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ATP synthase K + - and H + -flux drive ATP synthesis and enable mitochondrial K + -uniporter function

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/embj.201386392openalex-snapshot

In vivo inhibition of the mitochondrial H+‐ATP synthase in neurons promotes metabolic preconditioning

inferredcites →https://doi.org/10.1006/bbrc.1994.2282openalex-snapshot

Potassium Selective and Venturicidin Sensitive Conductances of Fo Purified from Bovine Heart Mitochondria, Reconstituted in Planar Lipid Bilayers

inferredcites →https://doi.org/10.1006/jmbi.1995.0586openalex-snapshot

A Double Mutation in Subunit c of the Na+-specific F1F0-ATPase ofPropionigenium modestumResults in a Switch from Na+to H+-coupled ATP Synthesis in theEscherichia coliHost Cells

inferredcites →https://doi.org/10.1007/s00335-012-9422-2openalex-snapshot

The mammalian gene function resource: the international knockout mouse consortium

inferredcites →https://doi.org/10.1007/springerreference_33998openalex-snapshot

Ion Channels/Excitable Membranes

inferredcites →https://doi.org/10.1016/0014-5793(91)81447-gopenalex-snapshot

The rate of ATP‐synthesis as a function of ΔpH and Δψ catalyzed by the active, reduced H+‐ATPase from chloroplasts

inferredcites →https://doi.org/10.1016/0146-2806(94)90008-6openalex-snapshot

Energy metabolism of the heart: From basic concepts to clinical applications applications

inferredcites →https://doi.org/10.1016/0959-440x(94)90274-7openalex-snapshot

The regulation of catalysis in ATP synthase

inferredcites →https://doi.org/10.1016/j.bbabio.2004.01.003openalex-snapshot

The human mitochondrial KATP channel is modulated by calcium and nitric oxide: a patch-clamp approach

inferredcites →https://doi.org/10.1016/j.bbabio.2006.05.006openalex-snapshot

Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation

inferredcites →https://doi.org/10.1016/j.bbabio.2009.08.002openalex-snapshot

Energetic performance is improved by specific activation of K+ fluxes through KCa channels in heart mitochondria

inferredcites →https://doi.org/10.1016/j.bcp.2004.02.001openalex-snapshot

Diazoxide affects the IF1 inhibitor protein binding to F1 sector of beef heart F0F1ATPsynthase

inferredcites →https://doi.org/10.1016/j.bpj.2011.05.027openalex-snapshot

Mitochondrial Energetics, pH Regulation, and Ion Dynamics: A Computational-Experimental Approach

inferredcites →https://doi.org/10.1016/j.cmet.2008.06.001openalex-snapshot

Regulation of Mitochondrial Structure and Function by the F1Fo-ATPase Inhibitor Protein, IF1

inferredcites →https://doi.org/10.1016/j.febslet.2004.08.065openalex-snapshot

The evolution of A‐, F‐, and V‐type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio

inferredcites →https://doi.org/10.1016/j.febslet.2005.01.077openalex-snapshot

Matrix Mg2+ regulates mitochondrial ATP‐dependent potassium channel from heart

inferredcites →https://doi.org/10.1016/j.gene.2004.02.017openalex-snapshot

Comparative genomics: the evolutionary history of the Bcl-2 family

inferredcites →https://doi.org/10.1016/j.jmb.2005.11.032openalex-snapshot

BCL-XL Dimerization by Three-dimensional Domain Swapping

inferredcites →https://doi.org/10.1016/j.molcel.2012.01.008openalex-snapshot

The Mitochondrial ATPase Inhibitory Factor 1 Triggers a ROS-Mediated Retrograde Prosurvival and Proliferative Response

inferredcites →https://doi.org/10.1016/j.tcb.2012.10.010openalex-snapshot

Evolution of Bcl-2 homology motifs: homology versus homoplasy

inferredcites →https://doi.org/10.1016/j.tibs.2015.10.006openalex-snapshot

Rotary ATPases: A New Twist to an Ancient Machine

inferredcites →https://doi.org/10.1016/s0005-2728(03)00109-9openalex-snapshot

Mitochondrial potassium transport: the role of the mitochondrial ATP-sensitive K+ channel in cardiac function and cardioprotection

inferredcites →https://doi.org/10.1016/s0005-2728(89)80378-0openalex-snapshot

The regulation of the matrix volume of mammalian mitochondria in vivo and in vitro and its role in the control of mitochondrial metabolism

inferredcites →https://doi.org/10.1016/s0005-2728(98)00179-0openalex-snapshot

Regulation of mitochondrial KATP channel by redox agents

inferredcites →https://doi.org/10.1016/s0006-3495(03)75079-6openalex-snapshot

An Integrated Model of Cardiac Mitochondrial Energy Metabolism and Calcium Dynamics

inferredcites →https://doi.org/10.1016/s0006-3495(99)77214-0openalex-snapshot

Measurement of Mitochondrial Membrane Potential Using Fluorescent Rhodamine Derivatives

inferredcites →https://doi.org/10.1016/s0021-9258(18)35717-xopenalex-snapshot

Reconstitution and partial purification of the glibenclamide-sensitive, ATP-dependent K+ channel from rat liver and beef heart mitochondria.

inferredcites →https://doi.org/10.1016/s0021-9258(18)82363-8openalex-snapshot

Specific protection by Na+ or Li+ of the F1F0-ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide

inferredcites →https://doi.org/10.1021/bi960628fopenalex-snapshot

The ATPase Inhibitor Protein from Bovine Heart Mitochondria: The Minimal Inhibitory Sequence

inferredcites →https://doi.org/10.1021/bi970831qopenalex-snapshot

Molecular Basis for the Coupling Ion Selectivity of F1F0 ATP Synthases: Probing the Liganding Groups for Na+ and Li+ in the c Subunit of the ATP Synthase from Propionigenium modestum

inferredcites →https://doi.org/10.1023/a:1005408029549openalex-snapshot

Reconstitution of the Mitochondrial ATP-Dependent Potassium Channel into Bilayer Lipid Membrane1

inferredcites →https://doi.org/10.1038/191144a0openalex-snapshot

Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism

inferredcites →https://doi.org/10.1038/370621a0openalex-snapshot

Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

inferredcites →https://doi.org/10.1038/386299a0openalex-snapshot

Direct observation of the rotation of F1-ATPase

inferredcites →https://doi.org/10.1038/421583aopenalex-snapshot

Chemiosmotic coupling: The cost of living

inferredcites →https://doi.org/10.1038/emboj.2008.35openalex-snapshot

Dimer ribbons of ATP synthase shape the inner mitochondrial membrane

inferredcites →https://doi.org/10.1038/msb.2011.75openalex-snapshot

Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega

inferredcites →https://doi.org/10.1038/ncb2330openalex-snapshot

Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase

inferredcites →https://doi.org/10.1038/nchembio.1166openalex-snapshot

PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis

inferredcites →https://doi.org/10.1038/nchembio.457openalex-snapshot

Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases

inferredcites →https://doi.org/10.1038/nsmb.2284openalex-snapshot

Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation

inferredcites →https://doi.org/10.1038/nsmb718openalex-snapshot

Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase

inferredcites →https://doi.org/10.1038/srep10609openalex-snapshot

Structural transition in Bcl-xL and its potential association with mitochondrial calcium ion transport

inferredcites →https://doi.org/10.1073/pnas.041619798openalex-snapshot

Solution structure of the antiapoptotic protein bcl-2

inferredcites →https://doi.org/10.1073/pnas.0707326104openalex-snapshot

How the regulatory protein, IF 1 , inhibits F 1 -ATPase from bovine mitochondria

inferredcites →https://doi.org/10.1073/pnas.1011099107openalex-snapshot

Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria

inferredcites →https://doi.org/10.1073/pnas.1103621108openalex-snapshot

Macromolecular organization of ATP synthase and complex I in whole mitochondria

inferredcites →https://doi.org/10.1073/pnas.1217823110openalex-snapshot

Dimers of mitochondrial ATP synthase form the permeability transition pore

inferredcites →https://doi.org/10.1073/pnas.1411560111openalex-snapshot

Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F 1 -ATPase

inferredcites →https://doi.org/10.1073/pnas.1421202112openalex-snapshot

On the principle of ion selectivity in Na + /H + -coupled membrane proteins: Experimental and theoretical studies of an ATP synthase rotor

inferredcites →https://doi.org/10.1073/pnas.231619298openalex-snapshot

Activated glycogen synthase-3β suppresses cardiac hypertrophy in vivo

inferredcites →https://doi.org/10.1074/jbc.m109.059956openalex-snapshot

Novel Components of an Active Mitochondrial K+/H+ Exchange

inferredcites →https://doi.org/10.1074/jbc.m110.144907openalex-snapshot

Structure of Dimeric F1F0-ATP Synthase

inferredcites →https://doi.org/10.1074/jbc.m111.335356openalex-snapshot

Kinetic Equivalence of Transmembrane pH and Electrical Potential Differences in ATP Synthesis

inferredcites →https://doi.org/10.1074/jbc.m401115200openalex-snapshot

Functional Distinctions between the Mitochondrial ATP-dependent K+ Channel (mitoKATP) and Its Inward Rectifier Subunit (mitoKIR)

inferredcites →https://doi.org/10.1080/10635150590947041openalex-snapshot

Joint Bayesian Estimation of Alignment and Phylogeny

inferredcites →https://doi.org/10.1084/jem.192.7.1001openalex-snapshot

Reactive Oxygen Species (Ros-Induced) Ros Release

inferredcites →https://doi.org/10.1085/jgp.88.5.589openalex-snapshot

Single adult rabbit and rat cardiac myocytes retain the Ca2+- and species-dependent systolic and diastolic contractile properties of intact muscle.

inferredcites →https://doi.org/10.1093/cvr/cvp151openalex-snapshot

Regulation and pharmacology of the mitochondrial permeability transition pore

inferredcites →https://doi.org/10.1093/molbev/mst197openalex-snapshot

MEGA6: Molecular Evolutionary Genetics Analysis Version 6.0

inferredcites →https://doi.org/10.1093/oxfordjournals.molbev.a040454openalex-snapshot

The neighbor-joining method: a new method for reconstructing phylogenetic trees.

inferredcites →https://doi.org/10.1101/gr.278202openalex-snapshot

CDART: Protein Homology by Domain Architecture

inferredcites →https://doi.org/10.1111/j.1432-1033.1997.0336a.xopenalex-snapshot

Turnover Number of Escherichia coli F0F1 ATP Synthase for ATP Synthesis in Membrane Vesicles

inferredcites →https://doi.org/10.1126/science.1074360openalex-snapshot

Cytoprotective Role of Ca 2+ - Activated K + Channels in the Cardiac Inner Mitochondrial Membrane

inferredcites →https://doi.org/10.1126/science.286.5445.1700openalex-snapshot

Molecular Architecture of the Rotary Motor in ATP Synthase

inferredcites →https://doi.org/10.1128/mcb.17.12.7040openalex-snapshot

Bad Is a BH3 Domain-Containing Protein That Forms an Inactivating Dimer with Bcl-X L

inferredcites →https://doi.org/10.1146/annurev.biochem.66.1.717openalex-snapshot

THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE

inferredcites →https://doi.org/10.1152/ajpheart.01031.2002openalex-snapshot

Isoflurane activates rat mitochondrial ATP-sensitive K+channels reconstituted in lipid bilayers

inferredcites →https://doi.org/10.1152/ajpheart.01084.2005openalex-snapshot

Characterization of human cardiac mitochondrial ATP-sensitive potassium channel and its regulation by phorbol ester in vitro

inferredcites →https://doi.org/10.1152/ajpheart.01296.2004openalex-snapshot

K+-dependent regulation of matrix volume improves mitochondrial function under conditions mimicking ischemia-reperfusion

inferredcites →https://doi.org/10.1152/physrev.00026.2013openalex-snapshot

Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release

inferredcites →https://doi.org/10.1161/01.res.83.1.110openalex-snapshot

Modulation of Mitochondrial ATP-Dependent K+Channels by Protein Kinase C

inferredcites →https://doi.org/10.1161/01.res.87.12.1172openalex-snapshot

The β2-Adrenergic Receptor Delivers an Antiapoptotic Signal to Cardiac Myocytes Through Gi-Dependent Coupling to Phosphatidylinositol 3′-Kinase

inferredcites →https://doi.org/10.1161/circresaha.109.197996openalex-snapshot

Role of Glycogen Synthase Kinase-3β in Cardioprotection

inferredcites →https://doi.org/10.1161/circresaha.112.266445openalex-snapshot

Mitochondrial ROMK Channel Is a Molecular Component of MitoK ATP

inferredcites →https://doi.org/10.1161/circulationaha.107.702795openalex-snapshot

Metabolic Mechanisms in Heart Failure

inferredcites →https://doi.org/10.1161/hh2401.101752openalex-snapshot

Characteristics and Superoxide-Induced Activation of Reconstituted Myocardial Mitochondrial ATP-Sensitive Potassium Channels

inferredcites →https://doi.org/10.1172/jci19906openalex-snapshot

Glycogen synthase kinase-3β mediates convergence of protection signaling to inhibit the mitochondrial permeability transition pore

inferredcites →https://doi.org/10.1196/annals.1420.023openalex-snapshot

The Identity and Regulation of the Mitochondrial Permeability Transition Pore

inferredcites →https://doi.org/10.1242/jeb.01548openalex-snapshot

Exercise-induced maximal metabolic rate scales with muscle aerobic capacity

inferredcites →https://doi.org/10.1529/biophysj.103.036962openalex-snapshot

The Proton-Driven Rotor of ATP Synthase: Ohmic Conductance (10 fS), and Absence of Voltage Gating

inferredcites →https://doi.org/10.2174/092986610790226003openalex-snapshot

Molecular Modeling of Human BAD, a Pro-Apoptotic Bcl-2 Family Member, Integrating Glycolysis and Apoptosis

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.bpc.2021.106579openalex-snapshot

Coupling mechanisms in ATP synthesis: Rejoinder to “Response to molecular-level understanding of biological energy coupling and transduction”

inferred← citeshttps://doi.org/10.1016/j.bpc.2021.106604openalex-snapshot

Charge transfer across biomembranes: A solution to the conundrum of high desolvation free energy penalty in ion transport

inferred← citeshttps://doi.org/10.1016/j.yjmcc.2020.01.010openalex-snapshot

Global knockout of ROMK potassium channel worsens cardiac ischemia-reperfusion injury but cardiomyocyte-specific knockout does not: Implications for the identity of mitoKATP

inferred← citeshttps://doi.org/10.1016/j.yjmcc.2020.11.013openalex-snapshot

Mitochondrial Ca2+, redox environment and ROS emission in heart failure: Two sides of the same coin?

inferred← citeshttps://doi.org/10.3390/biom11081172openalex-snapshot

Routes for Potassium Ions across Mitochondrial Membranes: A Biophysical Point of View with Special Focus on the ATP-Sensitive K+ Channel

inferred← citeshttps://doi.org/10.3390/cells10061554openalex-snapshot

Multidimensional Regulation of Cardiac Mitochondrial Potassium Channels

inferred← citeshttps://doi.org/10.3390/molecules27010299openalex-snapshot

Alternative Targets for Modulators of Mitochondrial Potassium Channels

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Growth and Yield of Shallot (Allium cepa L. Aggregatum Group) with Application of Amino Acid Biostimulant Dosages

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