Please use this identifier to cite or link to this item:
https://repositorio.uca.edu.ar/handle/123456789/15390
DC Field | Value | Language |
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dc.contributor.author | Baidanoff, Fernando Martín | es |
dc.contributor.author | Trebucq, Laura Lucía | es |
dc.contributor.author | Plano, Santiago Andrés | es |
dc.contributor.author | Eaton, Phillip | es |
dc.contributor.author | Golombek, Diego A. | es |
dc.contributor.author | Chiesa, Juan José | es |
dc.date.accessioned | 2022-11-03T12:11:52Z | - |
dc.date.available | 2022-11-03T12:11:52Z | - |
dc.date.issued | 2022 | - |
dc.identifier.citation | Baidanoff, F. M. et al. Cysteine oxidation promotes dimerization/oligomerization of circadian protein period [en línea]. Biomolecules. 2022, 12 (7). doi: 10.3390/biom12070892. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/15390 | es |
dc.identifier.issn | 2218-273X (oniline) | - |
dc.identifier.uri | https://repositorio.uca.edu.ar/handle/123456789/15390 | - |
dc.description.abstract | Abstract: The molecular circadian clock is based on a transcriptional/translational feedback loop in which the stability and half-life of circadian proteins is of importance. Cysteine residues of proteins are subject to several redox reactions leading to S-thiolation and disulfide bond formation, altering protein stability and function. In this work, the ability of the circadian protein period 2 (PER2) to undergo oxidation of cysteine thiols was investigated in HEK-293T cells. PER2 includes accessible cysteines susceptible to oxidation by nitroso cysteine (CysNO), altering its stability by decreasing its monomer form and subsequently increasing PER2 homodimers and multimers. These changes were reversed by treatment with 2-mercaptoethanol and partially mimicked by hydrogen peroxide. These results suggest that cysteine oxidation can prompt PER2 homodimer and multimer formation in vitro, likely by S-nitrosation and disulphide bond formation. These kinds of post-translational modifications of PER2 could be part of the redox regulation of the molecular circadian clock. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Multidisciplinary Digital Publishing Institute | es |
dc.rights | Acceso abierto | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.source | Biomolecules Vol.12, No.7, 2022 | es |
dc.subject | REDOX | es |
dc.subject | RELOJ CIRCADIANO | es |
dc.subject | S-NITROSACIÓN | es |
dc.subject | PER2 | es |
dc.title | Cysteine oxidation promotes dimerization/oligomerization of circadian protein period | es |
dc.type | Artículo | es |
dc.identifier.doi | 10.3390/biom12070892 | - |
dc.identifier.pmid | 35883448 | - |
uca.disciplina | MEDICINA | es |
uca.issnrd | 1 | es |
uca.affiliation | Fil: Baidanoff, Fernando Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina | es |
uca.affiliation | Fil: Baidanoff, Fernando Martín. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina | es |
uca.affiliation | Fil: Trebucq, Laura Lucía. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina | es |
uca.affiliation | Fil: Trebucq, Laura Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina | es |
uca.affiliation | Fil: Plano, Santiago Andrés. Pontificia Universidad Católica Argentina. Instituto de Investigaciones Biomédicas; Argentina | es |
uca.affiliation | Fil: Eaton, Phillip. Queen Mary University of London. William Harvey Research Institute; Reino Unido | es |
uca.affiliation | Fil: Golombek, Diego Andrés. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina | es |
uca.affiliation | Fil: Golombek, Diego Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina | es |
uca.affiliation | Fil: Chiesa, Juan José. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina | es |
uca.affiliation | Fil: Chiesa, Juan José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina | es |
uca.version | publishedVersion | es |
item.fulltext | With Fulltext | - |
item.grantfulltext | open | - |
item.languageiso639-1 | en | - |
crisitem.author.dept | Instituto de Investigaciones Biomédicas - BIOMED | - |
crisitem.author.dept | Laboratorio de Cronofisiología | - |
crisitem.author.dept | Consejo Nacional de Investigaciones Científicas y Técnicas | - |
crisitem.author.dept | Facultad de Ciencias Médicas | - |
crisitem.author.orcid | 0000-0002-7984-8826 | - |
crisitem.author.parentorg | Facultad de Ciencias Médicas | - |
crisitem.author.parentorg | Instituto de Investigaciones Biomédicas - BIOMED | - |
crisitem.author.parentorg | Pontificia Universidad Católica Argentina | - |
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cysteine-oxidation-promotes-dimerization.pdf | 671,62 kB | Adobe PDF | View/Open |
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