trimethyloxamine has been researched along with heme in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (50.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cotter, PA; Gunsalus, RP; Park, SJ | 1 |
| Giordano, G; Iobbi-Nivol, C; Méjean, V; Pommier, J | 1 |
| Bhattacharya, S; Falzone, CJ; Lecomte, JT; Scott, NL; Vu, BC; Wang, Y | 1 |
| Kraus, JP; Kruger, WD; Majtan, T; Singh, LR; Wang, L | 1 |
4 other study(ies) available for trimethyloxamine and heme
| Article | Year |
|---|---|
Regulation of malate dehydrogenase (mdh) gene expression in Escherichia coli in response to oxygen, carbon, and heme availability.
Topics: 2,2'-Dipyridyl; Aerobiosis; Anaerobiosis; Bacterial Outer Membrane Proteins; Bacterial Proteins; Carbon; Culture Media; Escherichia coli; Escherichia coli Proteins; Fumarates; Gene Expression Regulation, Bacterial; Glycerol; Heme; Iron Chelating Agents; Iron-Sulfur Proteins; Malate Dehydrogenase; Methylamines; Oxidants; Oxygen; Recombinant Fusion Proteins; Repressor Proteins | 1995 |
TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli.
Topics: Amino Acid Sequence; Bacterial Proteins; Cytoplasm; Escherichia coli; Escherichia coli Proteins; Heme; Methylamines; Molecular Chaperones; Molecular Sequence Data; Oxidoreductases, N-Demethylating; Protein Folding; Sequence Alignment; Transcription, Genetic | 1998 |
Structural and dynamic perturbations induced by heme binding in cytochrome b5.
Topics: Alanine; Amino Acid Substitution; Animals; Apoproteins; Carbon Monoxide; Crystallography, X-Ray; Cytochrome b Group; Cytochromes b; Cytochromes b5; Heme; Histidine; Macromolecular Substances; Methylamines; Nuclear Magnetic Resonance, Biomolecular; Oxidants; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Rats; Thermodynamics | 2001 |
Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone.
Topics: Allosteric Site; Cobalt; Cystathionine beta-Synthase; Escherichia coli; Heme; Homocysteine; Humans; Manganese; Metals; Methylamines; Porphyrins; Protein Denaturation; Protein Folding; Recombinant Proteins; S-Adenosylmethionine; Saccharomyces cerevisiae | 2008 |