Evidence map›Paper›PMID 28101860›Full record

ReviewSub-cellular biochemistry2017

The Structure and Topology of α-Helical Coiled Coils.

Andrei N Lupas, Jens Bassler, Stanislaw Dunin-Horkawicz

Open access · greenAbstract readReview
In one paragraph

Review in Sub-cellular biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
20.6field-weighted citation impact, top 1% 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

59 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026
    Article
  3. Fusion protein condensate formation via coiled-coil domains.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Resolving the structure and assembly of the honeybee silk heterotetrameric coiled coil.Protein science : a publication of the Protein Society · 2025
    Article
  13. Article
  14. Article
  15. Helical substructures of 4D constructions that determine the structure of α-helices.Acta crystallographica. Section A, Foundations and advances · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 2 countries.

Andrei N LupasDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, 72076, Tübingen, Germany. andrei.lupas@tuebingen.mpg.de.
Jens BasslerDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, 72076, Tübingen, Germany.
Stanislaw Dunin-HorkawiczStructural Bioinformatics Laboratory, Centre of New Technologies, University of Warsaw, 02-097, Warsaw, Poland.
Max Planck Institute for Developmental Biology · DEUniversity of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Helical coiled coils constitute one of the most diverse folds yet described. They range in length over two orders of magnitude; they form rods, segmented ropes, barrels, funnels, sheets, spirals, and rings, which encompass anywhere from two to more than 20 helices in parallel or antiparallel orientation; they assume different helix crossing angles, degrees of supercoiling, and packing geometries. This structural diversity supports a wide range of biological functions, allowing them to form mechanically rigid structures, provide levers for molecular motors, project domains across large distances, mediate oligomerization, transduce conformational changes and facilitate the transport of other molecules. Unlike almost any other protein fold known to us, their structure can be computed from parametric equations, making them an ideal model system for rational protein design. Here we outline the principles by which coiled coils are structured, review the determinants of their folding and stability, and present an overview of their diverse architectures.

Indexed as

Protein Conformation, alpha-HelicalAmino Acid SequenceAnimalsHumansModels, MolecularProtein FoldingProteinsProtein StabilityProteins

Identifiers

PMID28101860
PMCPMC7122542
OpenAlexW2575569425

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.