Evidence map›Paper›PMID 12885761›Full record

ArticleThe Journal of cell biology2003

Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport.

Janna Bednenko, Gino Cingolani, Larry Gerace

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

75 citing papers in PubMed, 135 citations in OpenAlex.

  1. Article
  2. Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Nitrogen deficiency tolerance conferred by introgression of a QTL derived from wild emmer into bread wheat.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024
    Article
  5. Review
  6. Article
  7. Review
  8. Unraveling docking and initiation of mRNA export through the nuclear pore complex.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
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  11. Review
  12. Review
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  14. Article
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  20. Article

15 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

3 authors at 1 institution in 1 country.

Janna BednenkoDepartment of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Gino Cingolani
Larry Gerace
Scripps Research Institute · US

Funding

MECHANISMS OF NUCLEAR PROTEIN IMPORTR01GM041955 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GERACE, LARRY R. · 1990 to 2006
$3.1M
NIGMS NIH HHS GM41955NIGMS NIH HHS R01 GM041955
6 · The paper itself

Abstract

Proteins containing a classical NLS are transported into the nucleus by the import receptor importin beta, which binds to cargoes via the adaptor importin alpha. The import complex is translocated through the nuclear pore complex by interactions of importin beta with a series of nucleoporins. Previous studies have defined a nucleoporin binding region in the NH2-terminal half of importin beta. Here we report the identification of a second nucleoporin binding region in its COOH-terminal half. Although the affinity of the COOH-terminal region for nucleoporins is dramatically weaker than that of the NH2-terminal region, sets of mutations that perturb the nucleoporin binding of either region reduce the nuclear import activity of importin beta to a similar extent ( approximately 50%). An importin beta mutant with a combination of mutations in the NH2- and COOH-terminal regions is completely inactive for nuclear import. Thus, importin beta possesses two nucleoporin binding sites, both of which are important for its nuclear import function.

Indexed as

Active Transport, Cell NucleusAmino Acidsbeta KaryopherinsBinding SitesCarboxylic AcidsDown-RegulationEukaryotic CellsHeLa CellsHumansNuclear PoreNuclear Pore Complex ProteinsPoint MutationProtein Structure, TertiaryProtein TransportAmino Acidsbeta KaryopherinsCarboxylic AcidsNuclear Pore Complex Proteins

Identifiers

PMID12885761
PMCPMC2172684
OpenAlexW2104564852

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.