Evidence map›Paper›PMID 17438295›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Molecular basis of coiled-coil formation.

Michel O Steinmetz, Ilian Jelesarov, William M Matousek, Srinivas Honnappa, Wolfgang Jahnke, John H Missimer, Sabine Frank, Andrei T Alexandrescu, Richard A Kammerer

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.Journal of the American Chemical Society · 2026
    Article
  2. Article
  3. High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.bioRxiv : the preprint server for biology · 2026
    Article
  4. Sudden Death-AssociatedbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Structural Basis for Plant MADS Transcription Factor Oligomerization.Computational and structural biotechnology journal · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. An Effective Strategy for Stabilizing Minimal Coiled Coil Mimetics.Journal of the American Chemical Society · 2015
    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

9 authors.

Michel O SteinmetzBiomolecular Research, Structural Biology, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland. michel.steinmetz@psi.ch
Ilian Jelesarov
William M Matousek
Srinivas Honnappa
Wolfgang Jahnke
John H Missimer
Sabine Frank
Andrei T Alexandrescu
Richard A Kammerer

Funding

Wellcome Trust
6 · The paper itself

Abstract

Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed "trigger sequence," that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation.

Indexed as

Leucine ZippersAmino Acid SubstitutionArginineBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsHydrogen-Ion ConcentrationKineticsMagnetic Resonance SpectroscopyMutant ProteinsPeptidesProtein FoldingSaccharomyces cerevisiae ProteinsSolutionsThermodynamicsTranscription FactorsArginineBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsGCN4 protein, S cerevisiaeMutant ProteinsPeptidesSaccharomyces cerevisiae ProteinsSolutionsTranscription Factors

Identifiers

PMID17438295
PMCPMC1855353

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.