2023
Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Shen Q, Feng Q, Wu C, Xiong Q, Tian T, Yuan S, Shi J, Bedwell G, Yang R, Aiken C, Engelman A, Lusk C, Lin C, Xiong Y. Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels. Nature Structural & Molecular Biology 2023, 30: 425-435. PMID: 36807645, PMCID: PMC10121901, DOI: 10.1038/s41594-023-00925-9.Peer-Reviewed Original ResearchConceptsNuclear pore complexHIV-1 nuclear entryNuclear entryNuclear importNPC central channelPore complexHost nucleusCapsid dockingVirus genomeAffinity gradientNup153Central channelMechanistic insightsMolecular interactionsCapsidNucleoporinsNup358Nup62GenomeNucleusVirusDockingVirus-1 infectionImportComplexes
2011
tRNA import into mitochondria: many organisms but not so many mechanisms
Alfonzo J, Randau L, Söll D. tRNA import into mitochondria: many organisms but not so many mechanisms. The FASEB Journal 2011, 25: 311.3-311.3. DOI: 10.1096/fasebj.25.1_supplement.311.3.Peer-Reviewed Original ResearchTRNA importMitochondrial genomeMammalian mitochondriaImport of tRNAsMajority of eukaryotesMitochondrial tRNA mutationsProtein importImport pathwayTRNA genesImport systemAdditional tRNAsTRNA mutationsTRNACellular ATPMitochondriaEukaryotesOrganismsGenomeRat liver mitochondriaLiver mitochondriaImportInnate abilityGenesTrypanosomesCytoplasm
2006
Ensembl 2006
Birney E, Andrews D, Caccamo M, Chen Y, Clarke L, Coates G, Cox T, Cunningham F, Curwen V, Cutts T, Down T, Durbin R, Fernandez-Suarez X, Flicek P, Gräf S, Hammond M, Herrero J, Howe K, Iyer V, Jekosch K, Kähäri A, Kasprzyk A, Keefe D, Kokocinski F, Kulesha E, London D, Longden I, Melsopp C, Meidl P, Overduin B, Parker A, Proctor G, Prlic A, Rae M, Rios D, Redmond S, Schuster M, Sealy I, Searle S, Severin J, Slater G, Smedley D, Smith J, Stabenau A, Stalker J, Trevanion S, Ureta-Vidal A, Vogel J, White S, Woodwark C, Hubbard T. Ensembl 2006. Nucleic Acids Research 2006, 34: d556-d561. PMID: 16381931, PMCID: PMC1347495, DOI: 10.1093/nar/gkj133.Peer-Reviewed Original ResearchConceptsGenome variation dataHuman genome variation dataNumber of genomesChordate genomesLarge genome sequencesMammalian genomesRegulatory annotationsYeast genomeRNA genesGenome sequenceCiona intestinalisGenomeVariation dataAnnotationGenesOpossumIntestinalisIntegrated sourceSequenceRhesus macaquesImport
2004
Inhibition of nuclear import and cell-cycle progression by mutated forms of the dynamin-like GTPase MxB
King MC, Raposo G, Lemmon MA. Inhibition of nuclear import and cell-cycle progression by mutated forms of the dynamin-like GTPase MxB. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 8957-8962. PMID: 15184662, PMCID: PMC428454, DOI: 10.1073/pnas.0403167101.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SubstitutionCell CycleCell NucleusCytoplasmGene ExpressionGTP-Binding ProteinsGuanosine TriphosphateHeLa CellsHumansInterferon-alphaMicroscopy, FluorescenceMicroscopy, ImmunoelectronMyxovirus Resistance ProteinsNuclear PoreNuclear Pore Complex ProteinsRecombinant Fusion ProteinsRNA InterferenceTransfectionConceptsNuclear importCell cycle progressionRNA interferenceDynamin-like proteinCell cycle defectsDynamin-like GTPasesNormal cellular functionNucleocytoplasmic traffickingCellular functionsNuclear poresCytoplasmic faceMx proteinCellular traffickingUnexpected roleMxBType I IFNTraffickingProteinI IFNImportAntiviral activityGTPasesMutantsSubfamiliesRoleTransportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR
Rebane A, Aab A, Steitz JA. Transportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR. RNA 2004, 10: 590-599. PMID: 15037768, PMCID: PMC1370549, DOI: 10.1261/rna.5224304.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SequenceAntigens, Surfacebeta KaryopherinsCell NucleusELAV ProteinsELAV-Like Protein 1HeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHumansMolecular Sequence DataMutationProtein Structure, Tertiaryran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsSequence Analysis, ProteinConceptsHnRNP A1Transportin-1Import factorsDigitonin-permeabilized HeLa cellsNuclear import factorsMRNA-binding proteinRecombinant hnRNP A1Binding of HuRImp betaImport pathwayCargo specificityNuclear importExport receptorTransportin-2TransportinTransport signalHeLa cellsLikely actsHuRTrn1ProteinInteraction studiesImportTRN2RanGTP
1998
Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121
Kaffman A, Rank N, O’Shea E. Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Genes & Development 1998, 12: 2673-2683. PMID: 9732266, PMCID: PMC317126, DOI: 10.1101/gad.12.17.2673.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCell NucleusCloning, MolecularCytoplasmDNA-Binding ProteinsEscherichia coliFungal ProteinsKineticsMembrane Transport ProteinsPhosphatesPhosphorylationReceptors, Cytoplasmic and NuclearRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors
1992
Distinct molecular signals for nuclear import of the nucleolar snRNA, U3.
Baserga S, Gilmore-Hebert M, Yang X. Distinct molecular signals for nuclear import of the nucleolar snRNA, U3. Genes & Development 1992, 6: 1120-1130. PMID: 1592260, DOI: 10.1101/gad.6.6.1120.Peer-Reviewed Original ResearchConceptsCap trimethylationNuclear importU3 RNADistinct molecular signalsXenopus oocytesRegulation of importU3 geneCytoplasmic phaseNucleolar snRNAOptimal importU3 snRNAMolecular signalsSnRNAU3 snRNPNucleotidesTrimethylationCytoplasmAutoantigenic proteinsRNAArtificial constructsStemImportOocytesBiogenesisSnRNPAntifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space
Koll H, Guiard B, Rassow J, Ostermann J, Horwich A, Neupert W, Hartl F. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 1992, 68: 1163-1175. PMID: 1347713, DOI: 10.1016/0092-8674(92)90086-r.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBiological TransportChaperonin 60ChaperoninsFungal ProteinsHeat-Shock ProteinsL-Lactate DehydrogenaseL-Lactate Dehydrogenase (Cytochrome)MitochondriaMolecular Sequence DataProtein ConformationProtein Sorting SignalsProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae
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