Evidence map›Paper›PMID 22126840›Full record

ReviewJournal of structural biology2012

Nuclear lamina at the crossroads of the cytoplasm and nucleus.

Larry Gerace, Michael D Huber

Open access · greenAbstract readReview
In one paragraph

Review in Journal of structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

71 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Force-dependent structural dynamics of the giant nesprin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Cytomegalovirus disrupts Lamin A/C to control microtubule-mediated nuclear movement and cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Decreased RYR2 Cluster Size and Abnormal SR CaAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. "Bone-SASP" in Skeletal Aging.Calcified tissue international · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. The Nuclear Lamina.Cold Spring Harbor perspectives in biology · 2022
    Review
  15. ATM Modulates Nuclear Mechanics by Regulating Lamin A Levels.Frontiers in cell and developmental biology · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

11 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.

Larry GeraceDepartment of Cell, The Scripps Research Institute, 10550 N Torrey Pines Rd, La Jolla, CA 92037, USA. lgerace@scripps.edu
Michael D Huber
Scripps Research Institute · US

Funding

STRUCTURE AND FUNCTIONS OF THE NUCLEAR ENVELOPER01GM028521 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GERACE, LARRY R. · 1985 to 2020
$7.0M
NIGMS NIH HHS R01 GM028521NIGMS NIH HHS R01GM28521
6 · The paper itself

Abstract

The nuclear lamina is a protein meshwork that lines the nuclear envelope in metazoan cells. It is composed largely of a polymeric assembly of lamins, which comprise a distinct sequence homology class of the intermediate filament protein family. On the basis of its structural properties, the lamina originally was proposed to provide scaffolding for the nuclear envelope and to promote anchoring of chromatin and nuclear pore complexes at the nuclear surface. This viewpoint has expanded greatly during the past 25 years, with a host of surprising new insights on lamina structure, molecular composition and functional attributes. It has been established that the self-assembly properties of lamins are very similar to those of cytoplasmic intermediate filament proteins, and that the lamin polymer is physically associated with components of the cytoplasmic cytoskeleton and with a multitude of chromatin and inner nuclear membrane proteins. Cumulative evidence points to an important role for the lamina in regulating signaling and gene activity, and in mechanically coupling the cytoplasmic cytoskeleton to the nucleus. The significance of the lamina has been vaulted to the forefront by the discovery that mutations in lamins and lamina-associated polypeptides lead to an array of human diseases. A key future challenge is to understand how the lamina integrates pathways for mechanics and signaling at the molecular level. Understanding the structure of the lamina from the atomic to supramolecular levels will be essential for achieving this goal.

Indexed as

AnimalsCell NucleusChromatinCytoskeletonHumansIntermediate Filament ProteinsLaminsMicroscopy, FluorescenceModels, MolecularMutationNuclear EnvelopeNuclear LaminaNuclear PoreChromatinIntermediate Filament ProteinsLamins

Identifiers

PMID22126840
PMCPMC3261324
OpenAlexW2029610799

What OpenQuestion holds

Textmetadata
LicenceTDM
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.