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Artigo de periodico
Goldilocks calcium concentrations and the regulation of oxidative phosphorylation: too much, too little, or just right (2023)
Vilas-Boas, Eloisa Aparecida ; Costa, João Victor Cabral ; Ramos, Vitor de Miranda ; Silva, Camille Cristine Caldeira da ; Kowaltowski, Alicia Juliana
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: METABOLISMO, MITOCÔNDRIAS
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ABNT
VILAS-BOAS, Eloisa Aparecida et al. Goldilocks calcium concentrations and the regulation of oxidative phosphorylation: too much, too little, or just right. Journal of Biological Chemistry, v. 299, p. 1-17 art. 102904, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2023.102904. Acesso em: 02 nov. 2024.
APA
Vilas-Boas, E. A., Costa, J. V. C., Ramos, V. de M., Silva, C. C. C. da, & Kowaltowski, A. J. (2023). Goldilocks calcium concentrations and the regulation of oxidative phosphorylation: too much, too little, or just right. Journal of Biological Chemistry, 299, 1-17 art. 102904. doi:10.1016/j.jbc.2023.102904
NLM
Vilas-Boas EA, Costa JVC, Ramos V de M, Silva CCC da, Kowaltowski AJ. Goldilocks calcium concentrations and the regulation of oxidative phosphorylation: too much, too little, or just right [Internet]. Journal of Biological Chemistry. 2023 ; 299 1-17 art. 102904.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2023.102904
Vancouver
Vilas-Boas EA, Costa JVC, Ramos V de M, Silva CCC da, Kowaltowski AJ. Goldilocks calcium concentrations and the regulation of oxidative phosphorylation: too much, too little, or just right [Internet]. Journal of Biological Chemistry. 2023 ; 299 1-17 art. 102904.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2023.102904
Artigo de periodico
Macromolecular crowding amplifies allosteric regulation of T-cell protein tyrosine phosphatase (2022)
Tun, May Thwe; Yang, Shen; Forti, Fabio Luis ; Santelli, Eugenio ; Bottini, Nunzio
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: AUTOIMUNIDADE, NEOPLASIAS
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ABNT
TUN, May Thwe et al. Macromolecular crowding amplifies allosteric regulation of T-cell protein tyrosine phosphatase. Journal of Biological Chemistry, v. 298 , n. 12, p. 1-11, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2022.102655. Acesso em: 02 nov. 2024.
APA
Tun, M. T., Yang, S., Forti, F. L., Santelli, E., & Bottini, N. (2022). Macromolecular crowding amplifies allosteric regulation of T-cell protein tyrosine phosphatase. Journal of Biological Chemistry, 298 ( 12), 1-11. doi:10.1016/j.jbc.2022.102655
NLM
Tun MT, Yang S, Forti FL, Santelli E, Bottini N. Macromolecular crowding amplifies allosteric regulation of T-cell protein tyrosine phosphatase [Internet]. Journal of Biological Chemistry. 2022 ; 298 ( 12): 1-11.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2022.102655
Vancouver
Tun MT, Yang S, Forti FL, Santelli E, Bottini N. Macromolecular crowding amplifies allosteric regulation of T-cell protein tyrosine phosphatase [Internet]. Journal of Biological Chemistry. 2022 ; 298 ( 12): 1-11.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2022.102655
Artigo de periodico
The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signalling (2021)
Russo, Lilian Cristina ; Tomasin, Rebeka; Matos, Isaac de Araújo ; Manucci, Antonio Carlos; Sowa, Sven T; Dale, Katie; Caldecott, Keith W; Lehtiö, Lari ; Schechtman, Deborah ; Meotti, Flavia Carla ; Bruni-Cardoso, Alexandre ; Hoch, Nicolas Carlos
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: CORONAVIRUS, COVID-19, ANTIVIRAIS
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ABNT
RUSSO, Lilian Cristina et al. The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signalling. Journal of Biological Chemistry, v. 297, n. 3, p. 1-14 art. 101041, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2021.101041. Acesso em: 02 nov. 2024.
APA
Russo, L. C., Tomasin, R., Matos, I. de A., Manucci, A. C., Sowa, S. T., Dale, K., et al. (2021). The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signalling. Journal of Biological Chemistry, 297( 3), 1-14 art. 101041. doi:10.1016/j.jbc.2021.101041
NLM
Russo LC, Tomasin R, Matos I de A, Manucci AC, Sowa ST, Dale K, Caldecott KW, Lehtiö L, Schechtman D, Meotti FC, Bruni-Cardoso A, Hoch NC. The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signalling [Internet]. Journal of Biological Chemistry. 2021 ; 297( 3): 1-14 art. 101041.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2021.101041
Vancouver
Russo LC, Tomasin R, Matos I de A, Manucci AC, Sowa ST, Dale K, Caldecott KW, Lehtiö L, Schechtman D, Meotti FC, Bruni-Cardoso A, Hoch NC. The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent ADP-ribosylation induced by interferon signalling [Internet]. Journal of Biological Chemistry. 2021 ; 297( 3): 1-14 art. 101041.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2021.101041
Artigo de periodico
Dietary sodium restriction alters muscle lipidomics that relates to insulin resistance in mice (2021)
Pinto, Paula Ramos ; Yoshinaga, Marcos Yukio ; Bianco, Vanessa Del; Bochi, Ana Paula Garcia; Ferreira, Guilherme S; Pinto, Isabella Fernanda Dantas ; Rodrigues, Letícia Gomes ; Nakandakare, Edna Regina ; Okamoto, Maristela Mitiko ; Machado, Ubiratan Fabres ; Miyamoto, Sayuri ; Catanozi, Sergio ; Passarelli, Marisa
Source: Journal of Biological Chemistry. Unidades: FM, ICB, IQ
Subjects: MÚSCULO ESQUELÉTICO, SÓDIO, RESISTÊNCIA À INSULINA, LIPÍDEOS, CAMUNDONGOS, FISIOLOGIA
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PINTO, Paula Ramos et al. Dietary sodium restriction alters muscle lipidomics that relates to insulin resistance in mice. Journal of Biological Chemistry, v. 296, p. 1-12 art. 100344, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2021.100344. Acesso em: 02 nov. 2024.
APA
Pinto, P. R., Yoshinaga, M. Y., Bianco, V. D., Bochi, A. P. G., Ferreira, G. S., Pinto, I. F. D., et al. (2021). Dietary sodium restriction alters muscle lipidomics that relates to insulin resistance in mice. Journal of Biological Chemistry, 296, 1-12 art. 100344. doi:10.1016/j.jbc.2021.100344
NLM
Pinto PR, Yoshinaga MY, Bianco VD, Bochi APG, Ferreira GS, Pinto IFD, Rodrigues LG, Nakandakare ER, Okamoto MM, Machado UF, Miyamoto S, Catanozi S, Passarelli M. Dietary sodium restriction alters muscle lipidomics that relates to insulin resistance in mice [Internet]. Journal of Biological Chemistry. 2021 ; 296 1-12 art. 100344.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2021.100344
Vancouver
Pinto PR, Yoshinaga MY, Bianco VD, Bochi APG, Ferreira GS, Pinto IFD, Rodrigues LG, Nakandakare ER, Okamoto MM, Machado UF, Miyamoto S, Catanozi S, Passarelli M. Dietary sodium restriction alters muscle lipidomics that relates to insulin resistance in mice [Internet]. Journal of Biological Chemistry. 2021 ; 296 1-12 art. 100344.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2021.100344
Artigo de periodico
Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2 (2021)
Peskin, Alexander V; Meotti, Flavia Carla ; Kean, Kelsey M; Göbl, Christoph ; Peixoto, Albert Souza ; Pace, Paul E; Horne, Christopher R ; Heath, Sarah G; Crowther, Jennifer M ; Dobson, Renwick C. J; Karplus, P. Andrew; Winterbourn, Christine C
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: PERÓXIDO DE HIDROGÊNIO, CINÉTICA, PEROXIDASE
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ABNT
PESKIN, Alexander V et al. Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2. Journal of Biological Chemistry, v. 296, p. 1-15, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2021.100494. Acesso em: 02 nov. 2024.
APA
Peskin, A. V., Meotti, F. C., Kean, K. M., Göbl, C., Peixoto, A. S., Pace, P. E., et al. (2021). Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2. Journal of Biological Chemistry, 296, 1-15. doi:10.1016/j.jbc.2021.100494
NLM
Peskin AV, Meotti FC, Kean KM, Göbl C, Peixoto AS, Pace PE, Horne CR, Heath SG, Crowther JM, Dobson RCJ, Karplus PA, Winterbourn CC. Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2 [Internet]. Journal of Biological Chemistry. 2021 ; 296 1-15.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2021.100494
Vancouver
Peskin AV, Meotti FC, Kean KM, Göbl C, Peixoto AS, Pace PE, Horne CR, Heath SG, Crowther JM, Dobson RCJ, Karplus PA, Winterbourn CC. Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2 [Internet]. Journal of Biological Chemistry. 2021 ; 296 1-15.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.jbc.2021.100494
Artigo de periodico
The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis (2020)
Sastre, Diego Emiliano; Pulschen, Andre A; Basso, Luís Guilherme Mansor; Pariente, Jhonathan Stivins Benites; Marques Netto, Caterina Gruenwaldt Cunha; Machinandiarena, Federico; Albanesi, Daniela; Navarro, Marcos Vicente de Albuquerque Salles ; Mendoza, Diego de; Gueiros Filho, Frederico José
Source: Journal of Biological Chemistry. Unidades: IFSC, IQ, FFCLRP
Subjects: BACTÉRIAS GRAM-POSITIVAS, LIPÍDEOS
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ABNT
SASTRE, Diego Emiliano et al. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis. Journal of Biological Chemistry, v. 295, n. 7, p. 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2, 2020Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA119.011147. Acesso em: 02 nov. 2024.
APA
Sastre, D. E., Pulschen, A. A., Basso, L. G. M., Pariente, J. S. B., Marques Netto, C. G. C., Machinandiarena, F., et al. (2020). The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis. Journal of Biological Chemistry, 295( 7), 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2. doi:10.1074/jbc.RA119.011147
NLM
Sastre DE, Pulschen AA, Basso LGM, Pariente JSB, Marques Netto CGC, Machinandiarena F, Albanesi D, Navarro MV de AS, Mendoza D de, Gueiros Filho FJ. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA119.011147
Vancouver
Sastre DE, Pulschen AA, Basso LGM, Pariente JSB, Marques Netto CGC, Machinandiarena F, Albanesi D, Navarro MV de AS, Mendoza D de, Gueiros Filho FJ. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA119.011147
Artigo de periodico
Nucleolar localization of the yeast RNA exosome subunit Rrp44 hints at early pre-rRNA processing as its main function (2020)
Okuda, Ellen Kazumi; Zubiate, Fernando Alexis Gonzales; Gadal, Olivier; Oliveira, Carla Columbano de
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: RNA, PROTEÍNAS NUCLEARES
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ABNT
OKUDA, Ellen Kazumi et al. Nucleolar localization of the yeast RNA exosome subunit Rrp44 hints at early pre-rRNA processing as its main function. Journal of Biological Chemistry, v. 295, n. 32, p. 11195-11213, 2020Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA120.013589. Acesso em: 02 nov. 2024.
APA
Okuda, E. K., Zubiate, F. A. G., Gadal, O., & Oliveira, C. C. de. (2020). Nucleolar localization of the yeast RNA exosome subunit Rrp44 hints at early pre-rRNA processing as its main function. Journal of Biological Chemistry, 295( 32), 11195-11213. doi:10.1074/jbc.RA120.013589
NLM
Okuda EK, Zubiate FAG, Gadal O, Oliveira CC de. Nucleolar localization of the yeast RNA exosome subunit Rrp44 hints at early pre-rRNA processing as its main function [Internet]. Journal of Biological Chemistry. 2020 ; 295( 32): 11195-11213.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA120.013589
Vancouver
Okuda EK, Zubiate FAG, Gadal O, Oliveira CC de. Nucleolar localization of the yeast RNA exosome subunit Rrp44 hints at early pre-rRNA processing as its main function [Internet]. Journal of Biological Chemistry. 2020 ; 295( 32): 11195-11213.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA120.013589
Artigo de periodico
Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria (2020)
Sastre, Diego Emiliano; Basso, Luís Guilherme Mansor; Trastoy, Beatriz; Cifuente, Javier O.; Contreras, Xabier; Gueiros Filho, Frederico José ; Mendoza, Diego de; Navarro, Marcos Vicente de Albuquerque Salles ; Guerin, Marcelo E.
Source: Journal of Biological Chemistry. Unidades: IQ, IFSC, FFCLRP
Subjects: FOSFOLIPÍDEOS, LIPÍDEOS
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ABNT
SASTRE, Diego Emiliano et al. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry, v. 295, n. 7, p. 2136-2147 + Supplementary materials Figs. S1-S9, 2020Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA119.011122. Acesso em: 02 nov. 2024.
APA
Sastre, D. E., Basso, L. G. M., Trastoy, B., Cifuente, J. O., Contreras, X., Gueiros Filho, F. J., et al. (2020). Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry, 295( 7), 2136-2147 + Supplementary materials Figs. S1-S9. doi:10.1074/jbc.RA119.011122
NLM
Sastre DE, Basso LGM, Trastoy B, Cifuente JO, Contreras X, Gueiros Filho FJ, Mendoza D de, Navarro MV de AS, Guerin ME. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2136-2147 + Supplementary materials Figs. S1-S9.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA119.011122
Vancouver
Sastre DE, Basso LGM, Trastoy B, Cifuente JO, Contreras X, Gueiros Filho FJ, Mendoza D de, Navarro MV de AS, Guerin ME. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2136-2147 + Supplementary materials Figs. S1-S9.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA119.011122
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: 02 nov. 2024.
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 2024 nov. 02 ] 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 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA119.008825
Artigo de periodico
Epidermal growth factor (EGF) triggers nuclear calcium signaling through the intranuclear phospholipase C delta-4 (PLCδ4) (2019)
Miranda, Marcelo Coutinho; Rodrigues, Michele Angela; Campos, Ana Carolina de Angelis; Faria, Jerusa Araújo Quintão Arantes; Lima, Marianna Kunrath; Mignery, Gregory A; Schechtman, Deborah ; Goes, Alfredo Miranda; Nathanson, Michael H; Gomes, Dawidson A
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: CÁLCIO, PROTEINASES, PROLIFERAÇÃO CELULAR
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ABNT
MIRANDA, Marcelo Coutinho et al. Epidermal growth factor (EGF) triggers nuclear calcium signaling through the intranuclear phospholipase C delta-4 (PLCδ4). Journal of Biological Chemistry, v. 294, n. 45, p. 16650-16662, 2019Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA118.006961. Acesso em: 02 nov. 2024.
APA
Miranda, M. C., Rodrigues, M. A., Campos, A. C. de A., Faria, J. A. Q. A., Lima, M. K., Mignery, G. A., et al. (2019). Epidermal growth factor (EGF) triggers nuclear calcium signaling through the intranuclear phospholipase C delta-4 (PLCδ4). Journal of Biological Chemistry, 294( 45), 16650-16662. doi:10.1074/jbc.RA118.006961
NLM
Miranda MC, Rodrigues MA, Campos AC de A, Faria JAQA, Lima MK, Mignery GA, Schechtman D, Goes AM, Nathanson MH, Gomes DA. Epidermal growth factor (EGF) triggers nuclear calcium signaling through the intranuclear phospholipase C delta-4 (PLCδ4) [Internet]. Journal of Biological Chemistry. 2019 ; 294( 45): 16650-16662.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA118.006961
Vancouver
Miranda MC, Rodrigues MA, Campos AC de A, Faria JAQA, Lima MK, Mignery GA, Schechtman D, Goes AM, Nathanson MH, Gomes DA. Epidermal growth factor (EGF) triggers nuclear calcium signaling through the intranuclear phospholipase C delta-4 (PLCδ4) [Internet]. Journal of Biological Chemistry. 2019 ; 294( 45): 16650-16662.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA118.006961
Artigo de periodico
The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source (2018)
Damasceno, Fernando Cruvinel; Condeles, André Luís; Lopes, Angélica Kodama Bueno; Facci, Romulo Rodrigues; Linares, Edlaine ; Truzzi, Daniela Ramos ; Augusto, Ohara ; Toledo Junior, José Carlos
Source: Journal of Biological Chemistry. Unidades: IQ, FFCLRP
Subjects: ÓXIDO NÍTRICO, ESTRESSE OXIDATIVO
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ABNT
DAMASCENO, Fernando Cruvinel et al. The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source. Journal of Biological Chemistry, v. 293, p. 8530-8542 : + Supplementary materials ( S1-S13), 2018Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA117.000883. Acesso em: 02 nov. 2024.
APA
Damasceno, F. C., Condeles, A. L., Lopes, A. K. B., Facci, R. R., Linares, E., Truzzi, D. R., et al. (2018). The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source. Journal of Biological Chemistry, 293, 8530-8542 : + Supplementary materials ( S1-S13). doi:10.1074/jbc.RA117.000883
NLM
Damasceno FC, Condeles AL, Lopes AKB, Facci RR, Linares E, Truzzi DR, Augusto O, Toledo Junior JC. The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source [Internet]. Journal of Biological Chemistry. 2018 ; 293 8530-8542 : + Supplementary materials ( S1-S13).[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA117.000883
Vancouver
Damasceno FC, Condeles AL, Lopes AKB, Facci RR, Linares E, Truzzi DR, Augusto O, Toledo Junior JC. The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source [Internet]. Journal of Biological Chemistry. 2018 ; 293 8530-8542 : + Supplementary materials ( S1-S13).[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA117.000883
Artigo de periodico
A bipartite periplasmic receptor–diguanylate cyclase pair (XAC2383–XAC2382) in the bacterium Xanthomonas citri (2018)
Teixeira, Raphael Dias; Carvalho, Cristiane Rodrigues Guzzo ; Arévalo, Santiago Justo; Andrade, Maxuel O; Abrahão, Josielle; Souza, Robson Francisco de ; Farah, Chuck Shaker
Source: Journal of Biological Chemistry. Unidades: ICB, IQ
Subjects: XANTHOMONAS, FITOPATÓGENOS, TRANSDUÇÃO DE SINAL CELULAR
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ABNT
TEIXEIRA, Raphael Dias et al. A bipartite periplasmic receptor–diguanylate cyclase pair (XAC2383–XAC2382) in the bacterium Xanthomonas citri. Journal of Biological Chemistry, v. 293, n. 2, p. 10767–10781, 2018Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA118.003475. Acesso em: 02 nov. 2024.
APA
Teixeira, R. D., Carvalho, C. R. G., Arévalo, S. J., Andrade, M. O., Abrahão, J., Souza, R. F. de, & Farah, C. S. (2018). A bipartite periplasmic receptor–diguanylate cyclase pair (XAC2383–XAC2382) in the bacterium Xanthomonas citri. Journal of Biological Chemistry, 293( 2), 10767–10781. doi:10.1074/jbc.RA118.003475
NLM
Teixeira RD, Carvalho CRG, Arévalo SJ, Andrade MO, Abrahão J, Souza RF de, Farah CS. A bipartite periplasmic receptor–diguanylate cyclase pair (XAC2383–XAC2382) in the bacterium Xanthomonas citri [Internet]. Journal of Biological Chemistry. 2018 ; 293( 2): 10767–10781.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA118.003475
Vancouver
Teixeira RD, Carvalho CRG, Arévalo SJ, Andrade MO, Abrahão J, Souza RF de, Farah CS. A bipartite periplasmic receptor–diguanylate cyclase pair (XAC2383–XAC2382) in the bacterium Xanthomonas citri [Internet]. Journal of Biological Chemistry. 2018 ; 293( 2): 10767–10781.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.RA118.003475
Artigo de periodico
Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase (2018)
Peixoto, Álbert Souza; Geyer, R. Ryan; Iqbal, Asif; Truzzi, Daniela Ramos ; Moretti, Ana Iochabel Soares; Laurindo, Francisco R. M; Augusto, Ohara
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: PERÓXIDO DE HIDROGÊNIO, CINÉTICA
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ABNT
PEIXOTO, Álbert Souza et al. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase. Journal of Biological Chemistry, v. 293, n. 4, p. 1450-1465, 2018Tradução . . Disponível em: http://www.jbc.org/content/early/2017/11/30/jbc.M117.807016. Acesso em: 02 nov. 2024.
APA
Peixoto, Á. S., Geyer, R. R., Iqbal, A., Truzzi, D. R., Moretti, A. I. S., Laurindo, F. R. M., & Augusto, O. (2018). Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase. Journal of Biological Chemistry, 293( 4), 1450-1465. doi:10.1074/jbc.M117.807016
NLM
Peixoto ÁS, Geyer RR, Iqbal A, Truzzi DR, Moretti AIS, Laurindo FRM, Augusto O. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase [Internet]. Journal of Biological Chemistry. 2018 ; 293( 4): 1450-1465.[citado 2024 nov. 02 ] Available from: http://www.jbc.org/content/early/2017/11/30/jbc.M117.807016
Vancouver
Peixoto ÁS, Geyer RR, Iqbal A, Truzzi DR, Moretti AIS, Laurindo FRM, Augusto O. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase [Internet]. Journal of Biological Chemistry. 2018 ; 293( 4): 1450-1465.[citado 2024 nov. 02 ] Available from: http://www.jbc.org/content/early/2017/11/30/jbc.M117.807016
Artigo de periodico
Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 in Saccharomyces cerevisiae (2017)
Zubiate, Fernando Alexis Gonzales; Okuda, Ellen K; Cunha, Julia P. C. da; Oliveira, Carla Columbano de
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: CICLO CELULAR, ESPECTROMETRIA DE MASSAS, RNA RIBOSSÔMICO
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ABNT
ZUBIATE, Fernando Alexis Gonzales et al. Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 in Saccharomyces cerevisiae. Journal of Biological Chemistry, v. 292, n. 29, p. 12267-12384, 2017Tradução . . Disponível em: https://doi.org/10.1074/jbc.M116.772376. Acesso em: 02 nov. 2024.
APA
Zubiate, F. A. G., Okuda, E. K., Cunha, J. P. C. da, & Oliveira, C. C. de. (2017). Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 in Saccharomyces cerevisiae. Journal of Biological Chemistry, 292( 29), 12267-12384. doi:10.1074/jbc.M116.772376
NLM
Zubiate FAG, Okuda EK, Cunha JPC da, Oliveira CC de. Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 in Saccharomyces cerevisiae [Internet]. Journal of Biological Chemistry. 2017 ; 292( 29): 12267-12384.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M116.772376
Vancouver
Zubiate FAG, Okuda EK, Cunha JPC da, Oliveira CC de. Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 in Saccharomyces cerevisiae [Internet]. Journal of Biological Chemistry. 2017 ; 292( 29): 12267-12384.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M116.772376
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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ABNT
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: 02 nov. 2024.
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 2024 nov. 02 ] 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 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M116.767657
Artigo de periodico
A novel mercuric reductase from the unique deep brine environment of Atlantis II in the Red Sea (2014)
Sayed, Ahmed; Ghazy, Mohamed A; Ferreira, Ari José Scattone; Setubal, João Carlos ; Chambergo Alcalde, Felipe Santiago ; Ouf, Amged; Adel, Mustafa; Dawe, Adam S; Archer, John A. C; Bajic, Vladimir B; Siam, Rania; El Dorry, Hamza Fahmi Ali
Source: Journal of Biological Chemistry. Unidades: IQ, EACH
Subjects: ECOLOGIA MICROBIANA, MERCÚRIO (ELEMENTO QUÍMICO)
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ABNT
SAYED, Ahmed et al. A novel mercuric reductase from the unique deep brine environment of Atlantis II in the Red Sea. Journal of Biological Chemistry, v. 289, n. ja 2014, p. 1675\20131687, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.493429. Acesso em: 02 nov. 2024.
APA
Sayed, A., Ghazy, M. A., Ferreira, A. J. S., Setubal, J. C., Chambergo Alcalde, F. S., Ouf, A., et al. (2014). A novel mercuric reductase from the unique deep brine environment of Atlantis II in the Red Sea. Journal of Biological Chemistry, 289( ja 2014), 1675\20131687. doi:10.1074/jbc.M113.493429
NLM
Sayed A, Ghazy MA, Ferreira AJS, Setubal JC, Chambergo Alcalde FS, Ouf A, Adel M, Dawe AS, Archer JAC, Bajic VB, Siam R, El Dorry HFA. A novel mercuric reductase from the unique deep brine environment of Atlantis II in the Red Sea [Internet]. Journal of Biological Chemistry. 2014 ; 289( ja 2014): 1675\20131687.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M113.493429
Vancouver
Sayed A, Ghazy MA, Ferreira AJS, Setubal JC, Chambergo Alcalde FS, Ouf A, Adel M, Dawe AS, Archer JAC, Bajic VB, Siam R, El Dorry HFA. A novel mercuric reductase from the unique deep brine environment of Atlantis II in the Red Sea [Internet]. Journal of Biological Chemistry. 2014 ; 289( ja 2014): 1675\20131687.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M113.493429
Artigo de periodico
Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme (2014)
Coelho, Fernando Rodrigues; Iqbal, Asif; Linares, Edlaine ; Silva, Daniel F; Lima, Filipe da Silva; Cuccovia, Iolanda Midea ; Augusto, Ohara
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: SUPERÓXIDO DISMUTASE, PEROXIDASE, ENZIMAS
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ABNT
COELHO, Fernando Rodrigues et al. Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme. Journal of Biological Chemistry, v. 289, n. 44, p. 30690-30701, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M114.586370. Acesso em: 02 nov. 2024.
APA
Coelho, F. R., Iqbal, A., Linares, E., Silva, D. F., Lima, F. da S., Cuccovia, I. M., & Augusto, O. (2014). Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme. Journal of Biological Chemistry, 289( 44), 30690-30701. doi:10.1074/jbc.M114.586370
NLM
Coelho FR, Iqbal A, Linares E, Silva DF, Lima F da S, Cuccovia IM, Augusto O. Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme [Internet]. Journal of Biological Chemistry. 2014 ; 289( 44): 30690-30701.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M114.586370
Vancouver
Coelho FR, Iqbal A, Linares E, Silva DF, Lima F da S, Cuccovia IM, Augusto O. Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme [Internet]. Journal of Biological Chemistry. 2014 ; 289( 44): 30690-30701.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M114.586370
Artigo de periodico
Neurolysin knockout mice generation and initial phenotype characterization (2014)
Cavalcanti, Diogo Manuel Lopes de Paiva; Castro, Leandro Mantovani de; Rosa Neto, José Cesar ; Seelaender, Marília Cerqueira Leite; Neves, Rodrigo Xavier das; Oliveira, Vitor; Forti, Fabio Luis ; Iwai, Leo Kei; Gozzo, Fabio Cesar; Todiras, Mihail; Schadock, Ines; Barros, Carlos Cesar; Bader, Michael; Ferro, Emer Suavinho
Source: Journal of Biological Chemistry. Unidades: ICB, IQ
Subjects: FENÓTIPOS, OLIGOPEPTÍDEOS
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ABNT
CAVALCANTI, Diogo Manuel Lopes de Paiva et al. Neurolysin knockout mice generation and initial phenotype characterization. Journal of Biological Chemistry, v. 289, n. 22, p. 15426-15440, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.539148. Acesso em: 02 nov. 2024.
APA
Cavalcanti, D. M. L. de P., Castro, L. M. de, Rosa Neto, J. C., Seelaender, M. C. L., Neves, R. X. das, Oliveira, V., et al. (2014). Neurolysin knockout mice generation and initial phenotype characterization. Journal of Biological Chemistry, 289( 22), 15426-15440. doi:10.1074/jbc.M113.539148
NLM
Cavalcanti DML de P, Castro LM de, Rosa Neto JC, Seelaender MCL, Neves RX das, Oliveira V, Forti FL, Iwai LK, Gozzo FC, Todiras M, Schadock I, Barros CC, Bader M, Ferro ES. Neurolysin knockout mice generation and initial phenotype characterization [Internet]. Journal of Biological Chemistry. 2014 ; 289( 22): 15426-15440.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M113.539148
Vancouver
Cavalcanti DML de P, Castro LM de, Rosa Neto JC, Seelaender MCL, Neves RX das, Oliveira V, Forti FL, Iwai LK, Gozzo FC, Todiras M, Schadock I, Barros CC, Bader M, Ferro ES. Neurolysin knockout mice generation and initial phenotype characterization [Internet]. Journal of Biological Chemistry. 2014 ; 289( 22): 15426-15440.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M113.539148
Artigo de periodico
Akt-dependent activation of mTORC1 complex involves phosphorylation of mTOR (Mammalian target of rapamycin) by IκB Kinase α (IKK α) (2014)
Dan, Han C; Ebbs, Aaron; Pasparakis, Manolis; Dyke, Terry Van; Bassères, Daniela Sanchez ; Baldwin, Albert S
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: PROTEÍNAS QUINASES, GENES SUPRESSORES
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ABNT
DAN, Han C et al. Akt-dependent activation of mTORC1 complex involves phosphorylation of mTOR (Mammalian target of rapamycin) by IκB Kinase α (IKK α). Journal of Biological Chemistry, v. 289, n. 36, p. 25227-25240, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M114.554881. Acesso em: 02 nov. 2024.
APA
Dan, H. C., Ebbs, A., Pasparakis, M., Dyke, T. V., Bassères, D. S., & Baldwin, A. S. (2014). Akt-dependent activation of mTORC1 complex involves phosphorylation of mTOR (Mammalian target of rapamycin) by IκB Kinase α (IKK α). Journal of Biological Chemistry, 289( 36), 25227-25240. doi:10.1074/jbc.M114.554881
NLM
Dan HC, Ebbs A, Pasparakis M, Dyke TV, Bassères DS, Baldwin AS. Akt-dependent activation of mTORC1 complex involves phosphorylation of mTOR (Mammalian target of rapamycin) by IκB Kinase α (IKK α) [Internet]. Journal of Biological Chemistry. 2014 ; 289( 36): 25227-25240.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M114.554881
Vancouver
Dan HC, Ebbs A, Pasparakis M, Dyke TV, Bassères DS, Baldwin AS. Akt-dependent activation of mTORC1 complex involves phosphorylation of mTOR (Mammalian target of rapamycin) by IκB Kinase α (IKK α) [Internet]. Journal of Biological Chemistry. 2014 ; 289( 36): 25227-25240.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M114.554881
Artigo de periodico
A novel intracellular peptide derived from `G IND. 1´/S cyclin D2 induces cell death (2014)
Araujo, Christiane Bezerra de; Russo, Lilian Cristina; Castro, Leandro Mantovani de; Forti, Fabio Luis ; Monte, Elisabete R. do; Rioli, Vanessa; Gozzo, Fabio Cesar; Colquhoun, Alison ; Ferro, Emer Suavinho
Source: Journal of Biological Chemistry. Unidades: ICB, IQ
Subjects: PEPTÍDEOS, METABOLISMO DE PROTEÍNA
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ABNT
ARAUJO, Christiane Bezerra de et al. A novel intracellular peptide derived from `G IND. 1´/S cyclin D2 induces cell death. Journal of Biological Chemistry, v. 289, n. 24, p. 16711-16726, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.537118. Acesso em: 02 nov. 2024.
APA
Araujo, C. B. de, Russo, L. C., Castro, L. M. de, Forti, F. L., Monte, E. R. do, Rioli, V., et al. (2014). A novel intracellular peptide derived from `G IND. 1´/S cyclin D2 induces cell death. Journal of Biological Chemistry, 289( 24), 16711-16726. doi:10.1074/jbc.M113.537118
NLM
Araujo CB de, Russo LC, Castro LM de, Forti FL, Monte ER do, Rioli V, Gozzo FC, Colquhoun A, Ferro ES. A novel intracellular peptide derived from `G IND. 1´/S cyclin D2 induces cell death [Internet]. Journal of Biological Chemistry. 2014 ; 289( 24): 16711-16726.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M113.537118
Vancouver
Araujo CB de, Russo LC, Castro LM de, Forti FL, Monte ER do, Rioli V, Gozzo FC, Colquhoun A, Ferro ES. A novel intracellular peptide derived from `G IND. 1´/S cyclin D2 induces cell death [Internet]. Journal of Biological Chemistry. 2014 ; 289( 24): 16711-16726.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1074/jbc.M113.537118

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