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benzohydroxamic acid and mocetinostat

benzohydroxamic acid has been researched along with mocetinostat in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (50.00)18.2507
2000's3 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Dugad, LB; Goff, HM1
Fukuyama, K; Itakura, H; Oda, Y1
Becucci, M; Feis, A; Indiani, C; Marzocchi, MP; Smulevich, G1
Fritz, G; Glatter, O; Hammel, M; Jerlich, A; Kharrazi, H; Schaur, RJ; Tschabuschnig, S1
Chouchane, S; Girotto, S; Kapetanaki, S; Magliozzo, RS; Schelvis, JP; Yu, S1
Gabdoulline, RR; Hallingbäck, HR; Wade, RC1

Other Studies

6 other study(ies) available for benzohydroxamic acid and mocetinostat

ArticleYear
Proton nuclear Overhauser effect study of the heme active site structure of Coprinus macrorhizus peroxidase.
    Biochimica et biophysica acta, 1992, Jul-13, Volume: 1122, Issue:1

    Topics: Binding Sites; Chemical Phenomena; Chemistry, Physical; Coprinus; Cytochrome-c Peroxidase; Heme; Histidine; Horseradish Peroxidase; Hydroxamic Acids; Magnetic Resonance Spectroscopy; Peroxidase

1992
Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X-ray crystallographic analysis of the complex at 1.6 A resolution.
    FEBS letters, 1997, Jul-21, Volume: 412, Issue:1

    Topics: Binding Sites; Crystallography, X-Ray; Hydrogen Bonding; Hydroxamic Acids; Mitosporic Fungi; Models, Molecular; Molecular Sequence Data; Molecular Structure; Peroxidase

1997
Peroxidase-benzhydroxamic acid complexes: spectroscopic evidence that a Fe-H2O distance of 2.6 A can correspond to hexa-coordinate high-spin heme.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 1999, Volume: 4, Issue:1

    Topics: Coprinus; Crystallization; Heme; Horseradish Peroxidase; Hydroxamic Acids; Iron; Isoenzymes; Metmyoglobin; Peroxidase; Recombinant Proteins; Solutions; Spectrum Analysis, Raman; Temperature; Water

1999
Comparison of HOCl traps with myeloperoxidase inhibitors in prevention of low density lipoprotein oxidation.
    Biochimica et biophysica acta, 2000, Aug-31, Volume: 1481, Issue:1

    Topics: Arteriosclerosis; Dose-Response Relationship, Drug; Enzyme Inhibitors; Fluorescence; Glycine; Humans; Hydroxamic Acids; Hydroxybenzoates; Hypochlorous Acid; Lipoproteins, LDL; Methionine; Neutrophils; Peroxidase; Potassium Cyanide; Salicylamides; Sodium Azide; Taurine; Tryptophan

2000
Conformational differences in Mycobacterium tuberculosis catalase-peroxidase KatG and its S315T mutant revealed by resonance Raman spectroscopy.
    Biochemistry, 2003, Apr-08, Volume: 42, Issue:13

    Topics: Amino Acid Substitution; Bacterial Proteins; Benzoates; Binding Sites; Catalase; Drug Resistance, Microbial; Electron Spin Resonance Spectroscopy; Ferric Compounds; Ferrous Compounds; Heme; Hydroxamic Acids; Isoniazid; Mutagenesis, Site-Directed; Mutation; Mycobacterium tuberculosis; Oxidation-Reduction; Peroxidase; Peroxidases; Protein Conformation; Recombinant Proteins; Spectrum Analysis, Raman; Spin Labels

2003
Comparison of the binding and reactivity of plant and mammalian peroxidases to indole derivatives by computational docking.
    Biochemistry, 2006, Mar-07, Volume: 45, Issue:9

    Topics: Animals; Binding Sites; Coumaric Acids; Heme; Horseradish Peroxidase; Hydroxamic Acids; Indoles; Kinetics; Mammals; Melatonin; Models, Molecular; Peroxidase; Peroxidases; Plants; Protein Binding; Serotonin; Static Electricity; Structure-Activity Relationship; Substrate Specificity

2006