Search results for "DASES"

showing 10 items of 485 documents

Optimization of peptidomimetic boronates bearing a P3 bicyclic scaffold as proteasome inhibitors

2014

Abstract A new series of pseudopeptide boronate proteasome inhibitors (2–3) was developed, through optimization of our previously described analogs of bortezomib, bearing a bicyclic 1,6-naphthyridin-5(6H)-one scaffold as P3 fragment (1). The biological evaluation on human 20S proteasome displayed a promising inhibition profile, especially for compounds bearing a P2 ethylene fragment, which exhibited Ki values in the nanomolar range for the ChT-L activity (e.g. 2a, Ki = 0.057 μM) and considerable selectivity for proteasome over bovine pancreatic α-chymotrypsin. Docking experiments into the yeast 20S proteasome revealed that the ligands are accommodated predominantly into the ChT-L site and t…

Proteasome Endopeptidase ComplexProtein ConformationStereochemistryPeptidomimeticAntineoplastic AgentsPeptidomimetic boronatePeptidomimetic boronates; Docing studies; Proteasome inhibitorsBortezomibchemistry.chemical_compoundCell Line TumorEndopeptidasesDrug DiscoverymedicineAnimalsHumansProteasome inhibitoranticancer drugTrypsinThreonineCell ProliferationPharmacologybiologyBicyclic moleculeBortezomibHydrolysisOrganic ChemistryActive siteGeneral MedicineBoronic AcidsCombinatorial chemistryMolecular Docking SimulationchemistryProteasomeDocking (molecular)Docking studieCaspasesDrug DesignPyrazinesProteolysisbiology.proteinCattlePeptidomimeticsProteasome InhibitorsLead compoundmedicine.drugEuropean Journal of Medicinal Chemistry
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SUMOylation of Blimp-1 promotes its proteasomal degradation

2011

Abstract B lymphocyte induced maturation protein-1 (Blimp-1) is a transcription repressor of the Krueppel-like family. Blimp-1 plays important roles in developmental processes, such as of germ cells and hair follicle stem cells. In B lymphocytes Blimp-1 orchestrates the terminal differentiation into plasma cells. We discovered that Blimp-1 undergoes SUMOylation by SUMO-1. This SUMOylation is modulated by the SUMO protease SENP1. While Blimp-1 is relatively stable in 293T cells, a fusion with SUMO1 rendered it to rapid proteasomal degradation. Increase in SENP1 activity stabilized Blimp-1, while a decrease promoted its degradation. Our data indicate that SUMOylation of Blimp-1 regulates its …

Proteasome Endopeptidase ComplexSENP1ImmunoprecipitationSUMO-1 ProteinBiophysicsSUMO proteinPlasma cellPlasma cellBiologyBiochemistryCell LineProtein–protein interactionSENP1Structural BiologyEndopeptidasesGeneticsmedicineHumansMolecular BiologyProteasomeProtein StabilityHEK 293 cellsSumoylationCell BiologyCell biologyRepressor ProteinsCysteine Endopeptidasesmedicine.anatomical_structureProteasomeSUMO proteasePositive Regulatory Domain I-Binding Factor 1IntracellularFEBS Letters
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Development and characterization of mouse anti-human LMP2, LMP7, TAP1 and TAP2 monoclonal antibodies.

2008

Low molecular mass polypeptides (LMP) 2 and LMP7 and transporter associated with antigen processing (TAP) subunits TAP1 and TAP2 play a crucial role in antigen processing and cell surface expression of HLA class I molecules. Since monoclonal antibodies (mAb) to these molecules will facilitate the analysis of their expression, structure and function in normal and transformed cells, in the present study we have developed these reagents. Specifically anti-LMP2 and LMP7 mAb were generated from BALB/c mice immunized with specific peptides, and anti-TAP1 and TAP2 mAb from BALB/c mice immunized with respective recombinant proteins. mAb VF101-39F7 and VF101-39G5 were shown to be specific for LMP2, …

Proteasome Endopeptidase Complexmedicine.drug_classRecombinant Fusion ProteinsImmunologyAntigen presentationBiologyMonoclonal antibodyBiochemistrylaw.inventionCell LineMicelawATP Binding Cassette Transporter Subfamily B Member 3Antibody SpecificityHLA AntigensMultienzyme ComplexesGeneticsmedicineImmunology and AllergyAnimalsHumansATP Binding Cassette Transporter Subfamily B Member 2DNA PrimersSkinAntigen PresentationMice Inbred BALB CHybridomasImmunoperoxidaseBase SequenceAntigen processingAntibodies MonoclonalProteinsGeneral MedicineTransporter associated with antigen processingMolecular biologyImmunohistochemistryCysteine EndopeptidasesCell cultureMonoclonalRecombinant DNAATP-Binding Cassette TransportersFemaleIndicators and ReagentsTissue antigens
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Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation

1995

Processing of the hepatitis C virus polyprotein is mediated by host cell signalases and at least two virally encoded proteinases. Of these, the serine-type proteinase encompassing the amino-terminal one-third of NS3 is responsible for cleavage at the four sites carboxy terminal of NS3. The activity of this proteinase is modulated by NS4A, a 54-amino-acid polyprotein cleavage product essential for processing at the NS3/4A, NS4A/4B, and NS4B/5A sites and enhancing cleavage efficiency between NS5A and NS5B. Using the vaccinia virus-T7 hybrid system to express hepatitis C virus polypeptides in BHK-21 cells, we studied the role of NS4A in proteinase activation. We found that the NS3 proteinase a…

Protein ConformationRecombinant Fusion ProteinsvirusesGenetic VectorsMolecular Sequence DataImmunologyVaccinia virusHepacivirusProtein Sorting SignalsViral Nonstructural ProteinsBiologyKidneyTransfectionCleavage (embryo)MicrobiologyAntibodiesCell LineSerineEpitopesViral Proteinschemistry.chemical_compoundProtein structureProteinase 3CricetinaeVirologyAnimalsAmino Acid SequenceProtein PrecursorsNS5BPeptide sequenceNS3Sequence Homology Amino AcidSerine Endopeptidasesvirus diseasesbiochemical phenomena metabolism and nutritiondigestive system diseasesNS2-3 proteaseBiochemistrychemistryInsect ScienceProtein Processing Post-TranslationalAlgorithmsRNA HelicasesResearch ArticleJournal of Virology
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Biocatalytic formation of synthetic melanin: The role of vanadium haloperoxidases, L-DOPA and iodide

2011

The vanadium haloperoxidase (V-HPO) enzyme, extracted from the brown alga Laminaria saccharina, is able to catalyze the formation of a black precipitate, using as precursor the amino acid L-dopa in the presence of hydrogen peroxide and iodide, in one-pot synthesis. The L-dopa oxidation is a multistep reaction with a crucial role played by the iodide in the enzyme catalyzed peroxidative production of dopachrome, a well known intermediate in the synthesis of melanin. Dopachrome is then converted to a synthetic form of melanin through a polymerization reaction. Factors, such as buffer composition and pH, influence significantly the reaction first steps, but further steps of melanin production …

Protein ConformationTyrosinaseIodideBuffersBiochemistryPolymerizationLevodopaInorganic ChemistryMelaninchemistry.chemical_compoundHaloperoxidaseOrganic chemistryIndolequinonesHydrogen peroxideMelaninschemistry.chemical_classificationChemistryVanadiumHydrogen PeroxideHydrogen-Ion ConcentrationIodidesKineticsPeroxidasesPolymerizationBiocatalysisBiocatalysisMicroscopy Electron ScanningDopachromeJournal of Inorganic Biochemistry
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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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Missense mutations of dual oxidase 2 (DUOX2) implicated in congenital hypothyroidism have impaired trafficking in cells reconstituted with DUOX2 matu…

2007

Abstract Dual oxidase 2 (DUOX2), a reduced NAD phosphate:O2 oxidoreductase flavoprotein, is a component of the thyrocyte H2O2 generator required for hormone synthesis at the apical plasma membrane. We recently identified a specific DUOX2 maturation factor (DUOXA2) that is necessary and sufficient for expression of functional DUOX2 in mammalian cell lines. We have now used a DUOXA2 reconstituted system to provide the first characterization of natural DUOX2 missense variants (Q36H, R376W, D506N) at the molecular level, analyzing their impact on H2O2 generation, trafficking, stability, folding, and DUOXA2 interaction. The Q36H and R376W mutations completely prevent routing of DUOX2 to the cell…

Protein FoldingMutantMutation MissenseBiologyEndoplasmic ReticulumCell membranesymbols.namesakeEndocrinologyMutant proteinPolysaccharidesCalnexinmedicineCongenital HypothyroidismAnimalsHumansMolecular BiologyCells CulturedFlavoproteinsOxidative foldingEndoplasmic reticulumCell MembraneMembrane ProteinsNADPH OxidasesDual oxidase 2General MedicineHydrogen PeroxideGolgi apparatusDual OxidasesRatsProtein Transportmedicine.anatomical_structureMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseBiochemistrysymbolsOxidation-ReductionMolecular endocrinology (Baltimore, Md.)
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Calcium negatively regulates meprin β activity and attenuates substrate cleavage

2015

The meprin β metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans and mice. Previous studies showed a diminished cleavage of certain meprin β substrates in the presence of calcium, although the mechanism was not clear. With the help of a specific fluorogenic peptide assay and the human amyloid precursor protein as substrate, we demonstrated that the influence of calcium is most likely a direct effect on human meprin β itself. Analyzing the crystal structures of pro- and mature meprin β helped to identify a cluster of negatively charged amino acids forming a potential calcium binding site. Mutation of 2 of these residues (D2…

Protein Foldingchemistry.chemical_elementCalciumEndoplasmic ReticulumBiochemistryCell LineSubstrate SpecificityAmyloid beta-Protein PrecursorChlorocebus aethiopsGeneticsAmyloid precursor proteinAnimalsHumansAmino Acid SequenceBinding siteProtein precursorMolecular BiologyCellular localizationSecretory pathwayMetalloproteinaseAmyloid beta-PeptidesBinding SitesbiologyEndoplasmic reticulumMetalloendopeptidasesCell biologyHEK293 CellschemistryCOS CellsMutationMetalloproteasesbiology.proteinCalciumAmyloid Precursor Protein SecretasesSequence AlignmentBiotechnologyThe FASEB Journal
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Bioinformatic flowchart and database to investigate the origins and diversity of Clan AA peptidases

2009

Abstract Background Clan AA of aspartic peptidases relates the family of pepsin monomers evolutionarily with all dimeric peptidases encoded by eukaryotic LTR retroelements. Recent findings describing various pools of single-domain nonviral host peptidases, in prokaryotes and eukaryotes, indicate that the diversity of clan AA is larger than previously thought. The ensuing approach to investigate this enzyme group is by studying its phylogeny. However, clan AA is a difficult case to study due to the low similarity and different rates of evolution. This work is an ongoing attempt to investigate the different clan AA families to understand the cause of their diversity. Results In this paper, we…

Protein familySequence analysisImmunologyProtein domainMolecular Sequence DataBiologycomputer.software_genreGeneral Biochemistry Genetics and Molecular BiologyProtein Structure SecondaryPhylogeneticsSequence Analysis ProteinSoftware DesignConsensus SequenceConsensus sequenceAspartic Acid EndopeptidasesClanAmino Acid SequenceDatabases ProteinPeptide sequencelcsh:QH301-705.5Ecology Evolution Behavior and SystematicsPhylogenyDatabaseAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)Applied MathematicsResearchComputational BiologyGenetic VariationGene AnnotationTemplates GeneticMarkov ChainsProtein Structure Tertiarylcsh:Biology (General)Modeling and SimulationGeneral Agricultural and Biological SciencescomputerBiology Direct
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Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 t…

2010

Abstract The metalloproteases meprin α and β are expressed in several tissues, leukocytes, and cancer cells. In skin, meprins are located in separate layers of human epidermis indicating distinct physiological functions, supported by effects on cultured keratinocytes. Meprin β induces a dramatic change in cell morphology and a significant reduction in cell number, whereas in vitro evidence suggests a role for meprin α in basal keratinocyte proliferation. Meprins are secreted as zymogens that are activated by tryptic proteolytical processing. Here, we identify human kallikrein-related peptidases (KLKs) 4, 5, and 8 to be specific activators of meprins. KLK5 is capable of activating both metal…

Proteolysismedicine.medical_treatmentClinical BiochemistryBiologyBiochemistrySubstrate SpecificitymedicineHumansAmino Acid SequenceProtein precursorMolecular BiologySkinSerine proteaseEnzyme PrecursorsMetalloproteinaseProteasemedicine.diagnostic_testMetalloendopeptidasesKLK5Trypsinddc:Enzyme Activationmedicine.anatomical_structureBiochemistrybiology.proteinKallikreinsKeratinocytemedicine.drug
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