Search results for "nuclear import"

showing 5 items of 5 documents

The severe phenotype of Diamond-Blackfan anemia is modulated by heat shock protein 70.

2017

International audience; Diamond-Blackfan anemia (DBA) is a rare congenital bone marrow failure syndrome that exhibits an erythroid-specific phenotype. In at least 70% of cases, DBA is related to a haploinsufficient germ line mutation in a ribosomal protein (RP) gene. Additional cases have been associated with mutations in GATA1. We have previously established that the RPL11+/Mut phenotype is more severe than RPS19+/Mut phenotype because of delayed erythroid differentiation and increased apoptosis of RPL11+/Mut erythroid progenitors. The HSP70 protein is known to protect GATA1, the major erythroid transcription factor, from caspase-3 mediated cleavage during normal erythroid differentiation.…

0301 basic medicinecongenital hereditary and neonatal diseases and abnormalitiesIdentificationApoptosis-Inducing FactorGata1 MutationsInhibits ApoptosisBiologyHsp7003 medical and health sciencesGermline mutationRed Cells Iron and Erythropoiesishemic and lymphatic diseasesmedicine[ SDV.MHEP.HEM ] Life Sciences [q-bio]/Human health and pathology/HematologyNuclear ImportErythropoiesisDiamond–Blackfan anemiaHuman ErythroblastsBone marrow failure[SDV.MHEP.HEM]Life Sciences [q-bio]/Human health and pathology/HematologyGATA1Hematologymedicine.diseasePhenotypeMolecular biology3. Good healthHsp70030104 developmental biologyRibosomal-ProteinsProtein Gene DeletionsErythropoiesisHaploinsufficiencyBlood advances
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Protoparvovirus Knocking at the Nuclear Door

2017

Protoparvoviruses target the nucleus due to their dependence on the cellular reproduction machinery during the replication and expression of their single-stranded DNA genome. In recent years, our understanding of the multistep process of the capsid nuclear import has improved, and led to the discovery of unique viral nuclear entry strategies. Preceded by endosomal transport, endosomal escape and microtubule-mediated movement to the vicinity of the nuclear envelope, the protoparvoviruses interact with the nuclear pore complexes. The capsids are transported actively across the nuclear pore complexes using nuclear import receptors. The nuclear import is sometimes accompanied by structural chan…

0301 basic medicinevirusesimportinsActive Transport Cell Nucleuslcsh:QR1-502Genome ViralReviewImportinKaryopherinsBiologyVirus Replicationlcsh:MicrobiologyParvovirusMice03 medical and health sciencesCapsidVirologynuclear pore complexmedicineAnimalsHumansInner membraneNuclear poreprotoparvovirusCell Nucleusnuclear localization sequence030102 biochemistry & molecular biologyta1182nuclear envelopeVirus InternalizationVirologynuclear importCell biologyCell nucleusnuclear envelope break down030104 developmental biologyInfectious Diseasesmedicine.anatomical_structureintracellular dynamicsEndosomal transportNuclear PoreentryCapsid ProteinsNucleoporinNuclear transportNuclear localization sequenceViruses
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XPO1E571K Mutation Modifies Exportin 1 Localisation and Interactome in B-cell Lymphoma

2020

The XPO1 gene encodes exportin 1 (XPO1) that controls the nuclear export of cargo proteins and RNAs. Almost 25% of primary mediastinal B-cell lymphoma (PMBL) and classical Hodgkin lymphoma (cHL) cases harboured a recurrent XPO1 point mutation (NM_003400, chr2:g61718472C&gt

Cancer ResearchMutantXPO1/CRM1[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]CRISPR–Cas9[SDV.BC.IC] Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]lcsh:RC254-282Article03 medical and health sciencesXPO10302 clinical medicineproteomics[SDV.CAN] Life Sciences [q-bio]/Cancerimmune system diseasesExportin-1hemic and lymphatic diseases[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]medicine[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]B-cell lymphomaNuclear export signalproximity ligation assay030304 developmental biology0303 health sciencesimportin β1ChemistryB-cell lymphomaPoint mutationlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensmedicine.diseaseMolecular biologynuclear importindirect immunofluorescenceOncology030220 oncology & carcinogenesisMutation (genetic algorithm)nuclear exportNuclear transportCRISPR-Cas9
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Midregion PTHrP and Human Breast Cancer Cells

2010

PTHrP is a polyhormone undergoing proteolytic processing into smaller bioactive forms, comprising an N-terminal peptide, which is the mediator of the “classical” PTH-like effect, as well as midregion and C-terminal peptides. The midregion PTHrP domain (38-94)-amide was found to restrain growth and invasionin vitroof some breast cancer cell lines, causing striking toxicity and accelerating death; the most responsive being MDA-MB231, whose tumorigenesis was also attenuatedin vivo. In addition, midregion PTHrP appears to be imported in the nucleoplasm of cultured MDA-MB231 cells andin vitro, it can bind chromatin of metaphase spread preparations and also an isolated 20-mer oligonucleotide, the…

Gene Expressionlcsh:MedicineBreast NeoplasmsDNA FragmentationBiologymedicine.disease_causelcsh:TechnologyGeneral Biochemistry Genetics and Molecular BiologyTranscription (biology)Cell Line TumorPTHrP breast cancer cancer cell gene expression cytotoxicityGene expressionmedicineHumansSettore BIO/06 - Anatomia Comparata E CitologiaMDA-MB231lcsh:ScienceDNA statusGeneral Environmental ScienceMini-Review ArticleNucleoplasmlcsh:Tmidregion PTHrPlcsh:RParathyroid Hormone-Related ProteinapoptosisGeneral MedicineMolecular biologynuclear importIn vitroCell biologyChromatinPTHrP (38-94)Cancer cellprotein degradationFemalelcsh:QCarcinogenesisReprogrammingbreast cancer cellsThe Scientific World Journal
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Chemical Proteomics-Guided Identification of a Novel Biological Target of the Bioactive Neolignan Magnolol

2019

Understanding the recognition process between bioactive natural products and their specific cellular receptors is of key importance in the drug discovery process. In this outline, some potential targets of Magnolol, a natural bioactive compound, have been identified by proteomic approaches. Among them, Importin-β1 has been considered as the most relevant one. A direct binding between Magnolol and this nuclear chaperone has been confirmed by DARTS and molecular docking, while its influence on Importin-β1 translocation has been evaluated by in vitro assays.

bioactive neolignans02 engineering and technologyComputational biology010402 general chemistryProteomics01 natural scienceslcsh:Chemistrychemistry.chemical_compoundchemical proteomicsdrug affinity responsive target stabilityOriginal Researchbioactive neolignans; chemical proteomics; drug affinity responsive target stability; molecular docking; nuclear importbiologyChemistryDrug discoveryIn vitro toxicologyGeneral Chemistrymolecular docking021001 nanoscience & nanotechnologynuclear importMagnololBioactive compound0104 chemical sciencesChemistrylcsh:QD1-999Biological targetChaperone (protein)Direct bindingbiology.protein0210 nano-technologyFrontiers in Chemistry
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