Artigo de periodico

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:
  • Demasi, Marilene - Instituto Butantan (IB)
  • Hand, Adrian - Instituto Butantan (IB)
  • Ohara, Erina - Instituto Butantan (IB)
  • Oliveira, Cristiano Luis Pinto de
  • Bicev, Renata N
  • Bertoncini, Clelia A - Universidade Federal de São Paulo (UNIFESP)
  • Netto, Luis Eduardo Soares
• 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 do periódico: Archives of Biochemistry and Biophysics
  • ISSN: 0003-9861
  • Volume/Número/Paginação/Ano: v. online, p. on-line, May 2014

Informações sobre o DOI: 10.1016/j.abb.2014.05.002 (Fonte: oaDOI API)
• Este periódico é de assinatura
• Este artigo NÃO é de acesso aberto
  
• Cor do Acesso Aberto: closed

---

Download do texto completo

Tipo	Nome	Link
	1-s2.0-S0003986114001519-...	Direct link

How to cite

A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas

• 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: 30 abr. 2024.

• 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 2024 abr. 30 ] 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 2024 abr. 30 ] Available from: https://doi.org/10.1016/j.abb.2014.05.002

Últimas obras dos mesmos autores vinculados com a USP cadastradas na BDPI:

• Small-Angle and Wide-Angle Scattering for Investigating Nanostructures
• Modelagem de dados de espalhamento e difração a baixos ângulos
• Investigating protein-surfactants complexes using small angle X-ray scattering
• Structural investigation of Proteasome Complex
• 20S proteasome: structural study using SAXS
• Engineering solid-like structures via an arrested spinodal decomposition
• Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant
• Modular hyperthermostable bacterial endo-'beta'-1,4-mannanase: molecular shape, flexibility and temperature-dependent conformational changes
• Controlling the Surface Functionalization of Ultrasmall Gold Nanoparticles by Sequence-Defined Macromolecules
• Structure and dimerization of translation initiation factor aIF5B in solution