Page last updated: 2024-08-23

heme and 1-pyrenebutanol

heme has been researched along with 1-pyrenebutanol in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (66.67)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Botchkareva, AE; Davydov, DR; Halpert, JR; He, YQ; Kumar, S1
Baas, BJ; Davydov, DR; Halpert, JR; Sligar, SG1
Davydov, DR; Halpert, JR; Rumfeldt, JA; Sineva, EV1

Other Studies

3 other study(ies) available for heme and 1-pyrenebutanol

ArticleYear
An electrostatically driven conformational transition is involved in the mechanisms of substrate binding and cooperativity in cytochrome P450eryF.
    Biochemistry, 2004, Jun-01, Volume: 43, Issue:21

    Topics: Allosteric Site; Amino Acid Substitution; Bacterial Proteins; Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Fluorescence Resonance Energy Transfer; Glutamic Acid; Heme; Mixed Function Oxygenases; Osmolar Concentration; Protein Conformation; Protein Structure, Secondary; Pyrenes; Static Electricity

2004
Allosteric mechanisms in cytochrome P450 3A4 studied by high-pressure spectroscopy: pivotal role of substrate-induced changes in the accessibility and degree of hydration of the heme pocket.
    Biochemistry, 2007, Jul-03, Volume: 46, Issue:26

    Topics: Allosteric Regulation; Bromocriptine; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Heme; Hydrostatic Pressure; Nanotechnology; Principal Component Analysis; Protein Conformation; Pyrenes; Spectrophotometry, Ultraviolet; Testosterone

2007
A large-scale allosteric transition in cytochrome P450 3A4 revealed by luminescence resonance energy transfer (LRET).
    PloS one, 2013, Volume: 8, Issue:12

    Topics: Allosteric Regulation; Bromocriptine; Cytochrome P-450 CYP3A; Heme; Ligands; Luminescent Measurements; Models, Molecular; Mutation; Protein Structure, Secondary; Protein Structure, Tertiary; Pyrenes

2013