Karl David Straub
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Also affiliated: AT&T (United States) (1979–1984); National Institute of Standards and Technology (1997); United States Department of Veterans Affairs (1977–1998); Duke University (1965–1998); University of California, Irvine (1988–1994); University of Arkansas Medical Center (1974–1983); Veterans Health Administration (1978–1998); Central Arkansas Veterans Healthcare System (1977–2024); Duke Medical Center (1969); John L. McClellan Memorial Veterans Hospital (1977–2013); Institute of Chemical Kinetics and Combustion (1997); University of Oklahoma Health Sciences Center (1984); Mississippi State University (1988)
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Karl David Straub's research program has historically focused on the metabolism of hydrogen sulfide (H2S) and its role in biological signaling, as well as the function of mitochondria. His work has investigated the production of reactive sulfur species by enzymes such as superoxide dismutase and catalase, exploring these processes in various biological contexts. Straub has also examined mitochondrial function in relation to oxygen extraction and myocardial reperfusion, drawing on studies that date back to the 1970s. His publications span a range of scientific disciplines, including nuclear physics and chemistry, alongside his primary focus on biochemistry and physiology.
With an h-index of 29 and over 2,900 citations across 136 publications, Straub is recognized as a highly cited researcher. His work on hydrogen sulfide, metabolism, and mitochondrial function has been published in peer-reviewed journals. He has also been involved in research related to energy relaxation mechanisms in porphyrins and the decay of atomic nuclei. Straub maintains an active laboratory website and has been recently active in research, with his most recent publication in 2024.
Metrics
- h-index: 26
- Publications: 113
- Citations: 2,458
Selected Publications
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The SOD1 Inhibitor, LCS-1, Oxidizes H2S to Reactive Sulfur Species, Directly and Indirectly, through Conversion of SOD1 to an Oxidase (2024)
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Reaction Mechanisms of H2S Oxidation by Naphthoquinones (2024)
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Redox and Nucleophilic Reactions of Naphthoquinones with Small Thiols and Their Effects on Oxidization of H2S to Inorganic and Organic Hydropolysulfides and Thiosulfate (2023)
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Naphthoquinones Oxidize H2S to Polysulfides and Thiosulfate, Implications for Therapeutic Applications (2022)
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The Effects of Antioxidant Nutraceuticals on Cellular Sulfur Metabolism and Signaling (2022)
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Coenzyme Q10 and related quinones oxidize H2S to polysulfides and thiosulfate (2022)
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‘Antioxidant’ berries, anthocyanins, resveratrol and rosmarinic acid oxidize hydrogen sulfide to polysulfides and thiosulfate: A novel mechanism underlying their biological actions (2021)
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Oxidation of Hydrogen Sulfide by Quinones: How Polyphenols Initiate Their Cytoprotective Effects (2021)
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Manganese Porphyrin-Based SOD Mimetics Produce Polysulfides from Hydrogen Sulfide (2019)
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An Effective Electric Dipole Model for Voltage-induced Gating Mechanism of Lysenin (2019)
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Fluorescence quenching by metal centered porphyrins and poryphyrin enzymes (2017)PMC OpenAlex
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Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase (2017)
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Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase (2017)
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Fluorescence quenching by metal centered porphyrins and poryphyrin enzymes (2017)
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Catalase as a sulfide-sulfur oxido-reductase: An ancient (and modern?) regulator of reactive sulfur species (RSS) (2017)PMC OpenAlex
Collaboration Network
Top Collaborators
- The Role of Hydrogen Sulfide in Evolution and the Evolution of Hydrogen Sulfide in Metabolism and Signaling
- Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase
- Catalase as a sulfide-sulfur oxido-reductase: An ancient (and modern?) regulator of reactive sulfur species (RSS)
- Manganese Porphyrin-Based SOD Mimetics Produce Polysulfides from Hydrogen Sulfide
- Oxidation of Hydrogen Sulfide by Quinones: How Polyphenols Initiate Their Cytoprotective Effects
Showing 5 of 16 shared publications
- Improvement of Mitochondrial Energy Production in Ischemic Myocardium by in Vivo Infusion of Ruthenium Reb
- Controlled versus hyperemic flow during reperfusion of jeopardized ischemic myocardium
- Ventricular performance and biochemical alteration of regional ischemic myocardium after reperfusion in the pig
- Effects of adenine nucleotide translocase inhibitors on dinitrophenol-induced Ca2+ efflux from pig heart mitochondria
- The relationship between hypertrophy and dilatation in the postmortem heart
Showing 5 of 12 shared publications
- Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase
- Catalase as a sulfide-sulfur oxido-reductase: An ancient (and modern?) regulator of reactive sulfur species (RSS)
- Manganese Porphyrin-Based SOD Mimetics Produce Polysulfides from Hydrogen Sulfide
- Oxidation of Hydrogen Sulfide by Quinones: How Polyphenols Initiate Their Cytoprotective Effects
- ‘Antioxidant’ berries, anthocyanins, resveratrol and rosmarinic acid oxidize hydrogen sulfide to polysulfides and thiosulfate: A novel mechanism underlying their biological actions
Showing 5 of 9 shared publications
- Controlled versus hyperemic flow during reperfusion of jeopardized ischemic myocardium
- Ventricular performance and biochemical alteration of regional ischemic myocardium after reperfusion in the pig
- Effects of reperfusion on myocardial wall thickness, oxidative phosphorylation, and Ca2+ metabolism following total and partial myocardial ischemia
- The adverse effect of systemic hypertension following myocardial reperfusion
- Wall motion and metabolic changes after coronary occlusion and reperfusion
Showing 5 of 8 shared publications
- Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase
- Catalase as a sulfide-sulfur oxido-reductase: An ancient (and modern?) regulator of reactive sulfur species (RSS)
- Manganese Porphyrin-Based SOD Mimetics Produce Polysulfides from Hydrogen Sulfide
- Fluorescence quenching by metal centered porphyrins and poryphyrin enzymes
- Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase
Showing 5 of 7 shared publications
- Picosecond spectroscopy of some metalloporphyrins
- Picosecond transient absorption spectra and kinetics of salicylidenaniline
- Picosecond Specttroscopy of Iron Porphyrins and Hemoproteins
- Picosecond Excited-State Relaxation of Some Iron Porphyrins and Hemoproteins
- <title>Picosecond Spectroscopy Of Metalloporphyrins And Hemoproteins</title>
Showing 5 of 6 shared publications
- Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase
- Catalase as a sulfide-sulfur oxido-reductase: An ancient (and modern?) regulator of reactive sulfur species (RSS)
- Fluorescence quenching by metal centered porphyrins and poryphyrin enzymes
- Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase
- Catalase as a sulfide-sulfur oxido-reductase: An ancient (and modern?) regulator of reactive sulfur species (RSS)
Showing 5 of 6 shared publications
- Improvement of Mitochondrial Energy Production in Ischemic Myocardium by in Vivo Infusion of Ruthenium Reb
- Ventricular performance and biochemical alteration of regional ischemic myocardium after reperfusion in the pig
- The adverse effect of systemic hypertension following myocardial reperfusion
- Wall motion and metabolic changes after coronary occlusion and reperfusion
- Systolic Time Intervals in the Experimental Animal with Aortic Outflow Obstruction
- Digitalis-Sensitive Na+,K+-ATPase
- The adverse effect of systemic hypertension following myocardial reperfusion
- Digoxin uptake into peripheral autonomic cardiac nerves: Possible mechanism of digitalis-induced antiarrhythmic and toxic electrophysiologic actions
- Comparison of the canine tissue distribution of digoxin after acute and chronic administration: Implications for digitalis therapy
- Systolic Time Intervals in the Experimental Animal with Aortic Outflow Obstruction
- Fluorescence quenching by metal centered porphyrins and poryphyrin enzymes
- Naphthoquinones Oxidize H2S to Polysulfides and Thiosulfate, Implications for Therapeutic Applications
- Redox and Nucleophilic Reactions of Naphthoquinones with Small Thiols and Their Effects on Oxidization of H2S to Inorganic and Organic Hydropolysulfides and Thiosulfate
- Reaction Mechanisms of H2S Oxidation by Naphthoquinones
- The SOD1 Inhibitor, LCS-1, Oxidizes H2S to Reactive Sulfur Species, Directly and Indirectly, through Conversion of SOD1 to an Oxidase
- Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase
- Manganese Porphyrin-Based SOD Mimetics Produce Polysulfides from Hydrogen Sulfide
- Fluorescence quenching by metal centered porphyrins and poryphyrin enzymes
- Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase
- Fluorescence quenching by metal centered porphyrins and poryphyrin enzymes
- Coenzyme Q10 and related quinones oxidize H2S to polysulfides and thiosulfate
- Naphthoquinones Oxidize H2S to Polysulfides and Thiosulfate, Implications for Therapeutic Applications
- Redox and Nucleophilic Reactions of Naphthoquinones with Small Thiols and Their Effects on Oxidization of H2S to Inorganic and Organic Hydropolysulfides and Thiosulfate
- Reaction Mechanisms of H2S Oxidation by Naphthoquinones
- The SOD1 Inhibitor, LCS-1, Oxidizes H2S to Reactive Sulfur Species, Directly and Indirectly, through Conversion of SOD1 to an Oxidase
- Coenzyme Q10 and related quinones oxidize H2S to polysulfides and thiosulfate
- Naphthoquinones Oxidize H2S to Polysulfides and Thiosulfate, Implications for Therapeutic Applications
- Redox and Nucleophilic Reactions of Naphthoquinones with Small Thiols and Their Effects on Oxidization of H2S to Inorganic and Organic Hydropolysulfides and Thiosulfate
- Reaction Mechanisms of H2S Oxidation by Naphthoquinones
- The SOD1 Inhibitor, LCS-1, Oxidizes H2S to Reactive Sulfur Species, Directly and Indirectly, through Conversion of SOD1 to an Oxidase
- Coenzyme Q10 and related quinones oxidize H2S to polysulfides and thiosulfate
- Naphthoquinones Oxidize H2S to Polysulfides and Thiosulfate, Implications for Therapeutic Applications
- Redox and Nucleophilic Reactions of Naphthoquinones with Small Thiols and Their Effects on Oxidization of H2S to Inorganic and Organic Hydropolysulfides and Thiosulfate
- Reaction Mechanisms of H2S Oxidation by Naphthoquinones
- The SOD1 Inhibitor, LCS-1, Oxidizes H2S to Reactive Sulfur Species, Directly and Indirectly, through Conversion of SOD1 to an Oxidase
- Coenzyme Q10 and related quinones oxidize H2S to polysulfides and thiosulfate
- The Effects of Antioxidant Nutraceuticals on Cellular Sulfur Metabolism and Signaling
- Naphthoquinones Oxidize H2S to Polysulfides and Thiosulfate, Implications for Therapeutic Applications
- The SOD1 Inhibitor, LCS-1, Oxidizes H2S to Reactive Sulfur Species, Directly and Indirectly, through Conversion of SOD1 to an Oxidase
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