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Methods in enzymology, ISSN 0076-6879, 1955
Journal
BIOCHEMICAL JOURNAL, ISSN 0264-6021, 10/2013, Volume 455, Issue 1, pp. 75 - 85
The resistance of mosquitoes to chemical insecticides is threatening vector control programmes worldwide. Cytochrome P450 monooxygenases (CYPs) are known to... 
DENGUE VECTOR | recombinant system | VECTOR AEDES-AEGYPTI | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | insecticide | IN-VITRO METABOLISM | ANOPHELES-GAMBIAE | resistance | mosquito | YEAST | MALARIA VECTOR | cytochrome P450 monooxygenase | metabolism | P450 | pyrethroid | Inactivation, Metabolic | Insecticides - chemistry | NADPH-Ferrihemoprotein Reductase - genetics | Saccharomyces cerevisiae - genetics | Benzoates - metabolism | Cytochrome P-450 Enzyme System - metabolism | Insecticide Resistance - genetics | NADPH-Ferrihemoprotein Reductase - chemistry | Saccharomyces cerevisiae - drug effects | Isoenzymes - chemistry | Pyrethrins - pharmacology | Insect Vectors - drug effects | Isoenzymes - metabolism | Insecticide Resistance - drug effects | Aedes - enzymology | Pyrethrins - metabolism | Insect Proteins - metabolism | Insect Vectors - enzymology | Insecticides - pharmacology | Benzaldehydes - chemistry | Escherichia coli - enzymology | NADPH-Ferrihemoprotein Reductase - metabolism | Oxidation-Reduction | Isoenzymes - genetics | Anopheles - drug effects | Insect Proteins - genetics | Benzaldehydes - pharmacology | Aedes - drug effects | Pyrethrins - chemistry | Anopheles - enzymology | Benzaldehydes - metabolism | Cytochrome P-450 Enzyme System - chemistry | Animals | Genetic Engineering | Insecticides - metabolism | Escherichia coli - genetics | Insect Proteins - chemistry | Cytochrome P-450 Enzyme System - genetics | Saccharomyces cerevisiae - enzymology | Molecular Docking Simulation | AeCPR, Aedes aegypti CPR | 7-OH, 7-hydroxycoumarin | SRS, substrate recognition site | CPR, NADPH-cytochrome P450-reductase | Rt, retention time | Cyt b5, cytochrome b5 | PBAld, 3-phenoxybenzaldehyde | qPCR, quantitative real-time PCR | PBA, 3-phenoxybenzoic acid | PBAlc, 3-phenoxybenzoic alcohol | TFA, trifluoroacetic acid
Journal Article
Biochemistry, ISSN 0006-2960, 05/2017, Volume 56, Issue 17, pp. 2294 - 2303
The toxicities of azole pollutants that have widespread agricultural and industrial uses are either poorly understood or unknown, particularly with respect to... 
DEHALOPEROXIDASE-HEMOGLOBIN | PEROXIDASE | SUBSTRATE-BINDING | INHIBITION | GLOBIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | CYTOCHROME P450BM3 | RESONANCE RAMAN | MARINE | DISTAL HISTIDINE | Benzimidazoles - toxicity | Triazoles - chemistry | Imidazoles - chemistry | Fungicides, Industrial - toxicity | Isoenzymes - chemistry | Environmental Pollutants - metabolism | Benzimidazoles - chemistry | Recombinant Fusion Proteins - metabolism | Fungicides, Industrial - metabolism | Peroxidases - antagonists & inhibitors | Triazoles - toxicity | Isoenzymes - metabolism | Peroxidases - chemistry | Enzyme Inhibitors - chemistry | Enzyme Inhibitors - toxicity | Peroxidases - metabolism | Imidazoles - toxicity | Environmental Pollutants - toxicity | Pesticides - metabolism | Polychaeta - enzymology | Imidazoles - metabolism | Recombinant Proteins - metabolism | Catalytic Domain | Indazoles - chemistry | Enzyme Inhibitors - metabolism | Computational Biology | Hemoglobins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Indazoles - metabolism | Recombinant Fusion Proteins - chemistry | Fungicides, Industrial - chemistry | Amino Acid Motifs | Triazoles - metabolism | Hemoglobins - antagonists & inhibitors | Hemoglobins - chemistry | Animals | Environmental Pollutants - chemistry | Hydrogen Bonding | Pesticides - toxicity | Benzimidazoles - metabolism | Indazoles - toxicity | Hydrophobic and Hydrophilic Interactions | Pesticides - chemistry | Ligands | Kinetics | Isoenzymes - antagonists & inhibitors | Azoles (Class of compounds) | Computational chemistry | Usage | Chemical properties | X-ray spectroscopy | Research | Index Medicus
Journal Article
Chemistry – A European Journal, ISSN 0947-6539, 07/2015, Volume 21, Issue 29, pp. 10306 - 10309
Multifunctional silica nanoparticles decorated with fluorescent and sulfonamide carbonic anhydrase (CA) inhibitors were prepared and investigated as... 
carbonic anhydrase | inhibitors | nanoparticles | sulfonamide | multivalency | Nanoparticles | Inhibitors | Multivalency | Sulfonamide | Carbonic anhydrase | THERAPEUTIC APPLICATIONS | CHEMISTRY, MULTIDISCIPLINARY | Nanoparticles - chemistry | Carbonic Anhydrase Inhibitors - chemistry | Humans | Cytosol - drug effects | Carbonic Anhydrase II - metabolism | Isoenzymes - chemistry | Structure-Activity Relationship | Carbonic Anhydrase I - metabolism | Antigens, Neoplasm - chemistry | Carbonic Anhydrase II - antagonists & inhibitors | Carbonic Anhydrases - metabolism | Dose-Response Relationship, Drug | Cytosol - enzymology | Neoplasms - chemistry | Isoenzymes - metabolism | Enzyme Inhibitors - chemistry | Antigens, Neoplasm - metabolism | Antineoplastic Agents - pharmacology | Molecular Structure | Silicon Dioxide - chemistry | Enzyme Inhibitors - pharmacology | Neoplasms - enzymology | Carbonic Anhydrase I - chemistry | Carbonic Anhydrase Inhibitors - pharmacology | Antineoplastic Agents - chemistry | Cytosol - chemistry | Neoplasms - drug therapy | Carbonic Anhydrase I - antagonists & inhibitors | Cell Line, Tumor | Isoenzymes - antagonists & inhibitors | Carbonic Anhydrase II - chemistry | Enzyme inhibitors | Isoenzymes | Sulfonamides | Silica | Enzymes | Binding | Fluorescence | Inhibition | Clustering | Silicon dioxide | Material chemistry | Chemical Sciences
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 11/2015, Volume 11, Issue 11, pp. 837 - 839
Phytoalexins are abundant in edible crucifers and have important biological activities, yet no dedicated gene for their biosynthesis is known. Here, we report... 
ARABIDOPSIS-THALIANA | INHIBITION | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENES | STRESS METABOLITES | BRASSICACEAE | YEAST EXPRESSION | BRASSININ | GLUCOSINOLATE METABOLISM | CAMALEXIN | Microsomes - metabolism | Thiazoles - metabolism | Sesquiterpenes - metabolism | Thiocarbamates - metabolism | Brassica rapa - enzymology | Cytochrome P-450 Enzyme System - metabolism | Molecular Sequence Data | Isoenzymes - chemistry | Brassica rapa - genetics | RNA, Messenger - metabolism | Indoles - metabolism | Vegetables - chemistry | Isoenzymes - metabolism | Plant Proteins - chemistry | Base Sequence | Escherichia coli - metabolism | Vegetables - metabolism | Plant Proteins - metabolism | Spiro Compounds - chemistry | Plant Leaves - chemistry | Recombinant Proteins - metabolism | Gene Expression | Biocatalysis | Sesquiterpenes - chemistry | Isoenzymes - genetics | RNA, Messenger - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Thiocarbamates - chemistry | Brassicaceae - genetics | Microsomes - chemistry | Plant Proteins - genetics | Cytochrome P-450 Enzyme System - chemistry | Cyclization | Plant Leaves - metabolism | Escherichia coli - genetics | Cytochrome P-450 Enzyme System - genetics | Thiazoles - chemistry | High-Throughput Nucleotide Sequencing | Kinetics | Indoles - chemistry | Brassicaceae - enzymology | Spiro Compounds - metabolism | Genetics | Biosynthesis | Biochemistry | Metabolites
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 45, pp. 18500 - 18517
Membrane tethering is a fundamental process essential for the compartmental specificity of intracellular membrane trafficking in eukaryotic cells. Rab-family... 
LOCALIZATION | SNARE PROTEINS | FUSION | SPECIFICITY | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | myosin | membrane tethering | liposome | MOLECULES | Rab | TRANSPORT | CARGO | Myo5 | SUPERFAMILY | membrane reconstitution | small GTPase | VESICLE | membrane trafficking | Myosin Heavy Chains - chemistry | Myosin Type V - chemistry | Succinates - chemistry | Intracellular Membranes - enzymology | Humans | Myosin Heavy Chains - genetics | rab GTP-Binding Proteins - agonists | rab GTP-Binding Proteins - genetics | Guanosine Triphosphate - metabolism | Isoenzymes - chemistry | Histidine - metabolism | Myosin Heavy Chains - metabolism | Protein Prenylation | Recombinant Fusion Proteins - metabolism | Endosomes - metabolism | Oleic Acids - metabolism | Isoenzymes - metabolism | Succinates - metabolism | Lysine - metabolism | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Acylation | rab GTP-Binding Proteins - metabolism | Lysine - analogs & derivatives | Peptide Fragments - metabolism | Myosin Type V - metabolism | Isoenzymes - genetics | Histidine - genetics | Recombinant Fusion Proteins - chemistry | Intracellular Membranes - chemistry | Protein Interaction Mapping | Peptide Fragments - chemistry | Myosin Type V - genetics | rab GTP-Binding Proteins - chemistry | Endosomes - enzymology | Protein Processing, Post-Translational | Kinetics | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Liposomes | Histidine - chemistry | Lysine - chemistry | Oleic Acids - chemistry | Intracellular Membranes - metabolism | Membrane Biology
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2017, Volume 292, Issue 28, pp. 11670 - 11681
Metalloenzymes catalyze complex and essential processes, such as photosynthesis, respiration, and nitrogen fixation. For example, bacteria and archaea use... 
CIRCULAR-DICHROISM SPECTRA | ACTIVE-SITE | STRUCTURAL BASIS | CARBON-MONOXIDE | NIFE HYDROGENASE MATURATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI K-12 | ACCESSORY PROTEINS | IRON | LARGE SUBUNIT | CATALYTIC CYCLE | Carboxyl and Carbamoyl Transferases - metabolism | Molecular Chaperones - metabolism | Hydrogenase - genetics | Protein Multimerization | Carboxyl and Carbamoyl Transferases - genetics | Enzyme Precursors - genetics | Isoenzymes - chemistry | Hydrogenase - chemistry | Molecular Chaperones - chemistry | GTP-Binding Proteins - genetics | Protein Subunits - metabolism | Coenzymes - metabolism | Endopeptidases - chemistry | Hydrogenase - metabolism | Isoenzymes - metabolism | Proteolysis | Carrier Proteins - chemistry | Dimerization | Protein Subunits - genetics | Recombinant Proteins - metabolism | Endopeptidases - metabolism | Escherichia coli - enzymology | Mutagenesis, Site-Directed | Enzyme Precursors - chemistry | GTP-Binding Proteins - chemistry | Isoenzymes - genetics | Molecular Chaperones - genetics | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Protein Folding | Carrier Proteins - genetics | Enzyme Precursors - metabolism | Carrier Proteins - metabolism | Endopeptidases - genetics | Escherichia coli Proteins - genetics | Protein Processing, Post-Translational | Protein Subunits - chemistry | Mutation | Escherichia coli Proteins - chemistry | Carboxyl and Carbamoyl Transferases - chemistry | GTP-Binding Proteins - metabolism | metalloprotein | circular dichroism (CD) | proteolytic enzyme | Enzymology | infrared spectroscopy (IR spectroscopy) | protein assembly
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 12981 - 12993
H-Ras, K-Ras, and N-Ras are small GTPases that are important in the control of cell proliferation, differentiation, and survival, and their mutants occur... 
EVOLUTIONARY TREE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | enzyme catalysis | Ras protein | allosteric regulation | conformational change | oncogene | enzyme structure | P21 | PHOSPHATE | STRUCTURAL BASIS | NUCLEOTIDE-FREE | ACTIVATING PROTEINS | EXPRESSION | GTP HYDROLYSIS | CONFORMATIONAL STATES | Proto-Oncogene Proteins p21(ras) - genetics | Allosteric Regulation | Humans | Crystallography, X-Ray | Guanosine Triphosphate - metabolism | Isoenzymes - chemistry | Dinucleoside Phosphates - chemistry | GTP Phosphohydrolases - chemistry | Isoenzymes - metabolism | Proto-Oncogene Proteins c-raf - chemistry | Proto-Oncogene Proteins p21(ras) - chemistry | Guanosine Triphosphate - chemistry | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Proto-Oncogene Proteins p21(ras) - metabolism | Recombinant Proteins - metabolism | Catalytic Domain | Peptide Fragments - metabolism | Biocatalysis | Proto-Oncogene Proteins c-raf - genetics | Isoenzymes - genetics | Membrane Proteins - genetics | Enzyme Stability | Guanosine Triphosphate - analogs & derivatives | Models, Molecular | Recombinant Proteins - chemistry | Dinucleoside Phosphates - metabolism | Proto-Oncogene Proteins c-raf - metabolism | Point Mutation | Peptide Fragments - chemistry | GTP Phosphohydrolases - metabolism | Membrane Proteins - chemistry | GTP Phosphohydrolases - genetics | Allosteric Site | Ligands | Protein Conformation | Amino Acid Substitution | Enzymology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 20, pp. 7880 - 7891
Cyanuric acid is a metabolic intermediate of s-triazines, such as atrazine (a common herbicide) and melamine (used in resins and plastics). Cyanuric acid is... 
bacteria | transamidosome | PSEUDOMONAS SP | AMIDOHYDROLASE | xenobiotic | Pseudomonas | protein complex | AMIDASE DOMAIN | enzyme structure | CLONING | small protein | complex | SEQUENCE | GENES | low-molecular-weight protein | enzyme | protein evolution | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLASMID | enzyme catalysis | biuret | ALLOPHANATE HYDROLASE | REFINEMENT | bacterial metabolism | cyanuric acid | triazine | SUPERFAMILY | amidase | Organophosphates - metabolism | Herbicides - chemistry | Protein Multimerization | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Isoenzymes - chemistry | Pseudomonas - enzymology | Isoenzymes - metabolism | Enzyme Inhibitors - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Triazines - chemistry | Protein Interaction Domains and Motifs | Herbicides - metabolism | Amidohydrolases - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Triazines - metabolism | Catalytic Domain | Gene Expression | Enzyme Inhibitors - metabolism | Genetic Vectors - chemistry | Isoenzymes - genetics | Operon | Amidohydrolases - genetics | Bacterial Proteins - genetics | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Amidohydrolases - chemistry | Hydrolysis | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Bacterial Proteins - metabolism | Organophosphates - chemistry | Kinetics | Pseudomonas - chemistry | Evolution, Molecular | Editors' Picks
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 08/2015, Volume 11, Issue 8, pp. 598 - 605
Journal Article
Protein and Peptide Letters, ISSN 0929-8665, 2017, Volume 24, Issue 8, pp. 723 - 728
Background: Peptide: N-glycanase is a deglycosylation enzyme releasing N-glycan from glycoproteins. Although glycan specificity analysis of this enzyme has... 
Peptide sequence | Peptide: N-glycanase | Synthetic substrate | Chitobiose-pentapeptide | Substrate specificity | Ultraperformance liquid chromatography mass spectrometry | GLYCOPEPTIDE PROBES | GLYCOSIDASE | peptide sequence | chitobiose-pentapeptide | BIOCHEMISTRY & MOLECULAR BIOLOGY | synthetic substrate | substrate specificity | GLYCOPROTEINS | ultra-performance liquid chromatography mass spectrometry | DEGLYCOSYLATION | Flavobacteriaceae - chemistry | Disaccharides - metabolism | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism | Bacterial Proteins - chemistry | Substrate Specificity | Isoenzymes - chemistry | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - genetics | Prunus dulcis - enzymology | Disaccharides - chemistry | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - chemistry | Isoenzymes - metabolism | Plant Proteins - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Plant Proteins - metabolism | Oligopeptides - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Leucine - metabolism | Gene Expression | Isoenzymes - genetics | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Flavobacteriaceae - enzymology | Prunus dulcis - chemistry | Glycosylation | Recombinant Proteins - genetics | Oligopeptides - metabolism | Saccharomyces cerevisiae Proteins - genetics | Serine - chemistry | Plasmids - metabolism | Serine - metabolism | Saccharomyces cerevisiae - chemistry | Leucine - chemistry | Plant Proteins - genetics | Escherichia coli - genetics | Plasmids - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Saccharomyces cerevisiae - enzymology | Bacterial Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry
Journal Article
Nature communications, ISSN 2041-1723, 2018, Volume 9, Issue 1, pp. 1874 - 11
Endoglycosidase S (EndoS) is a bacterial endo-beta-N-acetylglucosaminidase that specifically catalyzes the hydrolysis of the beta-1,4 linkage between the first... 
STREPTOCOCCUS-PYOGENES | BIOLOGICAL MACROMOLECULES | PROTEIN | SPECIFICITY | ACTIVE-SITE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | RESOLUTION | SUBSTRATE-ASSISTED CATALYSIS | ANTIBODY | GLYCOSYLATION | Antibodies, Monoclonal - biosynthesis | Glycoside Hydrolases - genetics | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Isoenzymes - chemistry | Trichoderma - enzymology | Vibrio cholerae - chemistry | Thermodynamics | Vibrio cholerae - enzymology | Isoenzymes - metabolism | Oligosaccharides - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Glycoside Hydrolases - chemistry | Protein Interaction Domains and Motifs | Streptococcus pyogenes - chemistry | Antibodies, Monoclonal - chemistry | Carbohydrate Sequence | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Genetic Vectors - chemistry | Isoenzymes - genetics | Streptomyces - chemistry | Bacterial Proteins - genetics | Genetic Vectors - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Oligosaccharides - metabolism | Amino Acid Motifs | Hydrolysis | Protein Conformation, beta-Strand | Escherichia coli - genetics | Streptococcus pyogenes - enzymology | Protein Binding | Bacterial Proteins - metabolism | Streptomyces - enzymology | Molecular Docking Simulation | Glycoside Hydrolases - metabolism | Kinetics | Trichoderma - chemistry | Bioengineering | N-Acetylglucosaminidase | N-Acetylglucosamine | Hydrolase | Immunoglobulin G | Grooves | Oligosaccharides | N-glycans | Antennae | Substrates | Molecular chains | Glycan | Polysaccharides | N-linked glycans | Substrate specificity | Monoclonal antibodies | Chemical synthesis | Binding sites | Glycoside hydrolase | Crystal structure
Journal Article