Search results for "Inhibition"

showing 10 items of 590 documents

Substituted 2-(3',4',5'-trimethoxybenzoyl)-benzo[b]thiophene derivatives as potent tubulin polymerization inhibitors.

2010

The central role of microtubules in cell division and mitosis makes them a particularly important target for anticancer agents. On our early publication, we found that a series of 2-(3',4',5'-trimethoxybenzoyl)-3-aminobenzo[b]thiophenes exhibited strong antiproliferative activity in the submicromolar range and significantly arrested cells in the G2-M phase of the cell cycle and induced apoptosis. In order to investigate the importance of the amino group at the 3-position of the benzo[b]thiophene skeleton, the corresponding 3-unsubstituted and methyl derivatives were prepared. A novel series of inhibitors of tubulin polymerization, based on the 2-(3,4,5-trimethoxybenzoyl)-benzo[b]thiophene m…

Models MolecularStereochemistryClinical BiochemistrySubstituentPharmaceutical ScienceAntineoplastic AgentsThiophenesAnisolesBiochemistryArticleAntineoplastic AgentAnisolechemistry.chemical_compoundStructure-Activity RelationshipThiopheneMicrotubuleTubulinTubulin ModulatorCell Line TumorNeoplasmsDrug DiscoveryThiopheneAnimalsHumansMolecular BiologyCell ProliferationbiologyBicyclic moleculeAnimalCell growthTubulin ModulatorsOrganic ChemistryCell CycleTubulin ModulatorsRatsTubulinchemistrybiology.proteinRatNeoplasmMolecular MedicineGrowth inhibitionHumanBioorganicmedicinal chemistry
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New alkaloid antibiotics that target the DNA topoisomerase I of Streptococcus pneumoniae

2011

16 pags, 3 figs, 3 tabs

Models MolecularTopoisomerase-I Inhibitormedicine.disease_causeMicrobiologyBiochemistryCell LineMicrobiology03 medical and health scienceschemistry.chemical_compoundAlkaloidsBacterial ProteinsStreptococcus pneumoniaemedicineHumansAporphineMolecular BiologyEscherichia coli030304 developmental biologychemistry.chemical_classification0303 health sciencesDose-Response Relationship Drugbiology030306 microbiologyTopoisomeraseCell BiologyPhenanthrenesProtein Structure TertiaryAnti-Bacterial Agents3. Good healthStreptococcus pneumoniaeEnzymeDNA Topoisomerases Type IchemistryBiochemistrybiology.proteinDNA supercoilTopoisomerase I InhibitorsGrowth inhibitionJournal of Biological Chemistry 286: 6402-6413 (2011)
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Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

2021

AbstractRhodesain is the lysosomal cathepsin L-like cysteine protease ofT. brucei rhodesiense, the causative agent of Human African Trypanosomiasis. The enzyme is essential for the proliferation and pathogenicity of the parasite as well as its ability to overcome the blood-brain barrier of the host. Lysosomal cathepsins are expressed as zymogens with an inactivating pro-domain that is cleaved under acidic conditions. A structure of the uncleaved maturation intermediate from a trypanosomal cathepsin L-like protease is currently not available. We thus established the heterologous expression ofT. brucei rhodesiensepro-rhodesain inE. coliand determined its crystal structure. The trypanosomal pr…

Models MolecularTrypanosoma brucei rhodesiense0301 basic medicinemedicine.medical_treatmentBiochemistrycysteine proteaseproenzymefluorescence correlation spectroscopy (FCS)Trypanosoma bruceiBBB blood–brain barrierCD circular dichroismchemistry.chemical_classificationEnzyme PrecursorsbiologyChemistryhsCathL human cathepsin LHydrogen-Ion ConcentrationCysteine proteaseFCS fluorescence correlation spectroscopyCysteine EndopeptidasesBiochemistryHAT Human African TrypanosomiasisNTD neglected tropical diseaseResearch Articlecrystal structureProteasesSEC size-exclusion chromatographyPET-FCS photoinduced electron transfer–fluorescence correlation spectroscopyAfrican Sleeping SicknessTrypanosoma bruceiCleavage (embryo)03 medical and health sciencesTbCathB T. brucei cathepsin BProtein DomainsZymogenmedicineMolecular BiologyzymogenrhodesainCathepsinProtease030102 biochemistry & molecular biologyActive siteTrypanosoma brucei rhodesienseCell Biologybiology.organism_classificationmolecular dynamicsEnzyme ActivationEnzyme030104 developmental biologybiology.proteinautoinhibitionHeterologous expressionJournal of Biological Chemistry
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Rational design of allosteric modulators of the aromatase enzyme: An unprecedented therapeutic strategy to fight breast cancer.

2019

Estrogens play a key role in cellular proliferation of estrogen-receptor-positive (ER+) breast cancers (BCs). Suppression of estrogen production by competitive inhibitors of the enzyme aromatase (AIs) is currently one of the most effective therapies against ER + BC. Yet, the development of acquired resistance, after prolonged treatments with AIs, represents a clinical major concern. Serendipitous findings indicate that aromatase may be non-competitively inhibited by clinically employed drugs and/or industrial chemicals. Here, by performing in silico screening on two putative allosteric sites, molecular dynamics and free energy simulations, supported by enzymatic and cell-based assays, we id…

Molecular dynamicmedicine.drug_classIn silicoAllosteric regulationCytochromes P450; Aromatase; Molecular dynamics; Aromatase inhibitors; Docking; Breast cancer; Resistance onset; Mixed inhibition mechanismAntineoplastic AgentsBreast NeoplasmsMolecular dynamicsMolecular Dynamics SimulationDockingStructure-Activity RelationshipBreast cancerBreast cancerAromataseAllosteric RegulationCell Line TumorDrug DiscoverymedicineResistance onsetHumansMixed inhibition mechanismAromataseEnzyme InhibitorsCell ProliferationPharmacologychemistry.chemical_classificationbiologyDose-Response Relationship DrugMolecular StructureChemistryOrganic ChemistryRational designAromatase inhibitorGeneral Medicinemedicine.diseaseEnzymeAromatase inhibitorsSettore CHIM/03 - Chimica Generale E InorganicaEstrogenDocking (molecular)Drug Designbiology.proteinCancer researchDrug Screening Assays AntitumorCytochromes P450European journal of medicinal chemistry
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Unusual target selectivity of perisomatic inhibitory cells in the hilar region of the rat hippocampus.

2000

Perisomatic inhibitory innervation of all neuron types profoundly affects their firing characteristics and vulnerability. In this study we examined the postsynaptic targets of perisomatic inhibitory cells in the hilar region of the dentate gyrus where the proportion of potential target cells (excitatory mossy cells and inhibitory interneurons) is approximately equal. Both cholecystokinin (CCK)- and parvalbumin-immunoreactive basket cells formed multiple contacts on the somata and proximal dendrites of mossy cells. Unexpectedly, however, perisomatic inhibitory terminals arriving from these cell types largely ignored hilar GABAergic cell populations. Eighty-ninety percent of various GABAergic…

Mossy fiber (hippocampus)MaleInterneuronCalcitonin Gene-Related PeptidePopulationPresynaptic TerminalsBiologyInhibitory postsynaptic potentialHippocampusBasket cellPostsynaptic potentialInterneuronsmedicineAnimalsReceptors AMPARats WistarARTICLEeducationeducation.field_of_studyGeneral NeuroscienceDentate gyrusNeural InhibitionDendritesAxonsRatsmedicine.anatomical_structureParvalbuminsnervous systemDentate GyrusMossy Fibers HippocampalExcitatory postsynaptic potentialCholecystokininNeuroscienceThe Journal of neuroscience : the official journal of the Society for Neuroscience
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Chapter 9 The effects of a prepulse on the StartReact phenomenon

2006

Publisher Summary This chapter presents a study to investigate whether the inhibitory effects of the prepulse are different in the condition of motor preparation with respect to that of unexpectancy and whether the inhibition of the startle reaction by a prepulse is associated with the inhibition of the StartReact phenomenon. The chapter demonstrates that the procedure could help in ascertaining whether reflex and volitional components are actually combined in the StartReact phenomenon. Eight healthy volunteers, six men and two women, aged between 25 and 52 years were investigated and the startle reaction was recorded with surface electrodes over the right orbicularis oculi muscle and, in t…

Motor taskReflexStimulus (physiology)Voluntary actionInhibitory postsynaptic potentialPsychologySternocleidomastoid muscleStartle reactionNeurosciencePrepulse inhibition
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Novel antiproliferative chimeric compounds with marked histone deacetylase inhibitory activity.

2014

Given our interest in finding potential antitumor agents and in view of the multifactorial mechanistic nature of cancer, in the present work, taking advantage of the multifunctional ligands approach, new chimeric molecules were designed and synthesized by combining in single chemical entities structural features of SAHA, targeting histone deacetylases (HDACs), with substituted stilbene or terphenyl derivatives previously obtained by us and endowed with antiproliferative and pro-apoptotic activity. The new chimeric derivatives were characterized with respect to their cytotoxic activity and their effects on cell cycle progression on different tumor cell lines, as well as their HDACs inhibitio…

Multifunctional ligandsCell cycle progressionHDAC inhibitionInhibitory postsynaptic potentialBiochemistrySettore BIO/13 - Biologia ApplicataHDACDrug DiscoverymedicineCytotoxic T cellHDAC inhibition; Multifunctional ligands; antiproliferative activity; chimeric compound; stilbeneCancerbiologyChemistryANTIPROLIFERATIVE ACTIVITYOrganic ChemistryMultifunctional ligandsCancermultifunctional ligandmedicine.diseaseCombinatorial chemistrySettore CHIM/08 - Chimica FarmaceuticastilbeneHistoneBiochemistrySTILBENESbiology.proteinchimeric compoundHDAC INHIBITORSEpigeneticsHistone deacetylaseChimeric molecules
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The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B

2021

Meprin β (Mβ) is a multidomain type-I membrane metallopeptidase that sheds membrane-anchored substrates, releasing their soluble forms. Fetuin-B (FB) is its only known endogenous protein inhibitor. Herein, we analyzed the interaction between the ectodomain of Mβ (MβΔC) and FB, which stabilizes the enzyme and inhibits it with subnanomolar affinity. The MβΔC:FB crystal structure reveals a ∼250-kDa, ∼160-Å polyglycosylated heterotetrameric particle with a remarkable glycan structure. Two FB moieties insert like wedges through a “CPDCP trunk” and two hairpins into the respective peptidase catalytic domains, blocking the catalytic zinc ions through an “aspartate switch” mechanism. Uniquely, the …

Multiprotein complexMetallopeptidaseCleavage (embryo)Cell LineMiceProtein structureAnimalsHumansEctoprotein sheddingProtease InhibitorsInhibitionBinding SitesMultidisciplinarybiologyChemistryMetallopeptidaseMetalloendopeptidasesActive siteBiological SciencesSheddaseFetuin-BLepidopteraMolecular Docking SimulationTransmembrane domainEctodomainbiology.proteinBiophysicsProtein structureMultiprotein complexAlzheimer’s diseaseProtein Binding
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Combined Targeting of the Menin-MLL1 Chromatin Complex and FLT3 As a Novel Therapeutic Concept Against NPM1 Mutant or MLL-Rearranged AML with Mutated…

2019

NPM1mutant (NPM1mut) and MLL1-rearranged (MLL-r) acute myeloid leukemias (AMLs) exhibit aberrant expression of HOX and MEIS1 transcription factors and commonly harbor an activating mutation in the receptor tyrosine kinase FLT3. Pharmacologic inhibition of the menin-MLL1 complex reverses leukemogenic gene expression including MEIS1 and FLT3 and represents a therapeutic opportunity for the treatment of these leukemias. Here, we investigate the contribution of the menin-MLL1 complex to leukemic FLT3 signaling and assess the therapeutic potential of dual menin-MLL1 and FLT3 targeting. First, we performed RNA sequencing to delineate transcriptional changes associated with menin-MLL1 inhibition (…

NPM1ImmunologyPonatinibCell BiologyHematologyBiologymedicine.diseaseBiochemistrychemistry.chemical_compoundLeukemiachemistryhemic and lymphatic diseasesGene expressionCancer researchmedicineEctopic expressionGrowth inhibitionCrenolanibQuizartinibBlood
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Biogenic iron-silver nanoparticles inhibit bacterial biofilm formation due to Ag+ release as determined by a novel phycoerythrin-based assay

2020

Silver nanoparticles (Ag-NPs) can be considered as a cost-effective alternative to antibiotics. In the presence of Fe(III)-citrate and Ag+, Klebsiella oxytoca DSM 29614 produces biogenic Ag-NPs embedded in its peculiar exopolysaccharide (EPS). K. oxytoca DSM 29614 was cultivated in a defined growth medium–containing citrate (as sole carbon source) and supplemented with Ag+ and either low or high Fe(III) concentration. As inferred from elemental analysis, transmission and scanning electron microscopy, Fourier transform infrared spectrometry and dynamic light scattering, Ag-EPS NPs were produced in both conditions and contained also Fe. The production yield of high-Fe/Ag-EPS NPs was 12 times …

Nanoparticle production yieldNanoparticleBacterial exopolysaccharide; Biofilm formation inhibition; Biogenic bimetal nanoparticles; Nanoparticle production yield; Phycoerythrin fluorescence–based assay; Silver ion release;Biogenic bimetal nanoparticlesSettore BIO/19 - Microbiologia GeneraleApplied Microbiology and BiotechnologySilver nanoparticleNOBacterial exopolysaccharide; Biofilm formation inhibition; Biogenic bimetal nanoparticles; Nanoparticle production yield; Phycoerythrin fluorescence–based assay; Silver ion release03 medical and health scienceschemistry.chemical_compoundDynamic light scatteringBiofilm formation inhibitionPhycoerythrin fluorescence–based assay030304 developmental biology0303 health sciencesGrowth mediumbiology030306 microbiologySilver ion releaseBiofilmKlebsiella oxytocaGeneral Medicinebiology.organism_classificationFluorescenceBacterial exopolysaccharidechemistryYield (chemistry)BiotechnologyNuclear chemistry
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