nitrosylprotoheme has been researched along with cytochrome c-t in 3 studies
Studies (nitrosylprotoheme) | Trials (nitrosylprotoheme) | Recent Studies (post-2010) (nitrosylprotoheme) | Studies (cytochrome c-t) | Trials (cytochrome c-t) | Recent Studies (post-2010) (cytochrome c-t) |
---|---|---|---|---|---|
25 | 0 | 3 | 11,809 | 21 | 5,125 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (66.67) | 29.6817 |
2010's | 1 (33.33) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bominaar, EL; Hill, BC; Pearce, LL; Peterson, J | 1 |
Basova, LV; Bayir, H; Belikova, NA; Jiang, J; Kagan, VE; Kapralov, AA; Kurnikov, IV; Tyurin, VA; Tyurina, YY; Vladimirov, YA; Vlasova, II; Zhao, Q | 1 |
Bouzhir-Sima, L; Liebl, U; Lobato, L; Vos, MH; Wilson, MT; Yamashita, T | 1 |
3 other study(ies) available for nitrosylprotoheme and cytochrome c-t
Article | Year |
---|---|
Reversal of cyanide inhibition of cytochrome c oxidase by the auxiliary substrate nitric oxide: an endogenous antidote to cyanide poisoning?
Topics: Animals; Brain; Catalysis; Cattle; Copper; Cyanides; Cytochromes c; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Electrons; Heme; Histidine; Iron; Kinetics; Magnetics; Mitochondria; Models, Chemical; Myocardium; Nitric Oxide; Oxygen; Potassium Cyanide; Spectrophotometry | 2003 |
The hierarchy of structural transitions induced in cytochrome c by anionic phospholipids determines its peroxidase activation and selective peroxidation during apoptosis in cells.
Topics: Animals; Apoptosis; Cardiolipins; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Activation; Etoposide; Fluorescence; Heme; Humans; Mice; Peroxidase; Phosphatidic Acids; Phosphatidylcholines; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylinositol Phosphates; Phosphatidylserines; Phospholipids; Protein Structure, Tertiary; Tryptophan | 2007 |
Dynamics of the heme-binding bacterial gas-sensing dissimilative nitrate respiration regulator (DNR) and activation barriers for ligand binding and escape.
Topics: Animals; Bacterial Proteins; Binding Sites; Carbon Monoxide; Cytochromes c; DNA, Bacterial; Fluorescence Polarization; Gene Expression Regulation, Bacterial; Heme; Horses; Kinetics; Ligands; Nitric Oxide; Promoter Regions, Genetic; Protein Binding; Pseudomonas aeruginosa; Transcription Factors | 2014 |