Search results for "Proteasome inhibitors"

showing 7 items of 27 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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Immunoproteasome and Non-Covalent Inhibition: Exploration by Advanced Molecular Dynamics and Docking Methods

2021

The selective inhibition of immunoproteasome is a valuable strategy to treat autoimmune, inflammatory diseases, and hematologic malignancies. Recently, a new series of amide derivatives as non-covalent inhibitors of the β1i subunit with Ki values in the low/submicromolar ranges have been identified. Here, we investigated the binding mechanism of the most potent and selective inhibitor, N-benzyl-2-(2-oxopyridin-1(2H)-yl)propanamide (1), to elucidate the steps from the ligand entrance into the binding pocket to the ligand-induced conformational changes. We carried out a total of 400 ns of MD-binding analyses, followed by 200 ns of plain MD. The trajectories clustering allowed identifying thre…

Proteasome Endopeptidase ComplexStereochemistryPharmaceutical ScienceOrganic chemistryinduced-fit dockingMolecular Dynamics Simulation01 natural sciencesArticlemetadynamicsAnalytical Chemistry03 medical and health scienceschemistry.chemical_compoundimmunoproteasomeQD241-441AmideDrug DiscoveryOrganosilicon CompoundsPhysical and Theoretical Chemistrynon-covalent inhibitor030304 developmental biology0303 health sciencesBinding Sites010405 organic chemistrymolecular dynamicnon-covalent inhibitorsMetadynamicsRational designDipeptidesLigand (biochemistry)PropanamideSettore CHIM/08 - Chimica Farmaceuticamolecular dynamics0104 chemical sciencesMolecular Docking SimulationchemistryChemistry (miscellaneous)Docking (molecular)MD bindingMolecular MedicinemetadynamicLead compoundOligopeptidesProteasome InhibitorsAcetamideProtein BindingMolecules
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BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins.

2010

Increasing evidence indicates the existence of selective autophagy pathways, but the manner in which substrates are recognized and targeted to the autophagy system is poorly understood. One strategy is transport of a particular substrate to the aggresome, a perinuclear compartment with high autophagic activity. In this paper, we identify a new cellular pathway that uses the specificity of heat-shock protein 70 (Hsp70) to misfolded proteins as the basis for aggresome-targeting and autophagic degradation. This pathway is regulated by the stress-induced co-chaperone Bcl-2-associated athanogene 3 (BAG3), which interacts with the microtubule-motor dynein and selectively directs Hsp70 substrates …

Protein FoldingRecombinant Fusion ProteinsDyneinGreen Fluorescent ProteinsAggrephagyMice TransgenicBAG3BiochemistryMiceJUNQ and IPODChlorocebus aethiopsGeneticsAutophagyAnimalsHumansPoint MutationHSP70 Heat-Shock ProteinsMolecular BiologyAdaptor Proteins Signal TransducingSequence DeletionInclusion BodiesMotor NeuronsbiologySuperoxide DismutaseAutophagyScientific ReportsDyneinsTransport proteinCell biologyProtein TransportAggresomeHEK293 CellsSpinal CordChaperone (protein)COS Cellsbiology.proteinApoptosis Regulatory ProteinsProteasome InhibitorsEMBO reports
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BAG3 Proteomic Signature under Proteostasis Stress

2020

The multifunctional HSP70 co-chaperone BAG3 (BCL-2-associated athanogene 3) represents a key player in the quality control of the cellular proteostasis network. In response to stress, BAG3 specifically targets aggregation-prone proteins to the perinuclear aggresome and promotes their degradation via BAG3-mediated selective macroautophagy. To adapt cellular homeostasis to stress, BAG3 modulates and functions in various cellular processes and signaling pathways. Noteworthy, dysfunction and deregulation of BAG3 and its pathway are pathophysiologically linked to myopathies, cancer, and neurodegenerative disorders. Here, we report a BAG3 proteomic signature under proteostasis stress. To elucidat…

ProteomicsautophagyCell signalingCellular homeostasisinteractomeBiologyBAG3InteractomeArticleStress PhysiologicalHumansddc:610Protein Interaction Mapsprotein quality controllcsh:QH301-705.5Adaptor Proteins Signal TransducingProto-Oncogene Proteins c-yesproteostasisBAG3AutophagyMolecular Sequence Annotationstress responseGeneral MedicineCell biologyGene OntologyHEK293 CellsAggresomeProteostasislcsh:Biology (General)Multivariate AnalysisSignal transductionApoptosis Regulatory ProteinsProteasome InhibitorsProtein BindingCells
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Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

2003

Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

Time FactorsLeupeptinsApoptosisRetinoblastoma ProteinAntioxidantsAmino Acid Chloromethyl KetonesMembrane Potentialschemistry.chemical_compoundSettore BIO/10 - BiochimicaMG132Caspase 8OsteosarcomaChemistryCaspase 3Cytochromes cFlow CytometryMitochondriaCysteine EndopeptidasesProto-Oncogene Proteins c-bcl-2CaspasesOsteosarcomamedicine.drugmusculoskeletal diseasesProteasome Endopeptidase ComplexCell SurvivalBlotting Westernbcl-X Proteinmacromolecular substancesTransfectionMultienzyme ComplexesCell Line Tumorparasitic diseasesmedicineHumansProtease InhibitorsneoplasmsMolecular BiologySaos-2 cellsDose-Response Relationship DrugCell Biologymedicine.diseaseAcetylcysteineApoptosis osteosarcoma proteasome inhibitorsMicroscopy FluorescenceApoptosisCancer researchProteasome inhibitorTumor Suppressor Protein p53Reactive Oxygen Specieshuman activities
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Proteasome comprising a beta1 inducible subunit acts as a negative regulator of NADPH oxidase during elicitation of plant defense reactions.

2005

Elicitation of defense reactions in tobacco by cryptogein, triggered a production of active oxygen species (AOS) via the NADPH oxidase, NtrbohD, and an accumulation of beta1din, a defense induced beta-type subunit of 20S proteasome. The proteasome inhibitor, MG132, stimulated this AOS production. Tobacco cells transformed with sense constructs of beta1din showed an inhibition of the AOS production following elicitin treatment, whereas the antisense transformed cells showed a strongly enhanced AOS production. In cells transformed with sense construct of beta1din, the NtrbohD transcripts failed to be induced by cryptogein as observed in control and antisense transformed cells. Conversely, in …

Tobacco BY-2 cellsHypersensitive responseProteasome Endopeptidase ComplexLeupeptinsBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyCysteine Proteinase InhibitorsBiochemistrychemistry.chemical_compoundStructural BiologyMG132Sense (molecular biology)TobaccoGeneticsmedicineNADPH OXIDASEPROTEASOMEMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSPlant ProteinsCRYPTOGEINNADPH oxidaseTOBACCO BY-2 CELLSNADPH OxidasesElicitinCell BiologyOligonucleotides AntisenseProtein SubunitsProteasomechemistryBiochemistryProteasome inhibitorbiology.proteinPLANT DEFENSEAOS PRODUCTIONReactive Oxygen SpeciesProteasome Inhibitorsmedicine.drugFEBS letters
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Prevention of venous thromboembolic events occurring in myeloma patients treated with second-generation novel agents

2021

Thrombosis and neoplasms are strictly linked, and the diagnosis of a malignancy is a relevant risk factor for venous thromboembolism (VTE). In particular, between gammopathies, the VTE risk is known to be increased in both monoclonal gammopathy of uncertain significance and in multiple myeloma, with a 3- and 9-fold increase respectively, when compared to the general population. The risk appears to be further increased in patients treated with immunomodulating drugs, such as thalidomide, especially when in combination with dexamethasone or conventional cytotoxic chemotherapies, and lenalidomide. In 2008 the International Myeloma Working Group put out thrombosis prophylaxis recommendations fo…

medicine.medical_specialtyPopulationAntineoplastic Agents030204 cardiovascular system & hematologyRisk Assessment03 medical and health sciencesAntineoplastic Agents Immunological0302 clinical medicineFibrinolytic AgentsRisk FactorsInternal medicinemedicineHumansImmunologic FactorsRisk factoreducationMultiple myelomaLenalidomideeducation.field_of_study030219 obstetrics & reproductive medicinebusiness.industryWarfarinAnticoagulantsVenous ThromboembolismGeneral MedicineEvidence-based medicinemedicine.diseaseThrombosisPrevention and controlThalidomideTreatment OutcomeMultiple MyelomabusinessProteasome Inhibitorsmedicine.drugPanminerva Medica
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