about
Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysAnalysis of nucleocytoplasmic trafficking of the HuR ligand APRIL and its influence on CD83 expressionThe nucleoporin-like protein NLP1 (hCG1) promotes CRM1-dependent nuclear protein exportPhosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitroTwo overlapping reading frames in a single exon encode interacting proteins--a novel way of gene usageDefective nuclear import of Tpr in Progeria reflects the Ran sensitivity of large cargo transport.Resolution doubling in fluorescence microscopy with confocal spinning-disk image scanning microscopyCombining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1-RanGTP-SPN1-Nup214 quaternary nuclear export complex.Functional characterization of the HuR:CD83 mRNA interaction.Acetylcholinesterase and butyrylcholinesterase genes coamplify in primary ovarian carcinomas.Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1.Importin 7 and Nup358 promote nuclear import of the protein component of human telomerase.MD simulations and FRET reveal an environment-sensitive conformational plasticity of importin-βIdentification of CRM1-dependent Nuclear Export Cargos Using Quantitative Mass SpectrometryHuman PDCD2L Is an Export Substrate of CRM1 That Associates with 40S Ribosomal Subunit Precursors.Nuclear Pore Complexes and Nucleocytoplasmic Transport: From Structure to Function to Disease.Distinct functions of the dual leucine zipper kinase depending on its subcellular localization.Emery-Dreifuss muscular dystrophy mutations impair TRC40-mediated targeting of emerin to the inner nuclear membrane.Novel approaches for the identification of nuclear transport receptor substrates.Analysis of nucleocytoplasmic transport in digitonin-permeabilized cells under different cellular conditions.In vitro analysis of nuclear mRNA export using molecular beacons for target detection.Stimulated expression of mRNAs in activated T cells depends on a functional CRM1 nuclear export pathway.Expression of CD83 is regulated by HuR via a novel cis-active coding region RNA element.Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation.The anti-inflammatory prostaglandin 15-deoxy-delta(12,14)-PGJ2 inhibits CRM1-dependent nuclear protein exportSeveral phenylalanine-glycine motives in the nucleoporin Nup214 are essential for binding of the nuclear export receptor CRM1.The Oncogenic Fusion Proteins SET-Nup214 and Sequestosome-1 (SQSTM1)-Nup214 Form Dynamic Nuclear Bodies and Differentially Affect Nuclear Protein and Poly(A)+ RNA Export.Characterization of the extra-large G protein alpha-subunit XLalphas. II. Signal transduction properties.CRM1-mediated nuclear export: to the pore and beyond.The nuclear pore component Nup358 promotes transportin-dependent nuclear import.Extensive identification and in-depth validation of importin 13 cargoes.The Nucleoporin Nup358/RanBP2 Promotes Nuclear Import in a Cargo- and Transport Receptor-Specific MannerTargeting of LRRC59 to the Endoplasmic Reticulum and the Inner Nuclear MembraneCharacterization of the extra-large G protein alpha-subunit XLalphas. I. Tissue distribution and subcellular localizationAnalysis of nuclear protein import and export in vitro using fluorescent cargoesNuclear import of c-Jun is mediated by multiple transport receptorsTransportin is a major nuclear import receptor for c-Fos: a novel mode of cargo interactionAnalysis of CRM1-Dependent Nuclear Export in Permeabilized CellsProbing the Environment of Emerin by Enhanced Ascorbate Peroxidase 2 (APEX2)-Mediated Proximity LabelingProteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Ralph H Kehlenbach
@ast
Ralph H Kehlenbach
@en
Ralph H Kehlenbach
@es
Ralph H Kehlenbach
@nl
Ralph H Kehlenbach
@sl
type
label
Ralph H Kehlenbach
@ast
Ralph H Kehlenbach
@en
Ralph H Kehlenbach
@es
Ralph H Kehlenbach
@nl
Ralph H Kehlenbach
@sl
prefLabel
Ralph H Kehlenbach
@ast
Ralph H Kehlenbach
@en
Ralph H Kehlenbach
@es
Ralph H Kehlenbach
@nl
Ralph H Kehlenbach
@sl
P106
P31
P496
0000-0003-4920-9916