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Refinado por: Base de dados/Biblioteca: HighWire Press (Free Journals) remover Nome da Publicação: Journal Of Biological Chemistry remover
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The Qrc Membrane Complex, Related to the Alternative Complex III, Is a Menaquinone Reductase Involved in Sulfate Respiration
The Qrc Membrane Complex, Related to the Alternative Complex III, Is a Menaquinone Reductase Involved in Sulfate Respiration
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The Qrc Membrane Complex, Related to the Alternative Complex III, Is a Menaquinone Reductase Involved in Sulfate Respiration

Venceslau, Sofia S. ; Lino, Rita R. ; Pereira, Ines A.C.

The Journal of biological chemistry, 2010-07, Vol.285 (30), p.22774-22783 [Periódico revisado por pares]

United States: Elsevier Inc

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2
Exploring the quinone/inhibitor-binding pocket in mitochondrial respiratory complex I by chemical biology approaches
Exploring the quinone/inhibitor-binding pocket in mitochondrial respiratory complex I by chemical biology approaches
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Exploring the quinone/inhibitor-binding pocket in mitochondrial respiratory complex I by chemical biology approaches

Uno, Shinpei ; Kimura, Hironori ; Murai, Masatoshi ; Miyoshi, Hideto

The Journal of biological chemistry, 2019-01, Vol.294 (2), p.679-696 [Periódico revisado por pares]

United States: Elsevier Inc

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3
Transient Kinetic Analysis of Hydrogen Sulfide Oxidation Catalyzed by Human Sulfide Quinone Oxidoreductase
Transient Kinetic Analysis of Hydrogen Sulfide Oxidation Catalyzed by Human Sulfide Quinone Oxidoreductase
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Transient Kinetic Analysis of Hydrogen Sulfide Oxidation Catalyzed by Human Sulfide Quinone Oxidoreductase

Mishanina, Tatiana V. ; Yadav, Pramod K. ; Ballou, David P. ; Banerjee, Ruma

The Journal of biological chemistry, 2015-10, Vol.290 (41), p.25072-25080 [Periódico revisado por pares]

United States: Elsevier Inc

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4
NMR Reveals Double Occupancy of Quinone-type Ligands in the Catalytic Quinone Binding Site of the Na+-translocating NADH:Quinone Oxidoreductase from Vibrio cholerae
NMR Reveals Double Occupancy of Quinone-type Ligands in the Catalytic Quinone Binding Site of the Na+-translocating NADH:Quinone Oxidoreductase from Vibrio cholerae
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NMR Reveals Double Occupancy of Quinone-type Ligands in the Catalytic Quinone Binding Site of the Na+-translocating NADH:Quinone Oxidoreductase from Vibrio cholerae

Nedielkov, Ruslan ; Steffen, Wojtek ; Steuber, Julia ; Möller, Heiko M.

The Journal of biological chemistry, 2013-10, Vol.288 (42), p.30597-30606 [Periódico revisado por pares]

United States: Elsevier Inc

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5
The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis
The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis
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The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis

Vitvitsky, Victor ; Kumar, Roshan ; Libiad, Marouane ; Maebius, Allison ; Landry, Aaron P. ; Banerjee, Ruma

The Journal of biological chemistry, 2021-01, Vol.296, p.100736, Article 100736 [Periódico revisado por pares]

United States: Elsevier Inc

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6
Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway
Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway
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Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway

Libiad, Marouane ; Yadav, Pramod Kumar ; Vitvitsky, Victor ; Martinov, Michael ; Banerjee, Ruma

The Journal of biological chemistry, 2014-11, Vol.289 (45), p.30901-30910 [Periódico revisado por pares]

United States: Elsevier Inc

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7
Steady-state Kinetics and Inhibitory Action of Antitubercular Phenothiazines on Mycobacterium tuberculosis Type-II NADH-Menaquinone Oxidoreductase (NDH-2)
Steady-state Kinetics and Inhibitory Action of Antitubercular Phenothiazines on Mycobacterium tuberculosis Type-II NADH-Menaquinone Oxidoreductase (NDH-2)
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Steady-state Kinetics and Inhibitory Action of Antitubercular Phenothiazines on Mycobacterium tuberculosis Type-II NADH-Menaquinone Oxidoreductase (NDH-2)

Yano, Takahiro ; Li, Lin-Sheng ; Weinstein, Edward ; Teh, Jiah-Shin ; Rubin, Harvey

The Journal of biological chemistry, 2006-04, Vol.281 (17), p.11456-11463 [Periódico revisado por pares]

United States: Elsevier Inc

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8
The anti-inflammatory activity of curcumin is mediated by its oxidative metabolites
The anti-inflammatory activity of curcumin is mediated by its oxidative metabolites
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The anti-inflammatory activity of curcumin is mediated by its oxidative metabolites

Edwards, Rebecca L. ; Luis, Paula B. ; Varuzza, Paolo V. ; Joseph, Akil I. ; Presley, Sai Han ; Chaturvedi, Rupesh ; Schneider, Claus

The Journal of biological chemistry, 2017-12, Vol.292 (52), p.21243-21252 [Periódico revisado por pares]

United States: Elsevier Inc

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9
Aspartic Acid 397 in Subunit B of the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae Forms Part of a Sodium-binding Site, Is Involved in Cation Selectivity, and Affects Cation-binding Site Cooperativity
Aspartic Acid 397 in Subunit B of the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae Forms Part of a Sodium-binding Site, Is Involved in Cation Selectivity, and Affects Cation-binding Site Cooperativity
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Aspartic Acid 397 in Subunit B of the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae Forms Part of a Sodium-binding Site, Is Involved in Cation Selectivity, and Affects Cation-binding Site Cooperativity

Shea, Michael E. ; Juárez, Oscar ; Cho, Jonathan ; Barquera, Blanca

The Journal of biological chemistry, 2013-10, Vol.288 (43), p.31241-31249 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Autoxidative and Cyclooxygenase-2 Catalyzed Transformation of the Dietary Chemopreventive Agent Curcumin
Autoxidative and Cyclooxygenase-2 Catalyzed Transformation of the Dietary Chemopreventive Agent Curcumin
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Autoxidative and Cyclooxygenase-2 Catalyzed Transformation of the Dietary Chemopreventive Agent Curcumin

Griesser, Markus ; Pistis, Valentina ; Suzuki, Takashi ; Tejera, Noemi ; Pratt, Derek A. ; Schneider, Claus

The Journal of biological chemistry, 2011-01, Vol.286 (2), p.1114-1124 [Periódico revisado por pares]

United States: Elsevier Inc

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