grant
Structure and Function of the Nuclear Pore Complex by Cryogenic-EM
Organization BOSTON UNIVERSITY MEDICAL CAMPUSLocation BOSTON, UNITED STATESPosted 1 May 2025Deadline 31 Mar 2030
NIHUS FederalResearch GrantFY2025BenchmarkingBest Practice AnalysisBinding SitesBiochemicalCarrier ProteinsCausalityCell BodyCell DifferentiationCell Differentiation processCell NucleusCell Nucleus Active TransportCellsCellular ExpansionCellular GrowthCombining SiteComplexContracting OpportunitiesContractsCytoplasmDataEtiologyEvolutionFrogGene ExpressionHumanImportinsIn SituKaryopherinsKnowledgeLateralMediatingMembraneMembrane Protein GeneMembrane ProteinsMembrane-Associated ProteinsMethodsModelingModern ManMolecular ConfigurationMolecular ConformationMolecular EvolutionMolecular StereochemistryNPCNon-Polyadenylated RNANuclearNuclear EnvelopeNuclear MembraneNuclear Pore ComplexNuclear Pore Complex ProteinsNuclear TransportNucleocytoplasmic ShuttlingNucleoporin GeneNucleoporinsNucleusNup ProteinPaperPermeabilityPopulationRNARNA Gene ProductsRanaReactive SiteResolutionRibonucleic AcidRoleSeriesStructureSurface ProteinsTransport Protein GeneTransport ProteinsTransporter ProteinTransportinsViral CancerViral DiseasesVirus DiseasesVisualizationWorkYeastsbenchmarkcausationcell growthcellular differentiationconformationconformationalconformational stateconformationallyconformationsconstrictioncryogenicsdisease causationelectron tomographyexperienceflexibilityflexiblehuman diseaseimprovedinsightmacromoleculemembrane structurenucleocytoplasmic transportparticleprotein complexresolutionsscaffoldscaffoldingsocial roleviral infectionvirus infectionvirus-induced disease
Description preview
Structure and Function of the Nuclear Pore Complex by Cryogenic-EM
Abstract
The nucleus is compartmentalized by double membranes of the Nuclear Envelope (NE) and
macromolecules must cross this barrier during cell growth and differentiation. The Nuclear Pore Complex
(NPC) forms a conduit for the bidirectional transport of proteins and RNA-protein…
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