4-hydroxymercuribenzoate has been researched along with cysteine in 22 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 7 (31.82) | 18.7374 |
1990's | 7 (31.82) | 18.2507 |
2000's | 7 (31.82) | 29.6817 |
2010's | 1 (4.55) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
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Bonet, ML; Cadenas, E; Llorca, FI | 1 |
Deshpande, V; Hinge, J; Rao, M | 1 |
Deshpande, VV; Keskar, SS; Srinivasan, MC | 1 |
DeNagel, DC; Slingsby, C; Yu, NT | 1 |
Brooker, RJ; Wilson, TH | 1 |
King, MM | 1 |
Ikeda, Y; Okamura-Ikeda, K; Tanaka, K | 1 |
Gabriel, JL; Pieringer, RA; Soprano, DR; Soprano, KJ; Wolfgang, CL; Zhang, Z | 1 |
Rao, M; Rawat, U | 1 |
Battiston, L; Passamonti, S; Sottocasa, GL | 1 |
Tinguely, JN; Wermuth, B | 1 |
Bates, JN; Hoque, A; Lewis, SJ | 1 |
Chen, A; Fuchs, SY; Gomez, C; Pan, ZQ; Tan, P; Wu, K | 1 |
George, SP; Rao, MB | 1 |
Pitts, KE; Summers, AO | 1 |
LEON, MA | 1 |
JEGANNATHAN, NS; SUBBARAO, PV; VAIDYANATHAN, CS | 1 |
Abramić, M; Cicin-Sain, L; Dolovcak, L; Osmak, M; Simaga, S; Vlahovicek, K; Vukelić, B | 1 |
Ghosh, D; Nakajin, S; Ohno, S; Sugiyama, T | 1 |
Barsacchi, R; Bramanti, E; Neglia, D; Pellegrini, MP; Raspi, G; Vecoli, C | 1 |
Jagtap, S; Rao, M | 1 |
Chen, IY; Kan, HI; Wang, CC; Zulfajri, M | 1 |
22 other study(ies) available for 4-hydroxymercuribenzoate and cysteine
Article | Year |
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Involvement of thiol groups in the reaction mechanism of Mn(2+)-activated alkaline p-nitrophenylphosphate phosphatase of the extreme halophilic archaebacterium Halobacterium halobium.
Topics: 4-Nitrophenylphosphatase; Catalysis; Cations, Divalent; Cysteine; Dithiothreitol; Enzyme Activation; Halobacterium salinarum; Hydrogen-Ion Concentration; Hydroxymercuribenzoates; Kinetics; Manganese; Mercaptoethanol; Potassium Cyanide; Sulfhydryl Compounds | 1992 |
Chemical modification of xylanases: evidence for essential tryptophan and cysteine residues at the active site.
Topics: Bacillus; Binding Sites; Bromosuccinimide; Cysteine; Dithionitrobenzoic Acid; Enzyme Inhibitors; Glycoside Hydrolases; Hot Temperature; Hydroxymercuribenzoates; Kinetics; Streptomyces; Tryptophan; Xylan Endo-1,3-beta-Xylosidase | 1990 |
Chemical modification of a xylanase from a thermotolerant Streptomyces. Evidence for essential tryptophan and cysteine residues at the active site.
Topics: 2-Hydroxy-5-nitrobenzyl Bromide; Binding Sites; Bromosuccinimide; Cysteine; Glycoside Hydrolases; Hot Temperature; Hydroxymercuribenzoates; Streptomyces; Tryptophan; Xylan Endo-1,3-beta-Xylosidase | 1989 |
Raman spectroscopy of calf lens gamma-II crystallin: direct evidence for the formation of mixed disulfide bonds with 2-mercaptoethanol and glutathione.
Topics: Animals; Cattle; Crystallins; Cysteine; Disulfides; Glutathione; Hydroxymercuribenzoates; Mercaptoethanol; Spectrum Analysis, Raman | 1989 |
Site-specific alteration of cysteine 176 and cysteine 234 in the lactose carrier of Escherichia coli.
Topics: Cysteine; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Hydroxymercuribenzoates; Kinetics; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutation; Symporters | 1986 |
Modification of the calmodulin-stimulated phosphatase, calcineurin, by sulfhydryl reagents.
Topics: Animals; Binding Sites; Calcium; Calmodulin-Binding Proteins; Cattle; Cysteine; Dithionitrobenzoic Acid; Ethylmaleimide; Hydroxymercuribenzoates; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Macromolecular Substances; Manganese; Nickel; Sulfhydryl Reagents | 1986 |
An essential cysteine residue located in the vicinity of the FAD-binding site in short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria.
Topics: Acyl-CoA Dehydrogenase, Long-Chain; Amino Acids; Animals; Binding Sites; Chloromercuribenzoates; Cysteine; Ethylmaleimide; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Hydroxymercuribenzoates; Kinetics; Methylmercury Compounds; Mitochondria, Liver; p-Chloromercuribenzoic Acid; Rats; Spectrophotometry | 1985 |
Identification of sulfhydryl-modified cysteine residues in the ligand binding pocket of retinoic acid receptor beta.
Topics: Binding Sites; Blotting, Western; Cysteine; Dithionitrobenzoic Acid; Ethylmaleimide; Hydroxymercuribenzoates; Mutagenesis, Site-Directed; Plasmids; Polymerase Chain Reaction; Protease Inhibitors; Receptors, Retinoic Acid; Retinoic Acid Receptor alpha; Retinoic Acid Receptor gamma; Structure-Activity Relationship; Sulfhydryl Reagents; Tretinoin | 1997 |
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 |
Bilitranslocase can exist in two metastable forms with different affinities for the substrates--evidence from cysteine and arginine modification.
Topics: Animals; Arginine; Bilirubin; Cell Membrane; Ceruloplasmin; Cysteine; Hydroxymercuribenzoates; In Vitro Techniques; Kinetics; Liver; Membrane Proteins; Mercaptoethanol; Rats; Sulfobromophthalein | 1998 |
Identification of the reactive cysteine residue (Cys227) in human carbonyl reductase.
Topics: Alcohol Oxidoreductases; Binding Sites; Circular Dichroism; Cysteine; Enzyme Inhibitors; Escherichia coli; Glutathione; Humans; Hydroxymercuribenzoates; Isoelectric Point; Kinetics; Mutagenesis, Site-Directed; Mutation; Placenta; Protein Binding; Recombinant Proteins; Sodium Chloride; Substrate Specificity | 1999 |
In vivo evidence that L-S-nitrosocysteine may exert its vasodilator effects by interaction with thiol residues in the vasculature.
Topics: Animals; Blood Vessels; Cysteine; Hemodynamics; Hydrazines; Hydroxymercuribenzoates; Male; Nitroprusside; Nitroso Compounds; Rats; Rats, Sprague-Dawley; S-Nitrosothiols; Sulfhydryl Compounds; Vasodilation; Vasodilator Agents | 1999 |
The conserved RING-H2 finger of ROC1 is required for ubiquitin ligation.
Topics: Amino Acid Sequence; Amino Acid Substitution; Anaphase-Promoting Complex-Cyclosome; Animals; Binding Sites; Cell Line; Conserved Sequence; Cysteine; Humans; Hydroxymercuribenzoates; Kinetics; Ligases; Mercuric Chloride; Mice; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Fusion Proteins; Sulfhydryl Reagents; Transfection; Ubiquitin-Conjugating Enzymes; Ubiquitin-Protein Ligase Complexes; Ubiquitin-Protein Ligases; Ubiquitins | 2000 |
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 |
The roles of thiols in the bacterial organomercurial lyase (MerB).
Topics: Amino Acid Sequence; Bacterial Proteins; Cysteine; Cytosol; Dithionitrobenzoic Acid; Dithiothreitol; Enzyme Activation; Ethylmaleimide; Glutathione; Hydroxymercuribenzoates; Iodoacetamide; Kinetics; Lyases; Molecular Sequence Data; Mutagenesis, Site-Directed; Organomercury Compounds; Sequence Homology, Amino Acid; Substrate Specificity; Sulfhydryl Compounds | 2002 |
COMPLEMENT: INACTIVATION OF SECOND COMPONENT BY P-HYDROXYMERCURIBENZOATE.
Topics: Benzoates; Centrifugation; Chemical Precipitation; Chromatography; Complement System Proteins; Cysteine; Dialysis; Edetic Acid; Hydroxymercuribenzoates; Indicators and Reagents; Pharmacology; Renal Dialysis; Research; Solutions; Sulfhydryl Compounds | 1965 |
ENZYMIC CONVERSION OF 3-HYDROXYANTHRANILIC ACID INTO CINNABARINIC ACID BY THE NUCLEAR FRACTION OF RAT LIVER.
Topics: 3-Hydroxyanthranilic Acid; Arsenicals; Benzoates; Cell Nucleus; Copper; Cysteine; Enzyme Inhibitors; Glutathione; Hydroxymercuribenzoates; Iron; Liver; Mercury; Metabolism; Molybdenum; ortho-Aminobenzoates; Oxazines; Oxidoreductases; Pharmacology; Rats; Research; Silver | 1965 |
Highly reactive cysteine residues are part of the substrate binding site of mammalian dipeptidyl peptidases III.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cysteine; Dipeptides; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; Erythrocytes; Female; Glutathione; Humans; Hydrogen Peroxide; Hydroxymercuribenzoates; Kidney; Kinetics; Molecular Sequence Data; Protease Inhibitors; Rats; Rats, Inbred Strains; Sequence Alignment; Sulfhydryl Compounds; Sulfhydryl Reagents | 2004 |
3alpha/beta,20beta-hydroxysteroid dehydrogenase (porcine testicular carbonyl reductase) also has a cysteine residue that is involved in binding of cofactor NADPH.
Topics: 20-Hydroxysteroid Dehydrogenases; Animals; Binding Sites; Cysteine; Dithionitrobenzoic Acid; Hydroxymercuribenzoates; Kinetics; Models, Molecular; NADP; Point Mutation; Protein Binding; Swine | 2004 |
Speciation and quantification of thiols by reversed-phase chromatography coupled with on-line chemical vapor generation and atomic fluorescence spectrometric detection: method validation and preliminary application for glutathione measurements in human wh
Topics: Autoanalysis; Cardiomyopathy, Dilated; Chromatography, Liquid; Cysteine; Dipeptides; Exercise Test; Glutathione; Glutathione Disulfide; Heart Rate; Homocysteine; Humans; Hydroxymercuribenzoates; Indicators and Reagents; S-Nitrosoglutathione; Spectrometry, Fluorescence; Spectrophotometry, Atomic; Sulfhydryl Compounds | 2005 |
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 |
Subunit disassembly pathway of human hemoglobin revealing the site-specific role of its cysteine residues.
Topics: Cysteine; Hemoglobins; Humans; Hydroxymercuribenzoates; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2013 |