methionine has been researched along with carbon monoxide in 24 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 7 (29.17) | 18.7374 |
| 1990's | 4 (16.67) | 18.2507 |
| 2000's | 8 (33.33) | 29.6817 |
| 2010's | 5 (20.83) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brittain, T; Greenwood, C | 1 |
| Daldal, F; Davidson, E; Gray, KA | 1 |
| Burger, PE; Davison, AJ; Helfet, D; Kaminsky, LS | 1 |
| Brunori, M; Dupré, S; Greenwood, C; Wilson, MT | 1 |
| Gersonde, K; Sick, H | 1 |
| Ben-Hayyim, G; Schejter, A | 1 |
| Okunuki, K; Wada, K | 1 |
| Alvares, AP; Kuntzman, R; Levin, W; Schilling, G | 1 |
| Bhuyan, A; Chan, CK; Eaton, WA; Henry, ER; Hofrichter, J; Hu, Y; Jones, CM; Luck, SD; Roder, H | 1 |
| Dai, Y; Mo, H; Pochapsky, SS; Pochapsky, TC | 1 |
| He, H; Wu, T; Wu, Y; Yuan, Y; Zhang, G | 1 |
| Kitagawa, T; Mizutani, Y; Sagami, I; Sasakura, Y; Sato, A; Shimizu, T; Sugiyama, S | 1 |
| Bhuyan, AK; Kumar, R | 1 |
| Larsen, RW | 1 |
| Araki, Y; Igarashi, J; Ito, O; Matsui, T; Sagami, I; Sasakura, Y; Shimizu, T; Sugiyama, S; Taguchi, S | 1 |
| Alvarez, DE; Buldain, G; de Montellano, PR; Huang, L; Lad, L; Niemevz, F; Poulos, TL; Wang, J | 1 |
| Alm, E; Arkin, A; Dubchak, I; Gelfand, MS; Rodionov, DA | 1 |
| Shimizu, T; Takahashi, H; Tanaka, A | 1 |
| Al-Shahrour, F; Dopazo, J; Nobre, LS; Saraiva, LM | 1 |
| Alvarez-Cohen, L; Bill, M; Brisson, VL; Conrad, ME; Feng, X; Men, Y; Tang, YJ; Yi, S; Zhuang, WQ | 1 |
| Colaço, HG; Giuffrè, A; Leandro, P; Sarti, P; Vicente, JB | 1 |
| Bowman, HE; Burstyn, JN; Dent, MR | 1 |
| Baratto, MC; Fittipaldi, M; Howes, BD; Milazzo, L; Piro, MC; Pogni, R; Santucci, R; Sinibaldi, F; Smulevich, G; Tognaccini, L | 1 |
| Chen, Y; Cho, GJ; Chung, HT; Joe, Y; Kim, HJ; Kim, J; Kim, SK; Kim, UH; Park, J; Park, SU; Ryter, SW; Ryu, J; Surh, YJ | 1 |
24 other study(ies) available for methionine and carbon monoxide
| Article | Year |
|---|---|
Kinetic studies on [methionine sulphoxide] cytochrome c.
Topics: Carbon Monoxide; Cytochrome c Group; Electron Transport; Isoelectric Focusing; Kinetics; Ligands; Methionine; Oxidation-Reduction; Protein Binding; Sulfoxides | 1976 |
Mutagenesis of methionine-183 drastically affects the physicochemical properties of cytochrome c1 of the bc1 complex of Rhodobacter capsulatus.
Topics: Amino Acid Sequence; Base Sequence; Carbon Monoxide; Chemical Phenomena; Chemistry, Physical; Cytochrome b Group; Cytochromes c1; Electrophoresis, Polyacrylamide Gel; Heme; Iron; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Restriction Mapping; Rhodobacter capsulatus; Spectrophotometry | 1992 |
Carbon monoxide as a probe for conformation changes of ferrocytochrome c.
Topics: Alcohols; Animals; Carbon Monoxide; Chemical Phenomena; Chemistry; Cytochrome c Group; Glycols; Horses; Methionine; Myocardium; Oxidation-Reduction; Protein Conformation; Spectrophotometry; Structure-Activity Relationship; Urea | 1972 |
Kinetics of carbon monoxide binding and electron transfer by cytochrome c polymers.
Topics: Animals; Binding Sites; Carbon Monoxide; Chromatography, Gel; Cytochrome c Group; Electron Transport; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Methionine; Methylation; Models, Biological; Myocardium; Photochemistry; Photolysis; Spectrophotometry; Sulfites | 1974 |
Ligand-specific Bohr effect in haemoglobins.
Topics: Animals; Binding Sites; Carbon Monoxide; Carboxyhemoglobin; Chromatography, Gel; Diphosphoglyceric Acids; Diptera; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Japan; Kinetics; Ligands; Macromolecular Substances; Magnetic Resonance Spectroscopy; Methionine; Oxygen; Oxyhemoglobins; Protein Binding; Protein Conformation; Species Specificity; Time Factors | 1974 |
Heme-linked properties of Euglena cytochrome f.
Topics: Alkylation; Carbon Monoxide; Cyanides; Cytochromes; Euglena; Heme; Hydrogen-Ion Concentration; Iron; Kinetics; Metalloproteins; Methionine; Molecular Conformation; Osmolar Concentration; Oxidation-Reduction; Spectrophotometry; Temperature; Thermodynamics | 1974 |
Studies on chemically modified cytochrome c. 3. The 22-acetyl-cytochrome c.
Topics: Acetates; Animals; Biochemical Phenomena; Biochemistry; Carbon Monoxide; Cattle; Cytochromes; Edetic Acid; Hydrogen-Ion Concentration; Iron; Lysine; Methionine; Oxidation-Reduction; Spectrophotometry; Tryptophan; Tyrosine | 1969 |
Alteration of the microsomal hemoprotein by 3-methylcholanthrene: effects of ethionine and actinomycin D.
Topics: Animals; Benzopyrenes; Carbon Monoxide; Cytochromes; Dactinomycin; Enzyme Induction; Ethionine; Liver; Male; Methionine; Methylcholanthrene; Microsomes; Mixed Function Oxygenases; Phenobarbital; Rats; Solubility; Spectrophotometry | 1968 |
Fast events in protein folding initiated by nanosecond laser photolysis.
Topics: Amino Acid Sequence; Animals; Binding Sites; Carbon Monoxide; Cytochrome c Group; Guanidine; Guanidines; Heme; Horses; Kinetics; Lasers; Methionine; Photolysis; Protein Conformation; Protein Folding; Protein Structure, Secondary; Spectrophotometry; Time Factors | 1993 |
1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae.
Topics: Amino Acid Sequence; Carbon Isotopes; Carbon Monoxide; Dioxygenases; Klebsiella pneumoniae; Methionine; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxygenases; Protons | 1999 |
Study on amino acid composition of HSP70 and the level of plasma free amino acids of workers with long-term exposure to harmful factors.
Topics: Amino Acids; Animals; Carbon Monoxide; Environmental Exposure; Hot Temperature; HSP70 Heat-Shock Proteins; Humans; K562 Cells; Methionine; Mice; Rabbits; Rats; Tryptophan | 1998 |
Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli.
Topics: Carbon Monoxide; Carrier Proteins; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Methionine; Mutation; Oxygen; Phosphoric Diester Hydrolases; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrum Analysis, Raman; Time Factors | 2002 |
Kinetic barriers to the folding of horse cytochrome C in the reduced state.
Topics: Animals; Binding Sites; Carbon Monoxide; Cytochrome c Group; Enzyme Stability; Ferrous Compounds; Guanidine; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Methionine; Models, Chemical; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 2002 |
Ligand binding subsequent to CO photolysis of methionine-modified cytochrome c.
Topics: Animals; Carbon Monoxide; Cytochrome c Group; Horses; Kinetics; Ligands; Methionine; Photolysis | 2003 |
Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli. Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met-95 mutants.
Topics: Carbon Monoxide; Carrier Proteins; Catalysis; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Heme; Kinetics; Light; Methionine; Mutation; Oxidation-Reduction; Oxygen; Phosphoric Diester Hydrolases; Protein Structure, Tertiary; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Time Factors | 2004 |
Human heme oxygenase oxidation of 5- and 15-phenylhemes.
Topics: Animals; Ascorbic Acid; Benzoic Acid; Biliverdine; Carbon Monoxide; Chromatography, High Pressure Liquid; Chromatography, Liquid; Crystallography, X-Ray; Electrons; Esters; Heme; Heme Oxygenase (Decyclizing); Horses; Humans; Ions; Lysine; Mass Spectrometry; Methionine; Models, Chemical; Models, Molecular; Myoglobin; NADPH-Ferrihemoprotein Reductase; Oxidoreductases Acting on CH-CH Group Donors; Oxygen; Spectrophotometry; Stereoisomerism; Time Factors; Ultraviolet Rays | 2004 |
Reconstruction of regulatory and metabolic pathways in metal-reducing delta-proteobacteria.
Topics: Bacterial Proteins; Base Sequence; Biological Transport; Biotin; Carbon Monoxide; Deltaproteobacteria; Desulfovibrio; Energy Metabolism; Gene Expression Regulation, Bacterial; Heat-Shock Proteins; Homeostasis; Iron-Sulfur Proteins; Lysine; Metals; Methionine; Molecular Sequence Data; Oxidation-Reduction; Oxidative Stress; Regulon; Riboflavin; Sulfates; Thiamine; Vitamin B 12 | 2004 |
Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward Cyclic diGMP.
Topics: 3',5'-Cyclic-AMP Phosphodiesterases; Carbon Monoxide; Catalysis; Cyclic GMP; Escherichia coli; Heme; Iron; Ligands; Methionine; Models, Molecular; Nitric Oxide; Oxygen; Phosphoric Diester Hydrolases; Protein Binding; Protein Conformation | 2007 |
Exploring the antimicrobial action of a carbon monoxide-releasing compound through whole-genome transcription profiling of Escherichia coli.
Topics: Biofilms; Carbon Monoxide; Escherichia coli; Escherichia coli Proteins; Gene Expression Profiling; Gene Expression Regulation, Bacterial; Genes, Bacterial; Genes, Regulator; Genetic Complementation Test; Methionine; Microbial Viability; Mutation; Oligonucleotide Array Sequence Analysis; Organometallic Compounds; Phenotype; RNA, Bacterial | 2009 |
Incomplete Wood-Ljungdahl pathway facilitates one-carbon metabolism in organohalide-respiring Dehalococcoides mccartyi.
Topics: Acetate-CoA Ligase; Acetates; Acetyl Coenzyme A; Aerobiosis; Bacteria, Anaerobic; Carbon; Carbon Isotopes; Carbon Monoxide; Coculture Techniques; Computational Biology; Genes, Bacterial; Halogenation; Hydrocarbons, Halogenated; Metabolic Networks and Pathways; Methionine; Methylenetetrahydrofolate Reductase (NADPH2); Pyruvates; Serine | 2014 |
S-Adenosyl-l-methionine Modulates CO and NO• Binding to the Human H2S-generating Enzyme Cystathionine β-Synthase.
Topics: Carbon Monoxide; Cystathionine beta-Synthase; Heme; Humans; Kinetics; Methionine; Nitric Oxide; Oxidation-Reduction; S-Adenosylmethionine | 2016 |
Met(104) is the CO-replaceable ligand at Fe(II) heme in the CO-sensing transcription factor BxRcoM-1.
Topics: Burkholderia; Carbon Monoxide; Ferrous Compounds; Heme; Ligands; Methionine; Transcription Factors | 2016 |
Unravelling the Non-Native Low-Spin State of the Cytochrome c-Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only.
Topics: Animals; Carbon Monoxide; Cardiolipins; Cloning, Molecular; Cytochromes c; Escherichia coli; Gene Expression; Genes, Synthetic; Histidine; Horses; Hydrogen Bonding; Methionine; Myocardium; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Unfolding; Recombinant Proteins; Temperature | 2017 |
Carbon monoxide protects against hepatic steatosis in mice by inducing sestrin-2 via the PERK-eIF2α-ATF4 pathway.
Topics: Activating Transcription Factor 4; AMP-Activated Protein Kinases; Animals; Autophagy; Carbon Monoxide; Choline Deficiency; Disease Models, Animal; eIF-2 Kinase; Eukaryotic Initiation Factor-2; Fatty Liver; Gene Expression Regulation; Hepatocytes; Liver; Male; Mechanistic Target of Rapamycin Complex 1; Methionine; Mice; Mice, Inbred C57BL; Mice, Transgenic; Mitochondria; Nuclear Proteins; Organometallic Compounds; Peroxidases; Primary Cell Culture; Reactive Oxygen Species; RNA, Small Interfering; Signal Transduction | 2017 |