histidine has been researched along with diepoxybutane in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (20.00) | 18.7374 |
1990's | 2 (40.00) | 18.2507 |
2000's | 2 (40.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Maksay, G | 1 |
Billi de Catabbi, S; Ríos de Molina, MC; San Martín de Viale, LC | 1 |
Beaumont, A; Roques, BP | 1 |
Bollettini, M; Lupidi, G; Marmocchi, F; Rotilio, G; Venardi, G | 1 |
Fournel-Gigleux, S; Gulberti, S; Levoin, N; Magdalou, J; Netter, P; Ouzzine, M | 1 |
5 other study(ies) available for histidine and diepoxybutane
Article | Year |
---|---|
Modification of benzodiazepine receptors supports the distinctive role of histidine residues.
Topics: Animals; Azides; Benzodiazepines; Brain; Diethyl Pyrocarbonate; Epoxy Compounds; Histidine; In Vitro Techniques; Male; Rats; Rats, Wistar; Receptors, GABA-A; Structure-Activity Relationship; Tetranitromethane; Tritium | 1992 |
Studies on the active centre of rat liver porphyrinogen carboxylase in vivo effect of hexachlorobenzene.
Topics: Animals; Arginine; Binding Sites; Carboxy-Lyases; Diethyl Pyrocarbonate; Epoxy Compounds; Female; Hexachlorobenzene; Histidine; Hydroxylamine; Hydroxylamines; Liver; Methylene Blue; Photochemistry; Porphyrias; Rats; Rats, Inbred Strains; Spectrophotometry; Uroporphyrinogens | 1991 |
Presence of a histidine at the active site of the neutral endopeptidase-24.11.
Topics: Animals; Binding Sites; Diethyl Pyrocarbonate; Endopeptidases; Epoxy Compounds; Histidine; Imidazoles; Neprilysin; Rabbits; Thermolysin; Time Factors | 1986 |
Functional residues on the enzyme active site of glyoxalase I from bovine brain.
Topics: Animals; Arginine; Binding Sites; Brain; Cattle; Diethyl Pyrocarbonate; Dimerization; Epoxy Compounds; Erythrocytes; Histidine; Humans; Kinetics; Lactoylglutathione Lyase; Molecular Weight; Phenylglyoxal; Spectrometry, Fluorescence; Structure-Activity Relationship; Titrimetry; Tryptophan; Yeasts | 2001 |
The donor substrate specificity of the human beta 1,3-glucuronosyltransferase I toward UDP-glucuronic acid is determined by two crucial histidine and arginine residues.
Topics: Arginine; Base Sequence; DNA Primers; Epoxy Compounds; Glucuronosyltransferase; Histidine; Humans; Models, Molecular; Mutagenesis, Site-Directed; Recombinant Proteins; Substrate Specificity; Uridine Diphosphate Glucuronic Acid | 2002 |