How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily (2015)
- Authors:
- Morais, Mariana A. B - Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)
- Giuseppe, Priscila O - Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)
- Souza, Tatiana Arruda Campos Brasil
- Alegria, Thiago Gerônimo Pires
- Oliveira, Marcos A - Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP)
- Netto, Luis Eduardo Soares

- Murakami, Mário Tyago - Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)
- USP affiliated authors: ALEGRIA, THIAGO GERONIMO PIRES - IB ; NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- DOI: 10.1074/jbc.M114.619205
- Subjects: PEROXIDASE; ESTRESSE OXIDATIVO; LEISHMANIA; BIOQUÍMICA CELULAR; PROTEÍNAS; CRISTALOGRAFIA; BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Source:
- Título: Journal of Biological Chemistry
- ISSN: 0021-9258
- Volume/Número/Paginação/Ano: v. 290, p. 8582-859, March 27, 2015
- Status:
- Artigo aberto em periódico híbrido (Hybrid Open Access)
- Versão do Documento:
- Versão publicada (Published version)
- Acessar versão aberta:
-
ABNT
MORAIS, Mariana A. B et al. How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily. Journal of Biological Chemistry, v. 290, p. 8582-859, 2015Tradução . . Disponível em: https://doi.org/10.1074/jbc.M114.619205. Acesso em: 31 mar. 2026. -
APA
Morais, M. A. B., Giuseppe, P. O., Souza, T. A. C. B., Alegria, T. G. P., Oliveira, M. A., Netto, L. E. S., & Murakami, M. T. (2015). How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily. Journal of Biological Chemistry, 290, 8582-859. doi:10.1074/jbc.M114.619205 -
NLM
Morais MAB, Giuseppe PO, Souza TACB, Alegria TGP, Oliveira MA, Netto LES, Murakami MT. How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily [Internet]. Journal of Biological Chemistry. 2015 ; 290 8582-859.[citado 2026 mar. 31 ] Available from: https://doi.org/10.1074/jbc.M114.619205 -
Vancouver
Morais MAB, Giuseppe PO, Souza TACB, Alegria TGP, Oliveira MA, Netto LES, Murakami MT. How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily [Internet]. Journal of Biological Chemistry. 2015 ; 290 8582-859.[citado 2026 mar. 31 ] Available from: https://doi.org/10.1074/jbc.M114.619205 - Enzymatic Ros-Scavenging System is regulated by calcium in trypanosomatids via tryparedoxin peroxidases
- Investigation on solubilization protocols in the refolding of the thioredoxin TsnC from Xylella fastidiosa by high hydrostatic pressure approach
- Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments
- Impaired antioxidant capacity causes a disruption of metabolic homeostasis in sickle erythrocytes
- A 14.7 KDa Protein from Francisella tularensis subsp. novicida (named FTN_1133) is Involved in the Response to Oxidative Stress Induced by Organic Peroxides but It Is Not Endowed with Thiol Peroxidase Activity
- Caracterização cinética e busca de inibidores de Ohr (Organic Hydroperoxide Resistance protein) de Xylella fastidiosa
- Roles of Ohr (a Cys based peroxidase) and OhrR (a redox regulated transcription factor) from Pseudomonas aeruginosa in a mouse infection model
- Kinetic characterization of the redox regulation of OhrR
- Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: crystallographic and molecular dynamics approaches
- Structural and biochemical comparative analysis among Cys-Based Ohr/OsmC protein family: insights on their high reactivity towards Hydroperoxides
Informações sobre a disponibilidade de versões do artigo em acesso aberto coletadas automaticamente via oaDOI API (Unpaywall).
Por se tratar de integração com serviço externo, podem existir diferentes versões do trabalho (como preprints ou postprints), que podem diferir da versão publicada.
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
