Searching journal content for Bioenergetics in section.

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  1. Bioenergetics - Methods and Resources:
    • Edward T. Chouchani,
    • Andrew M. James,
    • Carmen Methner,
    • Victoria R. Pell,
    • Tracy A. Prime,
    • Brian K. Erikson,
    • Marleen Forkink,
    • Gigi Y. Lau,
    • Thomas P. Bright,
    • Katja E. Menger,
    • Ian M. Fearnley,
    • Thomas Krieg,
    • and Michael P. Murphy
    Identification and Quantification of Protein S-nitrosation by Nitrite in the Mouse Heart during Ischemia J. Biol. Chem. jbc.M117.798744. doi:10.1074/jbc.M117.798744
  2. Microbiology - Bioenergetics:
    • Laurent Loiseau,
    • Cameron Fyfe,
    • Laurent Aussel,
    • Mahmoud Hajj Chehade,
    • Sara B. Hernández,
    • Bruno Faivre,
    • Djemel Hamdane,
    • Caroline Mellot-Draznieks,
    • Bérengère Rascalou,
    • Ludovic Pelosi,
    • Christophe Velours,
    • David Cornu,
    • Murielle Lombard,
    • Josep Casadesús,
    • Fabien Pierrel,
    • Marc Fontecave,
    • and Frédéric Barras
    The UbiK protein is an accessory factor necessary for bacterial ubiquinone (UQ) biosynthesis and forms a complex with the UQ biogenesis factor UbiJ J. Biol. Chem. 2017 292: 11937-. doi:10.1074/jbc.M117.789164
  3. Bioenergetics:
    • Deserah D. Strand,
    • Nicholas Fisher,
    • and David M. Kramer
    The higher plant plastid NAD(P)H dehydrogenase-like complex (NDH) is a high efficiency proton pump that increases ATP production by cyclic electron flow J. Biol. Chem. 2017 292: 11850-. doi:10.1074/jbc.M116.770792
  4. Metabolism - Bioenergetics:
    • Xiao Guo,
    • Natalie M. Niemi,
    • Joshua J. Coon,
    • and David J. Pagliarini
    Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase J. Biol. Chem. 2017 292: 11751-. doi:10.1074/jbc.M117.787341
  5. Accelerated Communications - Metabolism - Bioenergetics:
    • Melanie R. McReynolds,
    • Wenqing Wang,
    • Lauren M. Holleran,
    • and Wendy Hanna-Rose
    Uridine monophosphate synthetase enables eukaryotic de novo NAD+ biosynthesis from quinolinic acid J. Biol. Chem. 2017 292: 11147-. doi:10.1074/jbc.C117.795344
  6. Bioenergetics - Enzymology:
    • Priya Ragunathan,
    • Hendrik Sielaff,
    • Lavanya Sundararaman,
    • Goran Biuković,
    • Malathy Sony Subramanian Manimekalai,
    • Dhirendra Singh,
    • Subhashri Kundu,
    • Thorsten Wohland,
    • Wayne Frasch,
    • Thomas Dick,
    • and Gerhard Grüber
    The uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation J. Biol. Chem. 2017 292: 11262-. doi:10.1074/jbc.M117.784959
  7. Bioenergetics - Gene Regulation:
    • Rodolfo García-Villegas,
    • Yolanda Camacho-Villasana,
    • Miguel Ángel Shingú-Vázquez,
    • Alfredo Cabrera-Orefice,
    • Salvador Uribe-Carvajal,
    • Thomas D. Fox,
    • and Xochitl Pérez-Martínez
    The Cox1 C-terminal domain is a central regulator of cytochrome c oxidase biogenesis in yeast mitochondria J. Biol. Chem. 2017 292: 10912-. doi:10.1074/jbc.M116.773077
  8. Bioenergetics - Metabolism:
    • Julianna Dias Zeidler,
    • Lorena O. Fernandes-Siqueira,
    • Ana S. Carvalho,
    • Eduardo Cararo-Lopes,
    • Matheus H.S. Dias,
    • Luisa A. Ketzer,
    • Antonio Galina,
    • and Andrea T. Da Poian
    Short-term starvation is a strategy to unravel the cellular capacity of oxidizing specific exogenous/endogenous substrates in mitochondria J. Biol. Chem. jbc.M117.786582. doi:10.1074/jbc.M117.786582
  9. Bioenergetics - Microbiology:
    • Andreia F. Verisssimo,
    • Bahia Khalfaoui-Hassani,
    • Josephine Hwang,
    • Stefan Steimle,
    • Nur Selamoglu,
    • Carsten Sanders,
    • Camilo Khatchikian,
    • and Fevzi Daldal
    The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochrome c maturation J. Biol. Chem. jbc.M117.794586. doi:10.1074/jbc.M117.794586
  10. Bioenergetics - Metabolism:
    • Yiming Wang,
    • Aaron P. Landry,
    • and Huangen Ding
    The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone J. Biol. Chem. 2017 292: 10061-. doi:10.1074/jbc.M117.789800
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