sulfur has been researched along with coenzyme a in 23 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 10 (43.48) | 18.7374 |
| 1990's | 1 (4.35) | 18.2507 |
| 2000's | 6 (26.09) | 29.6817 |
| 2010's | 3 (13.04) | 24.3611 |
| 2020's | 3 (13.04) | 2.80 |
| Authors | Studies |
|---|---|
| Aarsland, A; Asiedu, D; Berge, RK; Skorve, J; Svardal, AM | 1 |
| Benedict, CR; Cooper, TC | 1 |
| Holloway, PW; Wakil, SJ | 1 |
| Lipmann, F | 1 |
| Kawachi, T; Rudney, H | 1 |
| Dorsey, JA; Kumar, S; Muesing, RA; Porter, JW | 1 |
| Burton, DN; Haavik, AG; Porter, JW | 1 |
| Engel, PC; Williamson, G | 1 |
| Furdui, C; Ragsdale, SW | 1 |
| LEOPOLD, AC; SEN, SP | 1 |
| DICKINSON, JE; KLOSS, RA | 1 |
| EGER-NEUFELDT, I; WEISS, L; WIELAND, O | 1 |
| Crane, EJ; Hummel, CS; Lancaster, KM | 1 |
| Raymond, J; Segrè, D | 1 |
| Adams, MW; Bridger, SL; Schut, GJ | 1 |
| Kursula, P; Meriläinen, G; Schmitz, W; Wierenga, RK | 1 |
| Boles, W; Claiborne, A; Furdui, CM; Karplus, PA; Mallett, TC; Parsonage, D; Wallen, JR | 1 |
| Kobayashi, K; Oda, A; Takahashi, O | 1 |
| Nolte, JC; Schepers, CL; Schürmann, M; Steinbüchel, A; Vogel, E; Wübbeler, JH | 1 |
| Cao, HY; Chen, XL; Li, CY; Peng, M; Shao, X; Shi, WL; Todd, JD; Wang, P; Wei, TD; Yuan, Z; Zhang, XH; Zhang, YZ; Zhao, F | 1 |
| Cotticelli, MG; Hauser, LA; Himes, BE; Ho, ES; Lynch, DR; Mesaros, C; Napierala, JS; Napierala, M; Wang, D; Wilson, RB; Xu, P | 1 |
| Du, ZX; Li, Y; Wang, ZJ; Yang, JH; Zhou, DM | 1 |
| Frey, J; Junghare, M; Naji, KM; Schink, B; Spiteller, D; Vaaje-Kolstad, G | 1 |
23 other study(ies) available for sulfur and coenzyme a
| Article | Year |
|---|---|
Fatty acid metabolism in liver of rats treated with hypolipidemic sulphur-substituted fatty acid analogues.
Topics: Animals; Carnitine O-Palmitoyltransferase; Cell Fractionation; Coenzyme A; Coenzyme A Ligases; Cyanides; Dicarboxylic Acids; Fatty Acids; Liver; Male; Microbodies; Organ Size; Oxidation-Reduction; Palmitoyl-CoA Hydrolase; Propionates; Proteins; Rats; Rats, Inbred Strains; Repressor Proteins; Saccharomyces cerevisiae Proteins; Sulfides; Sulfur; Time Factors; Triglycerides | 1990 |
Regulation of pyruvate carboxylase by coenzyme A and acyl coenzyme A thio esters.
Topics: Bicarbonates; Chromatography; Coenzyme A; Cyclic AMP; Esters; Hydrogen-Ion Concentration; Kinetics; Ligases; Pantothenic Acid; Pyruvates; Saccharomyces; Sulfur | 1968 |
Requirement for reduced diphosphopyridine nucleotide-cytochrome b5 reductase in stearly coenzyme A desaturation.
Topics: Alcohols; Animals; Bile Acids and Salts; Chemical Precipitation; Chickens; Chromatography, DEAE-Cellulose; Coenzyme A; Cytochromes; Ethylmaleimide; Female; Methods; Microsomes, Liver; NAD; Oxidoreductases; Quaternary Ammonium Compounds; Solubility; Stearic Acids; Sulfates; Sulfur; Ultracentrifugation | 1970 |
Attempts to map a process evolution of peptide biosynthesis.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Amino Acids; Anti-Bacterial Agents; Bacillus; Bacteria; Carbon Isotopes; Chromatography, Gel; Chromatography, Ion Exchange; Coenzyme A; Escherichia coli; Fatty Acids; Molecular Weight; Pantothenic Acid; Peptide Biosynthesis; Peptides, Cyclic; Polymers; Ribosomes; Sulfur; Tritium; Tyrothricin | 1971 |
Solubilization and purification of beta-hydroxy-beta-methylglutaryl coenzyme A reductase from rat liver.
Topics: Alcohol Oxidoreductases; Alcohols; Animals; Bile Acids and Salts; Carbon Isotopes; Chemical Phenomena; Chemistry; Cholesterol; Chromatography, Gel; Coenzyme A; Digitalis Glycosides; Edetic Acid; Female; Glutarates; Hydrogen-Ion Concentration; Iron; Microsomes, Liver; Molecular Weight; Phenanthrolines; Rats; Solubility; Sulfur; Tetroses | 1970 |
Comparative studies of the pigeon liver fatty acid synthetase complex and its subunits. Kinetics of partial reactions and the number of binding sites for acetyl and malonyl groups.
Topics: Acetates; Alcohols; Animals; Binding Sites; Caproates; Carbon Dioxide; Coenzyme A; Columbidae; Cysteamine; Dialysis; Fatty Acids; Glycine; Hydroxybutyrates; Kinetics; Liver; Malonates; Mercaptoethanol; Palmitic Acids; Phosphates; Sulfur; Tromethamine; Ultracentrifugation | 1970 |
Comparative studies of the rat and pigeon liver fatty acid synthetases.
Topics: Acetates; Amino Acids; Animals; Centrifugation, Density Gradient; Chromatography, Gel; Chromatography, Ion Exchange; Coenzyme A; Columbidae; Electrophoresis; Flavins; Hydrogen-Ion Concentration; Ligases; Liver; Malonates; Molecular Weight; Palmitic Acids; Rats; Sulfur; Ultracentrifugation | 1968 |
The effect on butyryl-CoA dehydrogenase of reagents specific for nucleophilic sulphur.
Topics: Butyryl-CoA Dehydrogenase; Chromatography, Gel; Coenzyme A; Dithionitrobenzoic Acid; Dithiothreitol; Fatty Acid Desaturases; Nitrobenzoates; Phenylmercuric Acetate; Phenylmercury Compounds; Spectrum Analysis; Sulfur; Veillonellaceae | 1983 |
The roles of coenzyme A in the pyruvate:ferredoxin oxidoreductase reaction mechanism: rate enhancement of electron transfer from a radical intermediate to an iron-sulfur cluster.
Topics: Amino Acid Sequence; Bacteria, Anaerobic; Coenzyme A; Electron Spin Resonance Spectroscopy; Electron Transport; Iron; Ketone Oxidoreductases; Kinetics; Molecular Sequence Data; Pyruvate Synthase; Sequence Homology, Amino Acid; Sulfur | 2002 |
Preparation of 32P and 35S labelled coenzyme A.
Topics: Coenzyme A; Coenzymes; Phosphorus; Phosphorus Radioisotopes; Sulfur; Sulfur Radioisotopes | 1955 |
Preparation of malonyl coenzyme A by thioester exchange.
Topics: Coenzyme A; Malonates; Malonyl Coenzyme A; Sulfhydryl Compounds; Sulfur Compounds | 1963 |
[INHIBITION OF ENZYMATIC CITRIC ACID SYNTHESIS BY LONG-CHAIN ACYL-THIOESTERS OF COENZYME A].
Topics: Animals; Citrates; Citric Acid; Coenzyme A; Enzyme Inhibitors; Heart; Liver; Mitochondria; Research; Sulfhydryl Compounds; Sulfur Compounds; Swine | 1964 |
Determination of coenzyme A levels in Pyrococcus furiosus and other Archaea: implications for a general role for coenzyme A in thermophiles.
Topics: Amino Acid Sequence; Coenzyme A; Molecular Sequence Data; Molecular Weight; Oxidation-Reduction; Oxidative Stress; Oxidoreductases; Pyrococcus furiosus; Sequence Homology, Amino Acid; Sulfhydryl Compounds; Sulfolobus solfataricus; Sulfur; Thermococcus | 2005 |
The effect of oxygen on biochemical networks and the evolution of complex life.
Topics: Adaptation, Physiological; Aerobiosis; Anaerobiosis; Animals; Biological Evolution; Coenzyme A; Computational Biology; Computer Simulation; Databases, Genetic; Enzymes; Eukaryotic Cells; Evolution, Molecular; Gene Duplication; Metabolism; Monte Carlo Method; Oxidation-Reduction; Oxygen; Photosynthesis; Phylogeny; Sulfur; Thermodynamics | 2006 |
Insights into the metabolism of elemental sulfur by the hyperthermophilic archaeon Pyrococcus furiosus: characterization of a coenzyme A- dependent NAD(P)H sulfur oxidoreductase.
Topics: Archaeal Proteins; Coenzyme A; Dimerization; Enzyme Induction; Flavoproteins; Gene Expression Regulation, Archaeal; Hydrogen; Hydrogen Sulfide; Hydrogenase; Molecular Weight; Multigene Family; NADP; Oligonucleotide Array Sequence Analysis; Oxidoreductases Acting on Sulfur Group Donors; Pyrococcus furiosus; Reverse Transcriptase Polymerase Chain Reaction; Sulfur; Time Factors | 2007 |
The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme.
Topics: Acetyl-CoA C-Acyltransferase; Bacterial Proteins; Binding Sites; Coenzyme A; Cysteine; Kinetics; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Pantothenic Acid; Serine; Substrate Specificity; Sulfhydryl Compounds; Sulfur | 2008 |
Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking.
Topics: Bacillus anthracis; Bacterial Proteins; Biological Transport, Active; Catalysis; Coenzyme A; Crystallization; Crystallography, X-Ray; Disulfides; Flavins; Isoenzymes; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Sulfur; Thiosulfate Sulfurtransferase | 2009 |
Computational study of the three-dimensional structure of N-acetyltransferase 2-acetyl coenzyme a complex.
Topics: Acetyl Coenzyme A; Acetyl-CoA C-Acetyltransferase; Binding Sites; Coenzyme A; Databases, Protein; Glutamic Acid; Glycine; Humans; Molecular Structure; Sulfur | 2010 |
Novel characteristics of succinate coenzyme A (Succinate-CoA) ligases: conversion of malate to malyl-CoA and CoA-thioester formation of succinate analogues in vitro.
Topics: Acyl Coenzyme A; Alcaligenaceae; Alcanivoraceae; Coenzyme A; Escherichia coli; Esters; Kinetics; Malates; Substrate Specificity; Succinate-CoA Ligases; Sulfur Compounds | 2014 |
Mechanistic insight into 3-methylmercaptopropionate metabolism and kinetical regulation of demethylation pathway in marine dimethylsulfoniopropionate-catabolizing bacteria.
Topics: Bacterial Proteins; Coenzyme A; Coenzyme A Ligases; Demethylation; Kinetics; Oceans and Seas; Oxidoreductases; Propionates; Roseobacter; Sulfonium Compounds; Sulfur | 2019 |
Skin fibroblast metabolomic profiling reveals that lipid dysfunction predicts the severity of Friedreich's ataxia.
Topics: 3-Hydroxybutyric Acid; Adenine; Carnitine; Ceramides; Coenzyme A; Fibroblasts; Friedreich Ataxia; Guanine; Humans; Iron; Phosphatidylglycerols; Sulfur; Triglycerides | 2022 |
[Bioinformatics analysis of differentially expressed genes associated with chronic schistosomiasis japonica-induced hepatic fibrosis].
Topics: Adenosine Monophosphate; Calcium; Coenzyme A; Computational Biology; Fatty Acids; Humans; Liver Cirrhosis; Mitogen-Activated Protein Kinases; Oxidoreductases; Phosphatidylinositol 3-Kinases; Phosphatidylinositols; Proto-Oncogene Proteins c-akt; Schistosomiasis japonica; Serine; Somatomedins; Sulfur Compounds; Threonine | 2022 |
Isophthalate:coenzyme A ligase initiates anaerobic degradation of xenobiotic isophthalate.
Topics: Acetyl Coenzyme A; Adenosine Monophosphate; Adenosine Triphosphate; Anaerobiosis; Base Composition; Benzoates; Carbon; Carcinogens; Coenzyme A; Coenzyme A Ligases; Diphosphates; Environmental Pollutants; Escherichia coli; Glutarates; Hydroxybenzoates; Mutagens; Oxygen; Phenylacetates; Phthalic Acids; Phylogeny; Plastics; RNA, Ribosomal, 16S; Sequence Analysis, DNA; Sulfur; Xenobiotics | 2022 |