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Artigo de periodico
Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation (2009)
Tahara, Erich Birelli; Navarete, Felipe Donizeti Teston; Kowaltowski, Alicia Juliana
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: RADICAIS LIVRES, ESTRESSE OXIDATIVO, MITOCÔNDRIAS
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ABNT
TAHARA, Erich Birelli e NAVARETE, Felipe Donizeti Teston e KOWALTOWSKI, Alicia Juliana. Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation. Free Radical Biology and Medicine, v. 46, n. 9, p. 1283-1297, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.02.008. Acesso em: 01 ago. 2024.
APA
Tahara, E. B., Navarete, F. D. T., & Kowaltowski, A. J. (2009). Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation. Free Radical Biology and Medicine, 46( 9), 1283-1297. doi:10.1016/j.freeradbiomed.2009.02.008
NLM
Tahara EB, Navarete FDT, Kowaltowski AJ. Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation [Internet]. Free Radical Biology and Medicine. 2009 ; 46( 9): 1283-1297.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.02.008
Vancouver
Tahara EB, Navarete FDT, Kowaltowski AJ. Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation [Internet]. Free Radical Biology and Medicine. 2009 ; 46( 9): 1283-1297.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.02.008
Artigo de periodico
Mitochondria and reactive oxygen species (2009)
Kowaltowski, Alicia Juliana ; Souza-Pinto, Nadja Cristhina de ; Castilho, Roger Frigério; Vercesi, Anibal Eugenio
Source: Free Radical Biology & Medicine. Unidade: IQ
Subjects: ESTRESSE OXIDATIVO, MITOCÔNDRIAS, RADICAIS LIVRES
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ABNT
KOWALTOWSKI, Alicia Juliana et al. Mitochondria and reactive oxygen species. Free Radical Biology & Medicine, v. 47, n. 4, p. 333-343, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.05.004. Acesso em: 01 ago. 2024.
APA
Kowaltowski, A. J., Souza-Pinto, N. C. de, Castilho, R. F., & Vercesi, A. E. (2009). Mitochondria and reactive oxygen species. Free Radical Biology & Medicine, 47( 4), 333-343. doi:10.1016/j.freeradbiomed.2009.05.004
NLM
Kowaltowski AJ, Souza-Pinto NC de, Castilho RF, Vercesi AE. Mitochondria and reactive oxygen species [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 4): 333-343.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.004
Vancouver
Kowaltowski AJ, Souza-Pinto NC de, Castilho RF, Vercesi AE. Mitochondria and reactive oxygen species [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 4): 333-343.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.004
Artigo de periodico
Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA (2009)
Prado, Fernanda Manso ; Oliveira, Mauricio César Bof de; Miyamoto, Sayuri ; Martinez, Glaucia Regina; Medeiros, Marisa Helena Gennari de ; Ronsein, Graziella Eliza ; Di Mascio, Paolo
Source: Free Radical Biology & Medicine. Unidade: IQ
Subjects: DANO AO DNA, RADICAIS LIVRES, CROMATOGRAFIA LÍQUIDA DE ALTA EFICIÊNCIA
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ABNT
PRADO, Fernanda Manso et al. Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA. Free Radical Biology & Medicine, v. 47, n. 4, p. 401-409, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.05.001. Acesso em: 01 ago. 2024.
APA
Prado, F. M., Oliveira, M. C. B. de, Miyamoto, S., Martinez, G. R., Medeiros, M. H. G. de, Ronsein, G. E., & Di Mascio, P. (2009). Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA. Free Radical Biology & Medicine, 47( 4), 401-409. doi:10.1016/j.freeradbiomed.2009.05.001
NLM
Prado FM, Oliveira MCB de, Miyamoto S, Martinez GR, Medeiros MHG de, Ronsein GE, Di Mascio P. Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 4): 401-409.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.001
Vancouver
Prado FM, Oliveira MCB de, Miyamoto S, Martinez GR, Medeiros MHG de, Ronsein GE, Di Mascio P. Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 4): 401-409.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.001
Artigo de periodico
A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif (2008)
Martins, Rafael Miyazawa; Amino, Rogerio; Daghastanli, Katia Regina Perez; Cuccovia, Iolanda Midea ; Juliano, Maria Aparecida; Schenkman, Sergio
Source: FEBS Journal. Unidade: IQ
Subjects: TRYPANOSOMA CRUZI, GLÂNDULAS SALIVARES, BIOQUÍMICA
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ABNT
MARTINS, Rafael Miyazawa et al. A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif. FEBS Journal, v. 275, n. 5, p. 994-1002, 2008Tradução . . Disponível em: https://doi.org/10.1111/j.1742-4658.2008.06260.x. Acesso em: 01 ago. 2024.
APA
Martins, R. M., Amino, R., Daghastanli, K. R. P., Cuccovia, I. M., Juliano, M. A., & Schenkman, S. (2008). A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif. FEBS Journal, 275( 5), 994-1002. doi:10.1111/j.1742-4658.2008.06260.x
NLM
Martins RM, Amino R, Daghastanli KRP, Cuccovia IM, Juliano MA, Schenkman S. A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif [Internet]. FEBS Journal. 2008 ;275( 5): 994-1002.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1742-4658.2008.06260.x
Vancouver
Martins RM, Amino R, Daghastanli KRP, Cuccovia IM, Juliano MA, Schenkman S. A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif [Internet]. FEBS Journal. 2008 ;275( 5): 994-1002.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1742-4658.2008.06260.x
Artigo de periodico
The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase (2008)
Mendonça, Lúcio Mário Ferreira de; Marana, Sandro Roberto
Source: FEBS Journal. Unidade: IQ
Subjects: CATÁLISE, ENZIMAS, BIOQUÍMICA
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ABNT
MENDONÇA, Lúcio Mário Ferreira de e MARANA, Sandro Roberto. The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase. FEBS Journal, v. 275, n. 10, p. 2536-2547, 2008Tradução . . Disponível em: https://doi.org/10.1111/j.1742-4658.2008.06402.x. Acesso em: 01 ago. 2024.
APA
Mendonça, L. M. F. de, & Marana, S. R. (2008). The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase. FEBS Journal, 275( 10), 2536-2547. doi:10.1111/j.1742-4658.2008.06402.x
NLM
Mendonça LMF de, Marana SR. The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase [Internet]. FEBS Journal. 2008 ;275( 10): 2536-2547.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1742-4658.2008.06402.x
Vancouver
Mendonça LMF de, Marana SR. The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase [Internet]. FEBS Journal. 2008 ;275( 10): 2536-2547.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1742-4658.2008.06402.x
Artigo de periodico
Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging (2008)
Linares, Edlaine ; Giorgio, Selma; Augusto, Ohara
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: ÓXIDO NÍTRICO, MACRÓFAGOS, RADICAIS LIVRES
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ABNT
LINARES, Edlaine e GIORGIO, Selma e AUGUSTO, Ohara. Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging. Free Radical Biology and Medicine, v. 44, n. 8, p. 1668-1676, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2008.01.027. Acesso em: 01 ago. 2024.
APA
Linares, E., Giorgio, S., & Augusto, O. (2008). Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging. Free Radical Biology and Medicine, 44( 8), 1668-1676. doi:10.1016/j.freeradbiomed.2008.01.027
NLM
Linares E, Giorgio S, Augusto O. Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging [Internet]. Free Radical Biology and Medicine. 2008 ;44( 8): 1668-1676.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2008.01.027
Vancouver
Linares E, Giorgio S, Augusto O. Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging [Internet]. Free Radical Biology and Medicine. 2008 ;44( 8): 1668-1676.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2008.01.027
Artigo de periodico
Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production (2007)
Facundo, Heberty Di Tarso Fernandes; Paula, Juliana Gabriela de; Kowaltowski, Alicia Juliana
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: MITOCÔNDRIAS, BIOQUÍMICA, PEROXIDASE
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ABNT
FACUNDO, Heberty Di Tarso Fernandes e PAULA, Juliana Gabriela de e KOWALTOWSKI, Alicia Juliana. Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production. Free Radical Biology and Medicine, v. 42, n. 7, p. 1039-1048, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2007.01.001. Acesso em: 01 ago. 2024.
APA
Facundo, H. D. T. F., Paula, J. G. de, & Kowaltowski, A. J. (2007). Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production. Free Radical Biology and Medicine, 42( 7), 1039-1048. doi:10.1016/j.freeradbiomed.2007.01.001
NLM
Facundo HDTF, Paula JG de, Kowaltowski AJ. Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production [Internet]. Free Radical Biology and Medicine. 2007 ; 42( 7): 1039-1048.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2007.01.001
Vancouver
Facundo HDTF, Paula JG de, Kowaltowski AJ. Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production [Internet]. Free Radical Biology and Medicine. 2007 ; 42( 7): 1039-1048.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2007.01.001
Artigo de periodico
Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity (2006)
Facundo, Heberty Di Tarso Fernandes; Carreira, Raquel S.; Paula, Juliana G. de; Santos, Célio Xavier da Costa dos; Ferranti, Renato; Laurindo, Francisco Rafael Martins; Kowaltowski, Alicia Juliana
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: RADICAIS LIVRES, BIOQUÍMICA
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ABNT
FACUNDO, Heberty Di Tarso Fernandes et al. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity. Free Radical Biology and Medicine, v. 40, n. 3, p. 469-479, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2005.08.041. Acesso em: 01 ago. 2024.
APA
Facundo, H. D. T. F., Carreira, R. S., Paula, J. G. de, Santos, C. X. da C. dos, Ferranti, R., Laurindo, F. R. M., & Kowaltowski, A. J. (2006). Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity. Free Radical Biology and Medicine, 40( 3), 469-479. doi:10.1016/j.freeradbiomed.2005.08.041
NLM
Facundo HDTF, Carreira RS, Paula JG de, Santos CX da C dos, Ferranti R, Laurindo FRM, Kowaltowski AJ. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity [Internet]. Free Radical Biology and Medicine. 2006 ; 40( 3): 469-479.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.08.041
Vancouver
Facundo HDTF, Carreira RS, Paula JG de, Santos CX da C dos, Ferranti R, Laurindo FRM, Kowaltowski AJ. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity [Internet]. Free Radical Biology and Medicine. 2006 ; 40( 3): 469-479.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.08.041
Artigo de periodico
Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells (2006)
Cristofoletti, Plinio Tadeu; Sousa, Flavia A. Mendonça de; Rahbé, Yvan; Terra, Walter Ribeiro
Source: FEBS Journal. Unidade: IQ
Subjects: BIOQUÍMICA, ENZIMAS
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ABNT
CRISTOFOLETTI, Plinio Tadeu et al. Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells. FEBS Journal, v. 273, n. 24, p. 5574-5588, 2006Tradução . . Disponível em: https://doi.org/10.1111/j.1742-4658.2006.05547.x. Acesso em: 01 ago. 2024.
APA
Cristofoletti, P. T., Sousa, F. A. M. de, Rahbé, Y., & Terra, W. R. (2006). Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells. FEBS Journal, 273( 24), 5574-5588. doi:10.1111/j.1742-4658.2006.05547.x
NLM
Cristofoletti PT, Sousa FAM de, Rahbé Y, Terra WR. Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells [Internet]. FEBS Journal. 2006 ; 273( 24): 5574-5588.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1742-4658.2006.05547.x
Vancouver
Cristofoletti PT, Sousa FAM de, Rahbé Y, Terra WR. Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells [Internet]. FEBS Journal. 2006 ; 273( 24): 5574-5588.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1742-4658.2006.05547.x
Artigo de periodico
Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen (2005)
Martinez, Glaucia Regina; Gasparutto, Didier; Ravanat, Jean-Luc; Cadet, Jean; Medeiros, Marisa Helena Gennari de ; Di Mascio, Paolo
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: DANO AO DNA, ESPECTROMETRIA DE MASSAS, RADICAIS LIVRES
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ABNT
MARTINEZ, Glaucia Regina et al. Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen. Free Radical Biology and Medicine, v. 38, n. 11, p. 1491-1500, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2005.02.008. Acesso em: 01 ago. 2024.
APA
Martinez, G. R., Gasparutto, D., Ravanat, J. -L., Cadet, J., Medeiros, M. H. G. de, & Di Mascio, P. (2005). Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen. Free Radical Biology and Medicine, 38( 11), 1491-1500. doi:10.1016/j.freeradbiomed.2005.02.008
NLM
Martinez GR, Gasparutto D, Ravanat J-L, Cadet J, Medeiros MHG de, Di Mascio P. Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen [Internet]. Free Radical Biology and Medicine. 2005 ; 38( 11): 1491-1500.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.02.008
Vancouver
Martinez GR, Gasparutto D, Ravanat J-L, Cadet J, Medeiros MHG de, Di Mascio P. Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen [Internet]. Free Radical Biology and Medicine. 2005 ; 38( 11): 1491-1500.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.02.008
Artigo de periodico
Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation (2005)
Lima, Emersom Silva; Bonini, Marcelo Gialluisi; Augusto, Ohara ; Barbeiro, Hermes Vieira; Souza, Heraldo Possolo de; Abdalla, Dulcinéia Saes Parra
Source: Free Radical Biology and Medicine. Unidades: IQ, FM, FCF
Subjects: ÓXIDO NÍTRICO, VASODILATAÇÃO, RESSONÂNCIA PARAMAGNÉTICA DE SPIN
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ABNT
LIMA, Emersom Silva et al. Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation. Free Radical Biology and Medicine, v. 39, n. 4, p. 532-539, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2005.04.005. Acesso em: 01 ago. 2024.
APA
Lima, E. S., Bonini, M. G., Augusto, O., Barbeiro, H. V., Souza, H. P. de, & Abdalla, D. S. P. (2005). Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation. Free Radical Biology and Medicine, 39( 4), 532-539. doi:10.1016/j.freeradbiomed.2005.04.005
NLM
Lima ES, Bonini MG, Augusto O, Barbeiro HV, Souza HP de, Abdalla DSP. Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation [Internet]. Free Radical Biology and Medicine. 2005 ; 39( 4): 532-539.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.04.005
Vancouver
Lima ES, Bonini MG, Augusto O, Barbeiro HV, Souza HP de, Abdalla DSP. Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation [Internet]. Free Radical Biology and Medicine. 2005 ; 39( 4): 532-539.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.04.005
Artigo de periodico
Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation (2005)
Fernandes, Denise C.; Medinas, Danilo Bilches ; Alves, Maria Júlia Manso ; Augusto, Ohara
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: ÓXIDO NÍTRICO, RADICAIS LIVRES
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ABNT
FERNANDES, Denise C. et al. Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation. Free Radical Biology and Medicine, v. 38, n. 2, p. 189-200, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2004.09.027. Acesso em: 01 ago. 2024.
APA
Fernandes, D. C., Medinas, D. B., Alves, M. J. M., & Augusto, O. (2005). Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation. Free Radical Biology and Medicine, 38( 2), 189-200. doi:10.1016/j.freeradbiomed.2004.09.027
NLM
Fernandes DC, Medinas DB, Alves MJM, Augusto O. Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation [Internet]. Free Radical Biology and Medicine. 2005 ; 38( 2): 189-200.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.027
Vancouver
Fernandes DC, Medinas DB, Alves MJM, Augusto O. Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation [Internet]. Free Radical Biology and Medicine. 2005 ; 38( 2): 189-200.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.027
Artigo de periodico
Identification of paramyosin T cell epitopes associated with human resistance to Schistosoma mansoni reinfection (2005)
Fonseca, Cristina Toscano; Cunha-Neto, Edécio; Goldberg, Anna Carla; Kalil Filho, Jorge Elias; Jesus, Amelia Maria Ribeiro de; Carvalho, Edgard M.; Corrêa-Oliveira, Rodrigo; Hammer, Jurgen; Sidney, John; Sette, Alessandro; Oliveira, Sérgio Costa
Source: Clinical and Experimental Immunology. Unidades: IQ, FM
Subjects: BIOQUÍMICA, IMUNOLOGIA, SCHISTOSOMA MANSONI
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ABNT
FONSECA, Cristina Toscano et al. Identification of paramyosin T cell epitopes associated with human resistance to Schistosoma mansoni reinfection. Clinical and Experimental Immunology, v. 142, n. 3, p. 539-547, 2005Tradução . . Disponível em: https://doi.org/10.1111/j.1365-2249.2005.02941.x. Acesso em: 01 ago. 2024.
APA
Fonseca, C. T., Cunha-Neto, E., Goldberg, A. C., Kalil Filho, J. E., Jesus, A. M. R. de, Carvalho, E. M., et al. (2005). Identification of paramyosin T cell epitopes associated with human resistance to Schistosoma mansoni reinfection. Clinical and Experimental Immunology, 142( 3), 539-547. doi:10.1111/j.1365-2249.2005.02941.x
NLM
Fonseca CT, Cunha-Neto E, Goldberg AC, Kalil Filho JE, Jesus AMR de, Carvalho EM, Corrêa-Oliveira R, Hammer J, Sidney J, Sette A, Oliveira SC. Identification of paramyosin T cell epitopes associated with human resistance to Schistosoma mansoni reinfection [Internet]. Clinical and Experimental Immunology. 2005 ; 142( 3): 539-547.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1365-2249.2005.02941.x
Vancouver
Fonseca CT, Cunha-Neto E, Goldberg AC, Kalil Filho JE, Jesus AMR de, Carvalho EM, Corrêa-Oliveira R, Hammer J, Sidney J, Sette A, Oliveira SC. Identification of paramyosin T cell epitopes associated with human resistance to Schistosoma mansoni reinfection [Internet]. Clinical and Experimental Immunology. 2005 ; 142( 3): 539-547.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1365-2249.2005.02941.x
Artigo de periodico
Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress (2004)
Kowaltowski, Alicia Juliana ; Fenton, Robert G.; Fiskum, Gary
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: RADICAIS LIVRES, APOPTOSE, ANTIOXIDANTES, NECROSE, BIOQUÍMICA
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ABNT
KOWALTOWSKI, Alicia Juliana e FENTON, Robert G. e FISKUM, Gary. Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress. Free Radical Biology and Medicine, v. 37, n. 11, p. 1845-1853, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2004.09.005. Acesso em: 01 ago. 2024.
APA
Kowaltowski, A. J., Fenton, R. G., & Fiskum, G. (2004). Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress. Free Radical Biology and Medicine, 37( 11), 1845-1853. doi:10.1016/j.freeradbiomed.2004.09.005
NLM
Kowaltowski AJ, Fenton RG, Fiskum G. Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress [Internet]. Free Radical Biology and Medicine. 2004 ; 37( 11): 1845-1853.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.005
Vancouver
Kowaltowski AJ, Fenton RG, Fiskum G. Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress [Internet]. Free Radical Biology and Medicine. 2004 ; 37( 11): 1845-1853.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.005
Artigo de periodico
A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization (2004)
Paulucci, Adriana Aparecida; Katsuyama, Ângela M.; Sousa, Aurea Denise de; Farah, Chuck Shaker
Source: European Journal of Biochemistry. Unidade: IQ
Subjects: BIOQUÍMICA, POLIMERIZAÇÃO, PROTEÍNAS MUSCULARES
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
PAULUCCI, Adriana Aparecida et al. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization. European Journal of Biochemistry, v. 271, n. 3, p. 589-600, 2004Tradução . . Disponível em: https://doi.org/10.1111/j.1432-1033.2003.03961.x. Acesso em: 01 ago. 2024.
APA
Paulucci, A. A., Katsuyama, Â. M., Sousa, A. D. de, & Farah, C. S. (2004). A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization. European Journal of Biochemistry, 271( 3), 589-600. doi:10.1111/j.1432-1033.2003.03961.x
NLM
Paulucci AA, Katsuyama ÂM, Sousa AD de, Farah CS. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization [Internet]. European Journal of Biochemistry. 2004 ; 271( 3): 589-600.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2003.03961.x
Vancouver
Paulucci AA, Katsuyama ÂM, Sousa AD de, Farah CS. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization [Internet]. European Journal of Biochemistry. 2004 ; 271( 3): 589-600.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2003.03961.x
Artigo de periodico
Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants (2004)
Augusto, Ohara ; Bonini, Marcelo Gialluisi; Trindade, Daniel F.
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: BIOQUÍMICA, ÓXIDO NÍTRICO, RADICAIS LIVRES
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
AUGUSTO, Ohara e BONINI, Marcelo Gialluisi e TRINDADE, Daniel F. Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants. Free Radical Biology and Medicine, v. 36, n. 10, p. 1224-1232, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2004.02.076. Acesso em: 01 ago. 2024.
APA
Augusto, O., Bonini, M. G., & Trindade, D. F. (2004). Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants. Free Radical Biology and Medicine, 36( 10), 1224-1232. doi:10.1016/j.freeradbiomed.2004.02.076
NLM
Augusto O, Bonini MG, Trindade DF. Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants [Internet]. Free Radical Biology and Medicine. 2004 ; 36( 10): 1224-1232.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.02.076
Vancouver
Augusto O, Bonini MG, Trindade DF. Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants [Internet]. Free Radical Biology and Medicine. 2004 ; 36( 10): 1224-1232.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.02.076
Artigo de periodico
Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis (2004)
Marana, Sandro Roberto ; Andrade, Eduardo Henrique Pereira; Ferreira, Clélia ; Terra, Walter Ribeiro
Source: European Journal of Biochemistry. Unidade: IQ
Subjects: BIOQUÍMICA, ENZIMAS, BIOENERGÉTICA (ANÁLISE)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
MARANA, Sandro Roberto et al. Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis. European Journal of Biochemistry, v. 271, n. 21, p. 4169-4177, 2004Tradução . . Disponível em: https://doi.org/10.1111/j.1432-1033.2004.04354.x. Acesso em: 01 ago. 2024.
APA
Marana, S. R., Andrade, E. H. P., Ferreira, C., & Terra, W. R. (2004). Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis. European Journal of Biochemistry, 271( 21), 4169-4177. doi:10.1111/j.1432-1033.2004.04354.x
NLM
Marana SR, Andrade EHP, Ferreira C, Terra WR. Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis [Internet]. European Journal of Biochemistry. 2004 ; 271( 21): 4169-4177.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2004.04354.x
Vancouver
Marana SR, Andrade EHP, Ferreira C, Terra WR. Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis [Internet]. European Journal of Biochemistry. 2004 ; 271( 21): 4169-4177.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2004.04354.x
Artigo de periodico
Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron (2004)
Rinaldi, Tatiana Alvarez; Tersariol, Ivarne Luis dos Santos; Dyszy, Fabio Henrique; Prado, Fernanda Manso ; Nascimento, Otaciro Rangel; Di Mascio, Paolo ; Nantes, Iseli Lourenço
Source: Free Radical Biology and Medicine. Unidades: IQ, IFSC
Subjects: RADICAIS LIVRES, ESPECTROMETRIA DE MASSAS, RESSONÂNCIA PARAMAGNÉTICA DE SPIN, BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
RINALDI, Tatiana Alvarez et al. Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron. Free Radical Biology and Medicine, v. 36, n. 6, p. 802-810, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2003.12.002. Acesso em: 01 ago. 2024.
APA
Rinaldi, T. A., Tersariol, I. L. dos S., Dyszy, F. H., Prado, F. M., Nascimento, O. R., Di Mascio, P., & Nantes, I. L. (2004). Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron. Free Radical Biology and Medicine, 36( 6), 802-810. doi:10.1016/j.freeradbiomed.2003.12.002
NLM
Rinaldi TA, Tersariol IL dos S, Dyszy FH, Prado FM, Nascimento OR, Di Mascio P, Nantes IL. Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron [Internet]. Free Radical Biology and Medicine. 2004 ; 36( 6): 802-810.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2003.12.002
Vancouver
Rinaldi TA, Tersariol IL dos S, Dyszy FH, Prado FM, Nascimento OR, Di Mascio P, Nantes IL. Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron [Internet]. Free Radical Biology and Medicine. 2004 ; 36( 6): 802-810.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2003.12.002
Artigo de periodico
Analysis of major histocompatibility complex and CTLA-4 alleles in Brazilian patients with primary biliary cirrhosis (2003)
Bittencourt, Paulo Lisboa; Palácios, Selma Aliotti; Farias, Alberto Queiroz; Abrantes-Lemos, Clarice Pires; Cançado, Eduardo Luiz Rachid; Carrilho, Flair José; Laudanna, Antônio Atílio; Kalil Filho, Jorge Elias; Goldberg, Anna Carla
Source: Journal of Gastroenterology and Hepatology. Unidades: IQ, FM
Subjects: CIRROSE HEPÁTICA, IMUNOLOGIA, POLIMORFISMO
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
BITTENCOURT, Paulo Lisboa et al. Analysis of major histocompatibility complex and CTLA-4 alleles in Brazilian patients with primary biliary cirrhosis. Journal of Gastroenterology and Hepatology, v. 18, n. 9, p. 1061-1066, 2003Tradução . . Disponível em: https://doi.org/10.1046/j.1440-1746.2003.03091.x. Acesso em: 01 ago. 2024.
APA
Bittencourt, P. L., Palácios, S. A., Farias, A. Q., Abrantes-Lemos, C. P., Cançado, E. L. R., Carrilho, F. J., et al. (2003). Analysis of major histocompatibility complex and CTLA-4 alleles in Brazilian patients with primary biliary cirrhosis. Journal of Gastroenterology and Hepatology, 18( 9), 1061-1066. doi:10.1046/j.1440-1746.2003.03091.x
NLM
Bittencourt PL, Palácios SA, Farias AQ, Abrantes-Lemos CP, Cançado ELR, Carrilho FJ, Laudanna AA, Kalil Filho JE, Goldberg AC. Analysis of major histocompatibility complex and CTLA-4 alleles in Brazilian patients with primary biliary cirrhosis [Internet]. Journal of Gastroenterology and Hepatology. 2003 ; 18( 9): 1061-1066.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1046/j.1440-1746.2003.03091.x
Vancouver
Bittencourt PL, Palácios SA, Farias AQ, Abrantes-Lemos CP, Cançado ELR, Carrilho FJ, Laudanna AA, Kalil Filho JE, Goldberg AC. Analysis of major histocompatibility complex and CTLA-4 alleles in Brazilian patients with primary biliary cirrhosis [Internet]. Journal of Gastroenterology and Hepatology. 2003 ; 18( 9): 1061-1066.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1046/j.1440-1746.2003.03091.x
Artigo de periodico
EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes (2003)
Linares, Edlaine ; Nakao, Lia Sumie; Augusto, Ohara ; Kadiiska, Maria B.
Source: Free Radical Biology and Medicine. Unidade: IQ
Subjects: RADICAIS LIVRES, BIOQUÍMICA, RESSONÂNCIA PARAMAGNÉTICA DE SPIN
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
LINARES, Edlaine et al. EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes. Free Radical Biology and Medicine, v. 34, n. 6, p. 766-773, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(02)01424-7. Acesso em: 01 ago. 2024.
APA
Linares, E., Nakao, L. S., Augusto, O., & Kadiiska, M. B. (2003). EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes. Free Radical Biology and Medicine, 34( 6), 766-773. doi:10.1016/s0891-5849(02)01424-7
NLM
Linares E, Nakao LS, Augusto O, Kadiiska MB. EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes [Internet]. Free Radical Biology and Medicine. 2003 ; 34( 6): 766-773.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/s0891-5849(02)01424-7
Vancouver
Linares E, Nakao LS, Augusto O, Kadiiska MB. EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes [Internet]. Free Radical Biology and Medicine. 2003 ; 34( 6): 766-773.[citado 2024 ago. 01 ] Available from: https://doi.org/10.1016/s0891-5849(02)01424-7

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