Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins (2016)
- Authors:
- USP affiliated authors: LINARES, EDLAINE - IQ ; AUGUSTO, OHARA - IQ
- Unidade: IQ
- DOI: 10.1038/ncomms12979
- Subjects: PROTEÍNAS; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Nature Communications
- ISSN: 2041-1723
- Volume/Número/Paginação/Ano: v. 7, p. 1-10 art. 12979, 2016
- Status:
- Artigo publicado em periódico de acesso aberto (Gold Open Access)
- Versão do Documento:
- Versão publicada (Published version)
- Acessar versão aberta:
-
ABNT
WELLER, Caroline E et al. Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins. Nature Communications, v. 7, p. 1-10 art. 12979, 2016Tradução . . Disponível em: https://doi.org/10.1038/ncomms12979. Acesso em: 01 abr. 2026. -
APA
Weller, C. E., Dhall, A., Ding, F., Linares, E., Whedon, S. D., Senger, N. A., et al. (2016). Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins. Nature Communications, 7, 1-10 art. 12979. doi:10.1038/ncomms12979 -
NLM
Weller CE, Dhall A, Ding F, Linares E, Whedon SD, Senger NA, Tyson EL, Bagert JD, Li X, Augusto O, Chatterjee C. Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins [Internet]. Nature Communications. 2016 ; 7 1-10 art. 12979.[citado 2026 abr. 01 ] Available from: https://doi.org/10.1038/ncomms12979 -
Vancouver
Weller CE, Dhall A, Ding F, Linares E, Whedon SD, Senger NA, Tyson EL, Bagert JD, Li X, Augusto O, Chatterjee C. Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins [Internet]. Nature Communications. 2016 ; 7 1-10 art. 12979.[citado 2026 abr. 01 ] Available from: https://doi.org/10.1038/ncomms12979 - Tempol inhibits macrophage leishmanicidal activity in infected mice
- Maintenance of blood-brain barrier integrity and decreased severity of experimental multiple sclerosis in mice treated with tempol
- Kinetics and mechanism of the reaction of a nitroxide radical (Tempol) with a phenolic antioxidant
- Tempol inhibits macrophage leishmanicidal activity in infected mice
- Argininosuccinate synthetase is a functional target for a snake venom anti-hypertensive peptide: role in arginine and nitric oxide production
- EPR studies of radical production In vivo by lypopolysaccharide. Potential role of iron mobilized from iron-nitrosyl complexes
- Maitenance of blood-brain barrier integrity and decreased severity of experimental multiple sclerosis in tempol-treated mice
- Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging
- Microglial cells activation by human superoxide dismutase (SOD1) and its oxidized forms
- Production of peroxymonocarbonate evidenced by boronate probes under steady-state micromolar H2O2 and in PMA-activated macrophages
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
