MS characterization of the human Sod1 covalent dimer produced from the enzyme peroxidase activity: implication to ALS (2009)
- Authors:
- Autor USP: AUGUSTO, OHARA - IQ
- Unidade: IQ
- Subjects: ENZIMAS; PEROXIDASE
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Free Radical Biology & Medicine
- Volume/Número/Paginação/Ano: v. 47, suppl. 1, p. S78 res. 198, 2009
- Conference titles: Annual Meeting of the Society for Free Radical and Medicine
-
ABNT
MEDINAS, Danilo Bilches et al. MS characterization of the human Sod1 covalent dimer produced from the enzyme peroxidase activity: implication to ALS. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. . Acesso em: 25 set. 2024. , 2009 -
APA
Medinas, D. B., Santos, L. F. A., Gozzo, F. C., & Augusto, O. (2009). MS characterization of the human Sod1 covalent dimer produced from the enzyme peroxidase activity: implication to ALS. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. -
NLM
Medinas DB, Santos LFA, Gozzo FC, Augusto O. MS characterization of the human Sod1 covalent dimer produced from the enzyme peroxidase activity: implication to ALS. Free Radical Biology & Medicine. 2009 ; 47 S78 res. 198.[citado 2024 set. 25 ] -
Vancouver
Medinas DB, Santos LFA, Gozzo FC, Augusto O. MS characterization of the human Sod1 covalent dimer produced from the enzyme peroxidase activity: implication to ALS. Free Radical Biology & Medicine. 2009 ; 47 S78 res. 198.[citado 2024 set. 25 ] - Oxidation of the protein disulfide isomerase by peroxynitrite: kinetics, products and biological implications
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