Evidence map›Paper›PMID 18227062›Full record

ArticleThe Journal of biological chemistry2008

Regulation of nuclear lamin polymerization by importin alpha.

Stephen A Adam, Kaushik Sengupta, Robert D Goldman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
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  4. Review
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  12. Review
  13. The Journal of biological chemistry · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Importin α: functions as a nuclear transport factor and beyond.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018
    Review
  18. Article
  19. Article
  20. Article
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.

Stephen A AdamDepartment of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. s-adam@northwestern.edu
Kaushik Sengupta
Robert D Goldman
Northwestern University · US

Funding

INTERMEDIATE FILAMENTS IN NORMAL AND TRANSFORMED CELLSR01CA031760 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOLDMAN, ROBERT D · 1985 to 2013
$4.9M
NCI NIH HHS 5 R01 CA 031760-25
6 · The paper itself

Abstract

Nuclear lamins are integral components of the nuclear envelope and are important for the regulation of many aspects of nuclear function, including gene transcription and DNA replication. During interphase, the lamins form an intranuclear intermediate filament network that must be disassembled and reassembled when cells divide. Little is known about factors regulating this assembly/disassembly cycle. Using in vitro nuclear assembly and lamin assembly assays, we have identified a role for the nuclear transport factor importin alpha in the regulation of lamin assembly. Exogenous importin alpha inhibited nuclear lamin assembly in Xenopus interphase egg nuclear assembly assays. Fractionation of the egg extract used for nuclear assembly identified a high molecular weight complex containing the major egg lamin, XLB3, importin alpha, and importin beta. This complex could be dissociated by RanGTP or a competing nuclear localization sequence, indicating that lamin assembly is Ran- and importin alpha-dependent in the egg extract. We show that the addition of importin alpha to purified lamin B3 prevents the assembly of lamins in solution. Lamin assembly assays show that importin alpha prevents the self-association of lamins required to assemble lamin filaments into the typical paracrystals formed in vitro. These results suggest a role for importin alpha in regulating lamin assembly and possibly modulating the interactions of lamins with lamin-binding proteins.

Indexed as

alpha KaryopherinsAnimalsCell NucleusCytosolFemaleLamin Type BMicroscopy, ElectronMolecular WeightOocytesProtein Bindingran GTP-Binding ProteinXenopusalpha KaryopherinsLamin Type Bran GTP-Binding Protein

Identifiers

PMID18227062
PMCPMC2417177
OpenAlexW2044085712

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.