Importin-β modulates the permeability of the nuclear pore complex in a Ran-dependent manner.
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Misdelivery at the Nuclear Pore Complex-Stopping a Virus Dead in Its TracksSystematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex.A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies.The molecular mechanism of nuclear transport revealed by atomic-scale measurements.Truncation of the TAR DNA-binding protein 43 is not a prerequisite for cytoplasmic relocalization, and is suppressed by caspase inhibition and by introduction of the A90V sequence variantSimple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex.How to operate a nuclear pore complex by Kap-centric controlSlide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex.Simple rules for passive diffusion through the nuclear pore complex.A ternary complex comprising transportin1, Rab8 and the ciliary targeting signal directs proteins to ciliary membranes.Cyanobacteria use micro-optics to sense light directionDeciphering the Structure and Function of Nuclear Pores Using Single-Molecule Fluorescence Approaches.The Nuclear Pore Complex as a Flexible and Dynamic GateProtein Transport by the Nuclear Pore Complex: Simple Biophysics of a Complex Biomachine.In vivo analysis of protein crowding within the nuclear pore complex in interphase and mitosis.Dissecting in vivo steady-state dynamics of karyopherin-dependent nuclear transport.Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.Dynamic Scaling Analysis of Molecular Motion within the LAT:Grb2:SOS Protein Network on Membranes.Investigating molecular crowding within nuclear pores using polarization-PALM.Mechanisms of nuclear pore complex assembly - two different ways of building one molecular machine.Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences.Karyopherins regulate nuclear pore complex barrier and transport function.A Programmable DNA Origami Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore Confinement.RAPGEF5 Regulates Nuclear Translocation of β-Catenin.Nuclear pore heterogeneity influences HIV-1 infection and the antiviral activity of MX2
P2860
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P2860
Importin-β modulates the permeability of the nuclear pore complex in a Ran-dependent manner.
description
2015 nî lūn-bûn
@nan
2015 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի մարտին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Importin-β modulates the perme ...... lex in a Ran-dependent manner.
@ast
Importin-β modulates the perme ...... lex in a Ran-dependent manner.
@en
type
label
Importin-β modulates the perme ...... lex in a Ran-dependent manner.
@ast
Importin-β modulates the perme ...... lex in a Ran-dependent manner.
@en
prefLabel
Importin-β modulates the perme ...... lex in a Ran-dependent manner.
@ast
Importin-β modulates the perme ...... lex in a Ran-dependent manner.
@en
P2093
P2860
P50
P356
P1433
P1476
Importin-β modulates the perme ...... lex in a Ran-dependent manner.
@en
P2093
Jaime Yassif
Jay T Groves
Jeffrey H Tang
William Y C Huang
P2860
P356
10.7554/ELIFE.04052
P407
P577
2015-03-06T00:00:00Z