Evidence map›Paper›PMID 23332057›Full record

ArticleBiophysical journal2013

Conserved spatial organization of FG domains in the nuclear pore complex.

Claire E Atkinson, Alexa L Mattheyses, Martin Kampmann, Sanford M Simon

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 30 citations in OpenAlex.

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  9. Mapping the native organization of the yeast nuclear pore complex using nuclear radial intensity measurements.Proceedings of the National Academy of Sciences of the United States of America · 2019
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Claire E AtkinsonLaboratory of Cellular Biophysics, The Rockefeller University, New York, New York, USA.
Alexa L Mattheyses
Martin Kampmann
Sanford M Simon
Rockefeller University · US

Funding

Selective fluorescent labeling of proteins in living cellsR01GM087977 · NIGMS · ROCKEFELLER UNIVERSITY · PI SIMON, SANFORD M · 2009 to 2012
$1.6M
NIGMS NIH HHS GM087977NIGMS NIH HHS R01 GM087977
6 · The paper itself

Abstract

Selective transport through the nuclear pore complex (NPC) requires nucleoporins containing natively unfolded phenylalanine-glycine (FG) domains. Several differing models for their dynamics within the pore have been proposed. We characterize the behavior of the FG nucleoporins in vivo using polarized fluorescence microscopy. Using nucleoporins tagged with green fluorescent protein along their FG domains, we show that some of these proteins are ordered, indicating an overall orientational organization within the NPC. This orientational ordering of the FG domains depends on their specific context within the NPC, but is independent of active transport and cargo load. For most nups, behavior does not depend on the FG motifs. These data support a model whereby local geometry constrains the orientational organization of the FG nups. Intriguingly, homologous yeast and mammalian proteins show conserved behavior, suggesting functional relevance. Our findings have implications for mechanistic models of NPC transport.

Indexed as

AnisotropyBiological Transport, ActiveDipeptidesGreen Fluorescent ProteinsHeLa CellsHumansLigandsModels, BiologicalNuclear PoreNuclear Pore Complex ProteinsProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsRepetitive Sequences, Amino AcidDipeptidesGreen Fluorescent ProteinsLigandsNuclear Pore Complex ProteinsphenylalanylglycineRecombinant Fusion Proteins

Identifiers

PMID23332057
PMCPMC3540264
OpenAlexW2112424419

What OpenQuestion holds

Textmetadata
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.