Bothrops Jararaca snake venom modulates key Cancer-related proteins in breast tumor cell lines (2021)
- Authors:
- Autor USP: FERRO, EMER SUAVINHO - ICB
- Unidade: ICB
- DOI: 10.3390/toxins13080519
- Subjects: FARMACOLOGIA; ESPECTROMETRIA DE MASSAS; PROTEÔMICA; CÉLULAS CULTIVADAS DE TUMOR; VENENOS DE ORIGEM ANIMAL; NEOPLASIAS MAMÁRIAS; COBRAS; PROTEÔMICA; CROMATOGRAFIA LÍQUIDA; PROLIFERAÇÃO CELULAR; CÉLULAS MORTAS
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
KISAKI, Carolina Yukiko et al. Bothrops Jararaca snake venom modulates key Cancer-related proteins in breast tumor cell lines. Toxins, v. 13, n. 8, p. 1-28, 2021Tradução . . Disponível em: https://doi.org/10.3390/toxins13080519. Acesso em: 27 jan. 2026. -
APA
Kisaki, C. Y., Arcos, S. S. S., Montoni, F., Santos, W. da S., Calacina, H. M., Lima, I. F., et al. (2021). Bothrops Jararaca snake venom modulates key Cancer-related proteins in breast tumor cell lines. Toxins, 13( 8), 1-28. doi:10.3390/toxins13080519 -
NLM
Kisaki CY, Arcos SSS, Montoni F, Santos W da S, Calacina HM, Lima IF, Carvalho DC, Ferro ES, Nishiyama Junior MY, Iwai LK. Bothrops Jararaca snake venom modulates key Cancer-related proteins in breast tumor cell lines [Internet]. Toxins. 2021 ; 13( 8): 1-28.[citado 2026 jan. 27 ] Available from: https://doi.org/10.3390/toxins13080519 -
Vancouver
Kisaki CY, Arcos SSS, Montoni F, Santos W da S, Calacina HM, Lima IF, Carvalho DC, Ferro ES, Nishiyama Junior MY, Iwai LK. Bothrops Jararaca snake venom modulates key Cancer-related proteins in breast tumor cell lines [Internet]. Toxins. 2021 ; 13( 8): 1-28.[citado 2026 jan. 27 ] Available from: https://doi.org/10.3390/toxins13080519 - Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)
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- The tellurium compound RF-17 is a selective inhibitor of thimet oligopeptidase
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- Acute cocaine treatment increases thimet oligopeptidase in the striatum of rat brain
- The intracellular pharmacokinetics of terminally capped peptides
- Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC3.4.24.16) comparison with thimet oligopeptidase (EC3.4.24.15) and neprilysin (EC3.4.24.11)
- Substrate binding and catalysis of the neuropeptide processing enzyme EC3.4.24.15 (EP24.15) and regulation of the neurome
- Identification of endogenous substrates of thimet oligopeptidase (EC 3.4.24.15) in human embryonic kidney cells
- Site specific determinants of protein oxidative oligomerization
Informações sobre o DOI: 10.3390/toxins13080519 (Fonte: oaDOI API)
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