Evidence map›Paper›PMID 29915389›Full record

ArticleNature structural & molecular biology2018

Structural basis of meiotic chromosome synapsis through SYCP1 self-assembly.

James M Dunce, Orla M Dunne, Matthew Ratcliff, Claudia Millán, Suzanne Madgwick, Isabel Usón, Owen R Davies

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

50 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
  5. Article
  6. The DNA mismatch repair protein Msh4 is essential for meiosis of male but not for female in zebrafish.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024
    Review
  14. A suppressor screenProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. A suppressor screenbioRxiv : the preprint server for biology · 2023
    Article
  17. Review
  18. Review
  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

7 authors at 4 institutions in 2 countries.

James M DunceInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.ORCID 0000-0002-5771-5600
Orla M DunneInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Matthew RatcliffInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Claudia MillánCrystallographic Methods, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Barcelona, Spain.ORCID 0000-0002-9283-2220
Suzanne MadgwickInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Isabel UsónCrystallographic Methods, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Barcelona, Spain.
Owen R DaviesInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK. owen.davies@newcastle.ac.uk.ORCID 0000-0002-3806-5403
Newcastle University · GBInstitució Catalana de Recerca i Estudis Avançats · ESInstitut de Biologia Molecular de Barcelona · ESUniversity of Cambridge · GB

Funding

Wellcome Trust 100088Wellcome Trust 104158
6 · The paper itself

Abstract

Meiotic chromosomes adopt unique structures in which linear arrays of chromatin loops are bound together in homologous chromosome pairs by a supramolecular protein assembly, the synaptonemal complex. This three-dimensional scaffold provides the essential structural framework for genetic exchange by crossing over and subsequent homolog segregation. The core architecture of the synaptonemal complex is provided by SYCP1. Here we report the structure and self-assembly mechanism of human SYCP1 through X-ray crystallographic and biophysical studies. SYCP1 has an obligate tetrameric structure in which an N-terminal four-helical bundle bifurcates into two elongated C-terminal dimeric coiled-coils. This building block assembles into a zipper-like lattice through two self-assembly sites. N-terminal sites undergo cooperative head-to-head assembly in the midline, while C-terminal sites interact back to back on the chromosome axis. Our work reveals the underlying molecular structure of the synaptonemal complex in which SYCP1 self-assembly generates a supramolecular lattice that mediates meiotic chromosome synapsis.

Indexed as

Biophysical PhenomenaChromosome PairingCrystallography, X-RayDNA-Binding ProteinsHumansMeiosisModels, MolecularNuclear ProteinsProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryStatic ElectricitySynaptonemal ComplexDNA-Binding ProteinsNuclear ProteinsSYCP1 protein, human

Identifiers

PMID29915389
PMCPMC6606445
OpenAlexW2805389181

What OpenQuestion holds

Textmetadata
LicenceTDM
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.