Evidence map›Paper›PMID 23212477›Full record

ReviewNature reviews. Molecular cell biology2013

The nuclear lamins: flexibility in function.

Brian Burke, Colin L Stewart

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 347 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
347citing papers in PubMed, 1 pooled it
16.1field-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

347 citing papers in PubMed, 1 synthesis or guideline pooled it, 538 citations in OpenAlex.

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287 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.

Brian BurkeInstitute of Medical Biology, 8A Biomedical Grove, Immunos 06-06, Singapore 138648. Brian.Burke@ imb.a-star.edu.sg
Colin L Stewart
Institute of Medical Biology · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear lamina is an important structural determinant for the nuclear envelope as a whole, attaching chromatin domains to the nuclear periphery and localizing some nuclear envelope proteins. The major components of the lamina are the A-type and B-type lamins, which are members of the intermediate filament protein family. Whereas the expression of A-type lamins is developmentally regulated, B-type lamins, as a class, are found in all cells. The association of B-type lamins with many aspects of nuclear function has led to the view that these are essential proteins, and there is growing evidence suggesting that they regulate cellular senescence. However, B-type lamins are dispensable in certain cell types in vivo, and neither A-type nor B-type lamins may be required in early embryos or embryonic stem cells. The picture that is beginning to emerge is of a complex network of interactions at the nuclear periphery that may be defined by cell- and tissue-specific functions.

Indexed as

Cellular SenescenceAging, PrematureAnimalsBone and BonesCell NucleusChromatinEmbryonic Stem CellsGene Expression Regulation, DevelopmentalHumansIntermediate FilamentsMiceMuscular Dystrophy, AnimalMutationNuclear LaminaNuclear ProteinsChromatinNuclear Proteins

Identifiers

PMID23212477
OpenAlexW2065776621

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.