Evidence map›Paper›PMID 21167872›Full record

ReviewBiochimica et biophysica acta2011

Single molecule studies of nucleocytoplasmic transport.

Li-Chun Tu, Siegfried M Musser

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Self-regulation of the nuclear pore complex enables clogging-free crowded transport.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Choreography of importin-α/CAS complex assembly and disassembly at nuclear pores.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Review
  18. Imaging flow cytometry: coping with heterogeneity in biological systems.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2012
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Li-Chun TuDepartment of Molecular and Cellular Medicine, College of Medicine, Texas A&M Health Science Center, College Station, TX 77843, USA.
Siegfried M Musser
Texas A&M Health Science Center · US

Funding

Single Molecule Analysis of Bacterial Protein TransportR01GM065534 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI MUSSER, SIEGFRIED M · 2003 to 2010
$1.6M
Mechanisms of Nucleocytoplasmic TransportR01GM084062 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI MUSSER, SIEGFRIED M · 2009 to 2012
$1.4M
Modulation of Dendritic Cells against HIV-1SC3GM084802 · NIGMS · WINSTON-SALEM STATE UNIVERSITY · PI SINGH, DINESH K. · 2008 to 2011
$401k
NIGMS NIH HHS GM065534NIGMS NIH HHS GM084802NIGMS NIH HHS R01 GM065534NIGMS NIH HHS R01 GM084062
6 · The paper itself

Abstract

Molecular traffic between the cytoplasm and the nucleoplasm of eukaryotic cells is mediated by nuclear pore complexes (NPCs). Hundreds, if not thousands, of molecules interact with and transit through each NPC every second. The pore is blocked by a permeability barrier, which consists of a network of intrinsically unfolded polypeptides containing thousands of phenylalanine-glycine (FG) repeat motifs. This FG-network rejects larger molecules and admits smaller molecules or cargos bound to nuclear transport receptors (NTRs). For a cargo transport complex, minimally consisting of a cargo molecule plus an NTR, access to the permeability barrier is provided by interactions between the NTR and the FG repeat motifs. Numerous models have been postulated to explain the controlled accessibility and the transport characteristics of the FG-network, but the amorphous, flexible nature of this structure has hindered characterization. A relatively recent development is the ability to monitor the real-time movement of single molecules through individual NPCs via single molecule fluorescence (SMF) microscopy. A major advantage of this approach is that it can be used to continuously monitor a series of specific molecular interactions in an active pore with millisecond time resolution, which therefore allows one to distinguish between kinetic and thermodynamic control. Novel insights and prospects for the future are outlined in this review. This article is part of a Special Issue entitled: Regulation of Signaling and Cellular Fate through Modulation of Nuclear Protein Import.

Indexed as

Active Transport, Cell NucleusHumansMicroscopy, FluorescenceModels, BiologicalNuclear PoreNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsPermeabilitySignal TransductionNuclear Pore Complex ProteinsNucleocytoplasmic Transport Proteins

Identifiers

PMID21167872
PMCPMC3140539
OpenAlexW2090102586

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.