Evidence map›Paper›PMID 24523288›Full record

ArticleMolecular biology of the cell2014

Concentration-dependent lamin assembly and its roles in the localization of other nuclear proteins.

Yuxuan Guo, Youngjo Kim, Takeshi Shimi, Robert D Goldman, Yixian Zheng

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

52 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. The molecular basis of lamin-specific chromatin interactions.Nature structural & molecular biology · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Nuclear damage inMolecular biology of the cell · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Components and Mechanisms of Nuclear Mechanotransduction.Annual review of cell and developmental biology · 2021
    Review
  17. Article
  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

5 authors at 3 institutions in 1 country.

Yuxuan GuoDepartment of Biology, Johns Hopkins University, Baltimore, MD 21218 Department of Embryology, Carnegie Institution for Science, Baltimore, MD 21218 Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611.
Youngjo Kim
Takeshi Shimi
Robert D Goldman
Yixian Zheng
Johns Hopkins University · USNorthwestern University · USCarnegie Institution for Science · US

Funding

INTERMEDIATE FILAMENTS IN NORMAL AND TRANSFORMED CELLSR01CA031760 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOLDMAN, ROBERT D · 1985 to 2013
$4.9M
Super-resolution microscopy of nuclear lamin and spindle envelope/matrix functionR01GM106023 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI GOLDMAN, ROBERT D, ZHENG, YIXIAN · 2013 to 2020
$3.5M
The function and assembly of the lamin-B spindle sheathR01GM056312 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI ZHENG, YIXIAN · 1997 to 2014
$2.7M
NCI NIH HHS CA031760NCI NIH HHS R01 CA031760NIGMS NIH HHS GM056312NIGMS NIH HHS GM106023NIGMS NIH HHS R01 GM056312NIGMS NIH HHS R01 GM106023
6 · The paper itself

Abstract

The nuclear lamina (NL) consists of lamin polymers and proteins that bind to the polymers. Disruption of NL proteins such as lamin and emerin leads to developmental defects and human diseases. However, the expression of multiple lamins, including lamin-A/C, lamin-B1, and lamin-B2, in mammals has made it difficult to study the assembly and function of the NL. Consequently, it has been unclear whether different lamins depend on one another for proper NL assembly and which NL functions are shared by all lamins or are specific to one lamin. Using mouse cells deleted of all or different combinations of lamins, we demonstrate that the assembly of each lamin into the NL depends primarily on the lamin concentration present in the nucleus. When expressed at sufficiently high levels, each lamin alone can assemble into an evenly organized NL, which is in turn sufficient to ensure the even distribution of the nuclear pore complexes. By contrast, only lamin-A can ensure the localization of emerin within the NL. Thus, when investigating the role of the NL in development and disease, it is critical to determine the protein levels of relevant lamins and the intricate shared or specific lamin functions in the tissue of interest.

Indexed as

AnimalsCell DifferentiationCells, CulturedEmbryonic Stem CellsLamin Type ALamin Type BMembrane ProteinsMiceNuclear LaminaNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsRNA InterferenceRNA, Small InterferingemerinLamin Type ALamin Type BMembrane ProteinsNuclear Pore Complex ProteinsNuclear ProteinsRNA, Small Interfering

Identifiers

PMID24523288
PMCPMC3982994
OpenAlexW2103609151

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.