Deciphering the Path of S-nitrosation of Human Thioredoxin: Evidence of an Internal NO Transfer and Implication for the Cellular Responses to NO

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Federal do Rio de Janeiro (UFRJ)-
Autor(es): dc.contributorRural Federal University of Rio de Janeiro (UFRRJ)-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversity of Lakki Marwat-
Autor(es): dc.creatorAlmeida, Vitor S.-
Autor(es): dc.creatorMiller, Lara L.-
Autor(es): dc.creatorDelia, João P. G.-
Autor(es): dc.creatorMagalhães, Augusto V.-
Autor(es): dc.creatorCaruso, Icaro P.-
Autor(es): dc.creatorIqbal, Anwar-
Autor(es): dc.creatorAlmeida, Fabio C. L.-
Data de aceite: dc.date.accessioned2025-08-21T19:54:08Z-
Data de disponibilização: dc.date.available2025-08-21T19:54:08Z-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2022-07-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/antiox11071236-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/241193-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/241193-
Descrição: dc.descriptionNitric oxide (NO) is a free radical with a signaling capacity. Its cellular functions are achieved mainly through S-nitrosation where thioredoxin (hTrx) is pivotal in the S-transnitrosation to specific cellular targets. In this study, we use NMR spectroscopy and mass spectrometry to follow the mechanism of S-(trans)nitrosation of hTrx. We describe a site-specific path for S-nitrosation by measuring the reactivity of each of the 5 cysteines of hTrx using cysteine mutants. We showed the interdependence of the three cysteines in the nitrosative site. C73 is the most reactive and is responsible for all S-transnitrosation to other cellular targets. We observed NO internal transfers leading to C62 S-nitrosation, which serves as a storage site for NO. C69-SNO only forms under nitrosative stress, leading to hTrx nuclear translocation.-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)-
Descrição: dc.descriptionInstitute of Medical Biochemistry Leopoldo de Meis (IBqM) Federal University of Rio de Janeiro (UFRJ)-
Descrição: dc.descriptionNational Center for Structural Biology and Bioimaging (CENABIO) Federal University of Rio de Janeiro (UFRJ)-
Descrição: dc.descriptionInstitute of Chemistry Rural Federal University of Rio de Janeiro (UFRRJ)-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) Department of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University (UNESP)-
Descrição: dc.descriptionDepartment of Chemical Sciences University of Lakki Marwat-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) Department of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University (UNESP)-
Descrição: dc.descriptionCNPq: 204432-
Descrição: dc.descriptionFAPERJ: 204432-
Descrição: dc.descriptionFAPERJ: 239229-
Idioma: dc.languageen-
Relação: dc.relationAntioxidants-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectmechanism of action-
Palavras-chave: dc.subjectNMR-
Palavras-chave: dc.subjectpost-translational modification-
Palavras-chave: dc.subjectS-nitrosation-
Palavras-chave: dc.subjectthioredoxin-
Título: dc.titleDeciphering the Path of S-nitrosation of Human Thioredoxin: Evidence of an Internal NO Transfer and Implication for the Cellular Responses to NO-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

Não existem arquivos associados a este item.