Capturing directed molecular motion in the nuclear pore complex of live cells. - Wikidata - awgldk - TriplyDB

Capturing directed molecular motion in the nuclear pore complex of live cells.

Capturing directed molecular motion in the nuclear pore complex of live cells.

http://www.wikidata.org/entity/Q36056461

about

Cellular and viral determinants of retroviral nuclear entry Physical motif clustering within intrinsically disordered nucleoporin sequences reveals universal functional features Disordered proteinaceous machines Orbital Single Particle Tracking on a commercial confocal microscope using piezoelectric stage feedback.Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.Promiscuous binding of Karyopherinβ1 modulates FG nucleoporin barrier function and expedites NTF2 transport kinetics.Nanoscale protein diffusion by STED-based pair correlation analysis.3D orbital tracking in a modified two-photon microscope: an application to the tracking of intracellular vesicles.From fast fluorescence imaging to molecular diffusion law on live cell membranes in a commercial microscope Electrically tunable lens speeds up 3D orbital tracking Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex.How to operate a nuclear pore complex by Kap-centric control A smart temperature and magnetic-responsive gating carbon nanotube membrane for ion and protein transportation.A lipid bound actin meshwork organizes liquid phase separation in model membranes Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.Quantifying intracellular dynamics using fluorescence fluctuation spectroscopy.Recent applications of fluorescence correlation spectroscopy in live systems.Advanced fluorescence microscopy methods for the real-time study of transcription and chromatin dynamics.The selective permeability barrier in the nuclear pore complex Dynamics of intracellular processes in live-cell systems unveiled by fluorescence correlation microscopy.Time-resolved biophysical approaches to nucleocytoplasmic transport.Measurement of nanoscale three-dimensional diffusion in the interior of living cells by STED-FCS.Diffusion Tensor Analysis by Two-Dimensional Pair Correlation of Fluorescence Fluctuations in Cells.Protoparvovirus Knocking at the Nuclear Door.Spatiotemporal Fluctuation Analysis of Molecular Diffusion Laws in Live-Cell Membranes.Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy.Visualization of barriers and obstacles to molecular diffusion in live cells by spatial pair-cross-correlation in two dimensions.Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering.Dynamic Distribution and Interaction of the Arabidopsis SRSF1 Subfamily Splicing Factors.

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P2860

Capturing directed molecular motion in the nuclear pore complex of live cells.

http://www.wikidata.org/entity/Q36056461

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

@zh-tw

2012年论文

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2012年论文

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2012年论文

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name

Capturing directed molecular motion in the nuclear pore complex of live cells.

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Capturing directed molecular motion in the nuclear pore complex of live cells.

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type

label

Capturing directed molecular motion in the nuclear pore complex of live cells.

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Capturing directed molecular motion in the nuclear pore complex of live cells.

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prefLabel

Capturing directed molecular motion in the nuclear pore complex of live cells.

@ast

Capturing directed molecular motion in the nuclear pore complex of live cells.

@en

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PNAS.1200486109

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Capturing directed molecular motion in the nuclear pore complex of live cells.

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P2093

Francesco Cardarelli

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Luca Lanzano

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P2860

Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded

Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import

Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells

The yeast nuclear pore complex: composition, architecture, and transport mechanism

FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties.

Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex.

Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle

Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study.

A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins.

Imaging of single-molecule translocation through nuclear pore complexes.

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9863-9868

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scholarly article

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10.1073/PNAS.1200486109

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25

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109

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