ReP USP - Resultado da busca

Artigo de periodico
Redox-guided DNA scanning by the dynamic repair enzyme Endonuclease III (2025)
Hassan, Ayaz ; Lima, Filipe C. D. A. ; Crespilho, Frank Nelson
Source: Biochemistry. Unidade: IQSC
Subjects: GENÉTICA, PEPTÍDEOS, PROTEÍNAS
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
HASSAN, Ayaz e LIMA, Filipe C. D. A. e CRESPILHO, Frank Nelson. Redox-guided DNA scanning by the dynamic repair enzyme Endonuclease III. Biochemistry, v. 64, n. 4, p. 749-966, 2025Tradução . . Disponível em: https://doi.org/10.1021/acs.biochem.4c00621. Acesso em: 27 nov. 2025.
APA
Hassan, A., Lima, F. C. D. A., & Crespilho, F. N. (2025). Redox-guided DNA scanning by the dynamic repair enzyme Endonuclease III. Biochemistry, 64( 4), 749-966. doi:10.1021/acs.biochem.4c00621
NLM
Hassan A, Lima FCDA, Crespilho FN. Redox-guided DNA scanning by the dynamic repair enzyme Endonuclease III [Internet]. Biochemistry. 2025 ; 64( 4): 749-966.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.4c00621
Vancouver
Hassan A, Lima FCDA, Crespilho FN. Redox-guided DNA scanning by the dynamic repair enzyme Endonuclease III [Internet]. Biochemistry. 2025 ; 64( 4): 749-966.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.4c00621
Artigo de periodico
Monomeric esterase: insights into cooperative behavior, hysteresis/allokairy (2024)
Vinces, Tania Geraldine Churasacari ; Souza, Anacleto Silva de ; Carvalho, Cecília Fonseca; Visnardi, Aline Biazola ; Teixeira, Raphael Dias ; Cornejo, Edgar Enrique Llontop ; Paranhos, Beatriz Aparecida Passos Bismara ; Vicente, Elisabete José ; Pereira, José Odair ; Souza, Robson Francisco de ; Yonamine, Maurício ; Marana, Sandro Roberto ; Farah, Chuck Shaker ; Guzzo, Cristiane Rodrigues
Source: Biochemistry. Unidades: FCF, ICB, IQ
Subjects: MICROBIOLOGIA, ENZIMAS HIDROLÍTICAS, HIDRÓLISE, CRISTALOGRAFIA DE RAIOS X, MICROBIOLOGIA DO SOLO, NITOSSOLOS, ENSAIOS DOS SOLOS, ATIVAÇÃO ENZIMÁTICA, CINÉTICA QUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
VINCES, Tania Geraldine Churasacari et al. Monomeric esterase: insights into cooperative behavior, hysteresis/allokairy. Biochemistry, v. 63, n. 9, p. 1178-1193, 2024Tradução . . Disponível em: https://doi.org/10.1021/acs.biochem.3c00668. Acesso em: 27 nov. 2025.
APA
Vinces, T. G. C., Souza, A. S. de, Carvalho, C. F., Visnardi, A. B., Teixeira, R. D., Cornejo, E. E. L., et al. (2024). Monomeric esterase: insights into cooperative behavior, hysteresis/allokairy. Biochemistry, 63( 9), 1178-1193. doi:10.1021/acs.biochem.3c00668
NLM
Vinces TGC, Souza AS de, Carvalho CF, Visnardi AB, Teixeira RD, Cornejo EEL, Paranhos BAPB, Vicente EJ, Pereira JO, Souza RF de, Yonamine M, Marana SR, Farah CS, Guzzo CR. Monomeric esterase: insights into cooperative behavior, hysteresis/allokairy [Internet]. Biochemistry. 2024 ; 63( 9): 1178-1193.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.3c00668
Vancouver
Vinces TGC, Souza AS de, Carvalho CF, Visnardi AB, Teixeira RD, Cornejo EEL, Paranhos BAPB, Vicente EJ, Pereira JO, Souza RF de, Yonamine M, Marana SR, Farah CS, Guzzo CR. Monomeric esterase: insights into cooperative behavior, hysteresis/allokairy [Internet]. Biochemistry. 2024 ; 63( 9): 1178-1193.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.3c00668
Artigo de periodico
Transglutaminase type 2 is involved in the hematopoietic stem cells homeostasis (2020)
Oliverio, S.; Beltran, Jackeline Soares de Oliveira; Occhigrossi, L.; Bordoni, V.; Agrati, C.; D’Eletto, M.; Rossin, F.; Borelli, Primavera ; Amarante-Mendes, João Gustavo Pessini ; Demidov, O.; Barlev, N. A.; Piacentini, M.
Source: Biochemistry. Unidades: FCF, ICB
Subjects: IMUNOLOGIA, CÉLULAS-TRONCO, HEMATOPOESE, HOMEOSTASE, PROTEÍNAS, CÉLULAS MORTAS, CAMUNDONGOS, MEDULA ÓSSEA DE ANIMAL
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
OLIVERIO, S. et al. Transglutaminase type 2 is involved in the hematopoietic stem cells homeostasis. Biochemistry, v. 85, n. 10, p. 1159-1168, 2020Tradução . . Disponível em: https://doi.org/10.1134/S0006297920100041. Acesso em: 27 nov. 2025.
APA
Oliverio, S., Beltran, J. S. de O., Occhigrossi, L., Bordoni, V., Agrati, C., D’Eletto, M., et al. (2020). Transglutaminase type 2 is involved in the hematopoietic stem cells homeostasis. Biochemistry, 85( 10), 1159-1168. doi:10.1134/S0006297920100041
NLM
Oliverio S, Beltran JS de O, Occhigrossi L, Bordoni V, Agrati C, D’Eletto M, Rossin F, Borelli P, Amarante-Mendes JGP, Demidov O, Barlev NA, Piacentini M. Transglutaminase type 2 is involved in the hematopoietic stem cells homeostasis [Internet]. Biochemistry. 2020 ; 85( 10): 1159-1168.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1134/S0006297920100041
Vancouver
Oliverio S, Beltran JS de O, Occhigrossi L, Bordoni V, Agrati C, D’Eletto M, Rossin F, Borelli P, Amarante-Mendes JGP, Demidov O, Barlev NA, Piacentini M. Transglutaminase type 2 is involved in the hematopoietic stem cells homeostasis [Internet]. Biochemistry. 2020 ; 85( 10): 1159-1168.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1134/S0006297920100041
Artigo de periodico
Importance of the beta 5-beta 6 Loop for the structure, catalytic efficiency, and stability of carbapenem-hydrolyzing class D beta-Lactamase subfamily OXA-143 (2019)
Antunes, Victor U. ; Llontop, Edgar E ; Vasconcelos, Fernanda Nogales da Costa; Santos, Yossef Lopez de los ; Oliveira, Ronaldo J. ; Lincopan, Nilton ; Farah, Chuck Shaker ; Doucet, Nicolas ; Mittermaier, Anthony ; Favaro, Denize Cristina
Source: Biochemistry. Unidades: IQ, ICB
Subjects: ENZIMAS, BIOQUÍMICA, ENZIMAS HIDROLÍTICAS, HIDRÓLISE, ATIVAÇÃO ENZIMÁTICA, MUTAÇÃO, CATALISADORES
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
ANTUNES, Victor U. et al. Importance of the beta 5-beta 6 Loop for the structure, catalytic efficiency, and stability of carbapenem-hydrolyzing class D beta-Lactamase subfamily OXA-143. Biochemistry, v. 58, n. 34, p. 3604-3616, 2019Tradução . . Disponível em: https://doi.org/10.1021/acs.biochem.9b00365. Acesso em: 27 nov. 2025.
APA
Antunes, V. U., Llontop, E. E., Vasconcelos, F. N. da C., Santos, Y. L. de los, Oliveira, R. J., Lincopan, N., et al. (2019). Importance of the beta 5-beta 6 Loop for the structure, catalytic efficiency, and stability of carbapenem-hydrolyzing class D beta-Lactamase subfamily OXA-143. Biochemistry, 58( 34), 3604-3616. doi:10.1021/acs.biochem.9b00365
NLM
Antunes VU, Llontop EE, Vasconcelos FN da C, Santos YL de los, Oliveira RJ, Lincopan N, Farah CS, Doucet N, Mittermaier A, Favaro DC. Importance of the beta 5-beta 6 Loop for the structure, catalytic efficiency, and stability of carbapenem-hydrolyzing class D beta-Lactamase subfamily OXA-143 [Internet]. Biochemistry. 2019 ; 58( 34): 3604-3616.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.9b00365
Vancouver
Antunes VU, Llontop EE, Vasconcelos FN da C, Santos YL de los, Oliveira RJ, Lincopan N, Farah CS, Doucet N, Mittermaier A, Favaro DC. Importance of the beta 5-beta 6 Loop for the structure, catalytic efficiency, and stability of carbapenem-hydrolyzing class D beta-Lactamase subfamily OXA-143 [Internet]. Biochemistry. 2019 ; 58( 34): 3604-3616.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.9b00365
Artigo de periodico
Glutaminase affects the transcriptional activity of peroxisome proliferator-activated receptor γ (PPARγ) via direct interaction (2018)
Cassago, Carolina Aparecida de Guzzi; Dias, Marília Meira; Pinheiro, Matheus Pinto; Pasquali, Camila Cristina; Bastos, Alliny Cristiny Silva; Islam, Zeyaul; Consonni, Sílvio Roberto; Oliveira, Juliana Ferreira de; Gomes, Emerson Machi; Ascenção, Carolline Fernanda Rodrigues; Honorato, Rodrigo; Pauletti, Bianca Alves; Indolfo, Nathalia de Carvalho; Ribeiro Filho, Helder Veras; Oliveira, Paulo Sergio Lopes de; Figueira, Ana Carolina Migliorini; Leme, Adriana Franco Paes; Ambrosio, Andre Luis Berteli ; Dias, Sandra Martha Gomes
Source: Biochemistry. Unidade: IFSC
Subjects: GLUTAMINA, PROTEÍNAS, REGULAÇÃO GÊNICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
CASSAGO, Carolina Aparecida de Guzzi et al. Glutaminase affects the transcriptional activity of peroxisome proliferator-activated receptor γ (PPARγ) via direct interaction. Biochemistry, v. 57, n. 44, p. 6293-6307, 2018Tradução . . Disponível em: https://doi.org/10.1021/acs.biochem.8b00773. Acesso em: 27 nov. 2025.
APA
Cassago, C. A. de G., Dias, M. M., Pinheiro, M. P., Pasquali, C. C., Bastos, A. C. S., Islam, Z., et al. (2018). Glutaminase affects the transcriptional activity of peroxisome proliferator-activated receptor γ (PPARγ) via direct interaction. Biochemistry, 57( 44), 6293-6307. doi:10.1021/acs.biochem.8b00773
NLM
Cassago CA de G, Dias MM, Pinheiro MP, Pasquali CC, Bastos ACS, Islam Z, Consonni SR, Oliveira JF de, Gomes EM, Ascenção CFR, Honorato R, Pauletti BA, Indolfo N de C, Ribeiro Filho HV, Oliveira PSL de, Figueira ACM, Leme AFP, Ambrosio ALB, Dias SMG. Glutaminase affects the transcriptional activity of peroxisome proliferator-activated receptor γ (PPARγ) via direct interaction [Internet]. Biochemistry. 2018 ; 57( 44): 6293-6307.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.8b00773
Vancouver
Cassago CA de G, Dias MM, Pinheiro MP, Pasquali CC, Bastos ACS, Islam Z, Consonni SR, Oliveira JF de, Gomes EM, Ascenção CFR, Honorato R, Pauletti BA, Indolfo N de C, Ribeiro Filho HV, Oliveira PSL de, Figueira ACM, Leme AFP, Ambrosio ALB, Dias SMG. Glutaminase affects the transcriptional activity of peroxisome proliferator-activated receptor γ (PPARγ) via direct interaction [Internet]. Biochemistry. 2018 ; 57( 44): 6293-6307.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.8b00773
Artigo de periodico
Structural and kinetic insights into the “Ceftazidimase” behavior of the extended-spectrum β‑Lactamase CTX-M-96 (2015)
Ghiglione, Barbara ; Dropa, Milena ; Bouillenne, Fabrice; Rodríguez, María Margarita ; Herman, Raphael ; Curto, Lucrecia ; Kerff, Frédéric ; Galleni, Moreno ; Charlier, Paulette; Gutkind, Gabriel ; Sauvage, Eric ; Power, Pablo
Source: Biochemistry. Unidade: FSP
Subjects: ANTIBIÓTICOS, INFECÇÕES BACTERIANAS GRAM-NEGATIVAS, MEDICAMENTO, RESISTÊNCIA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
GHIGLIONE, Barbara et al. Structural and kinetic insights into the “Ceftazidimase” behavior of the extended-spectrum β‑Lactamase CTX-M-96. Biochemistry, v. 54, n. 32, p. 5072-5082, 2015Tradução . . Disponível em: https://doi.org/10.1021/acs.biochem.5b00313. Acesso em: 27 nov. 2025.
APA
Ghiglione, B., Dropa, M., Bouillenne, F., Rodríguez, M. M., Herman, R., Curto, L., et al. (2015). Structural and kinetic insights into the “Ceftazidimase” behavior of the extended-spectrum β‑Lactamase CTX-M-96. Biochemistry, 54( 32), 5072-5082. doi:10.1021/acs.biochem.5b00313
NLM
Ghiglione B, Dropa M, Bouillenne F, Rodríguez MM, Herman R, Curto L, Kerff F, Galleni M, Charlier P, Gutkind G, Sauvage E, Power P. Structural and kinetic insights into the “Ceftazidimase” behavior of the extended-spectrum β‑Lactamase CTX-M-96 [Internet]. Biochemistry. 2015 ; 54( 32): 5072-5082.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.5b00313
Vancouver
Ghiglione B, Dropa M, Bouillenne F, Rodríguez MM, Herman R, Curto L, Kerff F, Galleni M, Charlier P, Gutkind G, Sauvage E, Power P. Structural and kinetic insights into the “Ceftazidimase” behavior of the extended-spectrum β‑Lactamase CTX-M-96 [Internet]. Biochemistry. 2015 ; 54( 32): 5072-5082.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/acs.biochem.5b00313
Artigo de periodico
Previous Article Next Article Table of Contents Apolipoprotein AI Deficiency Inhibits Serum Opacity Factor Activity against Plasma High Density Lipoprotein via a Stabilization Mechanism (2015)
Rosales, Corina; Patel, Niket; Gillard, Baiba K.; Yelamanchili, Dedipya; Yang, Yaliu; Courtney, Harry S.; Santos, Raul D.; Gotto Jr., Antonio M.; Pownall, Henry J.
Source: Biochemistry. Unidade: FM
Subjects: FATORES DE RISCO, MODELOS ANIMAIS, SORO, LIPOPROTEÍNAS, APOLIPOPROTEÍNAS (DEFICIÊNCIA)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
ROSALES, Corina et al. Previous Article Next Article Table of Contents Apolipoprotein AI Deficiency Inhibits Serum Opacity Factor Activity against Plasma High Density Lipoprotein via a Stabilization Mechanism. Biochemistry, v. 54, n. 14, p. 2295-2302, 2015Tradução . . Disponível em: http://pubs.acs.org/doi/pdf/10.1021/bi501486z. Acesso em: 27 nov. 2025.
APA
Rosales, C., Patel, N., Gillard, B. K., Yelamanchili, D., Yang, Y., Courtney, H. S., et al. (2015). Previous Article Next Article Table of Contents Apolipoprotein AI Deficiency Inhibits Serum Opacity Factor Activity against Plasma High Density Lipoprotein via a Stabilization Mechanism. Biochemistry, 54( 14), 2295-2302. doi:10.1021/bi501486z
NLM
Rosales C, Patel N, Gillard BK, Yelamanchili D, Yang Y, Courtney HS, Santos RD, Gotto Jr. AM, Pownall HJ. Previous Article Next Article Table of Contents Apolipoprotein AI Deficiency Inhibits Serum Opacity Factor Activity against Plasma High Density Lipoprotein via a Stabilization Mechanism [Internet]. Biochemistry. 2015 ; 54( 14): 2295-2302.[citado 2025 nov. 27 ] Available from: http://pubs.acs.org/doi/pdf/10.1021/bi501486z
Vancouver
Rosales C, Patel N, Gillard BK, Yelamanchili D, Yang Y, Courtney HS, Santos RD, Gotto Jr. AM, Pownall HJ. Previous Article Next Article Table of Contents Apolipoprotein AI Deficiency Inhibits Serum Opacity Factor Activity against Plasma High Density Lipoprotein via a Stabilization Mechanism [Internet]. Biochemistry. 2015 ; 54( 14): 2295-2302.[citado 2025 nov. 27 ] Available from: http://pubs.acs.org/doi/pdf/10.1021/bi501486z
Artigo de periodico
Cytochrome c reacts with cholesterol hydroperoxides to produce lipid- and protein-derived radicals (2015)
Mattos, Thiago Cardoso Genaro de; Queiroz, Raphael Ferreira; Cunha, Daniela; Appolinário, Patricia Postilione; Di Mascio, Paolo ; Nantes, Iseli L; Augusto, Ohara ; Miyamoto, Sayuri
Source: Biochemistry. Unidade: IQ
Subjects: LIPÍDEOS, PEROXIDASE
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
MATTOS, Thiago Cardoso Genaro de et al. Cytochrome c reacts with cholesterol hydroperoxides to produce lipid- and protein-derived radicals. Biochemistry, v. 54, n. 18, p. 2841-2850, 2015Tradução . . Disponível em: https://doi.org/10.1021/bi501409d. Acesso em: 27 nov. 2025.
APA
Mattos, T. C. G. de, Queiroz, R. F., Cunha, D., Appolinário, P. P., Di Mascio, P., Nantes, I. L., et al. (2015). Cytochrome c reacts with cholesterol hydroperoxides to produce lipid- and protein-derived radicals. Biochemistry, 54( 18), 2841-2850. doi:10.1021/bi501409d
NLM
Mattos TCG de, Queiroz RF, Cunha D, Appolinário PP, Di Mascio P, Nantes IL, Augusto O, Miyamoto S. Cytochrome c reacts with cholesterol hydroperoxides to produce lipid- and protein-derived radicals [Internet]. Biochemistry. 2015 ; 54( 18): 2841-2850.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi501409d
Vancouver
Mattos TCG de, Queiroz RF, Cunha D, Appolinário PP, Di Mascio P, Nantes IL, Augusto O, Miyamoto S. Cytochrome c reacts with cholesterol hydroperoxides to produce lipid- and protein-derived radicals [Internet]. Biochemistry. 2015 ; 54( 18): 2841-2850.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi501409d
Artigo de periodico
Cd hperfine interactions in DNA bases and DNA of mouse strains infected with trypanosoma cruzi investigated by perturbed angular correlation spectroscopy and ab initio calculations (2014)
Petersen, Philippe Alexandre Divina; Silva, Andreia S.; Lapolli, Andre L.; Carbonari, Artur W.; Goncalves, Marcos B.; Ferreira, Ana Maria da Costa ; Petrilli, Helena Maria
Source: Biochemistry. Unidades: IQ, IF
Subjects: ESPECTROSCOPIA, TRYPANOSOMA CRUZI
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
PETERSEN, Philippe Alexandre Divina et al. Cd hperfine interactions in DNA bases and DNA of mouse strains infected with trypanosoma cruzi investigated by perturbed angular correlation spectroscopy and ab initio calculations. Biochemistry, v. 53, n. ju 2014, p. 3446-3456, 2014Tradução . . Disponível em: https://doi.org/10.1021/bi401680h. Acesso em: 27 nov. 2025.
APA
Petersen, P. A. D., Silva, A. S., Lapolli, A. L., Carbonari, A. W., Goncalves, M. B., Ferreira, A. M. da C., & Petrilli, H. M. (2014). Cd hperfine interactions in DNA bases and DNA of mouse strains infected with trypanosoma cruzi investigated by perturbed angular correlation spectroscopy and ab initio calculations. Biochemistry, 53( ju 2014), 3446-3456. doi:10.1021/bi401680h
NLM
Petersen PAD, Silva AS, Lapolli AL, Carbonari AW, Goncalves MB, Ferreira AM da C, Petrilli HM. Cd hperfine interactions in DNA bases and DNA of mouse strains infected with trypanosoma cruzi investigated by perturbed angular correlation spectroscopy and ab initio calculations [Internet]. Biochemistry. 2014 ; 53( ju 2014): 3446-3456.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi401680h
Vancouver
Petersen PAD, Silva AS, Lapolli AL, Carbonari AW, Goncalves MB, Ferreira AM da C, Petrilli HM. Cd hperfine interactions in DNA bases and DNA of mouse strains infected with trypanosoma cruzi investigated by perturbed angular correlation spectroscopy and ab initio calculations [Internet]. Biochemistry. 2014 ; 53( ju 2014): 3446-3456.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi401680h
Artigo de periodico
Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity (2014)
Araujo, Thaís L. S.; Borges, Julio Cesar ; Ramos, Carlos Henrique Inacio; Meyer-Fernandes, José Roberto; Oliveira Júnior, Reinaldo S; Pascutti, Pedro Geraldo; Foguel, Debora; Palhano, Fernando L
Source: Biochemistry. Unidade: IQSC
Assunto: BIOLOGIA MOLECULAR
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
ARAUJO, Thaís L. S. et al. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry, v. 53, n. 18, p. 2884-2889, 2014Tradução . . Disponível em: https://doi.org/10.1021/bi500004q. Acesso em: 27 nov. 2025.
APA
Araujo, T. L. S., Borges, J. C., Ramos, C. H. I., Meyer-Fernandes, J. R., Oliveira Júnior, R. S., Pascutti, P. G., et al. (2014). Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry, 53( 18), 2884-2889. doi:10.1021/bi500004q
NLM
Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Júnior RS, Pascutti PG, Foguel D, Palhano FL. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity [Internet]. Biochemistry. 2014 ; 53( 18): 2884-2889.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi500004q
Vancouver
Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Júnior RS, Pascutti PG, Foguel D, Palhano FL. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity [Internet]. Biochemistry. 2014 ; 53( 18): 2884-2889.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi500004q
Artigo de periodico
Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ (2014)
Wichelecki, Daniel J.; Froese, D. Sean; Kopec, Jolanta; Muniz, João Renato Carvalho ; Yue, Wyatt W.; Gerlt, John A.
Source: Biochemistry. Unidade: IFSC
Subjects: ENZIMAS, BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
WICHELECKI, Daniel J. et al. Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ. Biochemistry, v. 53, n. 16, p. 2732-2738, 2014Tradução . . Disponível em: https://doi.org/10.1021/bi500349e. Acesso em: 27 nov. 2025.
APA
Wichelecki, D. J., Froese, D. S., Kopec, J., Muniz, J. R. C., Yue, W. W., & Gerlt, J. A. (2014). Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ. Biochemistry, 53( 16), 2732-2738. doi:10.1021/bi500349e
NLM
Wichelecki DJ, Froese DS, Kopec J, Muniz JRC, Yue WW, Gerlt JA. Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ [Internet]. Biochemistry. 2014 ; 53( 16): 2732-2738.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi500349e
Vancouver
Wichelecki DJ, Froese DS, Kopec J, Muniz JRC, Yue WW, Gerlt JA. Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ [Internet]. Biochemistry. 2014 ; 53( 16): 2732-2738.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi500349e
Artigo de periodico
Looking over toxin-K+ channel interactions: clues from the structural and functional characterization of 'alfa'-KTx toxin Tc32, a Kv1.3 channel blocker (2012)
Stehling, Eliana Guedes; Sforça, Maurício L.; Zanchin, Nilson I. T.; Oyama Júnior, Sérgio; Pignatelli, Angela; Belluzzi, Ottorino; Polverini, Eugenia; Corsini, Romina; Spisni, Alberto; Pertinhez, Thelma A.
Source: Biochemistry. Unidade: FCFRP
Subjects: TOXINAS, VENENOS DE ORIGEM ANIMAL (CARACTERÍSTICAS;TOXICIDADE), ESCORPIÕES, ESPECTROMETRIA, RESSONÂNCIA MAGNÉTICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
STEHLING, Eliana Guedes et al. Looking over toxin-K+ channel interactions: clues from the structural and functional characterization of 'alfa'-KTx toxin Tc32, a Kv1.3 channel blocker. Biochemistry, v. 51, n. 9, p. 1885-1894, 2012Tradução . . Disponível em: https://doi.org/10.1021/bi201713z. Acesso em: 27 nov. 2025.
APA
Stehling, E. G., Sforça, M. L., Zanchin, N. I. T., Oyama Júnior, S., Pignatelli, A., Belluzzi, O., et al. (2012). Looking over toxin-K+ channel interactions: clues from the structural and functional characterization of 'alfa'-KTx toxin Tc32, a Kv1.3 channel blocker. Biochemistry, 51( 9), 1885-1894. doi:10.1021/bi201713z
NLM
Stehling EG, Sforça ML, Zanchin NIT, Oyama Júnior S, Pignatelli A, Belluzzi O, Polverini E, Corsini R, Spisni A, Pertinhez TA. Looking over toxin-K+ channel interactions: clues from the structural and functional characterization of 'alfa'-KTx toxin Tc32, a Kv1.3 channel blocker [Internet]. Biochemistry. 2012 ; 51( 9): 1885-1894.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi201713z
Vancouver
Stehling EG, Sforça ML, Zanchin NIT, Oyama Júnior S, Pignatelli A, Belluzzi O, Polverini E, Corsini R, Spisni A, Pertinhez TA. Looking over toxin-K+ channel interactions: clues from the structural and functional characterization of 'alfa'-KTx toxin Tc32, a Kv1.3 channel blocker [Internet]. Biochemistry. 2012 ; 51( 9): 1885-1894.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi201713z
Artigo de periodico
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid (2011)
Azevedo, Estefania P. C.; Pereira, Humberto D'Muniz; Garratt, Richard Charles ; Kelly, Jeffery W.; Foguel, Debora; Palhano, Fernando L.
Source: Biochemistry. Unidade: IFSC
Subjects: PROTEÍNAS (ESTUDO), CRISTALOGRAFIA ESTRUTURAL, MODELOS (ESTRUTURA)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
AZEVEDO, Estefania P. C. et al. Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid. Biochemistry, v. 50, n. 51, p. 11070-11083, 2011Tradução . . Disponível em: https://doi.org/10.1021/bi201365r. Acesso em: 27 nov. 2025.
APA
Azevedo, E. P. C., Pereira, H. D. 'M., Garratt, R. C., Kelly, J. W., Foguel, D., & Palhano, F. L. (2011). Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid. Biochemistry, 50( 51), 11070-11083. doi:10.1021/bi201365r
NLM
Azevedo EPC, Pereira HD'M, Garratt RC, Kelly JW, Foguel D, Palhano FL. Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid [Internet]. Biochemistry. 2011 ; 50( 51): 11070-11083.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi201365r
Vancouver
Azevedo EPC, Pereira HD'M, Garratt RC, Kelly JW, Foguel D, Palhano FL. Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid [Internet]. Biochemistry. 2011 ; 50( 51): 11070-11083.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi201365r
Artigo de periodico
The Crystal structure of necrosis- and ethylene-inducing protein 2 from the causal agent of Caco's Witches' broom disease reveals key elements for its activity (2011)
Zaparoli, Gustavo; Barsottini, Mario Ramos de Oliveira; Oliveira, Juliana Ferreira de; Dyszy, Fabio; Teixeira, Paulo José Pereira Lima; Barau, Joan Grande; Garcia, Odalys; Costa Filho, Antônio José da; Ambrosio, Andre Luis Berteli ; Pereira, Gonçalo Amarante Guimarães; Dias, Sandra Martha Gomes
Source: Biochemistry. Unidade: FFCLRP
Subjects: PROTEÍNAS (ISOLAMENTO E PURIFICAÇÃO), FUNGOS, BASIDIOMYCOTA, GENÉTICA MOLECULAR, GENÉTICA MICROBIANA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
ZAPAROLI, Gustavo et al. The Crystal structure of necrosis- and ethylene-inducing protein 2 from the causal agent of Caco's Witches' broom disease reveals key elements for its activity. Biochemistry, v. 50, n. 45, p. 9901-9910, 2011Tradução . . Disponível em: https://doi.org/10.1021/bi201253b. Acesso em: 27 nov. 2025.
APA
Zaparoli, G., Barsottini, M. R. de O., Oliveira, J. F. de, Dyszy, F., Teixeira, P. J. P. L., Barau, J. G., et al. (2011). The Crystal structure of necrosis- and ethylene-inducing protein 2 from the causal agent of Caco's Witches' broom disease reveals key elements for its activity. Biochemistry, 50( 45), 9901-9910. doi:10.1021/bi201253b
NLM
Zaparoli G, Barsottini MR de O, Oliveira JF de, Dyszy F, Teixeira PJPL, Barau JG, Garcia O, Costa Filho AJ da, Ambrosio ALB, Pereira GAG, Dias SMG. The Crystal structure of necrosis- and ethylene-inducing protein 2 from the causal agent of Caco's Witches' broom disease reveals key elements for its activity [Internet]. Biochemistry. 2011 ; 50( 45): 9901-9910.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi201253b
Vancouver
Zaparoli G, Barsottini MR de O, Oliveira JF de, Dyszy F, Teixeira PJPL, Barau JG, Garcia O, Costa Filho AJ da, Ambrosio ALB, Pereira GAG, Dias SMG. The Crystal structure of necrosis- and ethylene-inducing protein 2 from the causal agent of Caco's Witches' broom disease reveals key elements for its activity [Internet]. Biochemistry. 2011 ; 50( 45): 9901-9910.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi201253b
Artigo de periodico
Structural transitions of translation initiation factor IF2 upon GDPNP and GDP binding in solution (2011)
Rasmussen, Louise Carøe Vohlander; Oliveira, Cristiano Luis Pinto de ; Pedersen, Jan Skov; Sperling-Petersen, Hans Uffe; Mortensen, Kim Kusk
Source: Biochemistry. Unidade: IF
Subjects: BIOQUÍMICA, BIOLOGIA MOLECULAR
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
RASMUSSEN, Louise Carøe Vohlander et al. Structural transitions of translation initiation factor IF2 upon GDPNP and GDP binding in solution. Biochemistry, v. 50, n. 45, p. 9779-9787, 2011Tradução . . Disponível em: https://doi.org/10.1021/bi200938q. Acesso em: 27 nov. 2025.
APA
Rasmussen, L. C. V., Oliveira, C. L. P. de, Pedersen, J. S., Sperling-Petersen, H. U., & Mortensen, K. K. (2011). Structural transitions of translation initiation factor IF2 upon GDPNP and GDP binding in solution. Biochemistry, 50( 45), 9779-9787. doi:10.1021/bi200938q
NLM
Rasmussen LCV, Oliveira CLP de, Pedersen JS, Sperling-Petersen HU, Mortensen KK. Structural transitions of translation initiation factor IF2 upon GDPNP and GDP binding in solution [Internet]. Biochemistry. 2011 ; 50( 45): 9779-9787.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi200938q
Vancouver
Rasmussen LCV, Oliveira CLP de, Pedersen JS, Sperling-Petersen HU, Mortensen KK. Structural transitions of translation initiation factor IF2 upon GDPNP and GDP binding in solution [Internet]. Biochemistry. 2011 ; 50( 45): 9779-9787.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi200938q
Artigo de periodico
Inhibition mechanism of rat 'alpha' IND. 3''beta' IND. 4' nicotinic acetylcholine receptor by the Alzheimer therapeutic tacrine (2011)
Cheffer, Arquimedes; Ulrich, Henning
Source: Biochemistry. Unidade: IQ
Subjects: RECEPTORES DE ACETILCOLINA, NEUROTRANSMISSORES
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
CHEFFER, Arquimedes e ULRICH, Henning. Inhibition mechanism of rat 'alpha' IND. 3''beta' IND. 4' nicotinic acetylcholine receptor by the Alzheimer therapeutic tacrine. Biochemistry, v. 50, n. 11, p. 1763-1770, 2011Tradução . . Disponível em: https://doi.org/10.1021/bi101789y. Acesso em: 27 nov. 2025.
APA
Cheffer, A., & Ulrich, H. (2011). Inhibition mechanism of rat 'alpha' IND. 3''beta' IND. 4' nicotinic acetylcholine receptor by the Alzheimer therapeutic tacrine. Biochemistry, 50( 11), 1763-1770. doi:10.1021/bi101789y
NLM
Cheffer A, Ulrich H. Inhibition mechanism of rat 'alpha' IND. 3''beta' IND. 4' nicotinic acetylcholine receptor by the Alzheimer therapeutic tacrine [Internet]. Biochemistry. 2011 ; 50( 11): 1763-1770.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi101789y
Vancouver
Cheffer A, Ulrich H. Inhibition mechanism of rat 'alpha' IND. 3''beta' IND. 4' nicotinic acetylcholine receptor by the Alzheimer therapeutic tacrine [Internet]. Biochemistry. 2011 ; 50( 11): 1763-1770.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi101789y
Artigo de periodico
Insights into the specificity of thioredoxin reductase−thioredoxin interactions: a structural and functional investigation of the yeast thioredoxin system (2010)
Oliveira, Marcos A; Discola, Karen Fulan; Alves, Simone Vidigal; Medrano, Francisco J; Guimarães, Beatriz G; Netto, Luis Eduardo Soares
Source: Biochemistry. Unidade: IB
Subjects: ENZIMAS OXIRREDUTORAS, PROTEÍNAS
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
OLIVEIRA, Marcos A et al. Insights into the specificity of thioredoxin reductase−thioredoxin interactions: a structural and functional investigation of the yeast thioredoxin system. Biochemistry, v. 49, n. 15, p. 3317-3326, 2010Tradução . . Disponível em: https://doi.org/10.1021/bi901962p. Acesso em: 27 nov. 2025.
APA
Oliveira, M. A., Discola, K. F., Alves, S. V., Medrano, F. J., Guimarães, B. G., & Netto, L. E. S. (2010). Insights into the specificity of thioredoxin reductase−thioredoxin interactions: a structural and functional investigation of the yeast thioredoxin system. Biochemistry, 49( 15), 3317-3326. doi:10.1021/bi901962p
NLM
Oliveira MA, Discola KF, Alves SV, Medrano FJ, Guimarães BG, Netto LES. Insights into the specificity of thioredoxin reductase−thioredoxin interactions: a structural and functional investigation of the yeast thioredoxin system [Internet]. Biochemistry. 2010 ; 49( 15): 3317-3326.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi901962p
Vancouver
Oliveira MA, Discola KF, Alves SV, Medrano FJ, Guimarães BG, Netto LES. Insights into the specificity of thioredoxin reductase−thioredoxin interactions: a structural and functional investigation of the yeast thioredoxin system [Internet]. Biochemistry. 2010 ; 49( 15): 3317-3326.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi901962p
Artigo de periodico
NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection (2010)
Xu, Xianzhong; Xu, Wei; Rayo, Josep; Ishida, Yuko; Leal, Walter Soares; Ames, James B
Source: Biochemistry. Unidade: ESALQ
Subjects: ACASALAMENTO, FEROMÔNIOS SEXUAIS, LAGARTAS, PROTEÍNAS, RESSONÂNCIA MAGNÉTICA NUCLEAR
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
XU, Xianzhong et al. NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection. Biochemistry, v. 49, n. 7, p. 1469-1476, 2010Tradução . . Disponível em: https://doi.org/10.1021/bi9020132. Acesso em: 27 nov. 2025.
APA
Xu, X., Xu, W., Rayo, J., Ishida, Y., Leal, W. S., & Ames, J. B. (2010). NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection. Biochemistry, 49( 7), 1469-1476. doi:10.1021/bi9020132
NLM
Xu X, Xu W, Rayo J, Ishida Y, Leal WS, Ames JB. NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection [Internet]. Biochemistry. 2010 ; 49( 7): 1469-1476.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi9020132
Vancouver
Xu X, Xu W, Rayo J, Ishida Y, Leal WS, Ames JB. NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection [Internet]. Biochemistry. 2010 ; 49( 7): 1469-1476.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi9020132
Artigo de periodico
Recognition by the thyroid hormone receptor of canonical DNA response elements (2010)
Figueira, Ana Carolina Migliorini; Lima, Luís Maurício T. R.; Lima, Leonardo H. F.; Ranzani, Américo T.; Mule, Guilherme dos Santos; Polikarpov, Igor
Source: Biochemistry. Unidade: IFSC
Subjects: HORMÔNIOS TIREOIDIANOS (ESTUDO), RECEPTORES, EXPRESSÃO GÊNICA, LIGANTES, DNA (MANIPULAÇÃO), FLUORESCÊNCIA (APLICAÇÕES)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
FIGUEIRA, Ana Carolina Migliorini et al. Recognition by the thyroid hormone receptor of canonical DNA response elements. Biochemistry, v. 49, n. 5, p. 893-904, 2010Tradução . . Disponível em: https://doi.org/10.1021/bi901282s. Acesso em: 27 nov. 2025.
APA
Figueira, A. C. M., Lima, L. M. T. R., Lima, L. H. F., Ranzani, A. T., Mule, G. dos S., & Polikarpov, I. (2010). Recognition by the thyroid hormone receptor of canonical DNA response elements. Biochemistry, 49( 5), 893-904. doi:10.1021/bi901282s
NLM
Figueira ACM, Lima LMTR, Lima LHF, Ranzani AT, Mule G dos S, Polikarpov I. Recognition by the thyroid hormone receptor of canonical DNA response elements [Internet]. Biochemistry. 2010 ; 49( 5): 893-904.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi901282s
Vancouver
Figueira ACM, Lima LMTR, Lima LHF, Ranzani AT, Mule G dos S, Polikarpov I. Recognition by the thyroid hormone receptor of canonical DNA response elements [Internet]. Biochemistry. 2010 ; 49( 5): 893-904.[citado 2025 nov. 27 ] Available from: https://doi.org/10.1021/bi901282s
Artigo de periodico
pH-sensitive binding of cytochrome C to the inner mitochondrial membrane: implications for the participation of the protein in cell respiration and apoptosis (2009)
Kawai, Cintia; Pessoto, Felipe Samuel; Rodrigues, Tiago; Mugnol, Katia Cristina Ugolini; Tórtora, Veronica; Castro, Laura; Milicchio, Vitor Augusto; Tersariol, Ivarne Luis dos Santos; Di Mascio, Paolo ; Radi, Rafael; Carmona-Ribeiro, Ana Maria ; Nantes, Iseli Lourenço
Source: Biochemistry. Unidade: IQ
Subjects: RESSONÂNCIA MAGNÉTICA NUCLEAR, ESPECTROSCOPIA, BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
KAWAI, Cintia et al. pH-sensitive binding of cytochrome C to the inner mitochondrial membrane: implications for the participation of the protein in cell respiration and apoptosis. Biochemistry, v. 48, n. 35, p. 8335-8342, 2009Tradução . . Disponível em: http://pubs.acs.org/doi/pdfplus/10.1021/bi9006463. Acesso em: 27 nov. 2025.
APA
Kawai, C., Pessoto, F. S., Rodrigues, T., Mugnol, K. C. U., Tórtora, V., Castro, L., et al. (2009). pH-sensitive binding of cytochrome C to the inner mitochondrial membrane: implications for the participation of the protein in cell respiration and apoptosis. Biochemistry, 48( 35), 8335-8342. Recuperado de http://pubs.acs.org/doi/pdfplus/10.1021/bi9006463
NLM
Kawai C, Pessoto FS, Rodrigues T, Mugnol KCU, Tórtora V, Castro L, Milicchio VA, Tersariol IL dos S, Di Mascio P, Radi R, Carmona-Ribeiro AM, Nantes IL. pH-sensitive binding of cytochrome C to the inner mitochondrial membrane: implications for the participation of the protein in cell respiration and apoptosis [Internet]. Biochemistry. 2009 ; 48( 35): 8335-8342.[citado 2025 nov. 27 ] Available from: http://pubs.acs.org/doi/pdfplus/10.1021/bi9006463
Vancouver
Kawai C, Pessoto FS, Rodrigues T, Mugnol KCU, Tórtora V, Castro L, Milicchio VA, Tersariol IL dos S, Di Mascio P, Radi R, Carmona-Ribeiro AM, Nantes IL. pH-sensitive binding of cytochrome C to the inner mitochondrial membrane: implications for the participation of the protein in cell respiration and apoptosis [Internet]. Biochemistry. 2009 ; 48( 35): 8335-8342.[citado 2025 nov. 27 ] Available from: http://pubs.acs.org/doi/pdfplus/10.1021/bi9006463

USP Schools

ReP

Filtros

USP Schools

Departament

Authors

USP affiliated authors

Date published

Subjects

Countries/Territories

Grupo de pesquisa

Funding Agencies

Indexado em

Normalized affiliation

Non normalized affiliation

Countries of institutions of collaboration