Evidence map›Paper›PMID 24508913›Full record

ReviewSeminars in cell & developmental biology2014

Lamina-associated polypeptide 1: protein interactions and tissue-selective functions.

Ji-Yeon Shin, William T Dauer, Howard J Worman

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  3. Review
  4. International journal of molecular sciences · 2023
    Review
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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

3 authors at 2 institutions in 1 country.

Ji-Yeon ShinDepartment of Medicine, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA; Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA.
William T DauerDepartment of Neurology, University of Michigan Medical School, 109 Zina Pitcher Place, Ann Arbor, MI, 48109, USA; Department of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, Ann Arbor, MI, 48109, USA. Electronic address: dauer@med.mich.edu.
Howard J WormanDepartment of Medicine, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA; Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA. Electronic address: hjw14@columbia.edu.
Columbia University · USUniversity of Michigan–Ann Arbor · US

Funding

Pathogenesis of Emery-Dreifuss Muscular DystrophyR01AR048997 · NIAMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI WORMAN, HOWARD J · 2003 to 2024
$7.1M
NIAMS NIH HHS R01 AR048997
6 · The paper itself

Abstract

Mutations in genes encoding widely expressed nuclear envelope proteins often lead to diseases that manifest in specific tissues. Lamina-associated polypeptide 1 (LAP1) is an integral protein of the inner nuclear membrane that is expressed in most cells and tissues. Within the nuclear envelope, LAP1 interacts physically with lamins, torsinA and emerin, suggesting it may serve as a key node for transducing signals across the inner nuclear membrane. Indeed, recent in vivo studies in genetically modified mice strongly support functional links between LAP1 and both torsinA (in neurons) and emerin (in muscle). These studies suggest that tissue-selective diseases caused by mutations in genes encoding nuclear envelope proteins may result, at least in part, from the selective disruption of discrete nuclear envelope protein complexes.

Indexed as

AnimalsCarrier ProteinsCytoskeletal ProteinsHumansLaminsMembrane ProteinsMiceMolecular ChaperonesMuscular DystrophiesMutationNuclear EnvelopeNuclear ProteinsSignal TransductionCarrier ProteinsCytoskeletal ProteinsemerinLaminsMembrane ProteinsMolecular ChaperonesNuclear ProteinsTOR1AIP1 protein, humanTOR1AIP2 protein, humanTOR1A protein, humanDystoniaLaminMuscular dystrophyNuclear envelopeNuclear membrane

Identifiers

PMID24508913
PMCPMC4040325
OpenAlexW1971712282

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.