Evidence map›Paper›PMID 32521238›Full record

ArticleBiophysical journal2020

Effect of Divalent Cations on the Structure and Mechanics of Vimentin Intermediate Filaments.

Huayin Wu, Yinan Shen, Dianzhuo Wang, Harald Herrmann, Robert D Goldman, David A Weitz

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 2026
    Article
  2. Article
  3. 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
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy.Journal of visualized experiments : JoVE · 2022
    Article
  12. Vimentin intermediate filaments and filamentous actin form unexpected interpenetrating networks that redefine the cell cortex.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Multiscale mechanics and temporal evolution of vimentin intermediate filament networks.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Article
  19. Review
  20. Article
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

6 authors at 3 institutions in 2 countries.

Huayin WuJohn A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts.
Yinan ShenDepartment of Physics, Harvard University, Cambridge, Massachusetts.
Dianzhuo WangJohn A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts; Department of Physics, University of Illinois at Urbana-Champaign, Urbana, Illinois.
Harald HerrmannDivision of Cell Biology, German Cancer Research Center (DKFZ), Heidelberg, Germany; Institute of Neuropathology, University Hospital Erlangen, Friedrich-Alexander Universität Erlangen-Nürnberg, Erlangen, Germany.
Robert D GoldmanDepartment of Cell and Developmental Biology, Northwestern University Feinberg School of Medicine, Chicago, Illinois.
David A WeitzJohn A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts; Department of Physics, Harvard University, Cambridge, Massachusetts. Electronic address: weitz@seas.harvard.edu.
Harvard University · USGerman Cancer Research Center · DENorthwestern University · US

Funding

Structural basis of the specific protein-protein interactions underlying IF assemP01GM096971 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOLDMAN, ROBERT D · 2011 to 2021
$16.8M
NIGMS NIH HHS P01 GM096971
6 · The paper itself

Abstract

Divalent cations behave as effective cross-linkers of intermediate filaments (IFs) such as vimentin IF (VIF). These interactions have been mostly attributed to their multivalency. However, ion-protein interactions often depend on the ion species, and these effects have not been widely studied in IFs. Here, we investigate the effects of two biologically important divalent cations, Zn

Indexed as

CytoskeletonIntermediate FilamentsCations, DivalentCytoplasmVimentinCations, DivalentVimentin

Identifiers

PMID32521238
PMCPMC7335910
OpenAlexW3028161147

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.