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Cardiac Mitochondria and Reactive Oxygen Species Generation

https://doi.org/10.1161/circresaha.114.300559
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Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

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The 103 checked references that resolve
resolves10.1126/science.283.5407.1482
Mitochondrial Diseases in Man and Mouse
resolves10.1146/annurev.genet.39.110304.095751
A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine
resolves10.1016/S0021-9258(19)57189-7
RESPIRATORY ENZYMES IN OXIDATIVE PHOSPHORYLATION
resolves10.1016/S0021-9258(19)57191-5
RESPIRATORY ENZYMES IN OXIDATIVE PHOSPHORYLATION
resolves10.1146/annurev.physiol.69.031905.163645
Preconditioning: The Mitochondrial Connection
resolves10.1042/bj1280617
The cellular production of hydrogen peroxide
resolves10.1152/ajpheart.01283.2006
Mitochondrial reactive oxygen species-mediated signaling in endothelial cells
resolves10.1161/01.res.0000091261.19387.ae
Mitochondrial Sources of H <sub>2</sub> O <sub>2</sub> Generation Play a Key Role in Flow-Mediated Dilation in Human Coronary Resistance Arteries
resolves10.1074/jbc.273.51.33972
Generation of Superoxide Anion by Succinate-Cytochromec Reductase from Bovine Heart Mitochondria
resolves10.1074/jbc.M109.017376
Membrane Potential Greatly Enhances Superoxide Generation by the Cytochrome bc1 Complex Reconstituted into Phospholipid Vesicles
resolves10.1016/S0006-291X(86)80529-0
The mitochondrial site of superoxide formation
resolves10.1046/j.1471-4159.2001.00548.x
ΔΨ<sub>m</sub>‐Dependent and ‐independent production of reactive oxygen species by rat brain mitochondria
resolves10.1042/BJ20040485
Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
resolves10.1016/0003-9861(77)90035-2
Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
resolves10.1042/bj1910421
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
resolves10.1016/0003-9861(85)90293-0
Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
resolves10.1074/jbc.M306312200
The Ubiquinone-binding Site of the Saccharomyces cerevisiae Succinate-Ubiquinone Oxidoreductase Is a Source of Superoxide
resolves10.1074/jbc.M204958200
Mechanism of Superoxide and Hydrogen Peroxide Formation by Fumarate Reductase, Succinate Dehydrogenase, and Aspartate Oxidase
resolves10.1038/29331
A mutation in succinate dehydrogenase cytochrome b causes oxidative stress and ageing in nematodes
resolves10.1016/j.cell.2005.05.025
Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II
resolves10.1074/jbc.M507741200
Protein Kinase A-mediated Phosphorylation Modulates Cytochrome c Oxidase Function and Augments Hypoxia and Myocardial Ischemia-related Injury
resolves10.1074/jbc.M607135200
Bovine Complex I Is a Complex of 45 Different Subunits
resolves10.1016/S0005-2728(98)00027-9
Iron–sulfur clusters/semiquinones in Complex I
resolves10.1016/j.freeradbiomed.2012.05.025
Protein thiyl radical mediates S-glutathionylation of complex I
resolves10.1074/jbc.M109.056846
Peptide-based Antibodies against Glutathione-binding Domains Suppress Superoxide Production Mediated by Mitochondrial Complex I
resolves10.1021/bi602580c
Site-Specific S-Glutathiolation of Mitochondrial NADH Ubiquinone Reductase
resolves10.1074/jbc.M406576200
Inhibitors of the Quinone-binding Site Allow Rapid Superoxide Production from Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I)
resolves10.1074/jbc.M503936200
Superoxide Generation from Mitochondrial NADH Dehydrogenase Induces Self-inactivation with Specific Protein Radical Formation
resolves10.1074/jbc.M310341200
Characterization of Superoxide-producing Sites in Isolated Brain Mitochondria
resolves10.1073/pnas.0510977103
The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
resolves10.1046/j.0022-3042.2002.00744.x
Generation of reactive oxygen species by the mitochondrial electron transport chain
resolves10.1007/s10863-005-4117-y
A Possible Site of Superoxide Generation in the Complex I Segment of Rat Heart Mitochondria
resolves10.1016/j.bbabio.2010.05.012
New insights into the superoxide generation sites in bovine heart NADH-ubiquinone oxidoreductase (Complex I): The significance of protein-associated ubiquinone and the dynamic shifting of generation sites between semiflavin and semiquinone radicals
resolves10.1023/A:1016083419979
EPR Characterization of Ubisemiquinones and Iron–Sulfur Cluster N2, Central Components of the Energy Coupling in the NADH-Ubiquinone Oxidoreductase (Complex I) In Situ
resolves10.1016/j.bbabio.2012.03.032
EPR detection of two protein-associated ubiquinone components (SQNf and SQNs) in the membrane in situ and in proteoliposomes of isolated bovine heart complex I
resolves10.1126/science.1123809
Structure of the Hydrophilic Domain of Respiratory Complex I from <i>Thermus thermophilus</i>
resolves10.1002/bip.21457
Design and use of peptide‐based antibodies decreasing superoxide production by mitochondrial complex I and complex II
resolves10.1074/jbc.M209359200
Reversible Glutathionylation of Complex I Increases Mitochondrial Superoxide Formation
resolves10.1074/jbc.M408011200
Glutaredoxin 2 Catalyzes the Reversible Oxidation and Glutathionylation of Mitochondrial Membrane Thiol Proteins
resolves10.1074/jbc.M803432200
Complex I within Oxidatively Stressed Bovine Heart Mitochondria Is Glutathionylated on Cys-531 and Cys-704 of the 75-kDa Subunit
resolves10.1126/science.1079605
Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation
resolves10.1074/jbc.M702294200
Mitochondrial Complex II in the Post-ischemic Heart
resolves10.1074/jbc.M513627200
Direct and Indirect Roles of Cytochrome b in the Mediation of Superoxide Generation and NO Catabolism by Mitochondrial Succinate-Cytochrome c Reductase
resolves10.1016/0003-9861(92)90365-4
Characterization of ubisemiquinone radicals in succinate-ubiquinone reductase
resolves10.1073/pnas.0702621104
A semiquinone intermediate generated at the Q <sub>o</sub> site of the cytochrome <i>bc</i> <sub>1</sub> complex: Importance for the Q-cycle and superoxide production
resolves10.1021/bi0342160
Architecture of the Q<sub>o</sub>Site of the Cytochrome<i>bc</i><sub>1</sub>Complex Probed by Superoxide Production
resolves10.1074/jbc.M409994200
Evidence for Electron Equilibrium between the Two Hemes bL in the Dimeric Cytochrome bc1 Complex
resolves10.1126/science.281.5373.64
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc <sub>1</sub> Complex
resolves10.1074/jbc.M207217200
Topology of Superoxide Production from Different Sites in the Mitochondrial Electron Transport Chain
resolves10.1074/jbc.M407715200
Complex III Releases Superoxide to Both Sides of the Inner Mitochondrial Membrane
resolves10.1152/ajpheart.00731.2011
Biphasic modulation of the mitochondrial electron transport chain in myocardial ischemia and reperfusion
resolves10.1126/science.283.5407.1488
Oxidative Phosphorylation at the <i>fin de siècle</i>
resolves10.1146/annurev.biophys.30.1.23
Structures and Proton-Pumping Strategies of Mitochondrial Respiratory Enzymes
resolves10.1126/science.280.5370.1723
Redox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase
resolves10.1074/jbc.274.6.3308
An Electron Spin Resonance Spin-trapping Investigation of the Free Radicals Formed by the Reaction of Mitochondrial Cytochromec Oxidase with H2O2
resolves10.1021/bi9911987
Direct Evidence for a Tyrosine Radical in the Reaction of Cytochrome <i>c</i> Oxidase with Hydrogen Peroxide
resolves10.1016/S0021-9258(18)55001-8
Superoxide sensitivity of the Escherichia coli aconitase.
resolves10.1016/S0021-9258(19)50343-X
Inactivation-reactivation of aconitase in Escherichia coli. A sensitive measure of superoxide radical.
resolves10.1073/pnas.91.25.12248
Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs.
resolves10.1074/jbc.275.19.14064
Mitochondrial Aconitase Is a Source of Hydroxyl Radical
resolves10.1084/jem.192.7.1001
Reactive Oxygen Species (Ros-Induced) Ros Release
resolves10.1172/JCI200524408
Oxygen, oxidative stress, hypoxia, and heart failure
resolves10.1161/circresaha.109.206359
Endogenous Activation of Mitochondrial K <sub>ATP</sub> Channels Protects Human Failing Myocardium From Hydroxyl Radical–Induced Stunning
resolves10.1172/JCI25371
The mitochondrial origin of postischemic arrhythmias
resolves10.1152/ajpregu.00124.2004
Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology
resolves10.1161/atvbaha.113.301591
Mitochondrial Oxidative Stress Corrupts Coronary Collateral Growth by Activating Adenosine Monophosphate Activated Kinase-α Signaling
resolves10.1161/circresaha.111.258871
H<sub>2</sub>O<sub>2</sub>-Induced Dilation in Human Coronary Arterioles: Role of Protein Kinase G Dimerization and Large-Conductance Ca<sup>2+</sup>-Activated K<sup>+</sup>Channel Activation
resolves10.1161/01.atv.0000249408.55796.da
Hydrogen Peroxide
resolves10.1152/ajpheart.00436.2007
Redox-dependent coronary metabolic dilation
resolves10.1152/ajpheart.00696.2006
H<sub>2</sub>O<sub>2</sub> activates redox- and 4-aminopyridine-sensitive K<sub>v</sub> channels in coronary vascular smooth muscle
resolves10.1007/978-1-4615-1833-4_8
Oxygen-Free Radicals at Myocardial Level: Effects of Ischaemia and Reperfusion
resolves10.1093/ajcn/53.1.215S
Role of oxygen free radicals in ischemic and reperfused myocardium
resolves10.1197/S1069-6563(03)00319-1
<i>Bench to Bedside:</i> The Role of Mitochondrial Medicine in the Pathogenesis and Treatment of Cellular Injury
resolves10.1016/j.cardiores.2006.02.025
The role of oxidants and free radicals in reperfusion injury
resolves10.1172/JCI113288
Allopurinol enhanced adenine nucleotide repletion after myocardial ischemia in the isolated rat heart.
resolves10.1161/circulationaha.104.527226
Endothelium-Derived Nitric Oxide Regulates Postischemic Myocardial Oxygenation and Oxygen Consumption by Modulation of Mitochondrial Electron Transport
resolves10.1124/jpet.108.143479
The Radical Trap 5,5-Dimethyl-1-Pyrroline N-Oxide Exerts Dose-Dependent Protection against Myocardial Ischemia-Reperfusion Injury through Preservation of Mitochondrial Electron Transport
resolves10.1152/ajpheart.00459.2006
β<sub>1</sub>-Adrenoreceptor activation contributes to ischemia-reperfusion damage as well as playing a role in ischemic preconditioning
resolves10.1152/ajpheart.00264.2006
Endothelial nitric oxide synthase (NOS3) knockout decreases NOS2 induction, limiting hyperoxygenation and conferring protection in the postischemic heart
resolves10.1016/S0005-2728(99)00018-3
Non-enzymatic nitric oxide synthesis in biological systems
resolves10.1038/nm0895-804
Enzyme-independent formation of nitric oxide in biological tissues
resolves10.1074/jbc.M311908200
Nitrosyl-Heme Complexes Are Formed in the Ischemic Heart
resolves10.1074/jbc.M802691200
Protein Tyrosine Nitration of the Flavin Subunit Is Associated with Oxidative Modification of Mitochondrial Complex II in the Post-ischemic Myocardium
resolves10.1016/j.bbapap.2008.12.008
Proteomic analysis of protein tyrosine nitration after ischemia reperfusion injury: Mitochondria as the major target
resolves10.1042/bse0470053
Mitochondrial proton and electron leaks
resolves10.1161/01.res.0000109416.56608.64
Decrease in Mitochondrial Complex I Activity in Ischemic/Reperfused Rat Heart
resolves10.1016/j.bbabio.2011.11.021
Damage to mitochondrial complex I during cardiac ischemia reperfusion injury is reduced indirectly by anti-anginal drug ranolazine
resolves10.1007/s11010-009-0283-2
Opening of the mitoKATP channel and decoupling of mitochondrial complex II and III contribute to the suppression of myocardial reperfusion hyperoxygenation
resolves10.1007/s00395-009-0001-y
The complex II inhibitor atpenin A5 protects against cardiac ischemia-reperfusion injury via activation of mitochondrial KATP channels
resolves10.1016/j.bbagen.2009.01.011
Ambivalent effects of diazoxide on mitochondrial ROS production at respiratory chain complexes I and III
resolves10.1161/01.CIR.97.24.2463
Mitochondrial ATP-Dependent Potassium Channels
resolves10.1016/S0140-6736(00)04378-6
Germline SDHD mutation in familial phaeochromocytoma
resolves10.1136/jmg.39.9.617
Hereditary paraganglioma targets diverse paraganglia: Table 1
resolves10.1126/science.287.5454.848
Mutations in <i>SDHD</i> , a Mitochondrial Complex II Gene, in Hereditary Paraganglioma
resolves10.1056/NEJMoa020152
Germ-Line Mutations in Nonsyndromic Pheochromocytoma
resolves10.1002/gcc.1144
Nearly all hereditary paragangliomas in The Netherlands are caused by two founder mutations in the <i>SDHD</i> gene
resolves10.1021/bi9018237
Peroxynitrite-Mediated Oxidative Modifications of Complex II: Relevance in Myocardial Infarction
resolves10.1073/pnas.84.5.1404
Direct measurement of free radical generation following reperfusion of ischemic myocardium.
resolves10.1172/JCI113264
Recombinant superoxide dismutase reduces oxygen free radical concentrations in reperfused myocardium.
resolves10.1096/fj.02-0729fje
Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: role of reactive oxygen species and cardiolipin
resolves10.1074/jbc.272.30.18808
Cellular Respiration during Hypoxia
resolves10.1161/circresaha.112.271320
Measurement of <i>S</i> -Nitrosylation Occupancy in the Myocardium With Cysteine-Reactive Tandem Mass Tags
resolves10.1152/ajpheart.00997.2010
Characterization of potential<i>S</i>-nitrosylation sites in the myocardium
The 1 reference without a DOI — listed, not checked
no DOI — not checkedFerrari R. Importance of oxygen free radicals during ischemia and reperfusion in the experimental and clinical setting. Oxygen free radicals and the heart. Am J Cardiovasc Pathol. 1992;4:103–114.
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