20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins (2014)
- Authors:
- USP affiliated authors: OLIVEIRA, CRISTIANO LUIS PINTO DE - IF ; NETTO, LUIS EDUARDO SOARES - IB
- Unidades: IF; IB
- DOI: 10.1016/j.abb.2014.05.002
- Subjects: METABOLISMO DE PROTEÍNA; SACCHAROMYCES; PROTEÍNAS; BIOQUÍMICA CELULAR; LEVEDURAS
- Language: Inglês
- Imprenta:
- Publisher place: Maryland Heights
- Date published: 2014
- Source:
- Título: Archives of Biochemistry and Biophysics
- ISSN: 0003-9861
- Volume/Número/Paginação/Ano: v. online, p. on-line, May 2014
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
DEMASI, Marilene et al. 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins. Archives of Biochemistry and Biophysics, v. online, p. on-line, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.05.002. Acesso em: 13 fev. 2026. -
APA
Demasi, M., Hand, A., Ohara, E., Oliveira, C. L. P. de, Bicev, R. N., Bertoncini, C. A., & Netto, L. E. S. (2014). 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins. Archives of Biochemistry and Biophysics, online, on-line. doi:10.1016/j.abb.2014.05.002 -
NLM
Demasi M, Hand A, Ohara E, Oliveira CLP de, Bicev RN, Bertoncini CA, Netto LES. 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins [Internet]. Archives of Biochemistry and Biophysics. 2014 ; online on-line.[citado 2026 fev. 13 ] Available from: https://doi.org/10.1016/j.abb.2014.05.002 -
Vancouver
Demasi M, Hand A, Ohara E, Oliveira CLP de, Bicev RN, Bertoncini CA, Netto LES. 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins [Internet]. Archives of Biochemistry and Biophysics. 2014 ; online on-line.[citado 2026 fev. 13 ] Available from: https://doi.org/10.1016/j.abb.2014.05.002 - Small-Angle and Wide-Angle Scattering for Investigating Nanostructures
- Redox control of 20S proteasome gating
- Structural and functional investigation of the T44 substitutions effects of the yeast Tsa1 protein
- Mecanismo de defesa antioxidante de bactérias é desvendado. [Depoimento a Karina Toledo]
- Disulfide biochemistry in 2-Cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin
- Yeast 20S proteasome redox forms generate diverse peptide sets from same protein substrates
- Characterization and Kinetic of Reduction of 1-Cys Peroxiredoxin from Aspergillus fumigatus by Ascorbate
- Estudo ajuda a entender funcionamento de enzima antioxidante. [Depoimento a Karina Toledo]
- Studies of Disulfide Reductase Activity and Phylogenetic Distribution of Xylella Fastidiosa YbbN Protein
- Structural characterization of proteins involved in the cellular response to oxidative stress
Informações sobre o DOI: 10.1016/j.abb.2014.05.002 (Fonte: oaDOI API)
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