Evidence map›Paper›PMID 3762708›Full record

ArticleNature

The nuclear lamina is a meshwork of intermediate-type filaments.

U Aebi, J Cohn, L Buhle, L Gerace

Abstract read
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In one paragraph

Article in Nature. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 362 papers.

0numbers the graph read from it
0cells of the map it votes in
362citing papers in PubMed
19.0field-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

362 citing papers in PubMed, 978 citations in OpenAlex.

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  20. Pathological α-Synuclein Perturbs Nuclear Integrity.bioRxiv : the preprint server for biology · 2025
    Article

302 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

U Aebi
J Cohn
L Buhle
L Gerace
Johns Hopkins Medicine · USUniversity of Pennsylvania · US

Funding

STRUCTURE AND FUNCTIONS OF THE NUCLEAR ENVELOPER01GM028521 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GERACE, LARRY R. · 1985 to 2020
$7.0M
STRUCTURE AND INTERACTIONS OF CELLULAR PROTEINSR01GM031940 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI EICHNER, RIVA F · 1985 to 1988
–
NIGMS NIH HHS GM28521NIGMS NIH HHS GM31940
6 · The paper itself

Abstract

The nuclear lamina, a protein meshwork lining the nucleoplasmic surface of the inner nuclear membrane, is thought to provide a framework for organizing nuclear envelope structure and an anchoring site at the nuclear periphery for interphase chromatin. In several higher eukaryotic cells, the lamina appears to be a polymer comprised mainly of one to three immunologically related polypeptides of relative molecular mass (Mr) 60,000-75,000 (60-70K) termed lamins. Three lamins (A, B, and C) are typically present in mammalian somatic cells. Previous studies on nuclear envelopes of rat liver and Xenopus oocytes suggested that the lamina has a fibrillar or filamentous substructure. Interestingly, protein sequences recently deduced for human lamins A and C from complementary DNA clones indicate that both of these polypeptides contain a region of approximately 350 amino acids very similar in sequence to the coiled-coil alpha-helical rod domain that characterizes all intermediate-type filament (IF) proteins. Here we analyse the supramolecular organization of the native nuclear lamina and the structure and assembly properties of purified lamins, and show that the lamins constitute a previously unrecognized class of IF polypeptides.

Indexed as

AnimalsCell NucleusCytoskeletonIntermediate FilamentsLaminsMacromolecular SubstancesMicroscopy, ElectronMolecular WeightNucleoproteinsOocytesSolubilityXenopus laevisLaminsMacromolecular SubstancesNucleoproteins

Identifiers

PMID3762708
OpenAlexW2032858454

What OpenQuestion holds

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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.