Evidence map›Paper›PMID 34572105›Full record

ReviewCells2021

Molecular Interactions Driving Intermediate Filament Assembly.

Pieter-Jan Vermeire, Giel Stalmans, Anastasia V Lilina, Jan Fiala, Petr Novak, Harald Herrmann, Sergei V Strelkov

Abstract readReview
In one paragraph

Review in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 2026
    Article
  2. 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
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Proteomic Analysis of Single Hairs.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  9. Review
  10. Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024
    Article
  11. Filament structure and subcellular organization of the bacterial intermediate filament-like protein crescentin.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. 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

7 authors.

Pieter-Jan VermeireLaboratory for Biocrystallography, KU Leuven, 3000 Leuven, Belgium.ORCID 0000-0003-0363-9558
Giel StalmansLaboratory for Biocrystallography, KU Leuven, 3000 Leuven, Belgium.ORCID 0000-0001-6570-6328
Anastasia V LilinaLaboratory for Biocrystallography, KU Leuven, 3000 Leuven, Belgium.ORCID 0000-0002-0218-9607
Jan FialaDepartment of Biochemistry, Charles University, 12800 Prague, Czech Republic.ORCID 0000-0002-7753-8170
Petr NovakDepartment of Biochemistry, Charles University, 12800 Prague, Czech Republic.ORCID 0000-0001-8688-529X
Harald HerrmannInstitute of Neuropathology, University Hospital Erlangen, Friedrich-Alexander University Erlangen-Nürnberg, 91054 Erlangen, Germany.
Sergei V StrelkovLaboratory for Biocrystallography, KU Leuven, 3000 Leuven, Belgium.ORCID 0000-0001-7189-4652

Funding

Horizon 2020 731077
6 · The paper itself

Abstract

Given the role of intermediate filaments (IFs) in normal cell physiology and scores of IF-linked diseases, the importance of understanding their molecular structure is beyond doubt. Research into the IF structure was initiated more than 30 years ago, and some important advances have been made. Using crystallography and other methods, the central coiled-coil domain of the elementary dimer and also the structural basis of the soluble tetramer formation have been studied to atomic precision. However, the molecular interactions driving later stages of the filament assembly are still not fully understood. For cytoplasmic IFs, much of the currently available insight is due to chemical cross-linking experiments that date back to the 1990s. This technique has since been radically improved, and several groups have utilized it recently to obtain data on lamin filament assembly. Here, we will summarize these findings and reflect on the remaining open questions and challenges of IF structure. We argue that, in addition to X-ray crystallography, chemical cross-linking and cryoelectron microscopy are the techniques that should enable major new advances in the field in the near future.

Indexed as

Cell Physiological PhenomenaAnimalsCytoskeletonHumansIntermediate Filamentsassemblychemical analytical cross-linkingcryoelectron microscopyintermediate filamentkeratinlaminvimentinX-ray crystallography

Identifiers

PMID34572105
PMCPMC8466517

What OpenQuestion holds

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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.