Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulations.
about
Nucleoporin's Like Charge Regions Are Major Regulators of FG Coverage and Dynamics Inside the Nuclear Pore ComplexCooperative Interactions between Different Classes of Disordered Proteins Play a Functional Role in the Nuclear Pore Complex of Baker's YeastA physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies.Energetics of Transport through the Nuclear Pore Complex.Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex.Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex.Simple rules for passive diffusion through the nuclear pore complex.Regulation of RNA-binding proteins affinity to export receptors enables the nuclear basket proteins to distinguish and retain aberrant mRNAs.The selective permeability barrier in the nuclear pore complexProtein Transport by the Nuclear Pore Complex: Simple Biophysics of a Complex Biomachine.Size-dependent leak of soluble and membrane proteins through the yeast nuclear pore complex.A coarse-grained computational model of the nuclear pore complex predicts Phe-Gly nucleoporin dynamics.Investigating molecular crowding within nuclear pores using polarization-PALM.Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences.A Programmable DNA Origami Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore Confinement.Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy.Spatial structure of disordered proteins dictates conductance and selectivity in Nuclear Pore Complex mimics.DNA origami scaffold for studying intrinsically disordered proteins of the nuclear pore complex.Super-resolution 3D tomography of interactions and competition in the nuclear pore complex.
P2860
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P2860
Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulations.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
Probing the disordered domain ...... olecular dynamics simulations.
@en
Probing the disordered domain ...... olecular dynamics simulations.
@nl
type
label
Probing the disordered domain ...... olecular dynamics simulations.
@en
Probing the disordered domain ...... olecular dynamics simulations.
@nl
prefLabel
Probing the disordered domain ...... olecular dynamics simulations.
@en
Probing the disordered domain ...... olecular dynamics simulations.
@nl
P2860
P50
P1433
P1476
Probing the disordered domain ...... olecular dynamics simulations.
@en
P2093
Liesbeth M Veenhoff
P2860
P304
P356
10.1016/J.BPJ.2014.07.060
P407
P577
2014-09-01T00:00:00Z