Evidence map›Paper›PMID 11889032›Full record

ArticleThe EMBO journal2002

Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly.

Sergei V Strelkov, Harald Herrmann, Norbert Geisler, Tatjana Wedig, Ralf Zimbelmann, Ueli Aebi, Peter Burkhard

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

105 citing papers in PubMed, 294 citations in OpenAlex.

  1. Trial
  2. Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026
    Article
  3. Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 2026
    Article
  4. Article
  5. Article
  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. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Filament assembly of theNucleus (Austin, Tex.) · 2022
    Article
  18. Stability profile of vimentin rod domain.Protein science : a publication of the Protein Society · 2022
    Article
  19. Article
  20. Article

45 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

7 authors at 4 institutions in 2 countries.

Sergei V StrelkovMaurice E.Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. sergei-v.strelkov@unibas.ch
Harald Herrmann
Norbert Geisler
Tatjana Wedig
Ralf Zimbelmann
Ueli Aebi
Peter Burkhard
University of Basel · CHGerman Cancer Research Center · DEHeidelberg University · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intermediate filaments (IFs) are key components of the cytoskeleton in higher eukaryotic cells. The elementary IF 'building block' is an elongated coiled-coil dimer consisting of four consecutive alpha-helical segments. The segments 1A and 2B include highly conserved sequences and are critically involved in IF assembly. Based on the crystal structures of three human vimentin fragments at 1.4-2.3 A resolution (PDB entries 1gk4, 1gk6 and 1gk7), we have established the molecular organization of these two segments. The fragment corresponding to segment 1A forms a single, amphipatic alpha-helix, which is compatible with a coiled-coil geometry. While this segment might yield a coiled coil within an isolated dimer, monomeric 1A helices are likely to play a role in specific dimer-dimer interactions during IF assembly. The 2B segment reveals a double-stranded coiled coil, which unwinds near residue Phe351 to accommodate a 'stutter'. A fragment containing the last seven heptads of 2B interferes heavily with IF assembly and also transforms mature vimentin filaments into a new kind of structure. These results provide the first insight into the architecture and functioning of IFs at the atomic level.

Indexed as

Conserved SequenceAmino Acid SequenceCrystallography, X-RayDimerizationHumansIntermediate FilamentsModels, MolecularMolecular Sequence DataProtein Structure, SecondarySequence Homology, Amino AcidVimentinVimentin

Identifiers

PMID11889032
PMCPMC125921
OpenAlexW2033452569

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.