acesso em: 27 nov. 2025.
APA
Kowaltowski, A. J., Netto, L. E. S., & Vercesi, A. E. (1998). The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Journal of Biological Chemistry, 273( 21), 12766-12769.
NLM
Kowaltowski AJ, Netto LES, Vercesi AE. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Journal of Biological Chemistry. 1998 ; 273( 21): 12766-12769.[citado 2025 nov. 27 ]
Vancouver
Kowaltowski AJ, Netto LES, Vercesi AE. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Journal of Biological Chemistry. 1998 ; 273( 21): 12766-12769.[citado 2025 nov. 27 ]
Artigo de periodico
Identification of c (b)-methylquanine in the hydrolysates of dna from rats administered 1,2-dimethylhydrazine. Evidence for in vivo dna alkylation by methyl radicals (1992)
Netto, Luis Eduardo Soares ; Ramakrishna, N V S; Kolar, C; Cavalieri, E L; Rogan, E G; Lawson, T A; Augusto, Ohara
Source: Journal of Biological Chemistry. Unidade: IQ
Assunto: BIOLOGIA MOLECULAR
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ABNT
NETTO, Luis Eduardo Soares et al. Identification of c (b)-methylquanine in the hydrolysates of dna from rats administered 1,2-dimethylhydrazine. Evidence for in vivo dna alkylation by methyl radicals. Journal of Biological Chemistry, v. 267, n. 30, p. 21524-7, 1992Tradução . . Acesso em: 27 nov. 2025.
APA
Netto, L. E. S., Ramakrishna, N. V. S., Kolar, C., Cavalieri, E. L., Rogan, E. G., Lawson, T. A., & Augusto, O. (1992). Identification of c (b)-methylquanine in the hydrolysates of dna from rats administered 1,2-dimethylhydrazine. Evidence for in vivo dna alkylation by methyl radicals. Journal of Biological Chemistry, 267( 30), 21524-7.
NLM
Netto LES, Ramakrishna NVS, Kolar C, Cavalieri EL, Rogan EG, Lawson TA, Augusto O. Identification of c (b)-methylquanine in the hydrolysates of dna from rats administered 1,2-dimethylhydrazine. Evidence for in vivo dna alkylation by methyl radicals. Journal of Biological Chemistry. 1992 ;267( 30): 21524-7.[citado 2025 nov. 27 ]
Vancouver
Netto LES, Ramakrishna NVS, Kolar C, Cavalieri EL, Rogan EG, Lawson TA, Augusto O. Identification of c (b)-methylquanine in the hydrolysates of dna from rats administered 1,2-dimethylhydrazine. Evidence for in vivo dna alkylation by methyl radicals. Journal of Biological Chemistry. 1992 ;267( 30): 21524-7.[citado 2025 nov. 27 ]

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