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Artigo de periodico
Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds (2021)
Liberato, Marcelo Vizona; Prates, Erica Teixeira; Gonçalves, Thiago Augusto; Bernardes, Amanda; Vilela, Nathalia ; Fattori, Juliana; Ematsu, Gabriela Cristina; Chinaglia, Mariana; Gomes, Emerson Rodrigo Machi; Figueira, Ana Carolina Migliorini; Damasio, André; Polikarpov, Igor ; Skaf, Munir S.; Squina, Fabio Marcio
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: BIOTECNOLOGIA, ENZIMAS HIDROLÍTICAS, POLISSACARÍDEOS
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ABNT
LIBERATO, Marcelo Vizona; PRATES, Erica Teixeira; GONÇALVES, Thiago Augusto; et al. Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds. Journal of Biological Chemistry, Rockville, v. 296, p. 100385-1-100385-13 + supporting information: S1-S15, 2021. DOI: 10.1016/j.jbc.2021.100385.
APA
Liberato, M. V., Prates, E. T., Gonçalves, T. A., Bernardes, A., Vilela, N., Fattori, J., et al. (2021). Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds. Journal of Biological Chemistry, 296, 100385-1-100385-13 + supporting information: S1-S15. doi:10.1016/j.jbc.2021.100385
NLM
Liberato MV, Prates ET, Gonçalves TA, Bernardes A, Vilela N, Fattori J, Ematsu GC, Chinaglia M, Gomes ERM, Figueira ACM, Damasio A, Polikarpov I, Skaf MS, Squina FM. Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds. Journal of Biological Chemistry. 2021 ; 296 100385-1-100385-13 + supporting information: S1-S15.
Vancouver
Liberato MV, Prates ET, Gonçalves TA, Bernardes A, Vilela N, Fattori J, Ematsu GC, Chinaglia M, Gomes ERM, Figueira ACM, Damasio A, Polikarpov I, Skaf MS, Squina FM. Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds. Journal of Biological Chemistry. 2021 ; 296 100385-1-100385-13 + supporting information: S1-S15.
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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ABNT
PINTO, Paula Ramos; YOSHINAGA, Marcos Yukio; BIANCO, Vanessa Del; et al. Dietary sodium restriction alters muscle lipidomics that relates to insulin resistance in mice. Journal of Biological Chemistry, Rockville, v. 296, p. 1-12 art. 100344, 2021. Disponível em: < http://dx.doi.org/10.1016/j.jbc.2021.100344 > DOI: 10.1016/j.jbc.2021.100344.
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.Available from: http://dx.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.Available from: http://dx.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; Karplus, P. Andrew; Winterbourn, Christine C; Meotti, Flavia Carla ; Kean, Kelsey M; Göbl, Christoph ; Peixoto, Albert Souza ; Heath, Sarah G; Crowther, Jennifer M ; Dobson, Renwick C. J; Pace, Paul E; Horne, Christopher R
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: PERÓXIDO DE HIDROGÊNIO, CINÉTICA, PEROXIDASE
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ABNT
PESKIN, Alexander V; KARPLUS, P. Andrew; WINTERBOURN, Christine C; et al. Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2. Journal of Biological Chemistry, Bethesda, 2021. Disponível em: < https://dx.doi.org/10.1016/j.jbc.2021.100494 > DOI: 10.1016/j.jbc.2021.100494.
APA
Peskin, A. V., Karplus, P. A., Winterbourn, C. C., Meotti, F. C., Kean, K. M., Göbl, C., et al. (2021). Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2. Journal of Biological Chemistry. doi:10.1016/j.jbc.2021.100494
NLM
Peskin AV, Karplus PA, Winterbourn CC, Meotti FC, Kean KM, Göbl C, Peixoto AS, Heath SG, Crowther JM, Dobson RCJ, Pace PE, Horne CR. Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2 [Internet]. Journal of Biological Chemistry. 2021 ;Available from: https://dx.doi.org/10.1016/j.jbc.2021.100494
Vancouver
Peskin AV, Karplus PA, Winterbourn CC, Meotti FC, Kean KM, Göbl C, Peixoto AS, Heath SG, Crowther JM, Dobson RCJ, Pace PE, Horne CR. Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2 [Internet]. Journal of Biological Chemistry. 2021 ;Available from: https://dx.doi.org/10.1016/j.jbc.2021.100494
Artigo de periodico
The genetic Ca2+ sensor GCaMP3 reveals multiple Ca2+ stores differentially coupled to Ca2+ entry in the human malaria parasite Plasmodium falciparum (2020)
Pereira, Lucas Borges; Thomas, Samantha J; Silva, Amanda Laizy dos Anjos e; Bartlett, Paula J; Thomas, Andrew P; Garcia, Célia Regina da Silva
Source: Journal of Biological Chemistry. Unidades: FCF, FCFRP
Subjects: MALÁRIA, PLASMODIUM FALCIPARUM
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ABNT
PEREIRA, Lucas Borges; THOMAS, Samantha J; SILVA, Amanda Laizy dos Anjos e; et al. The genetic Ca2+ sensor GCaMP3 reveals multiple Ca2+ stores differentially coupled to Ca2+ entry in the human malaria parasite Plasmodium falciparum. Journal of Biological Chemistry, Bethesda, v. 295, n. 44, p. 14998-15012, 2020. Disponível em: < http://dx.doi.org/10.1074/jbc.RA120.014906 > DOI: 10.1074/jbc.RA120.014906.
APA
Pereira, L. B., Thomas, S. J., Silva, A. L. dos A. e, Bartlett, P. J., Thomas, A. P., & Garcia, C. R. da S. (2020). The genetic Ca2+ sensor GCaMP3 reveals multiple Ca2+ stores differentially coupled to Ca2+ entry in the human malaria parasite Plasmodium falciparum. Journal of Biological Chemistry, 295( 44), 14998-15012. doi:10.1074/jbc.RA120.014906
NLM
Pereira LB, Thomas SJ, Silva AL dos A e, Bartlett PJ, Thomas AP, Garcia CR da S. The genetic Ca2+ sensor GCaMP3 reveals multiple Ca2+ stores differentially coupled to Ca2+ entry in the human malaria parasite Plasmodium falciparum [Internet]. Journal of Biological Chemistry. 2020 ; 295( 44): 14998-15012.Available from: http://dx.doi.org/10.1074/jbc.RA120.014906
Vancouver
Pereira LB, Thomas SJ, Silva AL dos A e, Bartlett PJ, Thomas AP, Garcia CR da S. The genetic Ca2+ sensor GCaMP3 reveals multiple Ca2+ stores differentially coupled to Ca2+ entry in the human malaria parasite Plasmodium falciparum [Internet]. Journal of Biological Chemistry. 2020 ; 295( 44): 14998-15012.Available from: http://dx.doi.org/10.1074/jbc.RA120.014906
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, Luis G. M; 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: IQ, IFSC
Subjects: BACTÉRIAS GRAM-POSITIVAS, LIPÍDEOS
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ABNT
SASTRE, Diego Emiliano; PULSCHEN, Andre A; BASSO, Luis G. M; et al. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis. Journal of Biological Chemistry, Bethesda, v. 295, n. 7, p. 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2, 2020. Disponível em: < https://doi.org/10.1074/jbc.RA119.011147 > DOI: 10.1074/jbc.RA119.011147.
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.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.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; ZUBIATE, Fernando Alexis Gonzales; GADAL, Olivier; OLIVEIRA, Carla Columbano de. Nucleolar localization of the yeast RNA exosome subunit Rrp44 hints at early pre-rRNA processing as its main function. Journal of Biological Chemistry, Bethesda, v. 295, n. 32, p. 11195-11213, 2020. Disponível em: < http://dx.doi.org/10.1074/jbc.RA120.013589 > DOI: 10.1074/jbc.RA120.013589.
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.Available from: http://dx.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.Available from: http://dx.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; Mendoza, Diego de; Navarro, Marcos Vicente de Albuquerque Salles ; Guerin, Marcelo E.; Gueiros Filho, Frederico José
Source: Journal of Biological Chemistry. Unidades: IQ, IFSC, FFCLRP
Subjects: FOSFOLIPÍDEOS, LIPÍDEOS
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ABNT
SASTRE, Diego Emiliano; BASSO, Luís Guilherme Mansor; TRASTOY, Beatriz; et al. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry, Bethesda, v. 295, n. 7, p. 2136-2147 + Supplementary materials Figs. S1-S9, 2020. DOI: 10.1074/jbc.RA119.011122.
APA
Sastre, D. E., Basso, L. G. M., Trastoy, B., Cifuente, J. O., Contreras, X., Mendoza, D. de, 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, Mendoza D de, Navarro MV de AS, Guerin ME, Gueiros Filho FJ. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry. 2020 ; 295( 7): 2136-2147 + Supplementary materials Figs. S1-S9.
Vancouver
Sastre DE, Basso LGM, Trastoy B, Cifuente JO, Contreras X, Mendoza D de, Navarro MV de AS, Guerin ME, Gueiros Filho FJ. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry. 2020 ; 295( 7): 2136-2147 + Supplementary materials Figs. S1-S9.
Artigo de periodico
Dual inhibition of glutaminase and carnitine palmitoyltransferase decreases growth and migration of glutaminase inhibition–resistant triple-negative breast cancer cells (2019)
Reis, Larissa Menezes dos ; Patroni, Fábio Malta de Sá; Dias, Marília Meira; Consonni, Sílvio Roberto ; Vieira, Pedro Manoel Mendes de Moraes; Silber, Ariel Mariano ; Dias, Sandra Martha Gomes; Adamoski, Douglas ; Souza,Rodolpho Ornitz Oliveira ; Ascenção, Carolline Fernanda Rodrigues ; Oliveira, Krishina Ratna Sousa de; Silva, Felipe Corrêa da
Source: Journal of Biological Chemistry. Unidade: ICB
Subjects: PARASITOLOGIA, METABOLISMO ENERGÉTICO, NEOPLASIAS MAMÁRIAS, OXIDAÇÃO, CÉLULAS CULTIVADAS DE TUMOR, GLUTAMINA, MITOCÔNDRIAS, EXPRESSÃO GÊNICA, TRANSCRIÇÃO GÊNICA, LIPÍDEOS
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ABNT
REIS, Larissa Menezes dos; PATRONI, Fábio Malta de Sá; DIAS, Marília Meira; et al. Dual inhibition of glutaminase and carnitine palmitoyltransferase decreases growth and migration of glutaminase inhibition–resistant triple-negative breast cancer cells. Journal of Biological Chemistry, Rockville, v. 294, n. 24, p. 9342–9357, 2019. Disponível em: < https://doi.org/10.1074/jbc.ra119.008180 > DOI: 10.1074/jbc.ra119.008180.
APA
Reis, L. M. dos, Patroni, F. M. de S., Dias, M. M., Consonni, S. R., Vieira, P. M. M. de M., Silber, A. M., et al. (2019). Dual inhibition of glutaminase and carnitine palmitoyltransferase decreases growth and migration of glutaminase inhibition–resistant triple-negative breast cancer cells. Journal of Biological Chemistry, 294( 24), 9342–9357. doi:10.1074/jbc.ra119.008180
NLM
Reis LM dos, Patroni FM de S, Dias MM, Consonni SR, Vieira PMM de M, Silber AM, Dias SMG, Adamoski D, Souza ROO, Ascenção CFR, Oliveira KRS de, Silva FC da. Dual inhibition of glutaminase and carnitine palmitoyltransferase decreases growth and migration of glutaminase inhibition–resistant triple-negative breast cancer cells [Internet]. Journal of Biological Chemistry. 2019 ; 294( 24): 9342–9357.Available from: https://doi.org/10.1074/jbc.ra119.008180
Vancouver
Reis LM dos, Patroni FM de S, Dias MM, Consonni SR, Vieira PMM de M, Silber AM, Dias SMG, Adamoski D, Souza ROO, Ascenção CFR, Oliveira KRS de, Silva FC da. Dual inhibition of glutaminase and carnitine palmitoyltransferase decreases growth and migration of glutaminase inhibition–resistant triple-negative breast cancer cells [Internet]. Journal of Biological Chemistry. 2019 ; 294( 24): 9342–9357.Available from: https://doi.org/10.1074/jbc.ra119.008180
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; COELHO, Fernando Rodrigues; PAVIANI, Veronica; et al. The bicarbonate/carbon dioxide pair increases hydrogen peroxide−mediated hyperoxidation of human peroxiredoxin 1. Journal of Biological Chemistry, 4,011, v. 294, n. 38, p. 14055-14067 :+Supplementary materials (S1-19), 2019. Disponível em: < http://dx.doi.org/10.1074/jbc.RA119.008825 > DOI: 10.1074/jbc.RA119.008825.
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).Available from: http://dx.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).Available from: http://dx.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; RODRIGUES, Michele Angela; CAMPOS, Ana Carolina de Angelis; et al. Epidermal growth factor (EGF) triggers nuclear calcium signaling through the intranuclear phospholipase C delta-4 (PLCδ4). Journal of Biological Chemistry, Bethesda, v. 294, n. 45, p. 16650-16662, 2019. Disponível em: < http://dx.doi.org/10.1074/jbc.RA118.006961 > DOI: 10.1074/jbc.RA118.006961.
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.Available from: http://dx.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.Available from: http://dx.doi.org/10.1074/jbc.RA118.006961
Artigo de periodico
A bipartite periplasmic receptor–diguanylate cyclase pair (XAC2383–XAC2382) in the bacterium Xanthomonas citri (2018)
Teixeira, Raphael Dias; Guzzo, Cristiane R; 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; GUZZO, Cristiane R; ARÉVALO, Santiago Justo; et al. A bipartite periplasmic receptor–diguanylate cyclase pair (XAC2383–XAC2382) in the bacterium Xanthomonas citri. Journal of Biological Chemistry, Rockville, v. 293, n. 2, p. 10767–10781, 2018. Disponível em: < http://dx.doi.org/10.1074/jbc.RA118.003475 > DOI: 10.1074/jbc.RA118.003475.
APA
Teixeira, R. D., Guzzo, C. R., 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, Guzzo CR, 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.Available from: http://dx.doi.org/10.1074/jbc.RA118.003475
Vancouver
Teixeira RD, Guzzo CR, 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.Available from: http://dx.doi.org/10.1074/jbc.RA118.003475
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; CONDELES, André Luís; LOPES, Angélica Kodama Bueno; 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, Rockville, v. 293, p. 8530-8542 : + Supplementary materials ( S1-S13), 2018. Disponível em: < http://dx.doi.org/10.1074/jbc.RA117.000883 > DOI: 10.1074/jbc.RA117.000883.
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).Available from: http://dx.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).Available from: http://dx.doi.org/10.1074/jbc.RA117.000883
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; GEYER, R. Ryan; IQBAL, Asif; et al. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase. Journal of Biological Chemistry, Bethesda, v. 293, n. 4, p. 1450-1465, 2018. Disponível em: < http://www.jbc.org/content/early/2017/11/30/jbc.M117.807016 > DOI: 10.1074/jbc.M117.807016.
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.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.Available from: http://www.jbc.org/content/early/2017/11/30/jbc.M117.807016
Artigo de periodico
Arabidopsis thaliana rapid alkalinization factor 1-mediated root growth inhibition is dependent on calmodulin-like protein 38 (2018)
Campos, Wellington F; Dressano, Keini; Ceciliato, Paulo H. O; Guerrero-Abad, Juan Carlos; Silva, Aparecida Leonir; Fiori, Celso S; Canto, Amanda Morato do; Bergonci, Tábata; Claus, Lucas A. N; Silva-Filho, Marcio de Castro; Moura, Daniel Scherer de
Source: Journal of Biological Chemistry. Unidade: ESALQ
Subjects: RAIZ, PAPAVERALES, CALMODULINA, INIBIDORES DE CRESCIMENTO VEGETAL, PEPTÍDEOS
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ABNT
CAMPOS, Wellington F; DRESSANO, Keini; CECILIATO, Paulo H. O; et al. Arabidopsis thaliana rapid alkalinization factor 1-mediated root growth inhibition is dependent on calmodulin-like protein 38. Journal of Biological Chemistry, Rockville, v. 293, 2018. Disponível em: < http://www.jbc.org/content/early/2017/12/27/jbc.M117.808881.full.pdf > DOI: 10.1074/jbc.m117.808881.
APA
Campos, W. F., Dressano, K., Ceciliato, P. H. O., Guerrero-Abad, J. C., Silva, A. L., Fiori, C. S., et al. (2018). Arabidopsis thaliana rapid alkalinization factor 1-mediated root growth inhibition is dependent on calmodulin-like protein 38. Journal of Biological Chemistry, 293. doi:10.1074/jbc.m117.808881
NLM
Campos WF, Dressano K, Ceciliato PHO, Guerrero-Abad JC, Silva AL, Fiori CS, Canto AM do, Bergonci T, Claus LAN, Silva-Filho M de C, Moura DS de. Arabidopsis thaliana rapid alkalinization factor 1-mediated root growth inhibition is dependent on calmodulin-like protein 38 [Internet]. Journal of Biological Chemistry. 2018 ; 293Available from: http://www.jbc.org/content/early/2017/12/27/jbc.M117.808881.full.pdf
Vancouver
Campos WF, Dressano K, Ceciliato PHO, Guerrero-Abad JC, Silva AL, Fiori CS, Canto AM do, Bergonci T, Claus LAN, Silva-Filho M de C, Moura DS de. Arabidopsis thaliana rapid alkalinization factor 1-mediated root growth inhibition is dependent on calmodulin-like protein 38 [Internet]. Journal of Biological Chemistry. 2018 ; 293Available from: http://www.jbc.org/content/early/2017/12/27/jbc.M117.808881.full.pdf
Artigo de periodico
Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments (2017)
Gomes, Fernando; Palma, Flávio Romero; Barros, Mário H; Tsuchida, Eduardo T; Turano, Helena G; Alegria, Thiago G. P; Demasi, Marilene; Netto, Luis E. S
Source: Journal of Biological Chemistry. Unidades: ICB, IB
Subjects: BIOLOGIA MOLECULAR, BIOQUÍMICA, LEVEDURAS, SACCHAROMYCES, PROTEÍNAS
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ABNT
GOMES, Fernando; PALMA, Flávio Romero; BARROS, Mário H; et al. Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments. Journal of Biological Chemistry, Bethesda, v. 292, n. 41, p. 17011-17024, 2017. Disponível em: < http://dx.doi.org/10.1074/jbc.M117.788588 > DOI: 10.1074/jbc.M117.788588.
APA
Gomes, F., Palma, F. R., Barros, M. H., Tsuchida, E. T., Turano, H. G., Alegria, T. G. P., et al. (2017). Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments. Journal of Biological Chemistry, 292( 41), 17011-17024. doi:10.1074/jbc.M117.788588
NLM
Gomes F, Palma FR, Barros MH, Tsuchida ET, Turano HG, Alegria TGP, Demasi M, Netto LES. Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments [Internet]. Journal of Biological Chemistry. 2017 ; 292( 41): 17011-17024.Available from: http://dx.doi.org/10.1074/jbc.M117.788588
Vancouver
Gomes F, Palma FR, Barros MH, Tsuchida ET, Turano HG, Alegria TGP, Demasi M, Netto LES. Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments [Internet]. Journal of Biological Chemistry. 2017 ; 292( 41): 17011-17024.Available from: http://dx.doi.org/10.1074/jbc.M117.788588
Artigo de periodico
Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites (2017)
Morais, Mariana A. B ; Giuseppe, Priscila O ; Souza, Tatiana A. C. B; Castro, Helena ; Honorato, Rodrigo V; Oliveira, Paulo S. L; Netto, Luis E. S ; Tomas, Ana M ; Murakami, Mário T
Source: Journal of Biological Chemistry. Unidade: IB
Subjects: BIOLOGIA MOLECULAR, PARASITOLOGIA, PEROXIDASE, BIOQUÍMICA, LEISHMANIA, ENZIMAS OXIRREDUTORAS
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ABNT
MORAIS, Mariana A. B; GIUSEPPE, Priscila O; SOUZA, Tatiana A. C. B; et al. Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites. Journal of Biological Chemistry, Bethesda, v. 292, n. 17, p. 7023-7039, 2017. Disponível em: < http://dx.doi.org/10.1074/jbc.M116.762039 > DOI: 10.1074/jbc.M116.762039.
APA
Morais, M. A. B., Giuseppe, P. O., Souza, T. A. C. B., Castro, H., Honorato, R. V., Oliveira, P. S. L., et al. (2017). Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites. Journal of Biological Chemistry, 292( 17), 7023-7039. doi:10.1074/jbc.M116.762039
NLM
Morais MAB, Giuseppe PO, Souza TACB, Castro H, Honorato RV, Oliveira PSL, Netto LES, Tomas AM, Murakami MT. Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites [Internet]. Journal of Biological Chemistry. 2017 ; 292( 17): 7023-7039.Available from: http://dx.doi.org/10.1074/jbc.M116.762039
Vancouver
Morais MAB, Giuseppe PO, Souza TACB, Castro H, Honorato RV, Oliveira PSL, Netto LES, Tomas AM, Murakami MT. Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites [Internet]. Journal of Biological Chemistry. 2017 ; 292( 17): 7023-7039.Available from: http://dx.doi.org/10.1074/jbc.M116.762039
Artigo de periodico
Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases (2017)
Castro-Fernandez, Víctor; Herrera-Morande, Alejandra; Zamora, Ricardo; Merino, Felipe; Gonzalez-Ordenes, Felipe; Padilla-Salinas, Felipe; Pereira, Humberto d'Muniz; Brandão-Neto, José; Garratt, Richard Charles; Guixe, Victoria
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: BIOFÍSICA, ENZIMAS, EVOLUÇÃO MOLECULAR
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ABNT
CASTRO-FERNANDEZ, Víctor; HERRERA-MORANDE, Alejandra; ZAMORA, Ricardo; et al. Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases. Journal of Biological Chemistry, Rockville, v. 292, n. 38, p. 15598-15993 + Supplemental data, 2017. Disponível em: < http://dx.doi.org/10.1074/jbc.M117.790865 > DOI: 10.1074/jbc.M117.790865.
APA
Castro-Fernandez, V., Herrera-Morande, A., Zamora, R., Merino, F., Gonzalez-Ordenes, F., Padilla-Salinas, F., et al. (2017). Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases. Journal of Biological Chemistry, 292( 38), 15598-15993 + Supplemental data. doi:10.1074/jbc.M117.790865
NLM
Castro-Fernandez V, Herrera-Morande A, Zamora R, Merino F, Gonzalez-Ordenes F, Padilla-Salinas F, Pereira H d'M, Brandão-Neto J, Garratt RC, Guixe V. Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases [Internet]. Journal of Biological Chemistry. 2017 ; 292( 38): 15598-15993 + Supplemental data.Available from: http://dx.doi.org/10.1074/jbc.M117.790865
Vancouver
Castro-Fernandez V, Herrera-Morande A, Zamora R, Merino F, Gonzalez-Ordenes F, Padilla-Salinas F, Pereira H d'M, Brandão-Neto J, Garratt RC, Guixe V. Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases [Internet]. Journal of Biological Chemistry. 2017 ; 292( 38): 15598-15993 + Supplemental data.Available from: http://dx.doi.org/10.1074/jbc.M117.790865
Artigo de periodico
Autophagy downstream of endosomal Toll-like receptor signaling in macrophages is a key mechanism for resistance to Leishmania major infection (2017)
Franco, Luís Henrique; Fleuri, Anna Karoline Aguiar; Pellison, Natália Carvalho; Quirino, Gustavo Fernando da Silva; Horta, Catarina Veltrini; Carvalho, Renan Villanova Homem de; Oliveira, Sérgio Costa; Zamboni, Dario Simões
Source: Journal of Biological Chemistry. Unidade: FMRP
Subjects: LEISHMANIA, MACRÓFAGOS
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ABNT
FRANCO, Luís Henrique; FLEURI, Anna Karoline Aguiar; PELLISON, Natália Carvalho; et al. Autophagy downstream of endosomal Toll-like receptor signaling in macrophages is a key mechanism for resistance to Leishmania major infection. Journal of Biological Chemistry, Baltimore, v. 292, n. 32, p. 13087-13096, 2017. Disponível em: < http://dx.doi.org/10.1074/jbc.m117.780981 > DOI: 10.1074/jbc.m117.780981.
APA
Franco, L. H., Fleuri, A. K. A., Pellison, N. C., Quirino, G. F. da S., Horta, C. V., Carvalho, R. V. H. de, et al. (2017). Autophagy downstream of endosomal Toll-like receptor signaling in macrophages is a key mechanism for resistance to Leishmania major infection. Journal of Biological Chemistry, 292( 32), 13087-13096. doi:10.1074/jbc.m117.780981
NLM
Franco LH, Fleuri AKA, Pellison NC, Quirino GF da S, Horta CV, Carvalho RVH de, Oliveira SC, Zamboni DS. Autophagy downstream of endosomal Toll-like receptor signaling in macrophages is a key mechanism for resistance to Leishmania major infection [Internet]. Journal of Biological Chemistry. 2017 ; 292( 32): 13087-13096.Available from: http://dx.doi.org/10.1074/jbc.m117.780981
Vancouver
Franco LH, Fleuri AKA, Pellison NC, Quirino GF da S, Horta CV, Carvalho RVH de, Oliveira SC, Zamboni DS. Autophagy downstream of endosomal Toll-like receptor signaling in macrophages is a key mechanism for resistance to Leishmania major infection [Internet]. Journal of Biological Chemistry. 2017 ; 292( 32): 13087-13096.Available from: http://dx.doi.org/10.1074/jbc.m117.780981
Artigo de periodico
Filaments and fingers: novel structural aspects of the single septin from Chlamydomonas reinhardtii (2017)
Pinto, Andressa Patricia Alves; Pereira, Humberto d'Muniz; Zeraik, Ana E.; Ciol, Heloisa; Ferreira, Frederico M.; Brandão-Neto, José; De Marco, Ricardo; Navarro, Marcos Vicente de Albuquerque Salles; Risi, Cristina; Galkin, Vitold E.; Garratt, Richard Charles; Araújo, Ana Paula Ulian de
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: CRISTALOGRAFIA, BIOFÍSICA, ALGAS (ESTUDO), PROTEÍNAS, DNA
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ABNT
PINTO, Andressa Patricia Alves; PEREIRA, Humberto d'Muniz; ZERAIK, Ana E.; et al. Filaments and fingers: novel structural aspects of the single septin from Chlamydomonas reinhardtii. Journal of Biological Chemistry, Rockville, v. 292, n. 26, p. 10899-10911, 2017. Disponível em: < http://dx.doi.org/10.1074/jbc.M116.762229 > DOI: 10.1074/jbc.M116.762229.
APA
Pinto, A. P. A., Pereira, H. d'M., Zeraik, A. E., Ciol, H., Ferreira, F. M., Brandão-Neto, J., et al. (2017). Filaments and fingers: novel structural aspects of the single septin from Chlamydomonas reinhardtii. Journal of Biological Chemistry, 292( 26), 10899-10911. doi:10.1074/jbc.M116.762229
NLM
Pinto APA, Pereira H d'M, Zeraik AE, Ciol H, Ferreira FM, Brandão-Neto J, De Marco R, Navarro MV de AS, Risi C, Galkin VE, Garratt RC, Araújo APU de. Filaments and fingers: novel structural aspects of the single septin from Chlamydomonas reinhardtii [Internet]. Journal of Biological Chemistry. 2017 ; 292( 26): 10899-10911.Available from: http://dx.doi.org/10.1074/jbc.M116.762229
Vancouver
Pinto APA, Pereira H d'M, Zeraik AE, Ciol H, Ferreira FM, Brandão-Neto J, De Marco R, Navarro MV de AS, Risi C, Galkin VE, Garratt RC, Araújo APU de. Filaments and fingers: novel structural aspects of the single septin from Chlamydomonas reinhardtii [Internet]. Journal of Biological Chemistry. 2017 ; 292( 26): 10899-10911.Available from: http://dx.doi.org/10.1074/jbc.M116.762229
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; OKUDA, Ellen K; CUNHA, Julia P. C. da; OLIVEIRA, Carla Columbano de. Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 in Saccharomyces cerevisiae. Journal of Biological Chemistry, Bethesda, v. 292, n. 29, p. 12267-12384, 2017. Disponível em: < http://dx.doi.org/10.1074/jbc.M116.772376 > DOI: 10.1074/jbc.M116.772376.
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.Available from: http://dx.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.Available from: http://dx.doi.org/10.1074/jbc.M116.772376

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