iodoacetamide and nitrophenols

iodoacetamide has been researched along with nitrophenols in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19906 (60.00)18.7374
1990's1 (10.00)18.2507
2000's3 (30.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Laue, MC; Quiocho, FA1
Dickinson, FM; Hart, GJ1
Burgum, AA; Matthews, KS; Yang, DS1
Gross, B; Westermann, P1
Asryants, RA; Kuzminskaya, EV; Nagradova, NK1
Barańczyk-Kuźma, A; Ciszewska-Piłczyńska, A1
Day, RA; Kirley, JW1
Gleason, KJ; Hanna, PE; Vath, GM; Wagner, CR; Wang, H1
Alam, M; Gilham, D; Lehner, R; Vance, DE1
Bishop, B; Born, TL; Yusupov, M; Ziegler, K1

Other Studies

10 other study(ies) available for iodoacetamide and nitrophenols

ArticleYear
Spectrochemical and ligand-binding studies of an active mercurinitrophenol-labeled creatine kinase.
    Biochemistry, 1977, Aug-23, Volume: 16, Issue:17

    Topics: Amino Acids; Animals; Chickens; Creatine Kinase; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Kinetics; Ligands; Muscles; Nitrophenols; Organomercury Compounds; Peptide Fragments; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Thiosulfonic Acids

1977
Kinetic properties of aldehyde dehydrogenase from sheep liver mitochondria.
    The Biochemical journal, 1978, Dec-01, Volume: 175, Issue:3

    Topics: Acetaldehyde; Acetates; Aldehyde Oxidoreductases; Aldehydes; Animals; Disulfiram; Hydrolysis; Iodoacetamide; Kinetics; Mitochondria, Liver; NAD; Nitrophenols; Oxidation-Reduction; Sheep; Substrate Specificity

1978
Modification of the cysteine residues of the lactose repressor protein using chromophoric probes.
    Biochimica et biophysica acta, 1977, Jul-22, Volume: 493, Issue:1

    Topics: Acetamides; Bacterial Proteins; Binding Sites; Cysteine; Escherichia coli; Iodoacetamide; Kinetics; Lactose; Nitrophenols; Peptide Fragments; Protein Binding

1977
Studies on proteins of animal ribosomes. XXIV. Localisation of proteins in ribosomal subunits of rat liver studied by chemical substitution with p-nitrophenyl acetate and methyl acetimidate.
    Chemico-biological interactions, 1976, Volume: 15, Issue:4

    Topics: Acetates; Animals; Binding Sites; Imides; Iodoacetamide; Liver; Nitrophenols; Protein Binding; Rats; Ribosomal Proteins; Ribosomes

1976
Rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase: half-of-the-sites reactivity of the enzyme modified at arginine residues.
    Biochemical and biophysical research communications, 1992, Sep-16, Volume: 187, Issue:2

    Topics: Animals; Apoenzymes; Arginine; Binding Sites; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrolysis; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Macromolecular Substances; Muscles; NAD; Nitrophenols; Protein Conformation; Rabbits; Structure-Activity Relationship

1992
Sulfation in male reproductive organs. Bull and boar testis phenol sulfotransferases.
    Biochemical pharmacology, 1989, Dec-01, Volume: 38, Issue:23

    Topics: Animals; Arylsulfotransferase; Cattle; Dithiothreitol; Epinephrine; Ethylmaleimide; Genitalia, Male; Hot Temperature; Hydrogen-Ion Concentration; Iodoacetamide; Male; Nitrophenols; Phenylglyoxal; Substrate Specificity; Swine; Testis

1989
Irreversible inhibition of carbonic anhydrase by the carbon dioxide analog cyanogen.
    Biochemical and biophysical research communications, 1985, Jan-16, Volume: 126, Issue:1

    Topics: Acetates; Acetazolamide; Animals; Carbon Dioxide; Carbonic Anhydrase Inhibitors; Cattle; Dogs; Humans; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Nitriles; Nitrophenols; Pyruvates; Rabbits

1985
Probing the mechanism of hamster arylamine N-acetyltransferase 2 acetylation by active site modification, site-directed mutagenesis, and pre-steady state and steady state kinetic studies.
    Biochemistry, 2004, Jun-29, Volume: 43, Issue:25

    Topics: Acetamides; Acetyl Coenzyme A; Acetylation; Alkylating Agents; Amino Acid Sequence; Amino Acid Substitution; Animals; Arylamine N-Acetyltransferase; Binding Sites; Cricetinae; Cysteine; Deuterium; Enzyme Inhibitors; Hydrogen-Ion Concentration; Iodoacetamide; Isoenzymes; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrophenols; Papain; Protein Conformation; Recombinant Proteins

2004
Mutation of F417 but not of L418 or L420 in the lipid binding domain decreases the activity of triacylglycerol hydrolase.
    Journal of lipid research, 2006, Volume: 47, Issue:2

    Topics: Acylation; Amino Acid Sequence; Animals; Binding Sites; Butyrates; Catalysis; Cell Line; Chlorocebus aethiops; COS Cells; Cysteine; Gene Deletion; Gene Expression; Humans; Hymecromone; Iodoacetamide; Lipase; Mercaptoethanol; Mutagenesis, Site-Directed; Mutation; Nitrophenols; Phenylalanine; Point Mutation; Protein Folding; Recombinant Proteins; Sequence Homology, Amino Acid; Spodoptera; Substrate Specificity; Transfection

2006
Substrate analysis of homoserine acyltransferase from Bacillus cereus.
    Biochemical and biophysical research communications, 2007, Sep-21, Volume: 361, Issue:2

    Topics: Bacillus cereus; Cloning, Molecular; Diethyl Pyrocarbonate; Enzyme Activation; Homoserine; Homoserine O-Succinyltransferase; Hydrogen-Ion Concentration; Iodoacetamide; Kinetics; Methionine; Mutant Proteins; Nitrophenols; Substrate Specificity

2007