Evidence map›Paper›PMID 30607510›Full record

ArticleChromosoma2019

Molecular structure of human synaptonemal complex protein SYCE1.

Orla M Dunne, Owen R Davies

Open access · hybridAbstract read
In one paragraph

Article in Chromosoma, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 49 citations in OpenAlex.

  1. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. A suppressor screenProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Review
  7. Article
  8. A suppressor screenbioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Alterations in synaptonemal complex coding genes and human infertility.International journal of biological sciences · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. ZYP1 is required for obligate cross-over formation and cross-over interference inProceedings of the National Academy of Sciences of the United States of America · 2021
    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

2 authors at 1 institution in 1 country.

Orla M DunneInstitute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK.
Owen R DaviesInstitute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK. owen.davies@newcastle.ac.uk.ORCID 0000-0002-3806-5403
Newcastle University · GB

Funding

Wellcome TrustWellcome Trust 104158/Z/14/Z
6 · The paper itself

Abstract

The reduction in chromosome number during meiosis is essential for the production of haploid germ cells and thereby fertility. To achieve this, homologous chromosomes are first synapsed together by a protein assembly, the synaptonemal complex (SC), which permits genetic exchange by crossing over and the subsequent accurate segregation of homologues. The mammalian SC is formed of a zipper-like array of SYCP1 molecules that bind together homologous chromosomes through self-assembly in the midline that is structurally supported by the central element. The SC central element contains five proteins-SYCE1, SYCE3, SIX6OS1, and SYCE2-TEX12-that permit SYCP1 assembly to extend along the chromosome length to achieve full synapsis. Here, we report the structure of human SYCE1 through solution biophysical methods including multi-angle light scattering and small-angle X-ray scattering. The structural core of SYCE1 is formed by amino acids 25-179, within the N-terminal half of the protein, which mediates SYCE1 dimerization. This α-helical core adopts a curved coiled-coil structure of 20-nm length in which the two chains are arranged in an anti-parallel configuration. This structure is retained within full-length SYCE1, in which long C-termini adopt extended conformations to achieve an elongated molecule of over 50 nm in length. The SYCE1 structure is compatible with it functioning as a physical strut that tethers other components to achieve structural stability of the SC central element.

Indexed as

MeiosisCell Cycle ProteinsDNA-Binding ProteinsDNA Breaks, Double-StrandedHumansProtein ConformationScattering, Small AngleSynaptonemal ComplexX-Ray DiffractionCell Cycle ProteinsDNA-Binding ProteinsSYCP1 protein, humanTEX12 protein, humanBiophysicsCentral elementChiasmataChromosome structureDouble-strand breakMeiosisSmall-angle X-ray scatteringSYCE1Synaptonemal complex

Identifiers

PMID30607510
PMCPMC6823292
OpenAlexW2907705775

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.