The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo.
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Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architectureNup214-Nup88 nucleoporin subcomplex is required for CRM1-mediated 60 S preribosomal nuclear exportThe nuclear pore complex and nuclear transportNup50/Npap60 function in nuclear protein import complex disassembly and importin recyclingFlexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport.Mechanisms and signals for the nuclear import of proteinsThe importin beta binding domain modulates the avidity of importin beta for the nuclear pore complexNucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complexSpecific cleavage of the nuclear pore complex protein Nup62 by a viral proteaseCaspases target only two architectural components within the core structure of the nuclear pore complex.Biology and biophysics of the nuclear pore complex and its componentsInteractome Mapping Reveals the Evolutionary History of the Nuclear Pore Complex.Translocation through the nuclear pore complex: selectivity and speed by reduction-of-dimensionality.The molecular mechanism of nuclear transport revealed by atomic-scale measurements.Conserved spatial organization of FG domains in the nuclear pore complex.Towards reconciling structure and function in the nuclear pore complex.Calmodulin-driven nuclear entry: trigger for sex determination and terminal differentiation.Functionalization of a nanopore: the nuclear pore complex paradigm.Ty3 nuclear entry is initiated by viruslike particle docking on GLFG nucleoporins.Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport.Nup153 affects entry of messenger and ribosomal ribonucleoproteins into the nuclear basket during export.Holes in the Nuclear Membrane as an Illustration of Gaps in the Understanding of the Biology by Biologists.Nup214 is required for CRM1-dependent nuclear protein export in vivo.Crystal structure of the Xpo1p nuclear export complex bound to the SxFG/PxFG repeats of the nucleoporin Nup42p.Comparative interactomics provides evidence for functional specialization of the nuclear pore complex.The selective permeability barrier in the nuclear pore complexSpecific nucleoporin requirement for Smad nuclear translocation.Two isoforms of Npap60 (Nup50) differentially regulate nuclear protein import.Managing free-energy barriers in nuclear pore transport.A simple kinetic model with explicit predictions for nuclear transport.Multiple conserved domains of the nucleoporin Nup124p and its orthologs Nup1p and Nup153 are critical for nuclear import and activity of the fission yeast Tf1 retrotransposon.Cargo surface hydrophobicity is sufficient to overcome the nuclear pore complex selectivity barrier.Nucleocytoplasmic transport: a thermodynamic mechanism.Ensemble characterization of an intrinsically disordered FG-Nup peptide and its F>A mutant in DMSO-d6.Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore.
P2860
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P2860
The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
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@zh
2004年學術文章
@zh-hant
name
The FG-repeat asymmetry of the ...... cytoplasmic transport in vivo.
@ast
The FG-repeat asymmetry of the ...... cytoplasmic transport in vivo.
@en
type
label
The FG-repeat asymmetry of the ...... cytoplasmic transport in vivo.
@ast
The FG-repeat asymmetry of the ...... cytoplasmic transport in vivo.
@en
prefLabel
The FG-repeat asymmetry of the ...... cytoplasmic transport in vivo.
@ast
The FG-repeat asymmetry of the ...... cytoplasmic transport in vivo.
@en
P2860
P356
P1476
The FG-repeat asymmetry of the ...... cytoplasmic transport in vivo.
@en
P2093
Bryan Zeitler
P2860
P304
P356
10.1083/JCB.200407156
P407
P50
P577
2004-11-01T00:00:00Z