myristic acid has been researched along with heme in 8 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 4 (50.00) | 18.2507 |
2000's | 3 (37.50) | 29.6817 |
2010's | 1 (12.50) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Govindaraj, S; Poulos, TL | 1 |
Gonvindaraj, S; Li, H; Poulos, TL | 1 |
Fulco, AJ; Klein, ML | 1 |
Finnegan, MG; Fujii, H; Johnson, MK | 1 |
Chapman, SK; Cheesman, MR; Fulco, AJ; Gustafsson, MC; Marshall, KR; Munro, AW; Noble, MA; Pessegueiro, A; Roitel, O; von Wachenfeldt, C | 1 |
Ascenzi, P; Bocedi, A; Fanali, G; Fasano, M | 1 |
Ascenzi, P; Coletta, M; De Sanctis, G; Fanali, G; Fasano, M; Gioia, M | 1 |
Dürre, P; Girhard, M; Malca, SH; Schuster, S; Urlacher, VB | 1 |
8 other study(ies) available for myristic acid and heme
Article | Year |
---|---|
Role of the linker region connecting the reductase and heme domains in cytochrome P450BM-3.
Topics: Amino Acid Sequence; Bacillus megaterium; Bacterial Proteins; Binding Sites; Cytochrome P-450 Enzyme System; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Heme; Hydroxylation; Kinetics; Mixed Function Oxygenases; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Myristic Acid; Myristic Acids; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Sequence Deletion; Sequence Homology, Amino Acid | 1995 |
Flavin supported fatty acid oxidation by the heme domain of Bacillus megaterium cytochrome P450BM-3.
Topics: Bacillus megaterium; Bacterial Proteins; Carbon Radioisotopes; Chromatography, High Pressure Liquid; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Heme; Mixed Function Oxygenases; Myristic Acid; Myristic Acids; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Radioisotope Dilution Technique; Spectrophotometry | 1994 |
The interaction of cytochrome c and the heme domain of cytochrome P-450BM-3 with the reductase domain of cytochrome P-450BM-3.
Topics: Bacillus megaterium; Binding Sites; Cytochrome c Group; Cytochrome P-450 Enzyme System; Heme; Hydroxylation; Myristic Acid; Myristic Acids; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction | 1994 |
The active form of the ferric heme in neutrophil cytochrome b(558) is low-spin in the reconstituted cell-free system in the presence of amphophil.
Topics: Animals; Arachidonic Acid; Cell-Free System; Circular Dichroism; Cyanides; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Heme; In Vitro Techniques; Myristic Acid; NADPH Oxidases; Neutrophils; Oxidation-Reduction; Superoxides; Swine | 1999 |
Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.
Topics: Bacillus megaterium; Bacillus subtilis; Bacterial Proteins; Carbon Monoxide; Cloning, Molecular; Coenzymes; Cytochrome P-450 Enzyme System; Fatty Acids; Flavoproteins; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Heme; Hydroxylation; Kinetics; Mixed Function Oxygenases; Myristic Acid; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Binding; Sequence Alignment; Sequence Homology, Amino Acid; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 2004 |
Modulation of heme and myristate binding to human serum albumin by anti-HIV drugs. An optical and NMR spectroscopic study.
Topics: Heme; Humans; Magnetic Resonance Spectroscopy; Models, Molecular; Myristic Acid; Reverse Transcriptase Inhibitors; Serum Albumin | 2007 |
Reversible two-step unfolding of heme-human serum albumin: a (1)H-NMR relaxometric and circular dichroism study.
Topics: Binding Sites; Circular Dichroism; Guanidine; Heme; Humans; Magnetic Resonance Spectroscopy; Models, Molecular; Myristic Acid; Protein Conformation; Protein Denaturation; Protein Folding; Protons; Serum Albumin | 2009 |
Expression, purification and characterization of two Clostridium acetobutylicum flavodoxins: potential electron transfer partners for CYP152A2.
Topics: Bacterial Proteins; Clostridium acetobutylicum; Cytochrome P-450 Enzyme System; Electron Transport; Escherichia coli; Flavodoxin; Gene Expression Regulation, Bacterial; Heme; Hydrogen Peroxide; Hydroxylation; Iron; Kinetics; Myristic Acid; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Protein Binding; Spectrometry, Fluorescence | 2011 |