histidine has been researched along with iodoacetamide in 29 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 11 (37.93) | 18.7374 |
| 1990's | 9 (31.03) | 18.2507 |
| 2000's | 9 (31.03) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Irie, M | 1 |
| Takahashi, K | 1 |
| Hashimoto, J; Takahashi, K | 1 |
| Bereman, RD; Ettinger, MJ; Giordano, RS; Kosman, DJ; Kwiatkowski, LD; Siconolfi, L; Weiner, RE | 1 |
| Gregory, EM | 1 |
| Ishii, S; Yokosawa, H | 1 |
| Chang, JY; Creaser, EH; Hughes, GJ | 1 |
| Carty, RP; Pincus, M; Thi, LL | 1 |
| Jaffar, MB; Kumble, KD; Kumble, S | 1 |
| Davis, JP; Van Etten, RL; Zhang, ZY | 1 |
| Caine, JM; McLeish, MJ | 1 |
| Beuzard, Y; Craescu, CT; Mispelter, J; Schaeffer, C | 1 |
| Harrison, JH; Hodges, CT; Jurgensen, SR | 1 |
| Jordan, F; Polgár, L | 1 |
| Accornero, P; Carrera, G; Curti, B; Vanoni, MA | 1 |
| McGlone, K; McIlhinney, RA; Patel, PB | 1 |
| Hausinger, RP; Park, IS | 1 |
| Lewendon, A; Shaw, WV | 1 |
| Bayley, H; Walker, B | 1 |
| Bobilya, DJ; Tibaduiza, EC | 1 |
| Fukuma, K; Kagami, J; Sankawa, U; Suh, DY | 1 |
| Jez, JM; Noel, JP | 1 |
| Britto, PJ; Knipling, L; Wolff, J | 1 |
| Popov, VO; Savel'eva, ND; Tikhonova, TV | 1 |
| Abdallah, J; Caldas, T; Cha, SS; Eckey, V; Kern, R; Kim, SJ; Malki, A; Mori, H; Richarme, G | 1 |
| Cho, B; Karki, P; Lee, J; Park, IS; Shin, SY | 1 |
| Bishop, B; Born, TL; Huddler, DP; Mutumanje, E; Noble, SM; Ziegler, K | 1 |
| Banerjee, T; Deo, SK; Rahimi, Y; Shrestha, S | 1 |
| He, M; Lou, J; Luo, C; Murray, BW; Ryan, K; Solowiej, J; Thomson, JA | 1 |
1 review(s) available for histidine and iodoacetamide
| Article | Year |
|---|---|
[Studies on the active site of ribonucleases from Aspergillus saitoi (author's transl)].
Topics: Aspergillus; Chemical Phenomena; Chemistry; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Nucleosides; Nucleotides; Oxidation-Reduction; Photochemistry; Ribonucleases; Tryptophan | 1976 |
28 other study(ies) available for histidine and iodoacetamide
| Article | Year |
|---|---|
The structure and function of ribonuclease T1. XXI. Modification of histidine residues in ribonuclease T1 with iodoacetamide.
Topics: Alanine; Amino Acids; Binding Sites; Chymotrypsin; Guanine Nucleotides; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Methylation; Peptides; Ribonuclease T1; Ribonucleases | 1976 |
Chemical modifications of ribonuclease U1.
Topics: Amino Acids; Arginine; Binding Sites; Citraconic Anhydrides; Glutamates; Glyoxal; Guanine Nucleotides; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Lysine; Protein Binding; Ribonuclease T1; Ribonucleases | 1977 |
Histidine as an essential residue in the active site of the copper enzyme galactose oxidase.
Topics: Alcohol Oxidoreductases; Binding Sites; Circular Dichroism; Copper; Cyanides; Electron Spin Resonance Spectroscopy; Galactose Oxidase; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Kinetics; Protein Conformation; Spectrometry, Fluorescence; Spectrophotometry; Spectrophotometry, Ultraviolet | 1977 |
Chemical modification of bovine heart mitochondrial malate dehydrogenase. Selective modification of cysteine and histidine.
Topics: Amino Acids; Animals; Carbon Radioisotopes; Cattle; Cysteine; Ethylmaleimide; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Malate Dehydrogenase; Malates; Mitochondria, Muscle; Molecular Weight; Myocardium; NAD; Oxaloacetates; Urea | 1975 |
Anhydrotrypsin and trypsin: subtle difference in the active-site conformations detected by chemical modification and CD spectroscopy.
Topics: Animals; Binding Sites; Cattle; Circular Dichroism; Guanidines; Histidine; Iodoacetamide; Kinetics; Protein Binding; Species Specificity; Spectrophotometry, Ultraviolet; Streptomyces griseus; Structure-Activity Relationship; Tosyllysine Chloromethyl Ketone; Trypsin | 1977 |
Improved coupling of proteins to the support for solid phase protein sequencing.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Chemical Phenomena; Chemistry; Diazonium Compounds; Glass; Histidine; Histidinol; Iodoacetamide; Proteins; Solubility; Thiocyanates; Tyrosine | 1977 |
The kinetics and specificity of the reaction of 2'(3')-O-bromoacetyluridine with bovine pancreatic ribonuclease A.
Topics: Amino Acids; Animals; Binding Sites; Cattle; Chromatography, Ion Exchange; Histidine; Iodoacetamide; Kinetics; Magnetic Resonance Spectroscopy; Mathematics; Pancreas; Peptide Fragments; Protein Binding; Protein Conformation; Ribonucleases; Spectrophotometry, Ultraviolet; Uridine | 1975 |
Inactivation of a beta-glucosidase from Arthrobotrys conoides by diethyl pyrocarbonate: evidence of histidine at the active site.
Topics: beta-Glucosidase; Binding Sites; Diethyl Pyrocarbonate; Histidine; Iodoacetamide; Mitosporic Fungi; Nitrophenylgalactosides; Pyridoxal Phosphate | 1992 |
Covalent modification and active site-directed inactivation of a low molecular weight phosphotyrosyl protein phosphatase.
Topics: Animals; Arginine; Arsenicals; Binding Sites; Binding, Competitive; Cattle; Cyclohexanones; Cysteine; Epoxy Compounds; Glutathione; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Molecular Weight; Phenylglyoxal; Protein Tyrosine Phosphatases | 1992 |
Chemical modification of PABA synthase.
Topics: Arginine; Cysteine; Diethyl Pyrocarbonate; Escherichia coli; Folic Acid; Histidine; Iodoacetamide; Phenylglyoxal; Sulfhydryl Reagents; Tetranitromethane; Transaminases; Tyrosine | 1991 |
A high resolution NMR study of localized dynamic and structural perturbations in human hemoglobin modified with thiol reagents.
Topics: Adult; Ethylmaleimide; Hemoglobins; Histidine; Humans; Iodoacetamide; Kinetics; Magnetic Resonance Spectroscopy; Sulfhydryl Reagents | 1985 |
Investigation of the pH dependence of proton uptake by porcine heart mitochondrial malate dehydrogenase upon binding of NADH.
Topics: Animals; Binding Sites; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Malate Dehydrogenase; Mitochondria, Heart; NAD; Protein Binding; Protons; Swine | 1980 |
Proton nuclear magnetic resonance evidence for the absence of a stable hydrogen bond between the active site aspartate and histidine residues of native subtilisins and for its presence in thiolsubtilisins.
Topics: Aspartic Acid; Binding Sites; Dithionitrobenzoic Acid; Histidine; Hydrogen Bonding; Iodoacetamide; Magnetic Resonance Spectroscopy; Subtilisins | 1981 |
The pH-dependent behavior of catalytic activities of Azospirillum brasilense glutamate synthase and iodoacetamide modification of the enzyme provide evidence for a catalytic Cys-His ion pair.
Topics: Amino Acid Sequence; Ammonia; Azospirillum brasilense; Catalysis; Cysteine; Glutamate Synthase; Glutamine; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Ketoglutaric Acids; Kinetics; Molecular Sequence Data; NADP; Sequence Analysis | 1994 |
Characterization of a polyhistidine-tagged form of human myristoyl-CoA: protein N-myristoyltransferase produced in Escherichia coli.
Topics: Acylation; Acyltransferases; Amino Acid Sequence; Base Sequence; Diethyl Pyrocarbonate; DNA Primers; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Fatty Acids; Histidine; Humans; Hydrogen-Ion Concentration; Iodoacetamide; Isoelectric Focusing; Kinetics; Molecular Sequence Data; Peptides; Recombinant Proteins; Substrate Specificity | 1994 |
Site-directed mutagenesis of Klebsiella aerogenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding, and catalysis.
Topics: Base Sequence; Binding Sites; Catalysis; Diethyl Pyrocarbonate; DNA, Bacterial; Enzyme Stability; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Kinetics; Klebsiella pneumoniae; Molecular Sequence Data; Mutagenesis, Site-Directed; Nickel; Urease | 1993 |
The pKa of the catalytic histidine residue of chloramphenicol acetyltransferase.
Topics: Benzenesulfonates; Binding Sites; Catalysis; Chloramphenicol O-Acetyltransferase; Cysteine; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Kinetics | 1993 |
Restoration of pore-forming activity in staphylococcal alpha-hemolysin by targeted covalent modification.
Topics: Animals; Bacterial Toxins; Cysteine; Electrophoresis, Polyacrylamide Gel; Erythrocytes; Hemolysin Proteins; Histidine; Iodoacetamide; Mutagenesis, Site-Directed; Point Mutation; Porins; Protein Engineering; Rabbits; Staphylococcus; Temperature | 1995 |
Zinc transport across an endothelium includes vesicular cotransport with albumin.
Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Animals; Biological Transport; Capillary Permeability; Cattle; Cells, Cultured; Endocytosis; Endothelium, Vascular; Ethylmaleimide; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Ionophores; Nigericin; Potassium; Pulmonary Artery; Serum Albumin; Temperature; Zinc | 1996 |
Evidence for catalytic cysteine-histidine dyad in chalcone synthase.
Topics: Acyltransferases; Amino Acid Substitution; Binding Sites; Catalysis; Cysteine; Diethyl Pyrocarbonate; Enzyme Inhibitors; Escherichia coli; Flavanones; Flavonoids; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Malonyl Coenzyme A; Mutagenesis, Site-Directed; Plants; Recombinant Fusion Proteins; Resveratrol; Stilbenes | 2000 |
Mechanism of chalcone synthase. pKa of the catalytic cysteine and the role of the conserved histidine in a plant polyketide synthase.
Topics: Acyltransferases; Alkylating Agents; Anions; Binding Sites; Carboxy-Lyases; Catalysis; Conserved Sequence; Cysteine; Dose-Response Relationship, Drug; Enzyme Inhibitors; Glutamine; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Kinetics; Models, Chemical; Models, Molecular; Protein Binding; Time Factors | 2000 |
The local electrostatic environment determines cysteine reactivity of tubulin.
Topics: Acetamides; Animals; Cysteine; Electrons; Enzyme Inhibitors; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Kinetics; Ligands; Lysine; Mass Spectrometry; Models, Molecular; Palmitic Acids; Peptides; Protein Binding; Rats; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Static Electricity; Sulfides; Time Factors; Trypsin; Tubulin | 2002 |
Chemical modification of catalytically essential functional groups of NAD-dependent hydrogenase from Ralstonia eutropha H16.
Topics: Cupriavidus necator; Cysteine; Diethyl Pyrocarbonate; Histidine; Hydrogen-Ion Concentration; Hydrogenase; Iodoacetamide; Kinetics; NAD | 2003 |
Peptidase activity of the Escherichia coli Hsp31 chaperone.
Topics: Adenosine Triphosphate; Alanine; Arginine; Catalysis; Cations; Chromatography; Chromatography, High Pressure Liquid; Crystallography, X-Ray; Cysteine Endopeptidases; Edetic Acid; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Histidine; Hydrogen-Ion Concentration; Hydrolysis; Iodoacetamide; Kinetics; Lysine; Mass Spectrometry; Molecular Chaperones; Mutation; Peptide Elongation Factor Tu; Peptides; Phenanthrolines; Protein Binding; Substrate Specificity; Temperature; Tryptophanase | 2005 |
Kinetic comparison of procaspase-3 and caspase-3.
Topics: Binding Sites; Caspase 3; Caspases; Catalysis; Crystallography, X-Ray; Cysteine; Diethyl Pyrocarbonate; Enzyme Activation; Enzyme Precursors; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Kinetics; Mutation | 2005 |
Identification of catalytic cysteine, histidine, and lysine residues in Escherichia coli homoserine transsuccinylase.
Topics: Catalysis; Cysteine; Escherichia coli; Histidine; Homoserine O-Succinyltransferase; Hydrogen-Ion Concentration; Iodoacetamide; Lysine; Models, Molecular; Mutagenesis, Site-Directed | 2007 |
Copper sensing based on the far-red fluorescent protein, HcRed, from Heteractis crispa.
Topics: Animals; Biosensing Techniques; Cations, Divalent; Circular Dichroism; Copper; Cysteine; Diethyl Pyrocarbonate; Histidine; Iodoacetamide; Luminescent Proteins; Sea Anemones; Sensitivity and Specificity; Spectrometry, Fluorescence | 2007 |
Steady-state and pre-steady-state kinetic evaluation of severe acute respiratory syndrome coronavirus (SARS-CoV) 3CLpro cysteine protease: development of an ion-pair model for catalysis.
Topics: Acrylates; Alkylation; Catalysis; Coronavirus 3C Proteases; Cysteine; Cysteine Endopeptidases; Dipeptides; Enzyme Activation; Enzyme Inhibitors; Enzyme Stability; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Ions; Kinetics; Models, Biological; Severe acute respiratory syndrome-related coronavirus; Solvents; Static Electricity; Transferases; Viral Proteins | 2008 |