Nucleocytoplasmic transport of intrinsically disordered proteins studied by high-speed super-resolution microscopy

scientific article published on 24 February 2020

Nucleocytoplasmic transport of intrinsically disordered proteins studied by high-speed super-resolution microscopy is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/PRO.3845
P932PMC publication ID7255516
P698PubMed publication ID32096308

P50authorWeidong YangQ89872458
P2093author name stringJiong Ma
Joseph M Kelich
Samuel L Junod
P2860cites workDendrite development regulated by CREST, a calcium-regulated transcriptional activatorQ24304307
Permeability of single nuclear poresQ24537305
Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfoldedQ24554044
A simple method for displaying the hydropathic character of a proteinQ26778481
Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex.Q27938407
Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporinsQ28131733
Intrinsic disorder in cell-signaling and cancer-associated proteinsQ28207698
The nuclear pore complex and nuclear transportQ28749193
Intrinsically unstructured proteinsQ29614784
IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy contentQ29615888
The Phyre2 web portal for protein modeling, prediction and analysisQ29616136
Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycleQ29619289
Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factorsQ29620194
Comparing and combining predictors of mostly disordered proteins.Q30350136
Understanding protein non-folding.Q30385084
Nup98 is a mobile nucleoporin with transcription-dependent dynamicsQ30475776
Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshotsQ30494436
A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporinsQ30496966
Structure and gating of the nuclear pore complexQ30656738
Charge as a selection criterion for translocation through the nuclear pore complexQ33565505
Selectivity mechanism of the nuclear pore complex characterized by single cargo trackingQ34166399
The human nuclear pore complex as revealed by cryo-electron tomography.Q34282959
Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import.Q34286042
The nuclear pore complex--structure and function at a glance.Q35029146
Nuclear import of plasmid DNA in digitonin-permeabilized cells requires both cytoplasmic factors and specific DNA sequencesQ35428699
The nuclear pore complex: nucleocytoplasmic transport and beyondQ35564601
Energetics of Transport through the Nuclear Pore ComplexQ35928500
Self-regulated viscous channel in the nuclear pore complexQ35982855
Natively unfolded proteinsQ36046424
Capturing directed molecular motion in the nuclear pore complex of live cellsQ36056461
Modularity within the architecture of the nuclear pore complex.Q36101124
The molecular mechanism of nuclear transport revealed by atomic-scale measurementsQ36208999
Regulated specific proteolysis of the Cajal body marker protein coilinQ36460273
Conserved spatial organization of FG domains in the nuclear pore complexQ36518503
Effect of charge, hydrophobicity, and sequence of nucleoporins on the translocation of model particles through the nuclear pore complexQ36653861
Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transportQ37477697
The conformation properties of proteins in solutionQ38053928
Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153.Q38597555
Sld2, which interacts with Dpb11 in Saccharomyces cerevisiae, is required for chromosomal DNA replicationQ39576309
Size-dependent leak of soluble and membrane proteins through the yeast nuclear pore complexQ41980902
Cargo surface hydrophobicity is sufficient to overcome the nuclear pore complex selectivity barrierQ42563372
The molecular mechanism of translocation through the nuclear pore complex is highly conserved.Q42813465
Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulationsQ42904612
The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA.Q44965707
Nucleoporin domain topology is linked to the transport status of the nuclear pore complexQ46620275
Intrinsically disordered proteins in the nucleus of human cellsQ47142042
Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy.Q48551782
The location of the transport gate in the nuclear pore complex.Q48945948
Binding site distribution of nuclear transport receptors and transport complexes in single nuclear pore complexes.Q50590376
Passive and facilitated transport in nuclear pore complexes is largely uncoupled.Q50705004
Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.Q52132803
Super-resolution 3D tomography of interactions and competition in the nuclear pore complex.Q55253495
Reply to ‘Deconstructing transport-distribution reconstruction in the nuclear-pore complex’Q62442238
Intrinsic protein disorder in complete genomesQ77145749
Nuclear export of mRNA molecules studied by SPEED microscopyQ91040897
3D Tracking-Free Approach for Obtaining 3D Super-Resolution Information in Rotationally Symmetric BiostructuresQ92221920
P577publication date2020-02-24
P1433published inProtein ScienceQ7251445
P1476titleNucleocytoplasmic transport of intrinsically disordered proteins studied by high-speed super-resolution microscopy

Reverse relations

Q104472045High-speed super-resolution imaging of rotationally symmetric structures using SPEED microscopy and 2D-to-3D transformationcites workP2860

Search more.