lysine has been researched along with 4-hydroxymercuribenzoate in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (40.00) | 18.7374 |
| 1990's | 1 (20.00) | 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 |
|---|---|
| Müller, RE; Traish, AM | 1 |
| Balinsky, JB; Peiser, L | 1 |
| Rao, M; Rawat, U | 1 |
| George, SP; Rao, MB | 1 |
| Jagtap, S; Rao, M | 1 |
1 review(s) available for lysine and 4-hydroxymercuribenzoate
| Article | Year |
|---|---|
The role of lysyl, arginyl, and sulfhydryl residues in estrogen receptor activation, 4S to 5S dimerization, and conversion of receptor from a state with low affinity into a state with higher affinity for estrogen.
Topics: Alkylation; Animals; Arginine; Cell Nucleus; Cyclohexanones; Dose-Response Relationship, Drug; Hydroxymercuribenzoates; Kinetics; Lysine; Mersalyl; Molecular Weight; Polymers; Protein Conformation; Pyridoxal Phosphate; Receptors, Estrogen; Structure-Activity Relationship; Sulfhydryl Compounds | 1986 |
4 other study(ies) available for lysine and 4-hydroxymercuribenzoate
| Article | Year |
|---|---|
Kinetic properties of arginase from Xenopus laevis.
Topics: Animals; Arginase; Canavanine; Enzyme Activation; Hydroxymercuribenzoates; Kinetics; Liver; Lysine; Manganese; Ornithine; Xenopus laevis | 1982 |
Site and significance of cysteine residues in xylose reductase from Neurospora crassa as deduced by fluorescence studies.
Topics: Aldehyde Reductase; Binding Sites; Binding, Competitive; Circular Dichroism; Cysteine; Enzyme Activation; Hydroxymercuribenzoates; Kinetics; Lysine; Neurospora crassa; o-Phthalaldehyde; Protein Conformation; Spectrometry, Fluorescence; Substrate Specificity | 1997 |
Conformation and polarity of the active site of xylanase I from Thermomonospora sp. as deduced by fluorescent chemoaffinity labeling. Site and significance of a histidine residue.
Topics: Actinomycetales; Affinity Labels; Amino Acids; Binding Sites; Circular Dichroism; Cysteine; Diethyl Pyrocarbonate; Dithionitrobenzoic Acid; Dose-Response Relationship, Drug; Enzyme Activation; Ethylmaleimide; Histidine; Hydroxymercuribenzoates; Indicators and Reagents; Kinetics; Lysine; Models, Chemical; o-Phthalaldehyde; Protease Inhibitors; Protein Binding; Protein Conformation; Sequence Analysis, Protein; Spectrometry, Fluorescence; Sulfhydryl Reagents; Time Factors; Trinitrobenzenesulfonic Acid; Urea; Xylan Endo-1,3-beta-Xylosidase; Xylosidases | 2001 |
Conformation and microenvironment of the active site of a low molecular weight 1,4-beta-D-glucan glucanohydrolase from an alkalothermophilic Thermomonospora sp.: involvement of lysine and cysteine residues.
Topics: Actinomycetales; Binding Sites; Carboxymethylcellulose Sodium; Circular Dichroism; Cysteine; Dose-Response Relationship, Drug; Enzyme Activation; Glucan 1,4-beta-Glucosidase; Hydroxymercuribenzoates; Kinetics; Lysine; Molecular Sequence Data; Molecular Weight; Protein Conformation; Sequence Alignment; Substrate Specificity; Trinitrobenzenesulfonic Acid | 2006 |