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1
The Oxidation of Selenocysteine Is Involved in the Inactivation of Glutathione Peroxidase by Nitric Oxide Donor
The Oxidation of Selenocysteine Is Involved in the Inactivation of Glutathione Peroxidase by Nitric Oxide Donor
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The Oxidation of Selenocysteine Is Involved in the Inactivation of Glutathione Peroxidase by Nitric Oxide Donor

Asahi, Michio ; Fujii, Junichi ; Takao, Toshifumi ; Kuzuya, Tsunehiko ; Hori, Masatsugu ; Shimonishi, Yasutsugu ; Taniguchi, Naoyuki

The Journal of biological chemistry, 1997-08, Vol.272 (31), p.19152-19157 [Periódico revisado por pares]

United States: Elsevier Inc

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2
Inhibition of Glutathione Reductase by Dinitrosyl-Iron-Dithiolate Complex
Inhibition of Glutathione Reductase by Dinitrosyl-Iron-Dithiolate Complex
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Inhibition of Glutathione Reductase by Dinitrosyl-Iron-Dithiolate Complex

Boese, Matthias ; Keese, Michael A. ; Becker, Katja ; Busse, Rudi ; Mülsch, Alexander

The Journal of biological chemistry, 1997-08, Vol.272 (35), p.21767-21773 [Periódico revisado por pares]

United States: Elsevier Inc

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3
Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite
Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite
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Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite

Marcelo G. Bonini Ohara Augusto

Journal of Biological Chemistry Bethesda v. 276, n. 13, p. 9749-9754, 2001

Bethesda 2001

Item não circula. Consulte sua biblioteca.(Acessar)

4
Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite
Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite
Material Type:
Artigo 		Adicionar ao Meu Espaço

Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite

Marcelo G. Bonini Ohara Augusto

Journal of Biological Chemistry Bethesda v. 276, n. 13, p. 9749-9754, 2001

Bethesda 2001

Item não circula. Consulte sua biblioteca.(Acessar)

5
Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
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Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate

Marcelo Gialluisi Bonini Sayuri Miyamoto; Paolo Di Mascio; Ohara Augusto

Journal of Biological Chemistry Bethesda v. 279, n. 50, p. 51836-51843, 2004

Bethesda 2004

Item não circula. Consulte sua biblioteca.(Acessar)

6
Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
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Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate

Marcelo Gialluisi Bonini Sayuri Miyamoto; Paolo Di Mascio; Ohara Augusto

Journal of Biological Chemistry Bethesda v. 279, n. 50, p. 51836-51843, 2004

Bethesda 2004

Item não circula. Consulte sua biblioteca.(Acessar)

7
Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical
Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical
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Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical

Yeong-Renn Chen Chwen-Lih Chen; Weiguo Chen; Jay L Zweier; Ohara Augusto; Rafael Radi; Ronald P Mason

Journal of Biological Chemistry Bethesda v. 279, n. 17, p. 18054-18062, 2004

Bethesda 2004

Item não circula. Consulte sua biblioteca.(Acessar)

8
Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical
Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical
Material Type:
Artigo 		Adicionar ao Meu Espaço

Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical

Yeong-Renn Chen Chwen-Lih Chen; Weiguo Chen; Jay L Zweier; Ohara Augusto; Rafael Radi; Ronald P Mason

Journal of Biological Chemistry Bethesda v. 279, n. 17, p. 18054-18062, 2004

Bethesda 2004

Item não circula. Consulte sua biblioteca.(Acessar)

9
The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source
The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source
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The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source

Fernando Cruvinel Damasceno André Luís Condeles; Angélica Kodama Bueno Lopes; Romulo Rodrigues Facci; Edlaine Linares; Daniela Ramos Truzzi; Ohara Augusto; José Carlos Toledo Junior

Journal of Biological Chemistry Rockville v. 293, p. 8530-8542 : + Supplementary materials (p. S1-S13), 2018

Rockville 2018

Localização: FFCLRP - Fac. Fil. Ciên. Let. de R. Preto    (pcd 2889070 Estantes Deslizantes )(Acessar)

10
The Effect of Nitric Oxide Release Rates on the Oxidation of Human Low Density Lipoprotein
The Effect of Nitric Oxide Release Rates on the Oxidation of Human Low Density Lipoprotein
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The Effect of Nitric Oxide Release Rates on the Oxidation of Human Low Density Lipoprotein

Goss, Steven P.A. ; Hogg, Neil ; Kalyanaraman, B.

The Journal of biological chemistry, 1997-08, Vol.272 (34), p.21647-21653 [Periódico revisado por pares]

United States: Elsevier Inc

Texto completo disponível

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Deste Autor:

  1. Augusto, O
  2. Bonini, M
  3. Radi, R
  4. Di Mascio, P
  5. Zweier, J

Neste Assunto:

  1. Óxido Nítrico
  2. Superóxido Dismutase
  3. Cell Biology
  4. Biochemistry
  5. Bioquímica

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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