Evidence map›Paper›PMID 30248895›Full record

ReviewCells2018

Vimentin Diversity in Health and Disease.

Frida Danielsson, McKenzie Kirsten Peterson, Helena Caldeira Araújo, Franziska Lautenschläger, Annica Karin Britt Gad

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed
14.5field-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

145 citing papers in PubMed, 269 citations in OpenAlex.

  1. Trial
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  6. Review
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  8. Article
  9. Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 2026
    Article
  10. Article
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  12. Article
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  18. Review
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  20. The important interplay between metal ions and the intermediate filament protein vimentin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Review

85 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

5 authors at 5 institutions in 4 countries.

Frida DanielssonScience for Life Laboratory, Royal Institute of Technology, 17165 Stockholm, Sweden. fridad@kth.se.
McKenzie Kirsten PetersonDepartment of Pathology, University of Utah School of Medicine, 84112 Salt Lake City, Utah, USA. mckenpeter@gmail.com.
Helena Caldeira AraújoCentro de Química da Madeira, Universidade da Madeira, 9020105 Funchal, Portugal. helena.caldeira@staff.uma.pt.
Franziska LautenschlägerCampus D2 2, Leibniz-Institut für Neue Materialien gGmbH (INM) and Experimental Physics, NT Faculty, E 2 6, Saarland University, 66123 Saarbrücken, Germany. franziska.lautenschlaeger@leibniz-inm.de.ORCID 0000-0001-8263-3386
Annica Karin Britt GadCentro de Química da Madeira, Universidade da Madeira, 9020105 Funchal, Portugal. annica.gad@staff.uma.pt.ORCID 0000-0002-1098-9129
Leibniz-Institute for New Materials · DEScience for Life Laboratory · SEUniversidade da Madeira · PTUniversity of Utah · USUppsala University · SE

Funding

Agência Regional para o Desenvolvimento da Investigaçaõ Tecnologia e Inovação M1420-01-0145-FEDER-000005Fundação para a Ciência e a Tecnologia PEst-OE/QUI/UI0674/2013
6 · The paper itself

Abstract

Vimentin is a protein that has been linked to a large variety of pathophysiological conditions, including cataracts, Crohn's disease, rheumatoid arthritis, HIV and cancer. Vimentin has also been shown to regulate a wide spectrum of basic cellular functions. In cells, vimentin assembles into a network of filaments that spans the cytoplasm. It can also be found in smaller, non-filamentous forms that can localise both within cells and within the extracellular microenvironment. The vimentin structure can be altered by subunit exchange, cleavage into different sizes, re-annealing, post-translational modifications and interacting proteins. Together with the observation that different domains of vimentin might have evolved under different selection pressures that defined distinct biological functions for different parts of the protein, the many diverse variants of vimentin might be the cause of its functional diversity. A number of review articles have focussed on the biology and medical aspects of intermediate filament proteins without particular commitment to vimentin, and other reviews have focussed on intermediate filaments in an in vitro context. In contrast, the present review focusses almost exclusively on vimentin, and covers both ex vivo and in vivo data from tissue culture and from living organisms, including a summary of the many phenotypes of vimentin knockout animals. Our aim is to provide a comprehensive overview of the current understanding of the many diverse aspects of vimentin, from biochemical, mechanical, cellular, systems biology and medical perspectives.

Indexed as

biomechanicscancer and metastasiscell‒extracellular matrix adhesionscell mechanical stiffness or elasticitycellular contractilityclinical biomarkersdrug targetepithelial‒mesenchymal transitionextracellular vimentinintermediate filamentstissue regenerationvimentin

Identifiers

PMID30248895
PMCPMC6210396
OpenAlexW2889835308

What OpenQuestion holds

Textmetadata
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.