Evidence map›Paper›PMID 22555292›Full record

ArticleEuropean journal of cell biology2012

LINC complex alterations in DMD and EDMD/CMT fibroblasts.

Surayya Taranum, Eva Vaylann, Peter Meinke, Sabu Abraham, Liu Yang, Sascha Neumann, Iakowos Karakesisoglou, Manfred Wehnert, Angelika A Noegel

Open access · greenAbstract read
In one paragraph

Article in European journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed, 60 citations in OpenAlex.

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  11. Nesprin-1 impact on tumorigenic cell phenotypes.Molecular biology reports · 2020
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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

9 authors at 3 institutions in 2 countries.

Surayya TaranumInstitute for Biochemistry I, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, Germany.
Eva Vaylann
Peter Meinke
Sabu Abraham
Liu Yang
Sascha Neumann
Iakowos Karakesisoglou
Manfred Wehnert
Angelika A Noegel
University of Cologne · DEUniversität Greifswald · DEDurham University · GB

Funding

Wellcome TrustWellcome Trust WT 087244/Z/08/Z
6 · The paper itself

Abstract

Emery-Dreifuss muscular dystrophy (EDMD) is a late onset-disease characterized by skeletal muscle wasting and heart defects with associated risk of sudden death. The autosomal dominant form of the disease is caused by mutations in the LMNA gene encoding LaminA and C, the X-linked form results from mutations in the gene encoding the inner nuclear membrane protein Emerin (STA). Both Emerin and LaminA/C interact with the nuclear envelope proteins Nesprin-1 and -2 and mutations in genes encoding C-terminal isoforms of Nesprin-1 and -2 have also been implicated in EDMD. Here we analyse primary fibroblasts from patients affected by either Duchenne muscular dystrophy (DMD) or Emery-Dreifuss muscular dystrophy/Charcot-Marie-Tooth syndrome (EDMD/CMT) that in addition to the disease causing mutations harbour mutations in the Nesprin-1 gene and in the SUN1 and SUN2 gene, respectively. SUN proteins together with the Nesprins form the core of the LINC complex which connects the nucleus with the cytoskeleton. The mutations are accompanied by changes in cell adhesion, cell migration, senescence, and stress response, as well as in nuclear shape and nuclear envelope composition which are changes characteristic for laminopathies. Our results point to a potential influence of mutations in components of the LINC complex on the clinical outcome and the molecular pathology in the patients.

Indexed as

Cell AdhesionCell MovementCell NucleusCell Nucleus ShapeCellular SenescenceCharcot-Marie-Tooth DiseaseCytoskeletal ProteinsFemaleFibroblastsHumansIntracellular Signaling Peptides and ProteinsLamin Type AMaleMembrane ProteinsMicrotubule-Associated ProteinsMultiprotein ComplexesCytoskeletal ProteinsemerinIntracellular Signaling Peptides and ProteinsLamin Type ALMNA protein, humanMembrane ProteinsMicrotubule-Associated ProteinsMultiprotein ComplexesNerve Tissue ProteinsNuclear ProteinsSUN1 protein, humanSUN2 protein, humanSYNE1 protein, human

Identifiers

PMID22555292
PMCPMC3778752
OpenAlexW2015463720

What OpenQuestion holds

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LicenceCC BY
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.