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1
Uncoupling protein-3 is a mediator of thermogenesis regulated by thyroid hormone, beta 3-adrenergic agonists, and leptin
Uncoupling protein-3 is a mediator of thermogenesis regulated by thyroid hormone, beta 3-adrenergic agonists, and leptin
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Uncoupling protein-3 is a mediator of thermogenesis regulated by thyroid hormone, beta 3-adrenergic agonists, and leptin

Gong, D.W. (NIH, Bethesda, MD.) ; He, Y ; Karas, M ; Reitman, M

The Journal of biological chemistry, 1997-09, Vol.272 (39), p.24129-24132 [Periódico revisado por pares]

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2
Obesity induces expression of uncoupling protein-2 in hepatocytes and promotes liver ATP depletion
Obesity induces expression of uncoupling protein-2 in hepatocytes and promotes liver ATP depletion
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Obesity induces expression of uncoupling protein-2 in hepatocytes and promotes liver ATP depletion

Chavin, K.D. (John Hopkins University, Baltimore, MD.) ; Yang, S ; Lin, H.Z ; Chatham, J ; Chacko, V.P ; Hoek, J.B ; Walajtys-Rode, E ; Rashid, A ; Chen, C.H ; Huang, C.C

The Journal of biological chemistry, 1999-02, Vol.274 (9), p.5692-5700 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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3
Fzo1p Is a Mitochondrial Outer Membrane Protein Essential for the Biogenesis of Functional Mitochondria in Saccharomyces cerevisiae
Fzo1p Is a Mitochondrial Outer Membrane Protein Essential for the Biogenesis of Functional Mitochondria in Saccharomyces cerevisiae
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Fzo1p Is a Mitochondrial Outer Membrane Protein Essential for the Biogenesis of Functional Mitochondria in Saccharomyces cerevisiae

Rapaport, Doron ; Brunner, Michael ; Neupert, Walter ; Westermann, Benedikt

The Journal of biological chemistry, 1998-08, Vol.273 (32), p.20150-20155 [Periódico revisado por pares]

United States: Elsevier Inc

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4
Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo
Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo
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Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo

Longo, V.D. (University of California, Los Angeles.) ; Gralla, E.B ; Valentine, J.S

The Journal of biological chemistry, 1996-05, Vol.271 (21), p.12275-12280 [Periódico revisado por pares]

United States

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5
Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
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Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)

Okun, J.G. (Universitatsklinikum Frankfurt, Germany.) ; Lummen, P ; Brandt, U

The Journal of biological chemistry, 1999-01, Vol.274 (5), p.2625-2630 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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6
Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria
Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria
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Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria

Zhang, L. (Oklahoma State University, Stillwater, OK.) ; Yu, L ; Yu, C.A

The Journal of biological chemistry, 1998-12, Vol.273 (51), p.33972 [Periódico revisado por pares]

United States

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7
Disruption of cholesterol 7 alpha-hydroxylase gene in mice. II. Bile acid deficiency is overcome by induction of oxysterol 7 alpha-hydroxylase
Disruption of cholesterol 7 alpha-hydroxylase gene in mice. II. Bile acid deficiency is overcome by induction of oxysterol 7 alpha-hydroxylase
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Disruption of cholesterol 7 alpha-hydroxylase gene in mice. II. Bile acid deficiency is overcome by induction of oxysterol 7 alpha-hydroxylase

Schwarz, M. (University of Texas Southwestern Medical Center, Dallas, TX.) ; Lund, E.G ; Setchell, K.D.R ; Kayden, H.J ; Zerwekh, J.E ; Bjorkhem, I ; Herz, J ; Russell, D.W

The Journal of biological chemistry, 1996, Vol.271 (30), p.18024-18031 [Periódico revisado por pares]

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8
Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70
Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70
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Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70

Brix, Jan ; Dietmeier, Klaus ; Pfanner, Nikolaus

The Journal of biological chemistry, 1997-08, Vol.272 (33), p.20730-20735 [Periódico revisado por pares]

United States: Elsevier Inc

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9
Identification of a mitochondrial Na+/H+ exchanger
Identification of a mitochondrial Na+/H+ exchanger
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Identification of a mitochondrial Na+/H+ exchanger

Numata, M ; Petrecca, K ; Lake, N ; Orlowski, J

The Journal of biological chemistry, 1998-03, Vol.273 (12), p.6951-6959 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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10
An EPR Investigation of the Products of the Reaction of Cytosolic and Mitochondrial Aconitases with Nitric Oxide
An EPR Investigation of the Products of the Reaction of Cytosolic and Mitochondrial Aconitases with Nitric Oxide
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An EPR Investigation of the Products of the Reaction of Cytosolic and Mitochondrial Aconitases with Nitric Oxide

Kennedy, M. Claire ; Antholine, William E. ; Beinert, Helmut

The Journal of biological chemistry, 1997-08, Vol.272 (33), p.20340-20347 [Periódico revisado por pares]

United States: Elsevier Inc

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