Search results for "Indole"

showing 10 items of 570 documents

TGF-β inhibitor Smad7 regulates dendritic cell-induced autoimmunity

2017

TGF-β is an anti-inflammatory cytokine whose signaling is negatively controlled by Smad7. Previously, we established a role for Smad7 in the generation of autoreactive T cells; however, the function of Smad7 in dendritic cells (DCs) remains elusive. Here, we demonstrate that DC-specific Smad7 deficiency resulted in elevated expression of the transcription factors Batf3 and IRF8, leading to increased frequencies of CD8(+)CD103(+) DCs in the spleen. Furthermore, Smad7-deficient DCs expressed higher levels of indoleamine 2,3-dioxygenase (IDO), an enzyme associated with tolerance induction. Mice devoid of Smad7 specifically in DCs are resistant to the development of experimental autoimmune ence…

0301 basic medicineEncephalomyelitis Autoimmune Experimentalmedicine.medical_treatmentCellular differentiationAutoimmunitychemical and pharmacologic phenomenaCD8-Positive T-LymphocytesBiologyT-Lymphocytes RegulatorySmad7 ProteinImmune toleranceMice03 medical and health sciences0302 clinical medicineTransforming Growth Factor betaImmune TolerancemedicineAnimalsIndoleamine-Pyrrole 23-DioxygenaseMultidisciplinaryintegumentary systemExperimental autoimmune encephalomyelitisCell Differentiationhemic and immune systemsDendritic CellsDendritic cellTransforming growth factor betamedicine.diseaseCell biologyMice Inbred C57BLTolerance inductionBasic-Leucine Zipper Transcription Factors030104 developmental biologyCytokinePNAS PlusInterferon Regulatory FactorsImmunologybiology.proteinCytokinesSpleenCD8Signal Transduction030215 immunology
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Visualising G-quadruplex DNA dynamics in live cells by fluorescence lifetime imaging microscopy

2020

Guanine rich regions of oligonucleotides fold into quadruple-stranded structures called G-quadruplexes (G4s). Increasing evidence suggests that these G4 structures form in vivo and play a crucial role in cellular processes. However, their direct observation in live cells remains a challenge. Here we demonstrate that a fluorescent probe (DAOTA-M2) in conjunction with fluorescence lifetime imaging microscopy (FLIM) can identify G4s within nuclei of live and fixed cells. We present a FLIM-based cellular assay to study the interaction of non-fluorescent small molecules with G4s and apply it to a wide range of drug candidates. We also demonstrate that DAOTA-M2 can be used to study G4 stability i…

0301 basic medicineFluorescence-lifetime imaging microscopyIndolesIntravital MicroscopyGuanineScienceGeneral Physics and Astronomy010402 general chemistryG-quadruplex01 natural sciencesGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compoundMiceCell Line TumorAnimalsHumans030304 developmental biologyFluorescent Dyes0303 health sciencesMultidisciplinaryChemistryOligonucleotideCellular AssayQDNA HelicasesGeneral ChemistryDNAFibroblastsFluorescenceSmall moleculeChemical biologyFanconi Anemia Complementation Group Proteins0104 chemical sciencesMolecular ImagingG-QuadruplexesDNA helicase activity030104 developmental biologyMicroscopy FluorescenceGene Knockdown TechniquesBiophysicsFluorescent probesMolecular imagingRNA HelicasesNature Communications
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Targeting RNA structure in SMN2 reverses spinal muscular atrophy molecular phenotypes

2018

Modification of SMN2 exon 7 (E7) splicing is a validated therapeutic strategy against spinal muscular atrophy (SMA). However, a target-based approach to identify small-molecule E7 splicing modifiers has not been attempted, which could reveal novel therapies with improved mechanistic insight. Here, we chose as a target the stem-loop RNA structure TSL2, which overlaps with the 5′ splicing site of E7. A small-molecule TSL2-binding compound, homocarbonyltopsentin (PK4C9), was identified that increases E7 splicing to therapeutic levels and rescues downstream molecular alterations in SMA cells. High-resolution NMR combined with molecular modelling revealed that PK4C9 binds to pentaloop conformati…

0301 basic medicineIndolesCOMPOUND LIBRARIESDrug Evaluation PreclinicalGeneral Physics and AstronomyBiotecnologiaAnimals Genetically ModifiedExonMolecular Targeted TherapyRegulatory Elements Transcriptionallcsh:ScienceHUMAN-DISEASE GENESBIOACTIVE SMALL MOLECULESMultidisciplinaryChemistryDrug discovery[CHIM.ORGA]Chemical Sciences/Organic chemistryQImidazolesMUTATION PATTERNExonsSMA*3. Good healthCell biologySurvival of Motor Neuron 2 ProteinPhenotypeCribratgeRNA splicingNUCLEOTIDE STRUCTUREDrosophilaMESSENGER-RNACOMPUTATIONAL TOOLSMedical screeningMYOTONIC-DYSTROPHYScienceMuscular atrophyArticleGeneral Biochemistry Genetics and Molecular BiologyGenètica molecularMuscular Atrophy Spinal03 medical and health sciencesddc:570SPLICING MODIFIERSmedicineAnimalsHumansHIV-1 TARRNA MessengerAtròfia muscularMessenger RNAAlternative splicingRNAGeneral ChemistrySpinal muscular atrophymedicine.diseaseAlternative Splicing030104 developmental biologyRNAlcsh:QRNA Splice SitesHeLa CellsNature Communications
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Synthesis, antitumor activity and CDK1 inhibiton of new thiazole nortopsentin analogues

2017

A new series of thiazole nortopsentin analogues was conveniently synthesized with fair overall yields. The antiproliferative activity of the new derivatives was tested against different human tumor cell lines of the NCI full panel. Four of them showed good antitumor activity with GI(50) values from micro to nanomolar level. The mechanism of the antiproliferative effect of these derivatives, was pro-apoptotic, being associated with externalization of plasma membrane phosphatidylserine and DNA fragmentation. The most active and selective of the new thiazoles confined viable cells in G2/M phase and markedly inhibited in vitro CDK1 activity. (C) 2017 Elsevier Masson SAS.

0301 basic medicineIndolesCell SurvivalStereochemistryMolecular ConformationNortopsentin analogues3-b]pyridinesAntineoplastic AgentsApoptosisMarine alkaloids Nortopsentin analogues Antiproliferative activity Apoptosis CDK1 inhibitors Thiazolyl-1H-pyrrolo[23-b]pyridinesAntiproliferative activity01 natural sciencesStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundMarine alkaloidsCDC2 Protein KinaseDrug DiscoveryHumansThiazoleProtein Kinase InhibitorsCell ProliferationPharmacologyCyclin-dependent kinase 1Dose-Response Relationship DrugMarine alkaloids; Nortopsentin analogues; Antiproliferative activity; Apoptosis; CDK1 inhibitors; Thiazolyl-1H-pyrrolo[2; 3-b]pyridines010405 organic chemistryOrganic ChemistryImidazolesGeneral MedicinePhosphatidylserineThiazolyl-1H-pyrrolo[2Settore CHIM/08 - Chimica FarmaceuticaCyclin-Dependent KinasesIn vitro0104 chemical sciencesCDK1 inhibitors030104 developmental biologyMembranechemistryCell cultureApoptosisMCF-7 CellsDNA fragmentationCaco-2 CellsDrug Screening Assays Antitumor
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Sunitinib in patients with pre-treated pancreatic neuroendocrine tumors: A real-world study.

2018

Abstract Introduction Besides data reported in a Phase-III trial, data on sunitinib in pancreatic Neuroendocrine Tumors (panNETs) are scanty. Aim To evaluate sunitinib efficacy and tolerability in panNETs patients treated in a real-world setting. Patients and methods Retrospective analysis of progressive panNETs treated with sunitinib. Efficacy was assessed by evaluating progression-free survival, overall survival, and disease control (DC) rate (stable disease (SD) + partial response + complete response). Data are reported as median (25th–75th IQR). Results Eighty patients were included. Overall, 71.1% had NET G2, 26.3% had NET G1, and 2.6% had NET G3 neoplasms. A total of 53 patients (66.3…

0301 basic medicineIndolesEndocrinology Diabetes and MetabolismNeuroendocrine tumorsPyrroleGastroenterologyTarget therapyEfficacyAntineoplastic Agent0302 clinical medicineEndocrinologyRetrospective StudieSunitinibPancreadiabetes and metabolismSunitinibGastroenterologyPancreatic NeoplasmMiddle AgedDiabetes and MetabolismNeuroendocrine TumorsTreatment OutcomeTolerabilityNeuroendocrine tumors; Pancreas; Progressive disease; Sunitinib; Target therapy; Endocrinology Diabetes and Metabolism; Hepatology; EndocrinologyItaly030220 oncology & carcinogenesisNeuroendocrine tumorsmedicine.drugHumanAdultmedicine.medical_specialtyAntineoplastic AgentsNeutropenia03 medical and health sciencesNeuroendocrine tumorInternal medicinemedicineHumansPyrrolesProgression-free survivalPancreasCancer stagingAgedRetrospective StudiesHepatologybusiness.industryProgressive diseasemedicine.diseasePancreatic Neoplasms030104 developmental biologyNeuroendocrine tumors; pancreas; progressive disease; Sunitinib; target therapy; endocrinology; diabetes and metabolism; hepatology; endocrinologyIndolebusinessProgressive diseasePancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.]
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Feedback Regulation of Syk by Protein Kinase C in Human Platelets

2019

The spleen tyrosine kinase (Syk) is essential for immunoreceptor tyrosine-based activation motif (ITAM)-dependent platelet activation, and it is stimulated by Src-family kinase (SFK)-/Syk-mediated phosphorylation of Y352 (interdomain-B) and Y525/526 (kinase domain). Additional sites for Syk phosphorylation and protein interactions are known but remain elusive. Since Syk S297 phosphorylation (interdomain-B) was detected in platelets, we hypothesized that this phosphorylation site regulates Syk activity via protein kinase C (PKC)-and cyclic adenosine monophosphate (cAMP)-dependent pathways. ADP, the GPVI-agonist convulxin, and the GPIb&alpha

0301 basic medicineIndolesPlatelet AggregationSyk030204 cardiovascular system & hematologyenvironment and public healthMaleimideslcsh:Chemistrychemistry.chemical_compound0302 clinical medicinePhosphorylationlcsh:QH301-705.5SpectroscopyFeedback PhysiologicalKinaseConvulxinhemic and immune systemsGeneral MedicineComputer Science ApplicationsCell biologyAdenosine DiphosphateplateletsPhosphorylationbiological phenomena cell phenomena and immunityBlood Plateletschemical and pharmacologic phenomenaViper Venomsspleen tyrosine kinase (Syk)CatalysisArticleInorganic Chemistryglycoprotein VIglycoprotein Ibα03 medical and health sciencesCrotalid VenomsHumansSyk KinaseCyclic adenosine monophosphateLectins C-TypePlatelet activationPhysical and Theoretical ChemistryMolecular BiologyProtein kinase CPhospholipase C gammaOrganic Chemistryenzymes and coenzymes (carbohydrates)030104 developmental biologyProtein kinase domainchemistrylcsh:Biology (General)lcsh:QD1-999Calciumcyclic adenosine monophosphate (cAMP)protein kinase CInternational Journal of Molecular Sciences
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N-(2-methyl-indol-1H-5-yl)-1-naphthalenesulfonamide : a novel reversible antimitotic agent inhibiting cancer cell motility

2016

Este es el post-print que se ha publicado de forma definitiva en: https://www.sciencedirect.com/science/article/abs/pii/S0006295216301423 A series of compounds containing the sulfonamide scaffold were synthesized and screened for their in vitro anticancer activity against a representative panel of human cancer cell lines, leading to the identification of N-(2-methyl-1H-indol-5-yl)-1-naphthalenesulfonamide (8e) as a compound showing a remarkable activity across the panel, with IC50 values in the nanomolar-to-low micromolar range. Cell cycle distribution analysis revealed that 8e promoted a severe G2/M arrest, which was followed by cellular senescence as indicated by the detection of senescen…

0301 basic medicineIndolesSulfonamides - Therapeutic use.MotilityApoptosisAntimitotic AgentsMicrotubulesBiochemistryJurkat Cells03 medical and health sciences0302 clinical medicineCell MovementTubulinMicrotubuleCélulas cancerosas - Motilidad.Apoptosis.HumansSulfamidas - Uso terapéutico.MitosisCell ProliferationPharmacologySulfonamidesMolecular StructurebiologyCancer cells - Motility.Cell cycleCell biologyMitosis.030104 developmental biologyTubulinCell cultureApoptosis030220 oncology & carcinogenesisCancer cellMCF-7 Cellsbiology.proteinDrug Screening Assays AntitumorDNA Damage
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Regulation of kynurenine biosynthesis during influenza virus infection.

2017

Influenza A viruses (IAVs) remain serious threats to public health because of the shortage of effective means of control. Developing more effective virus control modalities requires better understanding of virus–host interactions. It has previously been shown that IAV induces the production of kynurenine, which suppresses T-cell responses, enhances pain hypersensitivity and disturbs behaviour in infected animals. However, the regulation of kynurenine biosynthesis during IAV infection remains elusive. Here we showed that IAV infection induced expression of interferons (IFNs), which upregulated production of indoleamine-2,3-dioxygenase (IDO1), which catalysed the kynurenine biosynthesis. Furt…

0301 basic medicineIndoleshost-pathogen interactionViral Nonstructural Proteinsmedicine.disease_causeVirus ReplicationBiochemistryinfluenza viruschemistry.chemical_compoundMiceInfluenza A Virus H1N1 SubtypeInterferonOximesinnate immunityLungOxazolesKynurenineRegulation of gene expressionMice Inbred BALB CSulfonamidesTryptophaninterferon3. Good healthHost-Pathogen InteractionsFemaleMetabolic Networks and Pathwaysmedicine.drugHost–pathogen interaction030106 microbiologyPrimary Cell CultureBiologyta3111Antiviral AgentsVirus03 medical and health sciences3-dioxygenase (IDO1)Orthomyxoviridae InfectionsmedicineAnimalsHumansImmunologic FactorsIndoleamine-Pyrrole 23-DioxygenasePyrrolesMolecular BiologyInnate immune systemta1184Macrophagesta1183ta1182Cell BiologyVirologyindoleamine-pyrrole 2Thiazoles030104 developmental biologyHerpes simplex virusViral replicationchemistryGene Expression RegulationInterferonsTranscriptomeKynurenineThe FEBS journal
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AMPK phosphorylation modulates pain by activation of NLRP3 inflammasome

2016

et al.

0301 basic medicineMESH : Carrier Proteins/geneticsMaleMESH: Fibromyalgia/geneticsFibromyalgiaIndolesPhysiologyInflammasomesClinical BiochemistryInterleukin-1betaInjuryAMP-Activated Protein KinasesNeuropathic painBiochemistryPyrin domainMice0302 clinical medicineAMP-activated protein kinaseRestrictionSunitinibDiseasePhosphorylationGeneral Environmental Sciencebiologyintegumentary systemChemistryInterleukin-18InflammasomePain Perception[SDV.MHEP.EM]Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism[ SDV.MHEP.EM ] Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolismMiddle AgedMetforminCell biologyOriginal Research CommunicationsMESH : Fibromyalgia/geneticsHyperalgesiaPhosphorylationFemalemedicine.symptommedicine.drugMESH : Inflammasomes/metabolismAdultmedicine.medical_specialtyPain03 medical and health sciencesMESH: Carrier Proteins/geneticsInternal medicineNLR Family Pyrin Domain-Containing 3 ProteinmedicineAnimalsHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyPyrrolesProtein kinase AMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Inflammasomes/metabolismFibromialgia patientsAMPK ; fibromyalgia ; NLRP3 InflammasomeDangerAMPKCell BiologyAdenosineMESH: AMP-Activated Protein Kinases/genetics030104 developmental biologyEndocrinologyMetabolismProtein-Kinase AMPKbiology.proteinGeneral Earth and Planetary SciencesMESH : AMP-Activated Protein Kinases/geneticsAnalgesiaCarrier Proteins030217 neurology & neurosurgery
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Somatic copy number alterations are associated with EGFR amplification and shortened survival in patients with primary glioblastoma.

2019

Glioblastoma (GBM) is the most common malignant primary tumor of the central nervous system. With no effective therapy, the prognosis for patients is terrible poor. It is highly heterogeneous and EGFR amplification is its most frequent molecular alteration. In this light, we aimed to examine the genetic heterogeneity of GBM and to correlate it with the clinical characteristics of the patients. For that purpose, we analyzed the status of EGFR and the somatic copy number alterations (CNAs) of a set of tumor suppressor genes and oncogenes. Thus, we found GBMs with high level of EGFR amplification, low level and with no EGFR amplification. Highly amplified tumors showed histological features of…

0301 basic medicineMaleCancer ResearchBiopsyL-amp GB EGFR-low amplified glioblastomamedicine.disease_causewt wildtypeMYBPC3 myosin-binding protein C0302 clinical medicineHIC1 hypermethylated in cancer 1Gene duplicationIn Situ Hybridization FluorescenceIDH2 isocitrate dehydrogenase 2MutationRB-pat RB signaling pathwayEGFRvIII epidermal growth factor receptor variant number IIIPAH phenylalanine hydroxylaseGBM glioblastoma IDH-wildtype (glioblastoma multiforme primary glioblastoma).ANOVA ANalysis Of VArianceN-amp GB EGFR-no amplified glioblastomaMiddle AgedCDKN2A cyclin-dependent kinase inhibitor 2Alcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensPrognosisPrimary tumorImmunohistochemistryH-amp GB EGFR-high amplified glioblastomaErbB ReceptorsTKR-pat tyrosine-kinase receptors signaling pathway030220 oncology & carcinogenesisDisease ProgressionCDK6 cyclin-dependent kinase 6CDH1 Cadherin 1FemaleCREM cAMP response element modulatorIHC immunohistochemistryAdultOriginal articleDNA Copy Number VariationsCDKN1B cyclin-dependent kinase inhibitor 1BBiologyRARB retinoic acid receptor betaCNS central nervous systemlcsh:RC254-282IDH1 isocitrate dehydrogenase 1BCL2 B-cell cll/ lymphoma 2CNAs copy number algerationsWHO World Health Organization03 medical and health sciencesYoung Adultp53-pat p53 signaling pathwaymedicineBiomarkers TumorTMA tissue microarrayPTENHumansProtein kinase BPI3K/AKT/mTOR pathwaySurvival analysisAgedGenetic heterogeneityGene AmplificationGFAP glial fibrillary acidic proteinMLPA multiplex ligation-dependent probe amplificationmedicine.diseaseFISH fluorescence in situ hibridizationSurvival AnalysisCDKN2B cyclin-dependent kinase inhibitor 2BPTEN phosphatase and tensin homologEGFR epidermal growth factor receptorCNV-load load of copy number variations030104 developmental biologyMutationPARK2 parkinCancer researchbiology.proteinTCGA The Cancer Genome AtlasLARGE1 acetylglucosaminyltransferase-like protein 1GlioblastomaCHD7 Chromodomain Helicase DNA Binding Protein 7DAPI 4′6-diamidino-2-phenylindoleNeoplasia (New York, N.Y.)
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