Search results for "BINDING PROTEIN"

showing 10 items of 1292 documents

Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator

2017

17 páginas, 7 figuras, 1 tabla

0301 basic medicineModels MolecularSalmonella typhimuriumProtein Data Bank (RCSB PDB)Plasma protein bindingBiologyCrystallography X-RayDNA-binding protein03 medical and health sciencesBacterial ProteinsProtein DomainsStructural BiologyGeneticsAmino Acid SequencePhosphorylationTranscription factorSequence Homology Amino AcidEffectorPromoterDNACell biologyResponse regulator030104 developmental biologyRegulonBiochemistryNucleic Acid ConformationProtein BindingNucleic Acids Research
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In silico discovery of substituted pyrido[2,3-d]pyrimidines and pentamidine-like compounds with biological activity in myotonic dystrophy models

2016

Myotonic dystrophy type 1 (DM1) is a rare multisystemic disorder associated with an expansion of CUG repeats in mutant DMPK (dystrophia myotonica protein kinase) transcripts; the main effect of these expansions is the induction of pre-mRNA splicing defects by sequestering muscleblind-like family proteins (e.g. MBNL1). Disruption of the CUG repeats and the MBNL1 protein complex has been established as the best therapeutic approach for DM1, hence two main strategies have been proposed: targeted degradation of mutant DMPK transcripts and the development of CUG-binding molecules that prevent MBNL1 sequestration. Herein, suitable CUG-binding small molecules were selected using in silico approach…

0301 basic medicineMolecular biologyPhysiologyMutantMyotonic dystrophyDruggabilitylcsh:Medicine01 natural sciencesBiochemistryPhysical ChemistryMyoblastschemistry.chemical_compoundAnabolic AgentsMedicaments--InteraccióAnimal CellsDrug DiscoveryMedicine and Health SciencesMBNL1Drosophila ProteinsMyotonic Dystrophylcsh:ScienceRNA structureConnective Tissue CellsMultidisciplinaryMolecular StructureOrganic CompoundsStem CellsPhysicsRNA-Binding ProteinsBiological activityPhenotypeClimbingMolecular Docking SimulationNucleic acidsChemistryDrosophila melanogasterBiochemistryGenetic DiseasesConnective TissueRNA splicingPhysical SciencesCellular TypesAnatomyLocomotion57 - BiologiaSignal TransductionResearch ArticleBiotechnologyHydrogen bondingcongenital hereditary and neonatal diseases and abnormalitiesIn silicoPrimary Cell CultureComputational biologyBiology010402 general chemistryMyotonic dystrophyMyotonin-Protein KinaseDrug interactionsSmall Molecule Libraries03 medical and health sciencesStructure-Activity RelationshipmedicineAnimalsHumansRNA MessengerEnllaços d'hidrogenClinical GeneticsChemical PhysicsBiology and life sciencesChemical BondingBiological Locomotionlcsh:ROrganic ChemistryEstructura molecularChemical CompoundsHydrogen BondingCell BiologyFibroblastsmedicine.disease0104 chemical sciencesBenzamidinesAlternative SplicingDisease Models AnimalMacromolecular structure analysis030104 developmental biologyPyrimidinesBiological TissuechemistrySmall MoleculesRNAlcsh:QTrinucleotide Repeat ExpansionMolecular structure
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Identification of the Privileged Position in the Imidazo[1,2-a]pyridine Ring of Phosphonocarboxylates for Development of Rab Geranylgeranyl Transfera…

2017

Members of the Rab GTPase family are master regulators of vesicle trafficking. When disregulated, they are associated with a number of pathological states. The inhibition of RGGT, an enzyme responsible for post-translational geranylgeranylation of Rab GTPases represents one way to control the activity of these proteins. Because the number of molecules modulating RGGT is limited, we combined molecular modeling with biological assays to ascertain how modifications of phosphonocarboxylates, the first reported RGGT inhibitors, rationally improve understanding of their structure-activity relationship. We have identified the privileged position in the core scaffold of the imidazo[1,2-a]pyridine r…

0301 basic medicineMolecular modelPyridinesOrganophosphonatesProtein PrenylationAntineoplastic AgentsGTPase01 natural sciencesHeLa03 medical and health sciencesStructure-Activity RelationshipGeranylgeranylationPrenylationDrug DiscoveryStructure–activity relationshipHumansEnzyme Inhibitorsta116Cell Proliferationchemistry.chemical_classificationAlkyl and Aryl Transferasesbiology010405 organic chemistryrab geranylgeranyl transferaseta1182biology.organism_classification0104 chemical sciencesCell biologyMolecular Docking Simulation030104 developmental biologyEnzymechemistryBiochemistryrab GTP-Binding ProteinsMolecular MedicineRabHeLa CellsJournal of Medicinal Chemistry
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Transcriptomic data from panarthropods shed new light on the evolution of insulator binding proteins in insects : Insect insulator proteins.

2016

Background Body plan development in multi-cellular organisms is largely determined by homeotic genes. Expression of homeotic genes, in turn, is partially regulated by insulator binding proteins (IBPs). While only a few enhancer blocking IBPs have been identified in vertebrates, the common fruit fly Drosophila melanogaster harbors at least twelve different enhancer blocking IBPs. We screened recently compiled insect transcriptomes from the 1KITE project and genomic and transcriptomic data from public databases, aiming to trace the origin of IBPs in insects and other arthropods. Results Our study shows that the last common ancestor of insects (Hexapoda) already possessed a substantial number …

0301 basic medicineMost recent common ancestormedia_common.quotation_subjectInsectDipluraGene evolutionEvolution Molecular03 medical and health sciencesArthropod evolutionGeneticsAnimalsEnhancerArthropodsPhylogenymedia_commonGeneticsbiologyGene Expression ProfilingfungiComparative transcriptomic analysesbiology.organism_classificationInsulator binding proteinsNeopteraDNA-Binding Proteins030104 developmental biologyBody planDrosophila melanogasterEnhancer Elements GeneticInsulator ElementsDrosophila melanogasterHomeotic geneTranscriptomeBiotechnologyResearch ArticleBMC genomics
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Inherited variants in XRCC2 and the risk of breast cancer

2019

Background XRCC2 participates in homologous recombination and in DNA repair. XRCC2 has been reported to be a breast cancer susceptibility gene and is now included in several breast cancer susceptibility gene panels. Methods We sequenced XRCC2 in 617 Polish women with familial breast cancer and found a founder mutation. We then genotyped 12,617 women with breast cancer and 4599 controls for the XRCC2 founder mutation. Results We identified a recurrent truncating mutation of XRCC2 (c.96delT, p.Phe32fs) in 3 of 617 patients with familial breast cancer who were sequenced. The c.96delT mutation was then detected in 29 of 12,617 unselected breast cancer cases (0.23%) compared to 11 of 4599 cancer…

0301 basic medicineOncologyAdultCancer Researchmedicine.medical_specialtyGenotypeXRCC2DNA repairEpidemiologyBreast NeoplasmsXRCC203 medical and health sciences0302 clinical medicineBreast cancerBreast cancerMutation RateInternal medicinemedicineHumansGenetic TestingAlleleMutation frequencyskin and connective tissue diseasesGeneAllelesGenetic Association StudiesAgedbusiness.industryMiddle Agedmedicine.diseaseDNA-Binding Proteins030104 developmental biologyHereditaryOncology030220 oncology & carcinogenesisMutation (genetic algorithm)MutationFemalePolandbusinessHomologous recombinationBreast Cancer Research and Treatment
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Associations of Pathogenic Variants in MLH1, MSH2, and MSH6 With Risk of Colorectal Adenomas and Tumors and With Somatic Mutations in Patients With L…

2020

Contains fulltext : 220040.pdf (Publisher’s version ) (Closed access) BACKGROUND & AIMS: Lynch syndrome is caused by variants in DNA mismatch repair (MMR) genes and associated with an increased risk of colorectal cancer (CRC). In patients with Lynch syndrome, CRCs can develop via different pathways. We studied associations between Lynch syndrome-associated variants in MMR genes and risks of adenoma and CRC and somatic mutations in APC and CTNNB1 in tumors in an international cohort of patients. METHODS: We combined clinical and molecular data from 3 studies. We obtained clinical data from 2747 patients with Lynch syndrome associated with variants in MLH1, MSH2, or MSH6 from Germany, the Net…

0301 basic medicineOncologyMaleColorectal cancerDNA Mutational Analysisgenetic analysisHEREDITARYcancer riskGUIDELINESDNA Mismatch Repair0302 clinical medicineGermanyTumours of the digestive tract Radboud Institute for Molecular Life Sciences [Radboudumc 14]Prospective Studiesprognostic factorFinlandbeta CateninNetherlandsOutcomePrognostic FactorGastroenterologyGenetic AnalysisColonoscopyMiddle AgedCANCERLynch syndromeCancer Risk3. Good healthDNA-Binding ProteinsDEFICIENCYMutS Homolog 2 Proteinsyöpägeenitoutcome030211 gastroenterology & hepatologyDNA mismatch repairFemaleMutL Protein Homolog 1geenitutkimusAdenomaAdultmedicine.medical_specialtycongenital hereditary and neonatal diseases and abnormalitiesAdenoma3122 CancersAdenomatous Polyposis Coli ProteinINSTABILITYSOCIETYMLH103 medical and health sciencesInternal medicinemedicineMANAGEMENTHumansLynchin oireyhtymäneoplasmspaksusuolisyöpäHepatologybusiness.industryCancernutritional and metabolic diseasesennusteetmedicine.diseaseColorectal Neoplasms Hereditary Nonpolyposisdigestive system diseasesMSH6030104 developmental biologyMSH2Mutationbusiness
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Tetraspanin CD63 controls basolateral sorting of organic cation transporter 2 in renal proximal tubules.

2016

CD63 is a ubiquitously expressed member of the tetraspanin superfamily. Using a mating-based split-ubiquitin-yeast 2-hybrid system, pull-down experiments, total internal reflection fluorescence microscopy, Forster resonance energy transfer, and biotinylation assays, we found that CD63 interacts with human organic cation transporter 2 (hOCT2), which transports endogenous and exogenous substrates, such as neurotransmitters and drugs in several epithelial cells. CD63 overexpression affects cellular localization of hOCT2 expressed in human embryonic kidney (HEK)293 cells. Studies with CD63-knockout mice indicate that in renal proximal tubules, CD63 determines the insertion of the mouse ortholog…

0301 basic medicineOrganic Cation Transport ProteinsEndosomeEndosomesBiochemistryMadin Darby Canine Kidney CellsKidney Tubules Proximal03 medical and health sciencesMiceDogsTetraspaninGeneticsAnimalsHumansMolecular BiologyCellular localizationEpithelial polarityChemistryTetraspanin 30rab4 GTP-Binding ProteinsHEK 293 cellsCell MembraneOrganic Cation Transporter 2TransporterEpithelial CellsTransfectionCell biologyMice Inbred C57BLProtein Transport030104 developmental biologyHEK293 CellsMembrane proteinBiotechnologyProtein BindingFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Fasciola spp: Mapping of the MF6 epitope and antigenic analysis of the MF6p/HDM family of heme-binding proteins

2017

MF6p/FhHDM-1 is a small cationic heme-binding protein which is recognized by the monoclonal antibody (mAb) MF6, and abundantly present in parenchymal cells and secreted antigens of Fasciola hepatica. Orthologs of this protein (MF6p/HDMs) also exist in other causal agents of important foodborne trematodiasis, such as Clonorchis sinensis, Opisthorchis viverrini and Paragonimus westermani. Considering that MF6p/FhHDM-1 is relevant for heme homeostasis in Fasciola and was reported to have immunomodulatory properties, this protein is expected to be a useful target for vaccination. Thus, in this study we mapped the epitope recognized by mAb MF6 and evaluated its antigenicity in sheep. The sequenc…

0301 basic medicineParagonimus westermaniFasciola sppPhysiologyProtein ConformationFlatwormslcsh:MedicineProtein Structure PredictionBiochemistryEpitopeAntigenicEpitopes0302 clinical medicineAnimal CellsImmune PhysiologyMedicine and Health SciencesMacromolecular Structure AnalysisMF6p/HDMEnzyme-Linked Immunoassayslcsh:ScienceMammalsNeuronsImmune System ProteinsMultidisciplinaryFasciolabiologyVaccinationEukaryotaAntibodies MonoclonalRuminantsDendritic StructureVertebratesCellular TypesAntibodyResearch ArticleHemeproteinsProtein StructureAntigenicityFascioliasisHeme bindingImmunology030231 tropical medicineAntibodies HelminthEnzyme-Linked Immunosorbent AssayHemeResearch and Analysis MethodsTrematodesAntibodiesHeme-Binding Proteins03 medical and health sciencesHelminthsparasitic diseasesParasitic DiseasesFasciola hepaticaAnimalsImmunoassaysMolecular BiologySheeplcsh:ROrganismsBiology and Life SciencesProteinsCell BiologyDendritesNeuronal DendritesFasciola hepaticabiology.organism_classificationInvertebratesMolecular biologyFasciola030104 developmental biologyEpitope mappingCellular NeuroscienceAntigens HelminthAmniotesImmunologic Techniquesbiology.proteinlcsh:QCarrier ProteinsEpitope MappingNeuroscience
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Increased basal antioxidant levels in RCAN1 - deficient mice lowers oxidative injury after acute paraquat insult.

2020

RCAN1 is an inhibitor of the phosphatase calcineurin, which is involved in the regulation of oxidative stress and apoptosis, among other important cell processes. Here we have used RCAN1 deficient mice (RCAN1-/-) to elucidate its role after an acute oxidative insult such as paraquat injection. We have observed that RCAN1-/- mice show less oxidative damage than wildtype (WT) mice after treatment. Under basal conditions, RCAN1-/- animals express more calcineurin, heme oxygenase-1, Nrf2, and catalase compared to WT mice (controls). This may explain the less severe effect of paraquat treatment on RCAN1-/- mice compared to WT. We showed that oxidative stress is involved in the early stages of ap…

0301 basic medicineParaquatmedicine.medical_specialtyAntioxidantmedicine.medical_treatmentMuscle ProteinsOxidative phosphorylationmedicine.disease_causeBiochemistryAntioxidants03 medical and health scienceschemistry.chemical_compoundMiceParaquatInternal medicinemedicineAnimals030102 biochemistry & molecular biologybiologyCalcineurinGeneral MedicineGlutathioneCalcineurinDNA-Binding ProteinsOxidative Stress030104 developmental biologyEndocrinologychemistryCatalaseApoptosisbiology.proteinOxidative stressFree radical research
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PBRM1 loss is a late event during the development of cholangiocarcinoma

2017

Aims: Somatic mutations in genes encoding chromatin remodellers have been reported recently in several cancer types, including approximately half of cholangiocarcinomas. One of the most commonly mutated chromatin remodellers in cholangiocarcinoma is the Polybromo-1 (PBRM1) gene located on chromosome 3p21, which encodes a subunit of the SWI/SNF complex. The aim of this study was to determine the timing of PBRM1 mutations in biliary carcinogenesis. Methods and results: In order to accomplish this goal, we used immunohistochemistry to assess PBRM1 protein expression in a series of precursor lesions and invasive biliary carcinomas. Previous studies have correlated loss of protein expression on …

0301 basic medicinePathologymedicine.medical_specialtyHistologyBilIN; PBRM1; biliary dysplasia; cholangiocarcinoma; chromatin remodellingchromatin remodellingKaplan-Meier EstimateBiologymedicine.disease_causeArticleBilIN; PBRM1; biliary dysplasia; cholangiocarcinoma; chromatin remodelingChromatin remodelingchromatin remodelingPathology and Forensic MedicinePBRM1PBRM103 medical and health scienceschemistry.chemical_compound0302 clinical medicinemedicineHumansBilinIntrahepatic CholangiocarcinomaProportional Hazards ModelsBilINMutationNuclear ProteinsCancerGeneral MedicinePrognosismedicine.diseaseChromatinDNA-Binding Proteinsbiliary dysplasiaCell Transformation Neoplastic030104 developmental biologyBile Duct Neoplasmschemistry030220 oncology & carcinogenesisMutationCarcinogenesischolangiocarcinomaTranscription Factors
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