Search results for "DASE"

showing 10 items of 1891 documents

Preparation of two sets of 5,6,7-trioxygenated dihydroflavonol derivatives as free radical scavengers and neuronal cell protectors to oxidative damag…

2009

An unusual class of 5,6,7-trioxygenated dihydroflavonols (3a-e and 4a-j) were designed and prepared. Their antioxidative properties were assessed by examining their capacities in several in vitro models, including superoxide anion and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging, rat liver homogenate lipid peroxidation inhibition, PC12 cells protection from oxidative damage, and xanthine oxidase inhibition. These dihydroflavonols displayed positive quenching abilities towards O(2)(-) and DPPH free radicals, in which the majority exhibited superior antioxidant properties to Vitamin C. cis-Configurated compound (+/-)-3e demonstrated remarkable inhibition to LPO with an IC(50) value…

Models MolecularXanthine OxidaseAntioxidantFlavonolsmedicine.drug_classDPPHmedicine.medical_treatmentClinical BiochemistryMolecular ConformationPharmaceutical Sciencemedicine.disease_causeBiochemistryPC12 CellsAntioxidantsLipid peroxidationRats Sprague-Dawleychemistry.chemical_compoundStructure-Activity RelationshipDrug DiscoverymedicineAnimalsXanthine oxidaseMolecular BiologyXanthine oxidase inhibitorNeuronsSuperoxideOrganic ChemistryFree Radical ScavengersFree radical scavengerRatschemistryBiochemistryMolecular MedicineLipid PeroxidationReactive Oxygen SpeciesOxidative stressBioorganicmedicinal chemistry
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Mapping protein matrix cavities in human cytoglobin through Xe atom binding

2004

Abstract Cytoglobin is the fourth recognized globin type, almost ubiquitously distributed in human tissues; its function is still poorly understood. Cytoglobin displays a core region of about 150 residues, structurally related to hemoglobin and myoglobin, and two extra segments, about 20 residues each, at the N- and C-termini. The core region hosts a large apolar cavity, held to provide a ligand diffusion pathway to/from the heme, and/or ligand temporary docking sites. Here we report the crystal structure (2.4 A resolution, R -factor 19.1%) of a human cytoglobin mutant bearing the CysB2(38) → Ser and CysE9(83) → Ser substitutions (CYGB*), treated under pressurized xenon. Three Xe atoms bind…

Models MolecularXenonMacromolecular SubstancesProtein ConformationBiophysicsHemeCrystallography X-RayBiochemistrychemistry.chemical_compoundHumansComputer SimulationGlobinMolecular BiologyHemeBinding SitesCytoglobinCytoglobinOxygen transportCell BiologyGlobinsGlobin foldCrystallographyPeroxidasesMyoglobinchemistryNeuroglobinBiophysicsHemoglobinPorosityProtein BindingBiochemical and Biophysical Research Communications
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Candidate Targets for Hepatitis C Virus-Specific Antiviral Therapy

1997

The hepatitis C virus (HCV) was identified as the major causative agent of posttransfusion and community-acquired non-A, non-B hepatitis throughout the world. It is an enveloped virus with a plus-strand RNA genome encoding a polyprotein of about 3,010 amino acids. This polyprotein is cleaved co- and posttranslationally into mature viral proteins by host cell signal peptidases and 2 viral enzymes designated the NS2-3 proteinase and the NS3/4A proteinase complex. It is assumed that virus replication takes place in a membrane-associated complex containing at least 2 viral enzymatic activities: the NS3 nucleoside triphosphatase (NTPase)/helicase and the NS5B RNA-dependent RNA polymerase (RdRp).…

Models MolecularvirusesHepatitis C virusHepacivirusViral Nonstructural ProteinsBiologyVirus Replicationmedicine.disease_causechemistry.chemical_compoundViral life cycleViral envelopeVirologyRNA polymeraseEndopeptidasesmedicineHumansNS5BNS3DNA Helicasesvirus diseasesRNAbiochemical phenomena metabolism and nutritionRNA-Dependent RNA PolymeraseVirologydigestive system diseasesCysteine EndopeptidasesInfectious DiseaseschemistryViral replicationIntervirology
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Salivary myeloperoxidase and malondialdehyde are increased in patients exhibiting an asymptomatic mandibular impacted third molar

2019

Background To determine whether saliva is a good means of evaluating concentrations of oxidative stress biomarkers, analyzing the correlation between concentrations in saliva and in follicular tissue, and to compare biomarker concentrations in patients with one asymptomatic mandibular impacted third molar (MITM) (before extraction) with a healthy control, and to determine how biomarkers are modified by extraction. Material and Methods 80 patients with one asymptomatic MITM and 80 healthy controls were included. Saliva samples were collected from all subjects (before extraction in the study group) to evaluate Myeloperoxidase (MPO) and Malondialdehyde (MDA) concentrations. Follicular tissues …

Molarmedicine.medical_specialtySalivamedicine.disease_causeAsymptomaticGastroenterology03 medical and health scienceschemistry.chemical_compound0302 clinical medicineMalondialdehydeInternal medicineFollicular phasemedicineHumansSalivaGeneral DentistryPeroxidasebiologybusiness.industryResearchTooth Impacted030206 dentistry:CIENCIAS MÉDICAS [UNESCO]MalondialdehydeOtorhinolaryngologychemistryMyeloperoxidaseUNESCO::CIENCIAS MÉDICASbiology.proteinBiomarker (medicine)Molar ThirdSurgeryOral Surgerymedicine.symptombusinessBiomarkersOxidative stressMedicina Oral Patología Oral y Cirugia Bucal
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Comparison of clinical efficacy of methylprednisolone and serratiopeptidase for reduction of postoperative sequelae after lower third molar surgery

2015

Background: Surgical removal of mandibular third molars results in some degree of post-operative pain, swelling and trismus. These can be controlled by proper administration of local anesthesia, careful bone removal, minimal trauma to adjacent soft tissues and administration of methylprednisolone and serratiopeptidase drugs. The aim of the present study was to compare the efficacy of methylprednisolone and serratiopeptidase in controlling post- operative pain, swelling and trismus after surgical removal of impacted mandibular third molars. Material and Methods: The subjects were divided into two groups of 50 patients each undergoing surgical removal of mandibular third molars. Group A was g…

Molarmedicine.medical_specialtybusiness.industryResearchmedicine.medical_treatmentAnalgesicSoft tissueOdontología:CIENCIAS MÉDICAS [UNESCO]TrismusCiencias de la saludSurgeryMethylprednisoloneSerratiopeptidaseUNESCO::CIENCIAS MÉDICASmedicineLocal anesthesiaOral Surgerymedicine.symptombusinessGeneral DentistryReduction (orthopedic surgery)medicine.drugJournal of Clinical and Experimental Dentistry
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Caspase-mediated apoptosis in sponges: cloning and function of the phylogenetic oldest apoptotic proteases from Metazoa

2003

AbstractSponges (phylum Porifera) represent the phylogenetically oldest metazoan phylum. These animals have complex cell adhesion and powerful immune systems which allow the formation of a distinct body plan. Consequently, an apoptotic machinery has to be predicted that allows sponges to eliminate unwanted cells accumulating during development. With the marine sponge Geodia cydonium, it is shown that allografts of these animals undergo apoptosis as demonstrated by apoptotic DNA fragmentation. Extracts from allografts contain an enzymic activity characteristic for caspases; as substrate to determine the cleavage activity, Ac-DEVD-AMC was applied. cDNAs encoding predicted caspase-3-related pr…

Molecular Sequence DataApoptosisCaspase 3SpongeCoumarinsEndopeptidasesAnimalsInvertebrateAmino Acid SequenceCloning MolecularEnzyme InhibitorsMolecular BiologyPhylogenyCaspasebiologyCaspase 3Cell adhesion moleculeAlternative splicingApoptotic DNA fragmentationPotential proapoptotic molecule DD2Cell BiologyBcl-2 homologous proteinbiology.organism_classificationSuberites domunculaCaspaseCaspase InhibitorsPoriferaCell biologyIsoenzymesSuberites domunculaSpongeApoptosisCaspasesbiology.proteinOligopeptidesSequence AlignmentBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes

1999

The gene xynC encoding xylanase C from Bacillus sp. BP-23 was cloned and expressed in Escherichia coli. The nucleotide sequence of a 3538 bp DNA fragment containing xynC gene was determined, revealing an open reading frame of 3258 bp that encodes a protein of 120,567 Da. A comparison of the deduced amino acid sequence of xylanase C with known beta-glycanase sequences showed that the encoded enzyme is a modular protein containing three different domains. The central region of the enzyme is the catalytic domain, which shows high homology to family 10 xylanases. A domain homologous to family IX cellulose-binding domains is located in the C-terminal region of xylanase C, whilst the N-terminal r…

Molecular Sequence DataBacillusBiologymedicine.disease_causeMicrobiologyHomology (biology)Substrate Specificitychemistry.chemical_compoundCatalytic DomainEnzyme StabilityEscherichia colimedicineXylobioseAmino Acid SequenceCloning MolecularEscherichia coliPeptide sequencechemistry.chemical_classificationEndo-14-beta XylanasesSequence Homology Amino AcidThermophileTemperatureNucleic acid sequenceSequence Analysis DNAXylosidasesEnzymeBiochemistrychemistryGenes BacterialXylanaseSequence AlignmentMicrobiology
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Splice donor site mutation in the lysosomal neuraminidase gene causing exon skipping and complete loss of enzyme activity in a sialidosis patient.

2001

Sialidosis is a lysosomal storage disease caused by the deficiency of K K-N-acetylneuraminidase (NEU1; sialidase), the key enzyme for the intralysosomal catabolism of sialylated glycoconjugates. We have identified a homozygous transversion in the last intron (IVSE +1 Gs C) in neu1 of a sialidosis patient. Sequencing of the truncated cDNA revealed an alternatively spliced neu1 transcript which lacks the complete sequence of exon 5. Skipping of exon 5 leads to a frameshift and results in a premature termination codon. This is the first description of an intronic point mutation causing a complete deficiency of the lysosomal neuraminidase activity. fl 2001 Federation of Euro- pean Biochemical S…

Molecular Sequence DataBiophysicsNeuraminidaseBiochemistryFrameshift mutationNEU1ExonLysosomal neuraminidaseStructural BiologyMucolipidosesGeneticsLysosomal storage diseasemedicineHumansSialidosisAmino Acid SequenceMolecular BiologyGeneticsSialidosisSplice site mutationbiologySequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionDonor splice siteCell BiologyExonsFibroblastsmedicine.diseaseMolecular biologyExon skippingMutationbiology.proteinRNA Splice SitesLysosomesNeuraminidaseExon skippingGene DeletionFEBS letters
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Two α subunits and one β subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio

2007

Abstract Meprins are members of the astacin family of metalloproteases expressed in epithelial tissues, intestinal leukocytes and certain cancer cells. In mammals, there are two homologous subunits, which form complex glycosylated disulfide-bonded homo- and heterooligomers. Both human meprin α and meprin β cleave several basement membrane components, suggesting a role in epithelial differentiation and cell migration. There is also evidence that meprin β is involved in immune defence owing to its capability of activating interleukin-1β and the diminished mobility of intestinal leukocytes in meprin β-knockout mice. Here we show for the first time by reverse transcription PCR, immunoblotting a…

Molecular Sequence DataClinical BiochemistryDanioBiochemistryCatalysisChromosomesConserved sequenceAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyPeptide sequenceZebrafishConserved SequencePhylogenyZebrafishRegulation of gene expressionMessenger RNAbiologyMetalloendopeptidasesbiology.organism_classificationMolecular biologyProtein Structure TertiaryCell biologyProtein SubunitsZincGene Expression RegulationMicroscopy FluorescenceStructural Homology Proteinbiology.proteinAstacinSequence AlignmentATP synthase alpha/beta subunitsbchm
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Cloning and characterization of PRB1, a Candida albicans gene encoding a putative novel endoprotease B and factors affecting its expression

2002

Abstract Several cDNA fragments corresponding to transcripts differentially expressed under conditions that favor mycelial growth of Candida albicans were identified by the “differential display” technique. One of these was cloned and used as a probe to rescue the full gene from a genomic library of the fungus. The sequence identified a single, uninterrupted open reading frame of 1395 nucleotides encoding a putative protein of 465 residues and a theoretical molecular weight of 50.3 kDa, present in the genome as a single copy located at chromosome 2 in different strains. The gene product showed high homology with subtilisin-like proteases, mainly PRB1, the vacuolar B protease from Saccharomy…

Molecular Sequence DataMutantCatabolite repressionMicrobiologyFungal ProteinsGene productGene Expression Regulation FungalComplementary DNACandida albicansHumansAmino Acid SequenceCloning MolecularDNA FungalCandida albicansMolecular BiologyGeneGene LibraryDifferential displayBase SequencebiologyGene Expression ProfilingSerine EndopeptidasesSequence Analysis DNAGeneral Medicinebiology.organism_classificationMolecular biologyElectrophoresis Gel Pulsed-FieldBlotting SouthernOpen reading frameBiochemistryMutagenesisChromosomes FungalSequence AlignmentResearch in Microbiology
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