Evidence map›Paper›PMID 29549040›Full record

ReviewGastroenterology2018

Lamins and Lamin-Associated Proteins in Gastrointestinal Health and Disease.

Graham F Brady, Raymond Kwan, Juliana Bragazzi Cunha, Jared S Elenbaas, M Bishr Omary

Open access · bronzeAbstract readReview
In one paragraph

Review in Gastroenterology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 2 pooled it
1.4field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 2 syntheses or guidelines pooled it, 36 citations in OpenAlex.

  1. Pooled it
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  5. Gastro hep advances · 2025
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  19. Intermediate filaments as effectors of differentiation.Current opinion in cell biology · 2021
    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

5 authors at 3 institutions in 2 countries.

Graham F BradyDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan; Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, Michigan. Electronic address: gfbrady@med.umich.edu.
Raymond KwanDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan.
Juliana Bragazzi CunhaDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan.
Jared S ElenbaasMedical Scientist Training Program, Washington University, St Louis, Missouri.
M Bishr OmaryDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan; Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, Michigan; Åbo Akademi University, Turku, Finland.
University of Michigan · USÅbo Akademi University · FIWashington University in St. Louis · US

Funding

University of Michigan Center for Gastrointestinal ResearchP30DK034933 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1986 to 2021
$22.5M
Keratin Biology and Disease Aspects in Simple EpitheliaR01DK047918 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1995 to 2018
$6.6M
Mechanism of Proteotoxicity and Experimental Therapeutic Approaches in PorphyriaR01DK116548 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Bishr Omary · 2017 to 2026
$3.8M
NIDDK NIH HHS P30 DK034933NIDDK NIH HHS R01 DK047918NIDDK NIH HHS R01 DK116548
6 · The paper itself

Abstract

The nuclear lamina is a multi-protein lattice composed of A- and B-type lamins and their associated proteins. This protein lattice associates with heterochromatin and integral inner nuclear membrane proteins, providing links among the genome, nucleoskeleton, and cytoskeleton. In the 1990s, mutations in EMD and LMNA were linked to Emery-Dreifuss muscular dystrophy. Since then, the number of diseases attributed to nuclear lamina defects, including laminopathies and other disorders, has increased to include more than 20 distinct genetic syndromes. Studies of patients and mouse genetic models have pointed to important roles for lamins and their associated proteins in the function of gastrointestinal organs, including liver and pancreas. We review the interactions and functions of the lamina in relation to the nuclear envelope and genome, the ways in which its dysfunction is thought to contribute to human disease, and possible avenues for targeted therapies.

Indexed as

AnimalsCytoskeletonGastrointestinal DiseasesGenomeHumansLaminsLiverMiceNuclear LaminaPancreasLaminsEnvelopathiesLipodystrophyMyopathyNeuropathyNonalcoholic Fatty Liver DiseaseNucleoskeletonProgeria

Identifiers

PMID29549040
PMCPMC6038707
OpenAlexW2792244548

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.