ReP USP - Resultado da busca

Trabalho de evento-resumo periodico
Michael addition of peroxynitrite to acrolein generating formaldehyde and glyoxal from a Russell reaction (2019)
Bechara, Etelvino José Henriques ; Gonçalves, Letícia Christina Pires; Tavares, Marina Franco Maggi ; Augusto, Ohara ; Linares, Edlaine ; Licciardi, Saymon Alex Silva; Massari Filho, Júlio
Source: Free Radical Biology & Medicine. Conference titles: Annual Meeting of the Society for Redox Biology and Medicine/SFRBM. Unidade: IQ
Subjects: BIOQUÍMICA, PEROXIDASE
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ABNT
BECHARA, Etelvino José Henriques et al. Michael addition of peroxynitrite to acrolein generating formaldehyde and glyoxal from a Russell reaction. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2019.10.044. Acesso em: 16 nov. 2024. , 2019
APA
Bechara, E. J. H., Gonçalves, L. C. P., Tavares, M. F. M., Augusto, O., Linares, E., Licciardi, S. A. S., & Massari Filho, J. (2019). Michael addition of peroxynitrite to acrolein generating formaldehyde and glyoxal from a Russell reaction. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2019.10.044
NLM
Bechara EJH, Gonçalves LCP, Tavares MFM, Augusto O, Linares E, Licciardi SAS, Massari Filho J. Michael addition of peroxynitrite to acrolein generating formaldehyde and glyoxal from a Russell reaction [Internet]. Free Radical Biology & Medicine. 2019 ; 145 S18-S19 res. 06.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2019.10.044
Vancouver
Bechara EJH, Gonçalves LCP, Tavares MFM, Augusto O, Linares E, Licciardi SAS, Massari Filho J. Michael addition of peroxynitrite to acrolein generating formaldehyde and glyoxal from a Russell reaction [Internet]. Free Radical Biology & Medicine. 2019 ; 145 S18-S19 res. 06.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2019.10.044
Trabalho de evento-resumo periodico
Bicarbonate increases peroxiredoxin 1 susceptibility to hyperoxidation (2018)
Truzzi, Daniela Ramos ; Coelho, Fernando Rodrigues; Paviani, Veronica; Alves, Simone V; Netto, Luis Eduardo Soares ; Augusto, Ohara
Source: Free Radical Biology and Medicine. Conference titles: Biennial Meeting of the Society for Free Radical Research International/SFRRI. Unidades: IQ, IB
Subjects: PEROXIDASE, ANTIOXIDANTES, BIOQUÍMICA, RADICAIS LIVRES
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ABNT
TRUZZI, Daniela Ramos et al. Bicarbonate increases peroxiredoxin 1 susceptibility to hyperoxidation. Free Radical Biology and Medicine. New York: Instituto de Química, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2018.04.125. Acesso em: 16 nov. 2024. , 2018
APA
Truzzi, D. R., Coelho, F. R., Paviani, V., Alves, S. V., Netto, L. E. S., & Augusto, O. (2018). Bicarbonate increases peroxiredoxin 1 susceptibility to hyperoxidation. Free Radical Biology and Medicine. New York: Instituto de Química, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2018.04.125
NLM
Truzzi DR, Coelho FR, Paviani V, Alves SV, Netto LES, Augusto O. Bicarbonate increases peroxiredoxin 1 susceptibility to hyperoxidation [Internet]. Free Radical Biology and Medicine. 2018 ; 120 S37.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2018.04.125
Vancouver
Truzzi DR, Coelho FR, Paviani V, Alves SV, Netto LES, Augusto O. Bicarbonate increases peroxiredoxin 1 susceptibility to hyperoxidation [Internet]. Free Radical Biology and Medicine. 2018 ; 120 S37.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2018.04.125
Texto na web
Radical View (2017)
Augusto, Ohara ; Forni, Maria Fernanda Pereira de Araújo Demonte
Source: DOT Newsletter from the Society for Redox Biology and Medicine (SFRBM). Unidade: IQ
Assunto: BIOQUÍMICA
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AUGUSTO, Ohara e FORNI, Maria Fernanda Pereira de Araújo Demonte. Radical View. DOT Newsletter from the Society for Redox Biology and Medicine (SFRBM). Indianapolis: Instituto de Química, Universidade de São Paulo. Disponível em: https://sfrbm.org/publications/dot-newsletter/june-2017/radical-view. Acesso em: 16 nov. 2024. , 2017
APA
Augusto, O., & Forni, M. F. P. de A. D. (2017). Radical View. DOT Newsletter from the Society for Redox Biology and Medicine (SFRBM). Indianapolis: Instituto de Química, Universidade de São Paulo. Recuperado de https://sfrbm.org/publications/dot-newsletter/june-2017/radical-view
NLM
Augusto O, Forni MFP de AD. Radical View [Internet]. DOT Newsletter from the Society for Redox Biology and Medicine (SFRBM). 2017 ;(ju 2017):[citado 2024 nov. 16 ] Available from: https://sfrbm.org/publications/dot-newsletter/june-2017/radical-view
Vancouver
Augusto O, Forni MFP de AD. Radical View [Internet]. DOT Newsletter from the Society for Redox Biology and Medicine (SFRBM). 2017 ;(ju 2017):[citado 2024 nov. 16 ] Available from: https://sfrbm.org/publications/dot-newsletter/june-2017/radical-view
Trabalho de evento-resumo
Oxidation of the protein disulfide isomerase by peroxynitrite: kinetics, products and biological implications (2017)
Peixoto, Álbert Souza; Geyer, Robert Ryan; Laurindo, Francisco Rafael Martins; Augusto, Ohara
Source: Abstracts. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology. Unidade: IQ
Subjects: PROTEÍNAS, BIOQUÍMICA
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ABNT
PEIXOTO, Álbert Souza et al. Oxidation of the protein disulfide isomerase by peroxynitrite: kinetics, products and biological implications. 2017, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq, 2017. . Acesso em: 16 nov. 2024.
APA
Peixoto, Á. S., Geyer, R. R., Laurindo, F. R. M., & Augusto, O. (2017). Oxidation of the protein disulfide isomerase by peroxynitrite: kinetics, products and biological implications. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq.
NLM
Peixoto ÁS, Geyer RR, Laurindo FRM, Augusto O. Oxidation of the protein disulfide isomerase by peroxynitrite: kinetics, products and biological implications. Abstracts. 2017 ;[citado 2024 nov. 16 ]
Vancouver
Peixoto ÁS, Geyer RR, Laurindo FRM, Augusto O. Oxidation of the protein disulfide isomerase by peroxynitrite: kinetics, products and biological implications. Abstracts. 2017 ;[citado 2024 nov. 16 ]
Artigo de periodico
Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins (2016)
Weller, Caroline E; Dhall, Abhinav; Ding, Feizhi; Linares, Edlaine ; Whedon, Samuel D; Senger, Nicholas A; Tyson, Elizabeth L; Bagert, John D; Li, Xiaosong; Augusto, Ohara ; Chatterjee, Champak
Source: Nature Communications. Unidade: IQ
Subjects: PROTEÍNAS, BIOQUÍMICA
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WELLER, Caroline E et al. Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins. Nature Communications, v. 7, p. 1-10 art. 12979, 2016Tradução . . Disponível em: https://doi.org/10.1038/ncomms12979. Acesso em: 16 nov. 2024.
APA
Weller, C. E., Dhall, A., Ding, F., Linares, E., Whedon, S. D., Senger, N. A., et al. (2016). Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins. Nature Communications, 7, 1-10 art. 12979. doi:10.1038/ncomms12979
NLM
Weller CE, Dhall A, Ding F, Linares E, Whedon SD, Senger NA, Tyson EL, Bagert JD, Li X, Augusto O, Chatterjee C. Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins [Internet]. Nature Communications. 2016 ; 7 1-10 art. 12979.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1038/ncomms12979
Vancouver
Weller CE, Dhall A, Ding F, Linares E, Whedon SD, Senger NA, Tyson EL, Bagert JD, Li X, Augusto O, Chatterjee C. Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins [Internet]. Nature Communications. 2016 ; 7 1-10 art. 12979.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1038/ncomms12979
Artigo de periodico
Catalytic Thr or ser residue modulates structural switches in 2-Cys peroxiredoxin by distinct mechanisms (2016)
Tairum, Carlos A; Santos, Melina Cardoso; Breyer, Carlos A; Geyer, R. Ryan; Nieves, Cecilia J; Portillo-Ledesma, Stephanie; Ferrer-Sueta, Gerardo; Toledo Junior, José Carlos; Toyama, Marcos H; Augusto, Ohara ; Netto, Luis Eduardo Soares ; Oliveira, Marcos A. de
Source: Scientific Reports. Unidades: FFCLRP, IQ, IB
Subjects: CATÁLISE, BIOQUÍMICA, FERMENTOS, LEVEDURAS
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ABNT
TAIRUM, Carlos A et al. Catalytic Thr or ser residue modulates structural switches in 2-Cys peroxiredoxin by distinct mechanisms. Scientific Reports, v. 6, p. 1-12 art. 33133, 2016Tradução . . Disponível em: https://doi.org/10.1038/srep33133. Acesso em: 16 nov. 2024.
APA
Tairum, C. A., Santos, M. C., Breyer, C. A., Geyer, R. R., Nieves, C. J., Portillo-Ledesma, S., et al. (2016). Catalytic Thr or ser residue modulates structural switches in 2-Cys peroxiredoxin by distinct mechanisms. Scientific Reports, 6, 1-12 art. 33133. doi:10.1038/srep33133
NLM
Tairum CA, Santos MC, Breyer CA, Geyer RR, Nieves CJ, Portillo-Ledesma S, Ferrer-Sueta G, Toledo Junior JC, Toyama MH, Augusto O, Netto LES, Oliveira MA de. Catalytic Thr or ser residue modulates structural switches in 2-Cys peroxiredoxin by distinct mechanisms [Internet]. Scientific Reports. 2016 ; 6 1-12 art. 33133.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1038/srep33133
Vancouver
Tairum CA, Santos MC, Breyer CA, Geyer RR, Nieves CJ, Portillo-Ledesma S, Ferrer-Sueta G, Toledo Junior JC, Toyama MH, Augusto O, Netto LES, Oliveira MA de. Catalytic Thr or ser residue modulates structural switches in 2-Cys peroxiredoxin by distinct mechanisms [Internet]. Scientific Reports. 2016 ; 6 1-12 art. 33133.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1038/srep33133
Trabalho de evento-resumo periodico
Peroxiredoxin 1 coordination to the dinitrosyl iron complex of glutathione (2016)
Truzzi, Daniela Ramos ; Alves, Simone S. V; Netto, Luis Eduardo Soares ; Augusto, Ohara
Source: Free Radical Biology & Medicine. Conference titles: Annual Meeting Society for Redox Biology and Medicine (SFRBM). Unidades: IB, IQ
Subjects: PEROXIDASE, BIOQUÍMICA
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ABNT
TRUZZI, Daniela Ramos et al. Peroxiredoxin 1 coordination to the dinitrosyl iron complex of glutathione. Free Radical Biology & Medicine. New York: Instituto de Biociências, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2016.10.291. Acesso em: 16 nov. 2024. , 2016
APA
Truzzi, D. R., Alves, S. S. V., Netto, L. E. S., & Augusto, O. (2016). Peroxiredoxin 1 coordination to the dinitrosyl iron complex of glutathione. Free Radical Biology & Medicine. New York: Instituto de Biociências, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2016.10.291
NLM
Truzzi DR, Alves SSV, Netto LES, Augusto O. Peroxiredoxin 1 coordination to the dinitrosyl iron complex of glutathione [Internet]. Free Radical Biology & Medicine. 2016 ; 100 S113 res. 250.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2016.10.291
Vancouver
Truzzi DR, Alves SSV, Netto LES, Augusto O. Peroxiredoxin 1 coordination to the dinitrosyl iron complex of glutathione [Internet]. Free Radical Biology & Medicine. 2016 ; 100 S113 res. 250.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2016.10.291
Trabalho de evento-resumo
Determination of yeast cytosolic peroxiredoxin reduction rates by thioredoxins and PRX overoxidation through fluorescence approaches (2015)
Zurlo, F. M; Tairum, C. A; Geyer, R. R; Augusto, Ohara ; Netto, Luis Eduardo Soares ; Oliveira, M. A
Source: Abstracts Book. Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - IUBMB. Unidades: IQ, IB
Subjects: PEROXIDASE, BIOQUÍMICA
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ABNT
ZURLO, F. M et al. Determination of yeast cytosolic peroxiredoxin reduction rates by thioredoxins and PRX overoxidation through fluorescence approaches. 2015, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2015. . Acesso em: 16 nov. 2024.
APA
Zurlo, F. M., Tairum, C. A., Geyer, R. R., Augusto, O., Netto, L. E. S., & Oliveira, M. A. (2015). Determination of yeast cytosolic peroxiredoxin reduction rates by thioredoxins and PRX overoxidation through fluorescence approaches. In Abstracts Book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq).
NLM
Zurlo FM, Tairum CA, Geyer RR, Augusto O, Netto LES, Oliveira MA. Determination of yeast cytosolic peroxiredoxin reduction rates by thioredoxins and PRX overoxidation through fluorescence approaches. Abstracts Book. 2015 ;[citado 2024 nov. 16 ]
Vancouver
Zurlo FM, Tairum CA, Geyer RR, Augusto O, Netto LES, Oliveira MA. Determination of yeast cytosolic peroxiredoxin reduction rates by thioredoxins and PRX overoxidation through fluorescence approaches. Abstracts Book. 2015 ;[citado 2024 nov. 16 ]
Trabalho de evento-resumo
Peroxiredoxin 1 coordination to dinitrosyl iron complex (2015)
Truzzi, Daniela Ramos ; Alves, S. V; Netto, Luis Eduardo Soares ; Augusto, Ohara
Source: Abstracts Book. Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - IUBMB. Unidades: IB, IQ
Subjects: PEROXIDASE, BIOQUÍMICA
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ABNT
TRUZZI, Daniela Ramos et al. Peroxiredoxin 1 coordination to dinitrosyl iron complex. 2015, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2015. . Acesso em: 16 nov. 2024.
APA
Truzzi, D. R., Alves, S. V., Netto, L. E. S., & Augusto, O. (2015). Peroxiredoxin 1 coordination to dinitrosyl iron complex. In Abstracts Book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq).
NLM
Truzzi DR, Alves SV, Netto LES, Augusto O. Peroxiredoxin 1 coordination to dinitrosyl iron complex. Abstracts Book. 2015 ;[citado 2024 nov. 16 ]
Vancouver
Truzzi DR, Alves SV, Netto LES, Augusto O. Peroxiredoxin 1 coordination to dinitrosyl iron complex. Abstracts Book. 2015 ;[citado 2024 nov. 16 ]
Trabalho de evento-resumo
Production of ditryptophan cross-links in beta crystallin submitted to carbonate radical or to UV light (2015)
Paviani, Veronica; Augusto, Ohara
Source: Abstracts Book. Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - IUBMB. Unidade: IQ
Subjects: BIOQUÍMICA, PEROXIDASE, LISOZIMAS
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ABNT
PAVIANI, Veronica e AUGUSTO, Ohara. Production of ditryptophan cross-links in beta crystallin submitted to carbonate radical or to UV light. 2015, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2015. . Acesso em: 16 nov. 2024.
APA
Paviani, V., & Augusto, O. (2015). Production of ditryptophan cross-links in beta crystallin submitted to carbonate radical or to UV light. In Abstracts Book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq).
NLM
Paviani V, Augusto O. Production of ditryptophan cross-links in beta crystallin submitted to carbonate radical or to UV light. Abstracts Book. 2015 ;[citado 2024 nov. 16 ]
Vancouver
Paviani V, Augusto O. Production of ditryptophan cross-links in beta crystallin submitted to carbonate radical or to UV light. Abstracts Book. 2015 ;[citado 2024 nov. 16 ]
Trabalho de evento-resumo periodico
Peroxiredoxin S-nitrosation and high molecular weight DNIC formation (2015)
Truzzi, Daniela Ramos ; Alves, Simone S. V; Netto, Luis Eduardo Soares ; Augusto, Ohara
Source: Free Radical Biology & Medicine. Conference titles: Annual Meeting of the Society for Free Radical Biology and Medicine (SFRBM). Unidades: IB, IQ
Subjects: PEROXIDASE, BIOQUÍMICA
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ABNT
TRUZZI, Daniela Ramos et al. Peroxiredoxin S-nitrosation and high molecular weight DNIC formation. Free Radical Biology & Medicine. New York: Instituto de Biociências, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2015.10.214. Acesso em: 16 nov. 2024. , 2015
APA
Truzzi, D. R., Alves, S. S. V., Netto, L. E. S., & Augusto, O. (2015). Peroxiredoxin S-nitrosation and high molecular weight DNIC formation. Free Radical Biology & Medicine. New York: Instituto de Biociências, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2015.10.214
NLM
Truzzi DR, Alves SSV, Netto LES, Augusto O. Peroxiredoxin S-nitrosation and high molecular weight DNIC formation [Internet]. Free Radical Biology & Medicine. 2015 ; 87 S81 res. 172.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2015.10.214
Vancouver
Truzzi DR, Alves SSV, Netto LES, Augusto O. Peroxiredoxin S-nitrosation and high molecular weight DNIC formation [Internet]. Free Radical Biology & Medicine. 2015 ; 87 S81 res. 172.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2015.10.214
Artigo de periodico
Oligomerization of Cu,Zn-superoxide dismutase (SOD1) by docosahexaenoic acid and its hydroperoxides in vitro: aggregation dependence on fatty acid unsaturation and thiols (2015)
Appolinário, Patricia Postilione; Medinas, Danilo Bilches ; Chaves-Filho, Adriano B.; Genaro-Mattos, Thiago C.; Cussiol, José Renato Rosa; Netto, Luis Eduardo Soares ; Augusto, Ohara ; Miyamoto, Sayuri
Source: PLOS ONE. Unidades: IB, IQ
Subjects: BIOLOGIA MOLECULAR, BIOQUÍMICA, ÁCIDOS GRAXOS, PEROXIDASE
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ABNT
APPOLINÁRIO, Patricia Postilione et al. Oligomerization of Cu,Zn-superoxide dismutase (SOD1) by docosahexaenoic acid and its hydroperoxides in vitro: aggregation dependence on fatty acid unsaturation and thiols. PLOS ONE, v. 10, n. 4, p. e0125146, 2015Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0125146. Acesso em: 16 nov. 2024.
APA
Appolinário, P. P., Medinas, D. B., Chaves-Filho, A. B., Genaro-Mattos, T. C., Cussiol, J. R. R., Netto, L. E. S., et al. (2015). Oligomerization of Cu,Zn-superoxide dismutase (SOD1) by docosahexaenoic acid and its hydroperoxides in vitro: aggregation dependence on fatty acid unsaturation and thiols. PLOS ONE, 10( 4), e0125146. doi:10.1371/journal.pone.0125146
NLM
Appolinário PP, Medinas DB, Chaves-Filho AB, Genaro-Mattos TC, Cussiol JRR, Netto LES, Augusto O, Miyamoto S. Oligomerization of Cu,Zn-superoxide dismutase (SOD1) by docosahexaenoic acid and its hydroperoxides in vitro: aggregation dependence on fatty acid unsaturation and thiols [Internet]. PLOS ONE. 2015 ; 10( 4): e0125146.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1371/journal.pone.0125146
Vancouver
Appolinário PP, Medinas DB, Chaves-Filho AB, Genaro-Mattos TC, Cussiol JRR, Netto LES, Augusto O, Miyamoto S. Oligomerization of Cu,Zn-superoxide dismutase (SOD1) by docosahexaenoic acid and its hydroperoxides in vitro: aggregation dependence on fatty acid unsaturation and thiols [Internet]. PLOS ONE. 2015 ; 10( 4): e0125146.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1371/journal.pone.0125146
Artigo de jornal-dep/entr
Os radicais livres na mira da ciência (2015)
Augusto, Ohara ; Laurindo, Francisco Rafael Martins; Netto, Luis Eduardo Soares ; Medeiros, Marisa Helena Gennari de ; Kowaltowski, Alicia Juliana ; Fernandez, Carmen
Source: Jornal da USP. Unidades: IQ, IB
Subjects: RADICAIS LIVRES, CIÊNCIA, BIOQUÍMICA
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ABNT
AUGUSTO, Ohara et al. Os radicais livres na mira da ciência. Jornal da USP. São Paulo: Instituto de Química, Universidade de São Paulo. Disponível em: http://espaber.uspnet.usp.br/jorusp/?p=39742. Acesso em: 16 nov. 2024. , 2015
APA
Augusto, O., Laurindo, F. R. M., Netto, L. E. S., Medeiros, M. H. G. de, Kowaltowski, A. J., & Fernandez, C. (2015). Os radicais livres na mira da ciência. Jornal da USP. São Paulo: Instituto de Química, Universidade de São Paulo. Recuperado de http://espaber.uspnet.usp.br/jorusp/?p=39742
NLM
Augusto O, Laurindo FRM, Netto LES, Medeiros MHG de, Kowaltowski AJ, Fernandez C. Os radicais livres na mira da ciência [Internet]. Jornal da USP. 2015 ;23 fe 2015 7.[citado 2024 nov. 16 ] Available from: http://espaber.uspnet.usp.br/jorusp/?p=39742
Vancouver
Augusto O, Laurindo FRM, Netto LES, Medeiros MHG de, Kowaltowski AJ, Fernandez C. Os radicais livres na mira da ciência [Internet]. Jornal da USP. 2015 ;23 fe 2015 7.[citado 2024 nov. 16 ] Available from: http://espaber.uspnet.usp.br/jorusp/?p=39742
Trabalho de evento-resumo periodico
Cholesterol secosterol aldehydes are increased in amyotrophic lateral sclerosis rat model and induce covalent modification and aggregation of Cu, Zn-superoxide dismutase (2015)
Dantas, Lucas Souza; Chaves Filho, Adriano de Britto; Mattos, Thiago Cardoso Genaro de; Porter, Ned A; Appolinário, Patricia Postilione; Coelho, Fernando Rodrigues; Augusto, Ohara ; Medeiros, Marisa Helena Gennari de ; Miyamoto, Sayuri
Source: Free Radical Biology & Medicine. Conference titles: Annual Meeting of the Society for Free Radical Biology and Medicine (SFRBM). Unidade: IQ
Subjects: ALDEÍDOS, BIOQUÍMICA
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ABNT
DANTAS, Lucas Souza et al. Cholesterol secosterol aldehydes are increased in amyotrophic lateral sclerosis rat model and induce covalent modification and aggregation of Cu, Zn-superoxide dismutase. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. . Acesso em: 16 nov. 2024. , 2015
APA
Dantas, L. S., Chaves Filho, A. de B., Mattos, T. C. G. de, Porter, N. A., Appolinário, P. P., Coelho, F. R., et al. (2015). Cholesterol secosterol aldehydes are increased in amyotrophic lateral sclerosis rat model and induce covalent modification and aggregation of Cu, Zn-superoxide dismutase. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo.
NLM
Dantas LS, Chaves Filho A de B, Mattos TCG de, Porter NA, Appolinário PP, Coelho FR, Augusto O, Medeiros MHG de, Miyamoto S. Cholesterol secosterol aldehydes are increased in amyotrophic lateral sclerosis rat model and induce covalent modification and aggregation of Cu, Zn-superoxide dismutase. Free Radical Biology & Medicine. 2015 ; 87 S144 res. 320.[citado 2024 nov. 16 ]
Vancouver
Dantas LS, Chaves Filho A de B, Mattos TCG de, Porter NA, Appolinário PP, Coelho FR, Augusto O, Medeiros MHG de, Miyamoto S. Cholesterol secosterol aldehydes are increased in amyotrophic lateral sclerosis rat model and induce covalent modification and aggregation of Cu, Zn-superoxide dismutase. Free Radical Biology & Medicine. 2015 ; 87 S144 res. 320.[citado 2024 nov. 16 ]
Trabalho de evento-resumo
Cytochrome c reacts with cholesterol hydroperoxides producing protein and lipid carbon-centered radicals (2013)
Genaro-Mattos, Thiago Cardoso; Queiroz, Raphael Ferreira; Appolinário, Patricia Postilione; Cunha, D; Porter, N. A; Augusto, Ohara ; Miyamoto, Sayuri
Source: Abstracts. Conference titles: International Congress Society for Free Radical Biology and Medicine (SFRBM). Unidade: IQ
Subjects: PEROXIDASE, BIOQUÍMICA
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ABNT
GENARO-MATTOS, Thiago Cardoso et al. Cytochrome c reacts with cholesterol hydroperoxides producing protein and lipid carbon-centered radicals. 2013, Anais.. Buenos Aires: Society for Free Radical Biology and Medicine, 2013. . Acesso em: 16 nov. 2024.
APA
Genaro-Mattos, T. C., Queiroz, R. F., Appolinário, P. P., Cunha, D., Porter, N. A., Augusto, O., & Miyamoto, S. (2013). Cytochrome c reacts with cholesterol hydroperoxides producing protein and lipid carbon-centered radicals. In Abstracts. Buenos Aires: Society for Free Radical Biology and Medicine.
NLM
Genaro-Mattos TC, Queiroz RF, Appolinário PP, Cunha D, Porter NA, Augusto O, Miyamoto S. Cytochrome c reacts with cholesterol hydroperoxides producing protein and lipid carbon-centered radicals. Abstracts. 2013 ;[citado 2024 nov. 16 ]
Vancouver
Genaro-Mattos TC, Queiroz RF, Appolinário PP, Cunha D, Porter NA, Augusto O, Miyamoto S. Cytochrome c reacts with cholesterol hydroperoxides producing protein and lipid carbon-centered radicals. Abstracts. 2013 ;[citado 2024 nov. 16 ]
Trabalho de evento-resumo
Oxidative mechanisms in protein aggregation (2013)
Augusto, Ohara
Source: Program and Abstracts. Conference titles: Antioxidants and Redox Process in Health Bilateral Meeting Brazil-Japan. Unidade: IQ
Subjects: OXIDAÇÃO, BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
AUGUSTO, Ohara. Oxidative mechanisms in protein aggregation. 2013, Anais.. São Paulo: SBBq, 2013. . Acesso em: 16 nov. 2024.
APA
Augusto, O. (2013). Oxidative mechanisms in protein aggregation. In Program and Abstracts. São Paulo: SBBq.
NLM
Augusto O. Oxidative mechanisms in protein aggregation. Program and Abstracts. 2013 ;[citado 2024 nov. 16 ]
Vancouver
Augusto O. Oxidative mechanisms in protein aggregation. Program and Abstracts. 2013 ;[citado 2024 nov. 16 ]
Trabalho de evento-resumo periodico
The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol (2013)
Queiroz, Raphael Ferreira; Paviani, Veronica; Coelho, Fernando Rodrigues; Marques, Emerson Finco ; Di Mascio, Paolo ; Augusto, Ohara
Source: Free Radical Biology & Medicine. Conference titles: Annual Meeting of the Society for Free Radical Biology and Medicine (SFRBM). Unidade: IQ
Subjects: PEROXIDASE, BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
QUEIROZ, Raphael Ferreira et al. The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. . Acesso em: 16 nov. 2024. , 2013
APA
Queiroz, R. F., Paviani, V., Coelho, F. R., Marques, E. F., Di Mascio, P., & Augusto, O. (2013). The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo.
NLM
Queiroz RF, Paviani V, Coelho FR, Marques EF, Di Mascio P, Augusto O. The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol. Free Radical Biology & Medicine. 2013 ; 65 S93 res. 201.[citado 2024 nov. 16 ]
Vancouver
Queiroz RF, Paviani V, Coelho FR, Marques EF, Di Mascio P, Augusto O. The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol. Free Radical Biology & Medicine. 2013 ; 65 S93 res. 201.[citado 2024 nov. 16 ]
Trabalho de evento-resumo
The role of cysteine residues on sod1 oligomerization induced by docosahexaenoic acid (2013)
Appolinário, Patricia Postilione; Medinas, Danilo Bilches ; Mattos, Thiago Cardoso Genaro de; Kazaoka, Rafaella Mieko Araújo; Cussiol, José Renato Rosa; Netto, Luis Eduardo Soares ; Augusto, Ohara ; Miyamoto, Sayuri
Source: Program and Abstracts. Conference titles: Antioxidants and Redox Process in Health Bilateral Meeting Brazil-Japan. Unidades: IB, IQ
Assunto: BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
APPOLINÁRIO, Patricia Postilione et al. The role of cysteine residues on sod1 oligomerization induced by docosahexaenoic acid. 2013, Anais.. São Paulo: SBBq, 2013. . Acesso em: 16 nov. 2024.
APA
Appolinário, P. P., Medinas, D. B., Mattos, T. C. G. de, Kazaoka, R. M. A., Cussiol, J. R. R., Netto, L. E. S., et al. (2013). The role of cysteine residues on sod1 oligomerization induced by docosahexaenoic acid. In Program and Abstracts. São Paulo: SBBq.
NLM
Appolinário PP, Medinas DB, Mattos TCG de, Kazaoka RMA, Cussiol JRR, Netto LES, Augusto O, Miyamoto S. The role of cysteine residues on sod1 oligomerization induced by docosahexaenoic acid. Program and Abstracts. 2013 ;[citado 2024 nov. 16 ]
Vancouver
Appolinário PP, Medinas DB, Mattos TCG de, Kazaoka RMA, Cussiol JRR, Netto LES, Augusto O, Miyamoto S. The role of cysteine residues on sod1 oligomerization induced by docosahexaenoic acid. Program and Abstracts. 2013 ;[citado 2024 nov. 16 ]
Trabalho de evento-resumo
Characterization of a ditryptophan cross-link in hen lysozyme oxidized by the carbonate radical (2013)
Paviani, Veronica; Queiroz, Raphael Ferreira; Marques, Emerson Finco ; Di Mascio, Paolo ; Augusto, Ohara
Source: Abstracts. Conference titles: International Congress Society for Free Radical Biology and Medicine (SFRBM). Unidade: IQ
Subjects: LISOZIMAS, BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
PAVIANI, Veronica et al. Characterization of a ditryptophan cross-link in hen lysozyme oxidized by the carbonate radical. 2013, Anais.. Buenos Aires: Society for Free Radical Biology and Medicine, 2013. . Acesso em: 16 nov. 2024.
APA
Paviani, V., Queiroz, R. F., Marques, E. F., Di Mascio, P., & Augusto, O. (2013). Characterization of a ditryptophan cross-link in hen lysozyme oxidized by the carbonate radical. In Abstracts. Buenos Aires: Society for Free Radical Biology and Medicine.
NLM
Paviani V, Queiroz RF, Marques EF, Di Mascio P, Augusto O. Characterization of a ditryptophan cross-link in hen lysozyme oxidized by the carbonate radical. Abstracts. 2013 ;[citado 2024 nov. 16 ]
Vancouver
Paviani V, Queiroz RF, Marques EF, Di Mascio P, Augusto O. Characterization of a ditryptophan cross-link in hen lysozyme oxidized by the carbonate radical. Abstracts. 2013 ;[citado 2024 nov. 16 ]
Trabalho de evento-resumo
Inactivation and aggregation of protein disulfide isomerase by enzymatically and photolytically generated carbonate radical (2013)
Iqbal, Asif; Paviani, Veronica; Moretti, Ana Iochabel Soares; Laurindo, Francisco Rafael Martins; Augusto, Ohara
Source: Abstracts. Conference titles: International Congress Society for Free Radical Biology and Medicine (SFRBM). Unidade: IQ
Subjects: DOENÇAS NEURODEGENERATIVAS, BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
IQBAL, Asif et al. Inactivation and aggregation of protein disulfide isomerase by enzymatically and photolytically generated carbonate radical. 2013, Anais.. Buenos Aires: Society for Free Radical Biology and Medicine, 2013. . Acesso em: 16 nov. 2024.
APA
Iqbal, A., Paviani, V., Moretti, A. I. S., Laurindo, F. R. M., & Augusto, O. (2013). Inactivation and aggregation of protein disulfide isomerase by enzymatically and photolytically generated carbonate radical. In Abstracts. Buenos Aires: Society for Free Radical Biology and Medicine.
NLM
Iqbal A, Paviani V, Moretti AIS, Laurindo FRM, Augusto O. Inactivation and aggregation of protein disulfide isomerase by enzymatically and photolytically generated carbonate radical. Abstracts. 2013 ;[citado 2024 nov. 16 ]
Vancouver
Iqbal A, Paviani V, Moretti AIS, Laurindo FRM, Augusto O. Inactivation and aggregation of protein disulfide isomerase by enzymatically and photolytically generated carbonate radical. Abstracts. 2013 ;[citado 2024 nov. 16 ]

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