Evidence map›Paper›PMID 33190098›Full record

ReviewCurrent opinion in cell biology2021

Recent insight into intermediate filament structure.

Sherif A Eldirany, Ivan B Lomakin, Minh Ho, Christopher G Bunick

Abstract readReview
In one paragraph

Review in Current opinion in cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. 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
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Intermediate filaments and their associated molecules.Journal of biomedical research · 2025
    Article
  14. Article
  15. Review
  16. Article
  17. Dissecting neurofilament tail sequence-phosphorylation-structure relationships with multicomponent reconstituted protein brushes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Article
  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

4 authors.

Sherif A EldiranyDepartment of Dermatology, Yale University, New Haven, CT, 06520, USA.
Ivan B LomakinDepartment of Dermatology, Yale University, New Haven, CT, 06520, USA.
Minh HoDepartment of Dermatology, Yale University, New Haven, CT, 06520, USA.
Christopher G BunickDepartment of Dermatology, Yale University, New Haven, CT, 06520, USA; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA. Electronic address: christopher.bunick@yale.edu.

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Determining Structure and Function of Human Skin Barrier Proteins Using X-ray CrystallographyK08AR070290 · NIAMS · YALE UNIVERSITY · PI BUNICK, CHRISTOPHER GERARD · 2016 to 2020
$754k
Electron microscopy analysis of novel knob-pocket mechanism critical for intermediate filament assemblyR03AR076484 · NIAMS · YALE UNIVERSITY · PI BUNICK, CHRISTOPHER GERARD · 2020 to 2021
$165k
NCATS NIH HHS UL1 TR001863NIAMS NIH HHS K08 AR070290NIAMS NIH HHS R03 AR076484
6 · The paper itself

Abstract

Intermediate filaments (IFs) are key players in multiple cellular processes throughout human tissues. Their biochemical and structural properties are important for understanding filament assembly mechanisms, for interactions between IFs and binding partners, and for developing pharmacological agents that target IFs. IF proteins share a conserved coiled-coil central-rod domain flanked by variable N-terminal 'head' and C-terminal 'tail' domains. There have been several recent advances in our understanding of IF structure from the study of keratins, glial fibrillary acidic protein, and lamin. These include discoveries of (i) a knob-pocket tetramer assembly mechanism in coil 1B; (ii) a lamin-specific coil 1B insert providing a one-half superhelix turn; (iii) helical, yet flexible, linkers within the rod domain; and (iv) the identification of coil 2B residues required for mature filament assembly. Furthermore, the head and tail domains of some IFs contain low-complexity aromatic-rich kinked segments, and structures of IFs with binding partners show electrostatic surfaces are a major contributor to complex formation. These new data advance the connection between IF structure, pathologic mutations, and clinical diseases in humans.

Indexed as

Amino Acid SequenceAnimalsCytoskeletonHumansIntermediate Filament ProteinsIntermediate FilamentsLaminsModels, MolecularMutationIntermediate Filament ProteinsLaminsAssemblyBindingCrystallographyIntermediate filamentKeratinLaminStructureVimentin

Identifiers

PMID33190098
PMCPMC7925366

What OpenQuestion holds

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Registered trials

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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.