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Artigo de periodico
NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex (2025)
Machado, Luciana Elena de Souza Fraga ; Castellen, Patricia; Blasios, Valdir; Ribeiro Filho, Helder Veras ; Bisson-Filho, Alexandre Wilson ; Pariente, Jhonatan S. Benites; Nogueira, Maria L. C; Sforça, Mauricio Luis ; Honorato, Rodrigo V; Oliveira, Paulo S. Lopes de; Salinas, Roberto Kopke ; Andreu, José M; Zeri, Ana C ; Gueiros Filho, Frederico José
Source: Journal of Biological Chemistry. Unidades: IB, IQ
Subjects: RESSONÂNCIA MAGNÉTICA NUCLEAR, BACTÉRIAS
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MACHADO, Luciana Elena de Souza Fraga et al. NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex. Journal of Biological Chemistry, v. 301, n. 3, p. 1-15 art. 108169, 2025Tradução . . Disponível em: https://dx.doi.org/10.1016/j.jbc.2025.108169. Acesso em: 23 abr. 2026.
APA
Machado, L. E. de S. F., Castellen, P., Blasios, V., Ribeiro Filho, H. V., Bisson-Filho, A. W., Pariente, J. S. B., et al. (2025). NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex. Journal of Biological Chemistry, 301( 3), 1-15 art. 108169. doi:10.1016/j.jbc.2025.108169
NLM
Machado LE de SF, Castellen P, Blasios V, Ribeiro Filho HV, Bisson-Filho AW, Pariente JSB, Nogueira MLC, Sforça ML, Honorato RV, Oliveira PSL de, Salinas RK, Andreu JM, Zeri AC, Gueiros Filho FJ. NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex [Internet]. Journal of Biological Chemistry. 2025 ; 301( 3): 1-15 art. 108169.[citado 2026 abr. 23 ] Available from: https://dx.doi.org/10.1016/j.jbc.2025.108169
Vancouver
Machado LE de SF, Castellen P, Blasios V, Ribeiro Filho HV, Bisson-Filho AW, Pariente JSB, Nogueira MLC, Sforça ML, Honorato RV, Oliveira PSL de, Salinas RK, Andreu JM, Zeri AC, Gueiros Filho FJ. NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex [Internet]. Journal of Biological Chemistry. 2025 ; 301( 3): 1-15 art. 108169.[citado 2026 abr. 23 ] Available from: https://dx.doi.org/10.1016/j.jbc.2025.108169
Artigo de periodico
Profiling Tel1 signaling reveals a non-canonical motif targeting DNA repair and telomere control machineries (2025)
Comstock, William J. ; Bhattarai, Shrijan ; Sanford, Ethan James ; Navarro, Marcos Vicente de Albuquerque Salles ; Smolka, Marcus Bustamante
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: DNA, ESPECTROSCOPIA DE MASSA
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COMSTOCK, William J. et al. Profiling Tel1 signaling reveals a non-canonical motif targeting DNA repair and telomere control machineries. Journal of Biological Chemistry, v. 301, n. 3, p. 108194-1-108194-13 + supporting information, 2025Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2025.108194. Acesso em: 23 abr. 2026.
APA
Comstock, W. J., Bhattarai, S., Sanford, E. J., Navarro, M. V. de A. S., & Smolka, M. B. (2025). Profiling Tel1 signaling reveals a non-canonical motif targeting DNA repair and telomere control machineries. Journal of Biological Chemistry, 301( 3), 108194-1-108194-13 + supporting information. doi:10.1016/j.jbc.2025.108194
NLM
Comstock WJ, Bhattarai S, Sanford EJ, Navarro MV de AS, Smolka MB. Profiling Tel1 signaling reveals a non-canonical motif targeting DNA repair and telomere control machineries [Internet]. Journal of Biological Chemistry. 2025 ; 301( 3): 108194-1-108194-13 + supporting information.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2025.108194
Vancouver
Comstock WJ, Bhattarai S, Sanford EJ, Navarro MV de AS, Smolka MB. Profiling Tel1 signaling reveals a non-canonical motif targeting DNA repair and telomere control machineries [Internet]. Journal of Biological Chemistry. 2025 ; 301( 3): 108194-1-108194-13 + supporting information.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2025.108194
Artigo de periodico
Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2 (2025)
Peskin, Alexander V; Meotti, Flavia Carla ; Magon, Nicholas J; Souza, Luiz F. de; Salvador, Armindo ; Winterbourn, Christine
Source: Journal of Biological Chemistry. Unidade: IQ
Subjects: CINÉTICA, ANTIOXIDANTES
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PESKIN, Alexander V et al. Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2. Journal of Biological Chemistry, v. 301, n. 5, p. 1-15 art. 108503, 2025Tradução . . Disponível em: https://dx.doi.org/10.1016/j.jbc.2025.108503. Acesso em: 23 abr. 2026.
APA
Peskin, A. V., Meotti, F. C., Magon, N. J., Souza, L. F. de, Salvador, A., & Winterbourn, C. (2025). Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2. Journal of Biological Chemistry, 301( 5), 1-15 art. 108503. doi:10.1016/j.jbc.2025.108503
NLM
Peskin AV, Meotti FC, Magon NJ, Souza LF de, Salvador A, Winterbourn C. Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2 [Internet]. Journal of Biological Chemistry. 2025 ; 301( 5): 1-15 art. 108503.[citado 2026 abr. 23 ] Available from: https://dx.doi.org/10.1016/j.jbc.2025.108503
Vancouver
Peskin AV, Meotti FC, Magon NJ, Souza LF de, Salvador A, Winterbourn C. Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2 [Internet]. Journal of Biological Chemistry. 2025 ; 301( 5): 1-15 art. 108503.[citado 2026 abr. 23 ] Available from: https://dx.doi.org/10.1016/j.jbc.2025.108503
Artigo de periodico
AP-1γ2 is an adaptor protein 1 variant required for endosome-to-Golgi trafficking of the mannose-6-P receptor (CI-MPR) and ATP7B copper transporter (2024)
Tavares, Lucas Alves ; Rodrigues, Roger Luiz ; Costa, Cristina Santos da; Nascimento, Jonas Alburqueque ; Carvalho, Julianne Vargas de; Carvalho, Andreia Nogueira de ; Mardones, Gonzalo A.; Silva, Luis Lamberti Pinto da
Source: Journal of Biological Chemistry. Unidade: FMRP
Subjects: HOMEOSTASE, PROTEÍNAS, LISOSSOMOS
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TAVARES, Lucas Alves et al. AP-1γ2 is an adaptor protein 1 variant required for endosome-to-Golgi trafficking of the mannose-6-P receptor (CI-MPR) and ATP7B copper transporter. Journal of Biological Chemistry, v. 300, n. 3, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2024.105700. Acesso em: 23 abr. 2026.
APA
Tavares, L. A., Rodrigues, R. L., Costa, C. S. da, Nascimento, J. A., Carvalho, J. V. de, Carvalho, A. N. de, et al. (2024). AP-1γ2 is an adaptor protein 1 variant required for endosome-to-Golgi trafficking of the mannose-6-P receptor (CI-MPR) and ATP7B copper transporter. Journal of Biological Chemistry, 300( 3). doi:10.1016/j.jbc.2024.105700
NLM
Tavares LA, Rodrigues RL, Costa CS da, Nascimento JA, Carvalho JV de, Carvalho AN de, Mardones GA, Silva LLP da. AP-1γ2 is an adaptor protein 1 variant required for endosome-to-Golgi trafficking of the mannose-6-P receptor (CI-MPR) and ATP7B copper transporter [Internet]. Journal of Biological Chemistry. 2024 ; 300( 3):[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2024.105700
Vancouver
Tavares LA, Rodrigues RL, Costa CS da, Nascimento JA, Carvalho JV de, Carvalho AN de, Mardones GA, Silva LLP da. AP-1γ2 is an adaptor protein 1 variant required for endosome-to-Golgi trafficking of the mannose-6-P receptor (CI-MPR) and ATP7B copper transporter [Internet]. Journal of Biological Chemistry. 2024 ; 300( 3):[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2024.105700
Artigo de periodico
Structure and dynamics of the staphylococcal pyridoxal 5-phosphate synthase complex reveal transient interactions at the enzyme interface (2024)
Barra, Angélica Luana Carrilho ; Ullah, Najeeb; Brognaro, Hévila; Gutierrez, Raissa Ferreira ; Wrenger, Carsten ; Betzel, Christian ; Nascimento, Alessandro Silva
Source: Journal of Biological Chemistry. Unidades: ICB, IFSC
Subjects: CRISTALOGRAFIA, STAPHYLOCOCCUS, ENZIMAS, VITAMINA B6, FOSFATOS, PROTEÍNAS, FÁRMACOS, CRISTALOGRAFIA DE RAIOS X
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BARRA, Angélica Luana Carrilho et al. Structure and dynamics of the staphylococcal pyridoxal 5-phosphate synthase complex reveal transient interactions at the enzyme interface. Journal of Biological Chemistry, v. 300, n. 6, p. 107404-1-107404-12 + supporting information, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2024.107404. Acesso em: 23 abr. 2026.
APA
Barra, A. L. C., Ullah, N., Brognaro, H., Gutierrez, R. F., Wrenger, C., Betzel, C., & Nascimento, A. S. (2024). Structure and dynamics of the staphylococcal pyridoxal 5-phosphate synthase complex reveal transient interactions at the enzyme interface. Journal of Biological Chemistry, 300( 6), 107404-1-107404-12 + supporting information. doi:10.1016/j.jbc.2024.107404
NLM
Barra ALC, Ullah N, Brognaro H, Gutierrez RF, Wrenger C, Betzel C, Nascimento AS. Structure and dynamics of the staphylococcal pyridoxal 5-phosphate synthase complex reveal transient interactions at the enzyme interface [Internet]. Journal of Biological Chemistry. 2024 ; 300( 6): 107404-1-107404-12 + supporting information.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2024.107404
Vancouver
Barra ALC, Ullah N, Brognaro H, Gutierrez RF, Wrenger C, Betzel C, Nascimento AS. Structure and dynamics of the staphylococcal pyridoxal 5-phosphate synthase complex reveal transient interactions at the enzyme interface [Internet]. Journal of Biological Chemistry. 2024 ; 300( 6): 107404-1-107404-12 + supporting information.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2024.107404
Artigo de periodico
Structural and thermodynamic characterization of a highly amyloidogenic dimer of transthyretin involved in a severe cardiomyopathy (2024)
Martins, Lucas do Amaral; Ferreira, Priscila dos Santos; Santos, Otávio Augusto Leitão dos; Martins, Leticia Oliveira; Barroso, Luiz Gabriel Cabral Fernandes; Pereira, Humberto d'Muniz ; Cruz, Márcia Waddington; Palhano, Fernando Lucas; Foguel, Débora
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: PROTEÍNAS, CONFORMAÇÃO PROTEICA, TERMODINÂMICA (FÍSICO-QUÍMICA), MIOCARDIOPATIAS
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MARTINS, Lucas do Amaral et al. Structural and thermodynamic characterization of a highly amyloidogenic dimer of transthyretin involved in a severe cardiomyopathy. Journal of Biological Chemistry, v. 300, n. 8, p. 107495-1-107495-17 + supporting information, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2024.107495. Acesso em: 23 abr. 2026.
APA
Martins, L. do A., Ferreira, P. dos S., Santos, O. A. L. dos, Martins, L. O., Barroso, L. G. C. F., Pereira, H. d'M., et al. (2024). Structural and thermodynamic characterization of a highly amyloidogenic dimer of transthyretin involved in a severe cardiomyopathy. Journal of Biological Chemistry, 300( 8), 107495-1-107495-17 + supporting information. doi:10.1016/j.jbc.2024.107495
NLM
Martins L do A, Ferreira P dos S, Santos OAL dos, Martins LO, Barroso LGCF, Pereira H d'M, Cruz MW, Palhano FL, Foguel D. Structural and thermodynamic characterization of a highly amyloidogenic dimer of transthyretin involved in a severe cardiomyopathy [Internet]. Journal of Biological Chemistry. 2024 ; 300( 8): 107495-1-107495-17 + supporting information.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2024.107495
Vancouver
Martins L do A, Ferreira P dos S, Santos OAL dos, Martins LO, Barroso LGCF, Pereira H d'M, Cruz MW, Palhano FL, Foguel D. Structural and thermodynamic characterization of a highly amyloidogenic dimer of transthyretin involved in a severe cardiomyopathy [Internet]. Journal of Biological Chemistry. 2024 ; 300( 8): 107495-1-107495-17 + supporting information.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2024.107495
Artigo de periodico
In-depth mapping of DNA-PKcs signaling uncovers noncanonical features of its kinase specificity (2024)
Marshall, Shannon; Navarro, Marcos Vicente de Albuquerque Salles ; Ascenҫão, Carolline Fernanda Rodrigues ; Dibitetto, Diego; Smolka, Marcus Bustamante
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: LASER, ESPECTROSCOPIA
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MARSHALL, Shannon et al. In-depth mapping of DNA-PKcs signaling uncovers noncanonical features of its kinase specificity. Journal of Biological Chemistry, v. 300, n. 8, p. 107513-1-107513-11, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2024.107513. Acesso em: 23 abr. 2026.
APA
Marshall, S., Navarro, M. V. de A. S., Ascenҫão, C. F. R., Dibitetto, D., & Smolka, M. B. (2024). In-depth mapping of DNA-PKcs signaling uncovers noncanonical features of its kinase specificity. Journal of Biological Chemistry, 300( 8), 107513-1-107513-11. doi:10.1016/j.jbc.2024.107513
NLM
Marshall S, Navarro MV de AS, Ascenҫão CFR, Dibitetto D, Smolka MB. In-depth mapping of DNA-PKcs signaling uncovers noncanonical features of its kinase specificity [Internet]. Journal of Biological Chemistry. 2024 ; 300( 8): 107513-1-107513-11.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2024.107513
Vancouver
Marshall S, Navarro MV de AS, Ascenҫão CFR, Dibitetto D, Smolka MB. In-depth mapping of DNA-PKcs signaling uncovers noncanonical features of its kinase specificity [Internet]. Journal of Biological Chemistry. 2024 ; 300( 8): 107513-1-107513-11.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2024.107513
Artigo de periodico
Structural basis of nirmatrelvir and ensitrelvir activity against naturally occurring polymorphisms of the SARS-CoV-2 main protease (2023)
Noske, Gabriela Dias; Silva, Ellen de Souza; Godoy, Mariana Ortiz de ; Dolci, Isabela ; Fernandes, Rafaela Sachetto ; Guido, Rafael Victorio Carvalho ; Sjo, Peter ; Oliva, Glaucius ; Godoy, Andre Schutzer de
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: COVID-19, CORONAVIRUS, RESISTÊNCIA MICROBIANA ÀS DROGAS, MUTAÇÃO GENÉTICA, RAIOS X, ANTIVIRAIS
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NOSKE, Gabriela Dias et al. Structural basis of nirmatrelvir and ensitrelvir activity against naturally occurring polymorphisms of the SARS-CoV-2 main protease. Journal of Biological Chemistry, v. 299, n. 3, p. 103004-1-103004-10 + supporting information: 1-3, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2023.103004. Acesso em: 23 abr. 2026.
APA
Noske, G. D., Silva, E. de S., Godoy, M. O. de, Dolci, I., Fernandes, R. S., Guido, R. V. C., et al. (2023). Structural basis of nirmatrelvir and ensitrelvir activity against naturally occurring polymorphisms of the SARS-CoV-2 main protease. Journal of Biological Chemistry, 299( 3), 103004-1-103004-10 + supporting information: 1-3. doi:10.1016/j.jbc.2023.103004
NLM
Noske GD, Silva E de S, Godoy MO de, Dolci I, Fernandes RS, Guido RVC, Sjo P, Oliva G, Godoy AS de. Structural basis of nirmatrelvir and ensitrelvir activity against naturally occurring polymorphisms of the SARS-CoV-2 main protease [Internet]. Journal of Biological Chemistry. 2023 ; 299( 3): 103004-1-103004-10 + supporting information: 1-3.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2023.103004
Vancouver
Noske GD, Silva E de S, Godoy MO de, Dolci I, Fernandes RS, Guido RVC, Sjo P, Oliva G, Godoy AS de. Structural basis of nirmatrelvir and ensitrelvir activity against naturally occurring polymorphisms of the SARS-CoV-2 main protease [Internet]. Journal of Biological Chemistry. 2023 ; 299( 3): 103004-1-103004-10 + supporting information: 1-3.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2023.103004
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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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: 23 abr. 2026.
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 2026 abr. 23 ] 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 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2023.102904
Artigo de periodico
UHMK1 is a novel splicing regulatory kinase (2023)
Arfelli, Vanessa Cristina; Chang, Yun-Chien; Bagnoli, Johannes W.; Kerbs, Paul; Ciamponi, Felipe E.; Paz, Laissa Mayara da Silva; Pankivskyi, Serhii; Salone, Jean de Matha; Maucuer, Alexandre; Massirer, Katlin B.; Enard, Wolfgang; Kuster, Bernhard; Greif, Philipp A.; Archangelo, Leticia Fröhlich
Source: Journal of Biological Chemistry. Unidade: FMRP
Subjects: PROTEÍNAS QUINASES, RNA, FATORES DE TRANSCRIÇÃO
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ARFELLI, Vanessa Cristina et al. UHMK1 is a novel splicing regulatory kinase. Journal of Biological Chemistry, v. 299, n. 4, p. 1-22, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2023.103041. Acesso em: 23 abr. 2026.
APA
Arfelli, V. C., Chang, Y. -C., Bagnoli, J. W., Kerbs, P., Ciamponi, F. E., Paz, L. M. da S., et al. (2023). UHMK1 is a novel splicing regulatory kinase. Journal of Biological Chemistry, 299( 4), 1-22. doi:10.1016/j.jbc.2023.103041
NLM
Arfelli VC, Chang Y-C, Bagnoli JW, Kerbs P, Ciamponi FE, Paz LM da S, Pankivskyi S, Salone J de M, Maucuer A, Massirer KB, Enard W, Kuster B, Greif PA, Archangelo LF. UHMK1 is a novel splicing regulatory kinase [Internet]. Journal of Biological Chemistry. 2023 ; 299( 4): 1-22.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2023.103041
Vancouver
Arfelli VC, Chang Y-C, Bagnoli JW, Kerbs P, Ciamponi FE, Paz LM da S, Pankivskyi S, Salone J de M, Maucuer A, Massirer KB, Enard W, Kuster B, Greif PA, Archangelo LF. UHMK1 is a novel splicing regulatory kinase [Internet]. Journal of Biological Chemistry. 2023 ; 299( 4): 1-22.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2023.103041
Artigo de periodico
AMPKα1 negatively regulates osteoclastogenesis and mitigates pathological bone loss (2023)
Ribeiro, Mariana Soares Pena; Venturini, Lucas Gabriel Rodrigues; Hernandez, Cesar Augusto Speck; Alabarse, Paulo Vinicius ; Xavier, Thaís Aparecida; Taira, Thaise Mayumi ; Duffles, Leticia Fernanda ; Cunha, Fernando de Queiroz ; Fukada, Sandra Yasuyo
Source: Journal of Biological Chemistry. Unidades: FMRP, FCFRP
Subjects: OSTEOCLASTO, OSTEOPOROSE, OSTEOGÊNESE, DIFERENCIAÇÃO CELULAR
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ABNT
RIBEIRO, Mariana Soares Pena et al. AMPKα1 negatively regulates osteoclastogenesis and mitigates pathological bone loss. Journal of Biological Chemistry, v. 299, n. 12, p. 1-8, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2023.105379. Acesso em: 23 abr. 2026.
APA
Ribeiro, M. S. P., Venturini, L. G. R., Hernandez, C. A. S., Alabarse, P. V., Xavier, T. A., Taira, T. M., et al. (2023). AMPKα1 negatively regulates osteoclastogenesis and mitigates pathological bone loss. Journal of Biological Chemistry, 299( 12), 1-8. doi:10.1016/j.jbc.2023.105379
NLM
Ribeiro MSP, Venturini LGR, Hernandez CAS, Alabarse PV, Xavier TA, Taira TM, Duffles LF, Cunha F de Q, Fukada SY. AMPKα1 negatively regulates osteoclastogenesis and mitigates pathological bone loss [Internet]. Journal of Biological Chemistry. 2023 ; 299( 12): 1-8.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2023.105379
Vancouver
Ribeiro MSP, Venturini LGR, Hernandez CAS, Alabarse PV, Xavier TA, Taira TM, Duffles LF, Cunha F de Q, Fukada SY. AMPKα1 negatively regulates osteoclastogenesis and mitigates pathological bone loss [Internet]. Journal of Biological Chemistry. 2023 ; 299( 12): 1-8.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2023.105379
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: 23 abr. 2026.
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 2026 abr. 23 ] 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 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2022.102655
Artigo de periodico
Clathrin adaptor AP-1–mediated Golgi export of amyloid precursor protein is crucial for the production of neurotoxic amyloid fragments (2022)
Januário, Yunan Costa; Eden, Jessica; Oliveira, Luan S. de; De Pace, Raffaella; Tavares, Lucas A.; Silva-Januário, Mara E. da; Apolloni, Vinícius B.; Wilby, Elise L.; Altmeyer, Randolf; Burgos, Patricia V.; Corrêa, Sonia A. L.; Gershlick, David C.; Silva, Luis Lamberti Pinto da
Source: Journal of Biological Chemistry. Unidade: FMRP
Subjects: DOENÇA DE ALZHEIMER, PROTEÍNAS, PEPTÍDEOS, AMILOIDOSE, COMPLEXO DE GOLGI, FATOR DE TRANSCRIÇÃO AP-1
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ABNT
JANUÁRIO, Yunan Costa et al. Clathrin adaptor AP-1–mediated Golgi export of amyloid precursor protein is crucial for the production of neurotoxic amyloid fragments. Journal of Biological Chemistry, v. 298, n. 8, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2022.102172. Acesso em: 23 abr. 2026.
APA
Januário, Y. C., Eden, J., Oliveira, L. S. de, De Pace, R., Tavares, L. A., Silva-Januário, M. E. da, et al. (2022). Clathrin adaptor AP-1–mediated Golgi export of amyloid precursor protein is crucial for the production of neurotoxic amyloid fragments. Journal of Biological Chemistry, 298( 8). doi:10.1016/j.jbc.2022.102172
NLM
Januário YC, Eden J, Oliveira LS de, De Pace R, Tavares LA, Silva-Januário ME da, Apolloni VB, Wilby EL, Altmeyer R, Burgos PV, Corrêa SAL, Gershlick DC, Silva LLP da. Clathrin adaptor AP-1–mediated Golgi export of amyloid precursor protein is crucial for the production of neurotoxic amyloid fragments [Internet]. Journal of Biological Chemistry. 2022 ; 298( 8):[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2022.102172
Vancouver
Januário YC, Eden J, Oliveira LS de, De Pace R, Tavares LA, Silva-Januário ME da, Apolloni VB, Wilby EL, Altmeyer R, Burgos PV, Corrêa SAL, Gershlick DC, Silva LLP da. Clathrin adaptor AP-1–mediated Golgi export of amyloid precursor protein is crucial for the production of neurotoxic amyloid fragments [Internet]. Journal of Biological Chemistry. 2022 ; 298( 8):[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2022.102172
Artigo de periodico
Fluorescent sensors of siderophores produced by bacterial pathogens (2022)
Kumar, Ashish; Yang, Taihao ; Chakravorty, Somnath ; Majumdar, Aritri; Nairn, Brittany L.; Six, David A. ; Santos, Naara Marcondes dos ; Price, Sarah L. ; Lawrenz, Matthew B. ; Actis, Luis A. ; Marques, Marilis do Valle ; Russo, Thomas A. ; Newton, Salete M. ; Klebba, Phillip E.
Source: Journal of Biological Chemistry. Unidade: ICB
Subjects: MICROBIOLOGIA, COMPOSTOS ORGÂNICOS, BACTÉRIAS FIXADORAS DE NITROGÊNIO, CORANTES FLUORESCENTES, ESCHERICHIA COLI, BACTÉRIAS GRAM-NEGATIVAS, PROTEÍNAS DA MEMBRANA, FERRO, BACILOS GRAM-NEGATIVOS FACULTATIVAMENTE ANAERÓBICOS, MUTAGÊNESE, MOLÉCULA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
KUMAR, Ashish et al. Fluorescent sensors of siderophores produced by bacterial pathogens. Journal of Biological Chemistry, v. 298, n. 3, p. 1-16, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2022.101651. Acesso em: 23 abr. 2026.
APA
Kumar, A., Yang, T., Chakravorty, S., Majumdar, A., Nairn, B. L., Six, D. A., et al. (2022). Fluorescent sensors of siderophores produced by bacterial pathogens. Journal of Biological Chemistry, 298( 3), 1-16. doi:10.1016/j.jbc.2022.101651
NLM
Kumar A, Yang T, Chakravorty S, Majumdar A, Nairn BL, Six DA, Santos NM dos, Price SL, Lawrenz MB, Actis LA, Marques M do V, Russo TA, Newton SM, Klebba PE. Fluorescent sensors of siderophores produced by bacterial pathogens [Internet]. Journal of Biological Chemistry. 2022 ; 298( 3): 1-16.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2022.101651
Vancouver
Kumar A, Yang T, Chakravorty S, Majumdar A, Nairn BL, Six DA, Santos NM dos, Price SL, Lawrenz MB, Actis LA, Marques M do V, Russo TA, Newton SM, Klebba PE. Fluorescent sensors of siderophores produced by bacterial pathogens [Internet]. Journal of Biological Chemistry. 2022 ; 298( 3): 1-16.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2022.101651
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: 23 abr. 2026.
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 2026 abr. 23 ] 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 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2021.100494
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: 23 abr. 2026.
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 2026 abr. 23 ] 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 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2021.101041
Artigo de periodico-carta/editorial
Can NAD(P)+ transhydrogenase (NNT) mediate a physiologically meaningful increase in energy expenditure by mitochondria during H2O2 removal? [Carta] (2021)
Figueira, Tiago Rezende ; Francisco, Annelise; Treberg, Jason R.; Castilho, Roger Frigério
Source: Journal of Biological Chemistry. Unidade: EEFERP
Subjects: METABOLISMO ENERGÉTICO, PERÓXIDO DE HIDROGÊNIO, MITOCÔNDRIAS, MÚSCULO ESQUELÉTICO
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ABNT
FIGUEIRA, Tiago Rezende et al. Can NAD(P)+ transhydrogenase (NNT) mediate a physiologically meaningful increase in energy expenditure by mitochondria during H2O2 removal? [Carta]. Journal of Biological Chemistry. Bethesda: Escola de Educação Física e Esporte de Ribeirão Preto, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.jbc.2021.100377. Acesso em: 23 abr. 2026. , 2021
APA
Figueira, T. R., Francisco, A., Treberg, J. R., & Castilho, R. F. (2021). Can NAD(P)+ transhydrogenase (NNT) mediate a physiologically meaningful increase in energy expenditure by mitochondria during H2O2 removal? [Carta]. Journal of Biological Chemistry. Bethesda: Escola de Educação Física e Esporte de Ribeirão Preto, Universidade de São Paulo. doi:10.1016/j.jbc.2021.100377
NLM
Figueira TR, Francisco A, Treberg JR, Castilho RF. Can NAD(P)+ transhydrogenase (NNT) mediate a physiologically meaningful increase in energy expenditure by mitochondria during H2O2 removal? [Carta] [Internet]. Journal of Biological Chemistry. 2021 ; 296[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2021.100377
Vancouver
Figueira TR, Francisco A, Treberg JR, Castilho RF. Can NAD(P)+ transhydrogenase (NNT) mediate a physiologically meaningful increase in energy expenditure by mitochondria during H2O2 removal? [Carta] [Internet]. Journal of Biological Chemistry. 2021 ; 296[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2021.100377
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 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: 23 abr. 2026.
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 2026 abr. 23 ] 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 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2021.100344
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 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, v. 296, n. ja-ju 2021, p. 100385-1-100385-13 + supporting information: S1-S15, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2021.100385. Acesso em: 23 abr. 2026.
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( ja-ju 2021), 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 [Internet]. Journal of Biological Chemistry. 2021 ; 296( ja-ju 2021): 100385-1-100385-13 + supporting information: S1-S15.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2021.100385
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 [Internet]. Journal of Biological Chemistry. 2021 ; 296( ja-ju 2021): 100385-1-100385-13 + supporting information: S1-S15.[citado 2026 abr. 23 ] Available from: https://doi.org/10.1016/j.jbc.2021.100385
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: 23 abr. 2026.
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 2026 abr. 23 ] 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 2026 abr. 23 ] Available from: https://doi.org/10.1074/jbc.RA120.013589

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