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An updated view on horseradish peroxidases: recombinant production and biotechnological applications
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inferredcites →https://doi.org/10.1002/(sici)1097-0290(19960620)50:6<655::aid-bit6>3.0.co;2-jopenalex-snapshot
A comparative study of the purity, enzyme activity, and inactivation by hydrogen peroxide of commercially available horseradish peroxidase isoenzymes A and C
inferredcites →https://doi.org/10.1002/bit.1149openalex-snapshot
Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1002/bit.1194openalex-snapshot
Location of crosslinks in chemically stabilized horseradish peroxidase: Implications for design of crosslinks
inferredcites →https://doi.org/10.1002/bit.20851openalex-snapshot
Engineering of Pichia pastoris for improved production of antibody fragments
inferredcites →https://doi.org/10.1002/bit.25483openalex-snapshot
Engineering a horseradish peroxidase C stable to radical attacks by mutating multiple radical coupling sites
inferredcites →https://doi.org/10.1002/elps.11501401163openalex-snapshot
The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences
inferredcites →https://doi.org/10.1002/elps.1150150171openalex-snapshot
Reference points for comparisons of two‐dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions
inferredcites →https://doi.org/10.1002/jcb.10292openalex-snapshot
Mechanisms of cytotoxicity induced by horseradish peroxidase/indole‐3‐acetic acid gene therapy
inferredcites →https://doi.org/10.1006/abbi.1997.0559openalex-snapshot
Horseradish Peroxidase: Partial Rescue of the His-42 → Ala Mutant by a Concurrent Asn-70 → Asp Mutation
inferredcites →https://doi.org/10.1006/abbi.2001.2460openalex-snapshot
Catalase-like Oxygen Production by Horseradish Peroxidase Must Predominantly Be an Enzyme-Catalyzed Reaction
inferredcites →https://doi.org/10.1006/abio.1995.1313openalex-snapshot
Mild Chemical Deglycosylation of Horseradish Peroxidase Yields a Fully Active, Homogeneous Enzyme
inferredcites →https://doi.org/10.1007/bf00240725openalex-snapshot
Excretion of peroxidase from horseradish hairy root in combination with ion supplementation
inferredcites →https://doi.org/10.1007/s00216-013-7081-0openalex-snapshot
A new approach for quantitative analysis of l-phenylalanine using a novel semi-sandwich immunometric assay
inferredcites →https://doi.org/10.1007/s00216-014-8257-yopenalex-snapshot
A cellulose-based bioassay for the colorimetric detection of pathogen DNA
inferredcites →https://doi.org/10.1007/s00253-003-1273-zopenalex-snapshot
Vesicular transport route of horseradish C1a peroxidase is regulated by N- and C-terminal propeptides in tobacco cells
inferredcites →https://doi.org/10.1007/s00253-014-5856-7openalex-snapshot
Heterologous production of horseradish peroxidase C1a by the basidiomycete yeast Cryptococcus sp. S-2 using codon and signal optimizations
inferredcites →https://doi.org/10.1007/s00299-005-0972-6openalex-snapshot
Peroxidases have more functions than a Swiss army knife
inferredcites →https://doi.org/10.1007/s00449-008-0207-7openalex-snapshot
A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization
inferredcites →https://doi.org/10.1007/s00449-011-0543-xopenalex-snapshot
Amperometric biosensor for hydrogen peroxide based on horseradish peroxidase onto gold nanowires and TiO2 nanoparticles
inferredcites →https://doi.org/10.1007/s00449-012-0724-2openalex-snapshot
Cross-linking of horseradish peroxidase adsorbed on polycationic films: utilization for direct dye degradation
inferredcites →https://doi.org/10.1007/s007750100219openalex-snapshot
The inactivation of horseradish peroxidase isoenzyme AZ by hydrogen peroxide: an example of partial resistance due to the formation of a stable enzyme intermediate
inferredcites →https://doi.org/10.1007/s10529-006-0018-3openalex-snapshot
Co-lyophilization with d-proline Greatly Enhances Peroxidase’s Stereoselectivity in a Non-aqueous Medium
inferredcites →https://doi.org/10.1007/s10529-011-0540-9openalex-snapshot
Rachiplusia nu larva as a biofactory to achieve high level expression of horseradish peroxidase
inferredcites →https://doi.org/10.1007/s10529-014-1664-5openalex-snapshot
Horseradish peroxidase-encapsulated chitosan nanoparticles for enzyme-prodrug cancer therapy
inferredcites →https://doi.org/10.1007/s12010-014-1222-6openalex-snapshot
Evaluation of Textile Dye Degradation Due to the Combined Action of Enzyme Horseradish Peroxidase and Hydrogen Peroxide
inferredcites →https://doi.org/10.1007/s12010-014-1320-5openalex-snapshot
Techno-Economic Analysis of Horseradish Peroxidase Production Using a Transient Expression System in Nicotiana benthamiana
inferredcites →https://doi.org/10.1007/s12033-012-9588-6openalex-snapshot
Studies on the Refolding Process of Recombinant Horseradish Peroxidase
inferredcites →https://doi.org/10.1016/0003-9861(52)90470-0openalex-snapshot
The kinetics and stoichiometry of the transition from the primary to the secondary peroxidase peroxide complexes
inferredcites →https://doi.org/10.1016/0003-9861(53)90373-7openalex-snapshot
Flavoprotein and peroxidase as components of the indoleacetic acid oxidase system of peas
inferredcites →https://doi.org/10.1016/0003-9861(73)90043-xopenalex-snapshot
The reaction between indole 3-acetic acid and horseradish peroxidase
inferredcites →https://doi.org/10.1016/0003-9861(90)90754-mopenalex-snapshot
Enzymatic generation of triplet acetone by deglycosylated horseradish peroxidase
inferredcites →https://doi.org/10.1016/0003-9861(92)90641-9openalex-snapshot
Baculovirus expression and characterization of catalytically active horseradish peroxidase
inferredcites →https://doi.org/10.1016/0005-2744(74)90504-xopenalex-snapshot
The substrate profiles of the acidic and slightly basic horseradish peroxidases
inferredcites →https://doi.org/10.1016/0008-6215(96)00073-0openalex-snapshot
The glycans of horseradish peroxidase
inferredcites →https://doi.org/10.1016/0014-5793(76)80804-6openalex-snapshot
Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)
inferredcites →https://doi.org/10.1016/0040-4039(95)00713-mopenalex-snapshot
An efficient peroxidase-catalyzed oxidation of hydroxylaminoeverninomicin in aqueous-organic media
inferredcites →https://doi.org/10.1016/0040-4039(96)00504-7openalex-snapshot
Oxidation of arylamidoximes by hydrogen peroxide and horseradish peroxidase in water: Easy preparation and X-ray structure of O-(arylimidoyl)arylamidoximes
inferredcites →https://doi.org/10.1016/0167-4781(91)90060-yopenalex-snapshot
The cDNA sequence of a neutral horseradish peroxidase
inferredcites →https://doi.org/10.1016/0167-4838(90)90014-7openalex-snapshot
Inactivation of peroxidase by hydrogen peroxide and its protection by a reductant agent
inferredcites →https://doi.org/10.1016/0167-4838(90)90120-5openalex-snapshot
A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide
inferredcites →https://doi.org/10.1016/0168-1656(89)90019-9openalex-snapshot
Expression and characterisation of a protein specified by a synthetic horseradish peroxidase gene inEscherichia coli
inferredcites →https://doi.org/10.1016/0378-1119(90)90002-9openalex-snapshot
Genomic DNA structure of two new horseradish-peroxidase-encoding genes
inferredcites →https://doi.org/10.1016/0922-338x(94)90177-5openalex-snapshot
Growth-stimulation of tobacco plant introduced the horseradish peroxidase gene prxC1a
inferredcites →https://doi.org/10.1016/j.ab.2014.06.006openalex-snapshot
Continuous colorimetric screening assay for detection of d-amino acid aminotransferase mutants displaying altered substrate specificity
inferredcites →https://doi.org/10.1016/j.abb.2010.04.018openalex-snapshot
Mechanisms of catalase activity of heme peroxidases
inferredcites →https://doi.org/10.1016/j.aca.2005.05.037openalex-snapshot
Biosensor based on platinum chips for glucose determination
inferredcites →https://doi.org/10.1016/j.biochi.2007.03.013openalex-snapshot
Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide
inferredcites →https://doi.org/10.1016/j.biochi.2008.04.009openalex-snapshot
Consensus mutagenesis reveals that non-helical regions influence thermal stability of horseradish peroxidase
inferredcites →https://doi.org/10.1016/j.biochi.2008.05.008openalex-snapshot
Effects of mutations in the helix G region of horseradish peroxidase
inferredcites →https://doi.org/10.1016/j.biochi.2014.05.012openalex-snapshot
Stability properties of an ancient plant peroxidase
inferredcites →https://doi.org/10.1016/j.bioelechem.2012.12.004openalex-snapshot
Development of an amperometric biosensor based on peroxidases to quantify citrinin in rice samples
inferredcites →https://doi.org/10.1016/j.bios.2004.09.030openalex-snapshot
Ethanol biosensors based on alcohol oxidase
inferredcites →https://doi.org/10.1016/j.bios.2008.06.004openalex-snapshot
A novel hydrogen peroxide biosensor based on the immobilization of horseradish peroxidase onto Au-modified titanium dioxide nanotube arrays
inferredcites →https://doi.org/10.1016/j.bios.2009.03.020openalex-snapshot
Protein chips and nanomaterials for application in tumor marker immunoassays
inferredcites →https://doi.org/10.1016/j.bios.2013.03.027openalex-snapshot
Qualitative and quantitative detection of DNA amplified with HRP-modified SiO2 nanoparticles using scanning electrochemical microscopy
inferredcites →https://doi.org/10.1016/j.bios.2014.06.014openalex-snapshot
An electrochemical ELISA-like immunosensor for miRNAs detection based on screen-printed gold electrodes modified with reduced graphene oxide and carbon nanotubes
inferredcites →https://doi.org/10.1016/j.bios.2014.07.016openalex-snapshot
A sensitive electrochemical biosensor for detection of protein kinase A activity and inhibitors based on Phos-tag and enzymatic signal amplification
inferredcites →https://doi.org/10.1016/j.carbpol.2014.05.010openalex-snapshot
Horseradish peroxidase-catalyzed formation of hydrogels from chitosan and poly(vinyl alcohol) derivatives both possessing phenolic hydroxyl groups
inferredcites →https://doi.org/10.1016/j.chemosphere.2006.10.043openalex-snapshot
Treatment of phenolic wastewater by horseradish peroxidase immobilized by bioaffinity layering
inferredcites →https://doi.org/10.1016/j.chemosphere.2013.04.071openalex-snapshot
A novel mechanism of bisphenol A removal during electro-enzymatic oxidative process: Chain reactions from self-polymerization to cross-coupling oxidation
inferredcites →https://doi.org/10.1016/j.enzmictec.2013.02.010openalex-snapshot
A novel electrochemical biosensor based on horseradish peroxidase immobilized on Ag-nanoparticles/poly(l-arginine) modified carbon paste electrode toward the determination of pyrogallol/hydroquinone
inferredcites →https://doi.org/10.1016/j.enzmictec.2013.10.002openalex-snapshot
A two-stage enzymatic synthesis of conductive poly(3,4-ethylenedioxythiophene)
inferredcites →https://doi.org/10.1016/j.febslet.2006.01.073openalex-snapshot
Hydrogen peroxide is a mediator of indole‐3‐acetic acid/horseradish peroxidase‐induced apoptosis
inferredcites →https://doi.org/10.1016/j.gene.2013.01.062openalex-snapshot
The effect of α-mating factor secretion signal mutations on recombinant protein expression in Pichia pastoris
inferredcites →https://doi.org/10.1016/j.ijbiomac.2008.12.002openalex-snapshot
Application of immobilized horseradish peroxidase onto modified acrylonitrile copolymer membrane in removing of phenol from water
inferredcites →https://doi.org/10.1016/j.ijbiomac.2014.05.065openalex-snapshot
Enzyme–polysaccharide interaction: A method for improved stability of horseradish peroxidase
inferredcites →https://doi.org/10.1016/j.jbiotec.2005.05.015openalex-snapshot
Genetically engineered horseradish peroxidase for facilitated purification from baculovirus cultures by cation-exchange chromatography
inferredcites →https://doi.org/10.1016/j.jhazmat.2007.06.003openalex-snapshot
Toxicity of textile dyes and their degradation by the enzyme horseradish peroxidase (HRP)
inferredcites →https://doi.org/10.1016/j.jhazmat.2007.12.008openalex-snapshot
Enzymatic removal of phenol and p-chlorophenol in enzyme reactor: Horseradish peroxidase immobilized on magnetic beads
inferredcites →https://doi.org/10.1016/j.jhazmat.2008.12.026openalex-snapshot
Phenols removal by immobilized horseradish peroxidase
inferredcites →https://doi.org/10.1016/j.jhazmat.2013.04.023openalex-snapshot
Sonoenzymatic decolourization of an azo dye employing immobilized horse radish peroxidase (HRP): A mechanistic study
inferredcites →https://doi.org/10.1016/j.jviromet.2014.08.012openalex-snapshot
Development of an enzyme-linked immunospot assay for determination of rotavirus infectivity
inferredcites →https://doi.org/10.1016/j.leukres.2010.11.025openalex-snapshot
Antibody-targeted horseradish peroxidase associated with indole-3-acetic acid induces apoptosis in vitro in hematological malignancies
inferredcites →https://doi.org/10.1016/j.nbt.2010.06.019openalex-snapshot
Recombinant peroxidase production in species of lepidoptera frequently found in Argentina
inferredcites →https://doi.org/10.1016/j.pep.2003.12.001openalex-snapshot
System for the expression of recombinant hemoproteins in Escherichia coli
inferredcites →https://doi.org/10.1016/j.pep.2012.09.008openalex-snapshot
Purification of a recombinant plant peroxidase produced in Pichia pastoris by a simple 2-step strategy
inferredcites →https://doi.org/10.1016/j.pep.2013.12.003openalex-snapshot
Purification and basic biochemical characterization of 19 recombinant plant peroxidase isoenzymes produced in Pichia pastoris
inferredcites →https://doi.org/10.1016/j.plaphy.2005.11.002openalex-snapshot
Transgenic tobacco (Nicotiana tabacum L. cv. Samsun-NN) plants over-expressing a synthetic HRP-C gene are altered in growth, development and susceptibility to abiotic stress
inferredcites →https://doi.org/10.1016/j.procbio.2004.02.009openalex-snapshot
High-level expression and purification of recombinant horseradish peroxidase isozyme C in SF-9 insect cell culture
inferredcites →https://doi.org/10.1016/j.talanta.2009.03.015openalex-snapshot
A novel amperometric biosensor for the detection of nitrophenol
inferredcites →https://doi.org/10.1016/j.talanta.2014.05.020openalex-snapshot
Rapid chemiluminescent sandwich enzyme immunoassay capable of consecutively quantifying multiple tumor markers in a sample
inferredcites →https://doi.org/10.1016/j.talanta.2014.06.069openalex-snapshot
Nanoimmunoassay onto a screen printed electrode for HER2 breast cancer biomarker determination
inferredcites →https://doi.org/10.1016/j.talanta.2014.07.076openalex-snapshot
Electrochemical magnetoimmunosensing platform for determination of the milk allergen β-lactoglobulin
inferredcites →https://doi.org/10.1016/j.tet.2012.06.062openalex-snapshot
Development of a high-throughput screening method for racemase activity and its application to the identification of alanine racemase variants with activity towards l-arginine
inferredcites →https://doi.org/10.1016/j.tibtech.2006.06.007openalex-snapshot
Horseradish and soybean peroxidases: comparable tools for alternative niches?
inferredcites →https://doi.org/10.1016/j.toxlet.2003.12.067openalex-snapshot
The mechanism of indole acetic acid cytotoxicity
inferredcites →https://doi.org/10.1016/j.watres.2005.11.017openalex-snapshot
Horseradish peroxidase immobilized on aluminum-pillared interlayered clay for the catalytic oxidation of phenolic wastewater
inferredcites →https://doi.org/10.1016/s0006-2952(00)00498-6openalex-snapshot
Oxidative activation of indole-3-acetic acids to cytotoxic species— a potential new role for plant auxins in cancer therapy11Abbreviations: IAA, indole-3-acetic acid; HRP, horseradish peroxidase; TBA, thiobarbituric acid; MPO, myeloperoxidase; MOI, 3-methylene-2-oxindole; BSO, buthionine…
inferredcites →https://doi.org/10.1016/s0006-2952(98)00323-2openalex-snapshot
Peroxidase-catalyzed effects of indole-3-acetic acid and analogues on lipid membranes, DNA, and mammalian cells in vitro
inferredcites →https://doi.org/10.1016/s0014-5793(97)01573-1openalex-snapshot
Glycosylation and thermodynamic versus kinetic stability of horseradish peroxidase
inferredcites →https://doi.org/10.1016/s0021-9258(18)62046-0openalex-snapshot
Peroxidase Isoenzymes from Horseradish Roots
inferredcites →https://doi.org/10.1016/s0021-9258(18)68201-8openalex-snapshot
Singlet oxygen production from the peroxidase-catalyzed oxidation of indole-3-acetic acid.
inferredcites →https://doi.org/10.1016/s0021-9258(18)95985-5openalex-snapshot
Peroxidase Isozymes from Horseradish Roots
inferredcites →https://doi.org/10.1016/s0021-9258(18)96680-9openalex-snapshot
Peroxidase Isozymes from Horseradish Roots
inferredcites →https://doi.org/10.1016/s0021-9258(19)34177-8openalex-snapshot
Peroxidase Isoenzymes from Horseradish Roots
inferredcites →https://doi.org/10.1016/s0021-9258(19)38303-6openalex-snapshot
Expression of a synthetic gene for horseradish peroxidase C in Escherichia coli and folding and activation of the recombinant enzyme with Ca2+ and heme.
inferredcites →https://doi.org/10.1016/s0021-9258(19)70630-9openalex-snapshot
The stereochemistry of peroxidase catalysis.
inferredcites →https://doi.org/10.1016/s0167-7799(98)01288-8openalex-snapshot
Recent biotechnological developments in the use of peroxidases
inferredcites →https://doi.org/10.1016/s0360-3016(98)00297-1openalex-snapshot
Toward targeted “oxidation therapy” of cancer: peroxidase-catalysed cytotoxicity of indole-3-acetic acids
inferredcites →https://doi.org/10.1016/s0378-1119(02)00465-1openalex-snapshot
Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana
inferredcites →https://doi.org/10.1016/s0898-6568(03)00091-3openalex-snapshot
Oxidation of indole-3-acetic acid by horseradish peroxidase induces apoptosis in G361 human melanoma cells
inferredcites →https://doi.org/10.1016/s1387-2656(03)09003-3openalex-snapshot
Horseradish peroxidase: a valuable tool in biotechnology
inferredcites →https://doi.org/10.1021/bi010661oopenalex-snapshot
Differential Activity and Structure of Highly Similar Peroxidases. Spectroscopic, Crystallographic, and Enzymatic Analyses of Lignifying Arabidopsis thaliana Peroxidase A2 and Horseradish Peroxidase A2,
inferredcites →https://doi.org/10.1021/bi9609331openalex-snapshot
Rescue of the Horseradish Peroxidase His-170 → Ala Mutant Activity by Imidazole: Importance of Proximal Ligand Tethering
inferredcites →https://doi.org/10.1021/bi9725780openalex-snapshot
Improvement of Peroxygenase Activity by Relocation of a Catalytic Histidine within the Active Site of Horseradish Peroxidase
inferredcites →https://doi.org/10.1021/bi980234jopenalex-snapshot
Structural Interactions between Horseradish Peroxidase C and the Substrate Benzhydroxamic Acid Determined by X-ray Crystallography,
inferredcites →https://doi.org/10.1021/bm005537jopenalex-snapshot
Enzyme-Mediated Free Radical Polymerization of Styrene
inferredcites →https://doi.org/10.1021/bm005576vopenalex-snapshot
Horseradish Peroxidase Mediated Free Radical Polymerization of Methyl Methacrylate
inferredcites →https://doi.org/10.1021/ja00089a052openalex-snapshot
Molecular Engineering of Horseradish Peroxidase. Highly Enantioselective Sulfoxidation of Aryl Alkyl Sulfides by the Phe-41 .fwdarw. Leu Mutant
inferredcites →https://doi.org/10.1021/ja00132a003openalex-snapshot
Molecular Engineering of Horseradish Peroxidase: Thioether Sulfoxidation and Styrene Epoxidation by Phe-41 Leucine and Threonine Mutants
inferredcites →https://doi.org/10.1021/ja012075oopenalex-snapshot
Binding of Hydrophobic Hydroxamic Acids Enhances Peroxidase's Stereoselectivity in Nonaqueous Sulfoxidations
inferredcites →https://doi.org/10.1021/ja0676861openalex-snapshot
The Effect of a Water Molecule on the Mechanism of Formation of Compound 0 in Horseradish Peroxidase
inferredcites →https://doi.org/10.1021/ja903482uopenalex-snapshot
How a Single-Point Mutation in Horseradish Peroxidase Markedly Enhances Enantioselectivity
inferredcites →https://doi.org/10.1021/jp055412eopenalex-snapshot
The Poulos−Kraut Mechanism of Compound I Formation in Horseradish Peroxidase: A QM/MM Study
inferredcites →https://doi.org/10.1021/jp911170bopenalex-snapshot
On the Role of Water in Peroxidase Catalysis: A Theoretical Investigation of HRP Compound I Formation
inferredcites →https://doi.org/10.1023/b:phyt.0000047797.81958.69openalex-snapshot
Biotechnological applications of peroxidases
inferredcites →https://doi.org/10.1038/169488a0openalex-snapshot
Multiple Nature of the Enzymes of Aspergillus Oryzæ and of Horse-Radish: Horse-Radish Peroxidase
inferredcites →https://doi.org/10.1038/169612a0openalex-snapshot
Chemical Nature of the Secondary Hydrogen Peroxide Compound Formed by Cytochrome-C Peroxidase and Horseradish Peroxidase
inferredcites →https://doi.org/10.1038/21395openalex-snapshot
Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
inferredcites →https://doi.org/10.1038/417463aopenalex-snapshot
The catalytic pathway of horseradish peroxidase at high resolution
inferredcites →https://doi.org/10.1038/cgt.2011.65openalex-snapshot
Tumor-targeted gene therapy using Adv-AFP-HRPC/IAA prodrug system suppresses growth of hepatoma xenografted in mice
inferredcites →https://doi.org/10.1038/nsb1297-1032openalex-snapshot
Crystal structure of horseradish peroxidase C at 2.15 Å resolution
inferredcites →https://doi.org/10.1038/srep03279openalex-snapshot
Knockout of an endogenous mannosyltransferase increases the homogeneity of glycoproteins produced in Pichia pastoris
inferredcites →https://doi.org/10.1039/c0an00095gopenalex-snapshot
Ultrasensitive optical detection of hydrogen peroxide by triggered activation of horseradish peroxidase
inferredcites →https://doi.org/10.1039/c0an00752hopenalex-snapshot
Amperometric biosensors based on aluminananoparticles-chitosan-horseradish peroxidase nanobiocomposites for the determination of phenolic compounds
inferredcites →https://doi.org/10.1039/c39920000357openalex-snapshot
Horseradish peroxidase catalysed sulfoxidation is enantioselective
inferredcites →https://doi.org/10.1042/0264-6021:3540107openalex-snapshot
Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2
inferredcites →https://doi.org/10.1042/bj0490088openalex-snapshot
Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin
inferredcites →https://doi.org/10.1042/bj0540267openalex-snapshot
The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. 1. Titration with reducing agents
inferredcites →https://doi.org/10.1042/bj0560631openalex-snapshot
Multiple components in horse-radish peroxidase
inferredcites →https://doi.org/10.1042/bj3330223openalex-snapshot
Identification of skatolyl hydroperoxide and its role in the peroxidase-catalysed oxidation of indol-3-yl acetic acid
inferredcites →https://doi.org/10.1042/bst0171077aopenalex-snapshot
Expression of recombinant horseradish peroxidase C in Escherichia coli
inferredcites →https://doi.org/10.1042/bst020111sopenalex-snapshot
Expression of Active Horseradish Peroxidase in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1074/jbc.270.31.18413openalex-snapshot
Horseradish Peroxidase Phe172→ Tyr Mutant
inferredcites →https://doi.org/10.1074/jbc.270.33.19430openalex-snapshot
Horseradish Peroxidase His-42 → Ala, His-42 → Val, and Phe-41 → Ala Mutants
inferredcites →https://doi.org/10.1074/jbc.271.25.14891openalex-snapshot
Rescue of the Catalytic Activity of an H42A Mutant of Horseradish Peroxidase by Exogenous Imidazoles
inferredcites →https://doi.org/10.1074/jbc.271.40.24598openalex-snapshot
Rescue of His-42 → Ala Horseradish Peroxidase by a Phe-41 → His Mutation
inferredcites →https://doi.org/10.1093/aob/mch045openalex-snapshot
An N-terminal Peptide Extension Results in Efficient Expression, but not Secretion, of a Synthetic Horseradish Peroxidase Gene in Transgenic Tobacco
inferredcites →https://doi.org/10.1093/glycob/cwu047openalex-snapshot
Glyco-variant library of the versatile enzyme horseradish peroxidase
inferredcites →https://doi.org/10.1093/nar/gkn369openalex-snapshot
Promoter library designed for fine-tuned gene expression in Pichia pastoris
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a133496openalex-snapshot
Isolation and Properties of Basic Isoenzymes of Horseradish Peroxidase1
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a133961openalex-snapshot
Isolation and Characterization of Five Neutral Isoenzymes of Horseradish Peroxidase1
inferredcites →https://doi.org/10.1093/pcp/pcq205openalex-snapshot
Activity of the C-terminal-Dependent Vacuolar Sorting Signal of Horseradish Peroxidase C1a is Enhanced by its Secondary Structure
inferredcites →https://doi.org/10.1093/protein/13.5.377openalex-snapshot
Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris
inferredcites →https://doi.org/10.1104/pp.102.019794openalex-snapshot
Ectopic Expression of a Horseradish Peroxidase Enhances Growth Rate and Increases Oxidative Stress Resistance in Hybrid Aspen
inferredcites →https://doi.org/10.1104/pp.60.5.787openalex-snapshot
High Resolution of Peroxidase-Indoleacetic Acid Oxidase Isoenzymes from Horseradish by Isoelectric Focusing
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inferred← citeshttps://doi.org/10.1016/j.mtchem.2023.101694openalex-snapshot
Acoustomicrofluidic synthesis of ZIF-8/HRP metal–organic framework composites with enhanced enzymatic activity and stability
inferred← citeshttps://doi.org/10.1016/j.nbt.2019.10.009openalex-snapshot
A compact nanobody-DNAzyme conjugate enables antigen detection and signal amplification
inferred← citeshttps://doi.org/10.1016/j.omton.2026.201310openalex-snapshot
Engineered indoleamine 2,3-dioxygenase variant: Oxidative activation of prodrug indole-3-acetic acid against cancer cells for targeted therapy
inferred← citeshttps://doi.org/10.1016/j.pep.2026.106952openalex-snapshot
Recombinant indoleamine 2,3-dioxygenase as a reliable alternative to HRP with enhanced cumulative output in immunoassays
inferred← citeshttps://doi.org/10.1016/j.procbio.2021.02.005openalex-snapshot
Spongy membranes for peroxidase purification from Brassica oleracea roots
inferred← citeshttps://doi.org/10.1016/j.rineng.2021.100312openalex-snapshot
Metal-supported self-assembled bilayer lipid membrane incorporated with peroxidase for the detection of peroxide
inferred← citeshttps://doi.org/10.1016/j.saa.2017.06.046openalex-snapshot
Conformation and activity alteration of horseradish peroxidase induced by the interaction with gene carrier polyethyleneimines
inferred← citeshttps://doi.org/10.1016/j.scitotenv.2021.150500openalex-snapshot
Peroxidase enzymes as green catalysts for bioremediation and biotechnological applications: A review
inferred← citeshttps://doi.org/10.1016/j.scp.2023.101233openalex-snapshot
Style decolorization treatment of denim fabric: Decomposition of indigo dyes via horseradish peroxidase/H2O2 system at room temperature
inferred← citeshttps://doi.org/10.1016/j.talanta.2024.126951openalex-snapshot
Revisiting the catalytic activity of single horseradish peroxidase clusters through electrochemical collision technique: Effect of electrolyte and substrate
inferred← citeshttps://doi.org/10.1016/j.tet.2015.12.078openalex-snapshot
Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase
inferred← citeshttps://doi.org/10.1016/j.tibtech.2018.11.005openalex-snapshot
Engineering Biocatalytic and Biosorptive Materials for Environmental Applications
inferred← citeshttps://doi.org/10.1016/j.tifs.2025.105016openalex-snapshot
Enzyme- and nanozyme-based food allergen detections: from natural biocatalysts to rational engineering approaches
inferred← citeshttps://doi.org/10.1016/j.trac.2025.118494openalex-snapshot
Strategies for enhancing the signal-to-noise ratio in optical lateral flow immunoassay: A review
inferred← citeshttps://doi.org/10.1021/acs.analchem.7b00423openalex-snapshot
Spectrophotometric Quantification of Peroxidase with p-Phenylene-diamine for Analyzing Peroxidase-Encapsulating Lipid Vesicles
inferred← citeshttps://doi.org/10.1021/acs.analchem.9b04751openalex-snapshot
Inhibitors in Commercially Available 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonate) Affect Enzymatic Assays
inferred← citeshttps://doi.org/10.1021/acs.bioconjchem.2c00542openalex-snapshot
Carbon Electrode-Based Biosensing Enabled by Biocompatible Surface Modification with DNA and Proteins
inferred← citeshttps://doi.org/10.1021/acs.biomac.3c01127openalex-snapshot
Designing Configurable Soft Microgelsomes as a Smart Biomimetic Protocell
inferred← citeshttps://doi.org/10.1021/acs.chemrestox.0c00430openalex-snapshot
Adsorption of Horseradish Peroxidase on Metallic Nanoparticles: Effects on Reactive Oxygen Species Detection Using 2′,7′-Dichlorofluorescin Diacetate
inferred← citeshttps://doi.org/10.1021/acs.chemrestox.3c00263openalex-snapshot
Antioxidant Activity and Skin Sensitization of Eugenol and Isoeugenol: Two Sides of the Same Coin?
inferred← citeshttps://doi.org/10.1021/acs.chemrev.9b00429openalex-snapshot
Probing Structure and Reaction Dynamics of Proteins Using Time-Resolved Resonance Raman Spectroscopy
inferred← citeshttps://doi.org/10.1021/acs.jafc.2c09117openalex-snapshot
Stepwise Optimization of Inducible Expression System for the Functional Secretion of Horseradish Peroxidase in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1021/acs.jchemed.3c00746openalex-snapshot
A Full-Semester Biochemistry Laboratory Synchronous with Lecture to Enhance Student Learning and Engagement
inferred← citeshttps://doi.org/10.1021/acs.jcim.3c01303openalex-snapshot
Mechanisms and Opportunities for Rational In Silico Design of Enzymes to Degrade Per- and Polyfluoroalkyl Substances (PFAS)
inferred← citeshttps://doi.org/10.1021/acs.jcim.4c00803openalex-snapshot
Exploring Chemical Spaces in the Billion Range: Is Docking a Computational Alternative to DNA-Encoded Libraries?
inferred← citeshttps://doi.org/10.1021/acs.langmuir.4c01180openalex-snapshot
Immobilization of Thiol-Modified Horseradish Peroxidase on Gold Nanoparticles Enhances Enzyme Stability and Prevents Proteolytic Digestion
inferred← citeshttps://doi.org/10.1021/acs.nanolett.6b01298openalex-snapshot
Photocatalytic Reactive Oxygen Species Formation by Semiconductor–Metal Hybrid Nanoparticles. Toward Light-Induced Modulation of Biological Processes
inferred← citeshttps://doi.org/10.1021/acsabm.4c00240openalex-snapshot
Dual-Mode Virus Detection: Combining Electrochemical and Fluorescence Modalities for Enhanced Sensitivity and Reliability
inferred← citeshttps://doi.org/10.1021/acsami.6c01215openalex-snapshot
Alkyne Nitro Tag Enables Stable and Efficient Protein Functionalization of Gold Nanoparticles
inferred← citeshttps://doi.org/10.1021/acsbiomaterials.5c01395openalex-snapshot
Calcium Peroxide Embedded in Dopamine-Grafted Hyaluronic Acid Hydrogel with Tunable Physicochemical Properties and Biocompatibility for Soft Tissue Regeneration
inferred← citeshttps://doi.org/10.1021/acscatal.1c01555openalex-snapshot
Granum-Inspired Photoenzyme-Coupled Catalytic System via Stacked Polymeric Carbon Nitride
inferred← citeshttps://doi.org/10.1021/acsfoodscitech.3c00394openalex-snapshot
Highly Active Peroxidase (Prx34) Derived from Moss, Physcomitrium patens, Is Produced as a Soluble Form in Escherichia coli
inferred← citeshttps://doi.org/10.1021/acsomega.3c05748openalex-snapshot
Nanocellulose/Fe 3 O 4 /Ag Nanozyme with Robust Peroxidase Activity for Enhanced Antibacterial and Wound Healing Applications
inferred← citeshttps://doi.org/10.1021/acsomega.6c02913openalex-snapshot
Electrochemical Dopamine Biosensor Based on Plant-Derived Peroxidase Immobilized on Titanate Nanowires
inferred← citeshttps://doi.org/10.1021/acssensors.7b00830openalex-snapshot
Inner Filter Effect-Based Sensor for Horseradish Peroxidase and Its Application to Fluorescence Immunoassay
inferred← citeshttps://doi.org/10.1021/jacs.5b06796openalex-snapshot
The Molecular Mechanism of the Catalase-like Activity in Horseradish Peroxidase
inferred← citeshttps://doi.org/10.1021/jacs.5c00453openalex-snapshot
Stabilization of the Ferryl═Oxoheme Form of Staphylococcus aureus IsdG by Electron Transfer from a Second-Sphere Tryptophan
inferred← citeshttps://doi.org/10.1038/s41428-020-0344-7openalex-snapshot
Poly(ethylene glycol)-based biofunctional hydrogels mediated by peroxidase-catalyzed cross-linking reactions
inferred← citeshttps://doi.org/10.1038/s41467-017-01585-2openalex-snapshot
Thermostable exoshells fold and stabilize recombinant proteins
inferred← citeshttps://doi.org/10.1038/s41467-023-39800-yopenalex-snapshot
The allotetraploid horseradish genome provides insights into subgenome diversification and formation of critical traits
inferred← citeshttps://doi.org/10.1038/s41592-024-02512-2openalex-snapshot
Efficient and highly amplified imaging of nucleic acid targets in cellular and histopathological samples with pSABER
inferred← citeshttps://doi.org/10.1038/s41598-017-15550-yopenalex-snapshot
SnO2 hollow nanotubes: a novel and efficient support matrix for enzyme immobilization
inferred← citeshttps://doi.org/10.1039/c5tb02207jopenalex-snapshot
Photo-induced chemistry for the design of oligonucleotide conjugates and surfaces
inferred← citeshttps://doi.org/10.1039/c6cy01044jopenalex-snapshot
Alkaline versatile peroxidase by directed evolution
inferred← citeshttps://doi.org/10.1039/c6ra24586bopenalex-snapshot
Magnetic iron oxide nanoparticles encapsulating horseradish peroxidase (HRP): synthesis, characterization and carrier for the generation of free radicals for potential applications in cancer therapy
inferred← citeshttps://doi.org/10.1039/c9ay00201dopenalex-snapshot
A hemin-functionalized GroEL nanocage as an artificial peroxidase and its application in chromogenic detection
inferred← citeshttps://doi.org/10.1039/c9nr04771aopenalex-snapshot
Metal and metal-oxide nanozymes: bioenzymatic characteristics, catalytic mechanism, and eco-environmental applications
inferred← citeshttps://doi.org/10.1039/d0cc06575gopenalex-snapshot
Nanocrystals of platinum-group metals as peroxidase mimics for in vitro diagnostics
inferred← citeshttps://doi.org/10.1039/d0cs01387kopenalex-snapshot
Harnessing the physicochemical properties of DNA as a multifunctional biomaterial for biomedical and other applications
inferred← citeshttps://doi.org/10.1039/d0gc01972kopenalex-snapshot
The molecular mechanism of the photocatalytic oxidation reactions by horseradish peroxidase in the presence of histidine
inferred← citeshttps://doi.org/10.1039/d1ra00733eopenalex-snapshot
Monitoring the heme iron state in horseradish peroxidase to detect ultratrace amounts of hydrogen peroxide in alcohols
inferred← citeshttps://doi.org/10.1039/d2su00127fopenalex-snapshot
Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
inferred← citeshttps://doi.org/10.1039/d3nj05330jopenalex-snapshot
Nanoarchitectonics of CdFe 2 O 4 nanoparticles with different morphologies synthesized using a thermal decomposition approach and studies of their peroxidase-like activity
inferred← citeshttps://doi.org/10.1039/d5py00223kopenalex-snapshot
Harnessing enzymes for greener polymerisations: advances in chain and step growth processes
inferred← citeshttps://doi.org/10.1080/00986445.2024.2341264openalex-snapshot
Horseradish peroxidase immobilized in calcium alginate-gelatin hybrid beads with high stability against metallic ions and organic solvents
inferred← citeshttps://doi.org/10.1080/09168451.2019.1621156openalex-snapshot
A simple, real-time assay of horseradish peroxidase using biolayer interferometry
inferred← citeshttps://doi.org/10.1080/1061186x.2020.1720218openalex-snapshot
Biointerface: a nano-modulated way for biological transportation
inferred← citeshttps://doi.org/10.1080/14786419.2023.2248644openalex-snapshot
Simple two-step purification and characterisation of peroxidase from Citrullus colocynthis
inferred← citeshttps://doi.org/10.1080/17425247.2026.2712528openalex-snapshot
Synthesis strategies and functional properties of polysaccharide hydrogels for controlled drug delivery applications
inferred← citeshttps://doi.org/10.1080/17435889.2025.2520736openalex-snapshot
Cancer therapy with engineered nanozymes: from molecular design to tumour-responsive catalysis
inferred← citeshttps://doi.org/10.1080/17576180.2026.2658612openalex-snapshot
Vendor-specific HRP antibody conjugate differences lead to unexpected immunoassay reagent interactions
inferred← citeshttps://doi.org/10.1083/jcb.201709115openalex-snapshot
A toolbox of anti–mouse and anti–rabbit IgG secondary nanobodies
inferred← citeshttps://doi.org/10.1093/femsyr/foaf019openalex-snapshot
Metabolic engineering of yeast to efficiently synthesize heme and hemoproteins: recent advance and prospects
inferred← citeshttps://doi.org/10.1104/pp.18.01165openalex-snapshot
Healthy Roots and Leaves: Comparative Genome Structure of Horseradish and Watercress
inferred← citeshttps://doi.org/10.1109/jstqe.2016.2617818openalex-snapshot
GaInN Quantum Wells as Optochemical Transducers for Chemical Sensors and Biosensors
inferred← citeshttps://doi.org/10.1128/jvi.02289-24openalex-snapshot
Research strategies of the N-peptide fusion inhibitor: a promising direction for discovering novel antivirals
inferred← citeshttps://doi.org/10.1134/s0006350924700660openalex-snapshot
The Kinetics of Oxidation of 3-Aminopyridin-2(1H)-ones by Hydrogen Peroxide in the Presence of Horseradish Peroxidase
inferred← citeshttps://doi.org/10.1155/2021/5599204openalex-snapshot
Recent Advances in Enzymes for the Bioremediation of Pollutants
inferred← citeshttps://doi.org/10.1186/s11671-016-1605-4openalex-snapshot
Enhancement of Peroxidase Stability Against Oxidative Self-Inactivation by Co-immobilization with a Redox-Active Protein in Mesoporous Silicon and Silica Microparticles
inferred← citeshttps://doi.org/10.1371/journal.pone.0214004openalex-snapshot
Design of stable magnetic hybrid nanoparticles of Si-entrapped HRP
inferred← citeshttps://doi.org/10.15368/theses.2016.103openalex-snapshot
Development and Characterization of Reagent Pencils for Microfluidic Paper Based Analytical Devices
inferred← citeshttps://doi.org/10.1557/adv.2020.218openalex-snapshot
Thin hydrogel coatings formation catalyzed by immobilized enzyme horseradish peroxidase
inferred← citeshttps://doi.org/10.17392/1421-21openalex-snapshot
Rats’ umbilical-cord mesenchymal stem cells ameliorate mast cells and Hsp70 on ovalbumin-induced allergic rhinitis rats
inferred← citeshttps://doi.org/10.18097/pbmc20247005349openalex-snapshot
Registration of activity of a single molecule of horseradish peroxidase using a detector based on a solid-state nanopore
inferred← citeshttps://doi.org/10.20944/preprints202403.0304.v1openalex-snapshot
AFM Study of the Influence of Stopped Glycerol Flow in a Coil on Peroxidase Enzyme
inferred← citeshttps://doi.org/10.21203/rs.3.rs-6661361/v1openalex-snapshot
FK-1000: A Promising Antimicrobial Alternative for Shiga Toxin-Producing E. coli Infections
inferred← citeshttps://doi.org/10.21203/rs.3.rs-95899/v1openalex-snapshot
Field effect transistor to enable registration of reaction energy pathways
inferred← citeshttps://doi.org/10.2147/ijn.s323802openalex-snapshot
Horseradish Peroxidase-Functionalized Gold Nanoconjugates for Breast Cancer Treatment Based on Enzyme Prodrug Therapy
inferred← citeshttps://doi.org/10.2174/1389203723666220704090416openalex-snapshot
Comparison of Laccases and Hemeproteins Systems in Bioremediation of Organic Pollutants
inferred← citeshttps://doi.org/10.22184/1993-8578.2026.19.1.20.31openalex-snapshot
ВЛИЯНИЕ ИНКУБАЦИИ РАСТВОРА ПЕРОКСИДАЗЫ ХРЕНА НА ТЕЛЕ ЧЕЛОВЕКА НА АДСОРБЦИОННЫЕ СВОЙСТВА И АКТИВНОСТЬ ФЕРМЕНТА: РАЗЛИЧИЯ В НОРМЕ И ПРИ СЕРДЕЧНО-СОСУДИСТОЙ ПАТОЛОГИИ
inferred← citeshttps://doi.org/10.26434/chemrxiv-2022-bt457openalex-snapshot
Oxidative coupling for facile, stable carbon modification with DNA and proteins
inferred← citeshttps://doi.org/10.26434/chemrxiv-2023-10q7xopenalex-snapshot
Optimization of the diaminobenzidine substrate composition improves the performance of peroxidase-like Prussian Blue nanozymes in colorimetric assays
inferred← citeshttps://doi.org/10.31857/s0006302924040012openalex-snapshot
Kinetics of Oxidation of 3-Aminopyridin-2(1H)-ones by Hydrogen Peroxide in the Presence of Horseradish Peroxidase
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