Evidence map›Paper›PMID 22833565›Full record

ArticleMolecular biology of the cell2012

Sequence and structural analyses of nuclear export signals in the NESdb database.

Darui Xu, Alicia Farmer, Garen Collett, Nick V Grishin, Yuh Min Chook

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

93 citing papers in PubMed, 143 citations in OpenAlex.

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33 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Darui XuDepartment of Pharmacology, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75390, USA.
Alicia Farmer
Garen Collett
Nick V Grishin
Yuh Min Chook
The University of Texas Southwestern Medical Center · USHoward Hughes Medical Institute · US

Funding

Structures and Mechanisms of Nuclear Import and ExportR01GM069909 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 2004 to 2020
$5.8M
Computational methods for structural-functional studies of proteinsR01GM094575 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GRISHIN, NICK V. · 2010 to 2017
$2.4M
Database and Prediction Algorithm for the Leucine-rich Nuclear Export SignalsF32GM093493 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI XU, DARUI · 2010 to 2011
$99k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM093493NIGMS NIH HHS F32GM093493NIGMS NIH HHS R01 GM069909NIGMS NIH HHS R01-GM069909NIGMS NIH HHS R01 GM094575NIGMS NIH HHS R01-GM094575
6 · The paper itself

Abstract

We compiled >200 nuclear export signal (NES)-containing CRM1 cargoes in a database named NESdb. We analyzed the sequences and three-dimensional structures of natural, experimentally identified NESs and of false-positive NESs that were generated from the database in order to identify properties that might distinguish the two groups of sequences. Analyses of amino acid frequencies, sequence logos, and agreement with existing NES consensus sequences revealed strong preferences for the Φ1-X(3)-Φ2-X(2)-Φ3-X-Φ4 pattern and for negatively charged amino acids in the nonhydrophobic positions of experimentally identified NESs but not of false positives. Strong preferences against certain hydrophobic amino acids in the hydrophobic positions were also revealed. These findings led to a new and more precise NES consensus. More important, three-dimensional structures are now available for 68 NESs within 56 different cargo proteins. Analyses of these structures showed that experimentally identified NESs are more likely than the false positives to adopt α-helical conformations that transition to loops at their C-termini and more likely to be surface accessible within their protein domains or be present in disordered or unobserved parts of the structures. Such distinguishing features for real NESs might be useful in future NES prediction efforts. Finally, we also tested CRM1-binding of 40 NESs that were found in the 56 structures. We found that 16 of the NES peptides did not bind CRM1, hence illustrating how NESs are easily misidentified.

Indexed as

Databases, ProteinActive Transport, Cell NucleusAmino AcidsAmino Acid SequenceAnimalsBinding SitesCell NucleusElectrophoresis, Polyacrylamide GelExportin 1 ProteinHumansHydrophobic and Hydrophilic InteractionsInternetKaryopherinsModels, MolecularMolecular Sequence DataNuclear Export SignalsAmino AcidsExportin 1 ProteinKaryopherinsNuclear Export SignalsProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID22833565
PMCPMC3442415
OpenAlexW2105544978

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.