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1
All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain
All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain
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All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain

Marcelo Cerqueira César John E Wilson

Archives of Biochemistry and Biophysics v. 422, n. 2, p. 191-196, 2004

San Diego 2004

Acesso online. A biblioteca também possui exemplares impressos.

2
Further studies on the coupling of mitochondrially bound hexokinase to intramitochondrially compartmented ATP, generated oxidative phosphorylation
Further studies on the coupling of mitochondrially bound hexokinase to intramitochondrially compartmented ATP, generated oxidative phosphorylation
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Further studies on the coupling of mitochondrially bound hexokinase to intramitochondrially compartmented ATP, generated oxidative phosphorylation

Marcelo Cerqueira César John E Wilson

Archives of Biochemistry and Biophysics New York v. 350, n. 1, feb.1, p. 109-117, 1998

1998

Localização: FZEA - Fac. Zoot. Eng. de Alimentos    (PCD 1998 Fur )(Acessar)

3
All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain
All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain
Material Type:
Artigo 		Adicionar ao Meu Espaço

All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain

Marcelo Cerqueira César John E Wilson

Archives of Biochemistry and Biophysics v. 422, n. 2, p. 191-196, 2004

San Diego 2004

Acesso online. A biblioteca também possui exemplares impressos.

4
Crystal structure of arginase from Leishmania mexicana and implications for the inhibition of polyamine biosynthesis in parasitic infections
Crystal structure of arginase from Leishmania mexicana and implications for the inhibition of polyamine biosynthesis in parasitic infections
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Crystal structure of arginase from Leishmania mexicana and implications for the inhibition of polyamine biosynthesis in parasitic infections

D’Antonio, Edward L. ; Ullman, Buddy ; Roberts, Sigrid C. ; Dixit, Upasna Gaur ; Wilson, Mary E. ; Hai, Yang ; Christianson, David W.

Archives of biochemistry and biophysics, 2013-07, Vol.535 (2), p.163-176 [Periódico revisado por pares]

United States: Elsevier Inc

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5
All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain
All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain
Material Type:
Artigo 		Adicionar ao Meu Espaço

All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain

Cesar, Marcelo de Cerqueira ; Wilson, John E

Archives of biochemistry and biophysics, 2004-02, Vol.422 (2), p.191-196 [Periódico revisado por pares]

United States: Elsevier Inc

Texto completo disponível

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6
Functional Characteristics of Hexokinase Bound to the Type A and Type B Sites of Bovine Brain Mitochondria
Functional Characteristics of Hexokinase Bound to the Type A and Type B Sites of Bovine Brain Mitochondria
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Functional Characteristics of Hexokinase Bound to the Type A and Type B Sites of Bovine Brain Mitochondria

de Cerqueira Cesar, Marcelo ; Wilson, John E.

Archives of biochemistry and biophysics, 2002-01, Vol.397 (1), p.106-112 [Periódico revisado por pares]

United States: Elsevier Inc

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7
Further Studies on the Coupling of Mitochondrially Bound Hexokinase to Intramitochondrially Compartmented ATP, Generated by Oxidative Phosphorylation
Further Studies on the Coupling of Mitochondrially Bound Hexokinase to Intramitochondrially Compartmented ATP, Generated by Oxidative Phosphorylation
Material Type:
Artigo 		Adicionar ao Meu Espaço

Further Studies on the Coupling of Mitochondrially Bound Hexokinase to Intramitochondrially Compartmented ATP, Generated by Oxidative Phosphorylation

de Cerqueira Cesar, Marcelo ; Wilson, John E.

Archives of biochemistry and biophysics, 1998-02, Vol.350 (1), p.109-117 [Periódico revisado por pares]

United States: Elsevier Inc

Texto completo disponível

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8
Membrane Potential-Dependent Conformational Changes in Mitochondrially Bound Hexokinase of Brain
Membrane Potential-Dependent Conformational Changes in Mitochondrially Bound Hexokinase of Brain
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Membrane Potential-Dependent Conformational Changes in Mitochondrially Bound Hexokinase of Brain

Hashimoto, Mitsuru ; Wilson, John E.

Archives of biochemistry and biophysics, 2000-12, Vol.384 (1), p.163-173 [Periódico revisado por pares]

United States: Elsevier Inc

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9
Structural Determinants for the Intracellular Localization of the Isozymes of Mammalian Hexokinase: Intracellular Localization of Fusion Constructs Incorporating Structural Elements from the Hexokinase Isozymes and the Green Fluorescent Protein
Structural Determinants for the Intracellular Localization of the Isozymes of Mammalian Hexokinase: Intracellular Localization of Fusion Constructs Incorporating Structural Elements from the Hexokinase Isozymes and the Green Fluorescent Protein
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Structural Determinants for the Intracellular Localization of the Isozymes of Mammalian Hexokinase: Intracellular Localization of Fusion Constructs Incorporating Structural Elements from the Hexokinase Isozymes and the Green Fluorescent Protein

Sui, Dexin ; Wilson, John E.

Archives of biochemistry and biophysics, 1997-09, Vol.345 (1), p.111-125 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Functional Organization of Mammalian Hexokinases: Both N- and C-Terminal Halves of the Rat Type II Isozyme Possess Catalytic Sites
Functional Organization of Mammalian Hexokinases: Both N- and C-Terminal Halves of the Rat Type II Isozyme Possess Catalytic Sites
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Functional Organization of Mammalian Hexokinases: Both N- and C-Terminal Halves of the Rat Type II Isozyme Possess Catalytic Sites

Tsai, Henry J. ; Wilson, John E.

Archives of biochemistry and biophysics, 1996-05, Vol.329 (1), p.17-23 [Periódico revisado por pares]

United States: Elsevier Inc

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Deste Autor:

  1. Wilson, J
  2. César, M

Neste Assunto:

  1. Biophysics
  2. Biochemistry & Molecular Biology
  3. Life Sciences & Biomedicine
  4. Science & Technology
  5. Animals

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

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