Evidence map›Paper›PMID 24355792›Full record

ReviewCurrent biology : CB2013

Nuclear mechanics and mechanotransduction in health and disease.

Philipp Isermann, Jan Lammerding

Open access · bronzeAbstract readReview
In one paragraph

Review in Current biology : CB, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 206 papers.

0numbers the graph read from it
0cells of the map it votes in
206citing papers in PubMed
13.0field-weighted citation impact, top 1% 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

206 citing papers in PubMed, 375 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. The Nemp1-Nesprin complex mediates cellular responses to matrix mechanics.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  12. Review
  13. Endothelial Nuclear and Cytoskeletal Responses to Mechanical Stresses.Advances in experimental medicine and biology · 2026
    Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

146 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

2 authors at 1 institution in 1 country.

Philipp Isermann *Department of Biomedical Engineering & Weill Institute for Cell and Molecular Biology Cornell University; Ithaca, NY 14853.
Jan Lammerding *Department of Biomedical Engineering & Weill Institute for Cell and Molecular Biology Cornell University; Ithaca, NY 14853.
Cornell University · US

Funding

TRANS-NETWORK PROJECTSU54CA143876 · NCI · CORNELL UNIVERSITY · PI SHULER, MICHAEL L · 2009 to 2014
$12.6M
Nuclear mechanics and mechanotransduction in muscular laminopathiesR01HL082792 · NHLBI · CORNELL UNIVERSITY · PI LAMMERDING, JAN · 2007 to 2023
$4.8M
Nuclear-cytoskeletal coupling in muscular laminopathiesR01NS059348 · NINDS · CORNELL UNIVERSITY · PI LAMMERDING, JAN · 2007 to 2011
$1.3M
NCI NIH HHS U54 CA143876NCI NIH HHS U54CA143876NHLBI NIH HHS R01 HL082792NINDS NIH HHS R01 NS059348
6 · The paper itself

Abstract

The nucleus is the defining feature of eukaryotic cells and often represents the largest organelle. Over the past decade, it has become apparent that the nucleus is tightly integrated into the structural network of the cell through so-called LINC (linker of the nucleoskeleton and cytoskeleton) complexes, which enable transmission of forces between the nucleus and cytoskeleton. This physical connection between the nucleus and the cytoskeleton is essential for a broad range of cellular functions, including intracellular nuclear movement and positioning, cytoskeletal organization, cell polarization, and cell migration. Recent reports further indicate that forces transmitted from the extracellular matrix to the nucleus via the cytoskeleton may also directly contribute to the cell's ability to probe its mechanical environment by triggering force-induced changes in nuclear structures. In addition, it is now emerging that the physical properties of the nucleus play a crucial role during cell migration in three-dimensional (3D) environments, where cells often have to transit through narrow constrictions that are smaller than the nuclear diameter, e.g., during development, wound healing, or cancer metastasis. In this review, we provide a brief overview of how LINC complex proteins and lamins facilitate nucleo-cytoskeletal coupling, highlight recent findings regarding the role of the nucleus in cellular mechanotransduction and cell motility in 3D environments, and discuss how mutations and/or changes in the expression of these nuclear envelope proteins can result in a broad range of human diseases, including muscular dystrophy, dilated cardiomyopathy, and premature aging.

Indexed as

Models, BiologicalAging, PrematureCardiomyopathy, DilatedCell MovementCell NucleusCytoskeletonHumansMechanotransduction, CellularMuscular DystrophiesNuclear Matrix-Associated ProteinsNuclear Matrix-Associated Proteins

Identifiers

PMID24355792
PMCPMC3883624
OpenAlexW2056002615

What OpenQuestion holds

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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.