PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
about
Calreticulin Is a receptor for nuclear export.40LoVe interacts with Vg1RBP/Vera and hnRNP I in binding the Vg1-localization element.Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesisCRM1 controls the composition of nucleoplasmic pre-snoRNA complexes to licence them for nucleolar transportGemin8 is required for the architecture and function of the survival motor neuron complexLarge-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complexExp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasmMolecular dissection of the eukaryotic initiation factor 4E (eIF4E) export-competent RNPOngoing U snRNP biogenesis is required for the integrity of Cajal bodiesmRNA export through an additional cap-binding complex consisting of NCBP1 and NCBP3RanBP3 influences interactions between CRM1 and its nuclear protein export substrates.Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation.Structural basis for m3G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1Interaction between the small-nuclear-RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuronCross-talk between snurportin1 subdomains.Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domainsExportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNAThe evolutionarily conserved region of the U snRNA export mediator PHAX is a novel RNA-binding domain that is essential for U snRNA exportProtein ligands mediate the CRM1-dependent export of HuR in response to heat shock.Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAsA molecular link between SR protein dephosphorylation and mRNA exportA multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex proteinSMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin betaProtein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding proteinImportin-beta-like nuclear transport receptorsStructural Basis of Targeting the Exportin CRM1 in CancerRan-dependent nuclear export mediators: a structural perspectiveRNA Export through the NPC in EukaryotesVersatile microRNA biogenesis in animals and their virusesPostage for the messenger: designating routes for nuclear mRNA exportCrystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTPThe molecular basis for the regulation of the cap-binding complex by the importinsStructure and RNA recognition by the snRNA and snoRNA transport factor PHAXIntracellular trafficking of yeast telomerase components.Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export.The tRNA aminoacylation co-factor Arc1p is excluded from the nucleus by an Xpo1p-dependent mechanism.Biogenesis of yeast telomerase depends on the importin mtr10A targeted bypass screen identifies Ynl187p, Prp42p, Snu71p, and Cbp80p for stable U1 snRNP/Pre-mRNA interaction.prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP maturation defect in yeast
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P2860
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
description
2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im April 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/04/14)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/04/14)
@nl
наукова стаття, опублікована у квітні 2000
@uk
مقالة علمية (نشرت في 14-4-2000)
@ar
name
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@ast
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@en
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@nl
type
label
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@ast
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@en
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@nl
prefLabel
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@ast
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@en
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@nl
P2093
P3181
P1433
P1476
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
@en
P2093
P304
P3181
P356
10.1016/S0092-8674(00)80829-6
P407
P577
2000-04-14T00:00:00Z