Evidence map›Paper›PMID 29290403›Full record

ReviewTrends in genetics : TIG2018

Zipping and Unzipping: Protein Modifications Regulating Synaptonemal Complex Dynamics.

Jinmin Gao, Monica P Colaiácovo

Open access · greenAbstract readReview
In one paragraph

Review in Trends in genetics : TIG, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.5field-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

77 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
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  3. Review
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  9. Article
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  13. Histone H3 tail modifications required for meiosis inbioRxiv : the preprint server for biology · 2024
    Article
  14. Article
  15. Article
  16. Make it or break it: Protein homeostasis in the synaptonemal complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Review

17 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

2 authors at 2 institutions in 2 countries.

Jinmin GaoInstitute of Biomedical Sciences, College of Life Sciences, Key Laboratory of Animal Resistance Biology of Shandong Province, Shandong Normal University, Jinan, Shandong, 250014, China; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
Monica P ColaiácovoDepartment of Genetics, Harvard Medical School, Boston, MA 02115, USA. Electronic address: mcolaiacovo@genetics.med.harvard.edu.
Harvard University · USShandong Normal University · CN

Funding

Synaptonemal Complex Assembly and Function in MeiosisR01GM072551 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Monica P Colaiacovo · 2005 to 2026
$7.5M
NIGMS NIH HHS R01 GM072551
6 · The paper itself

Abstract

The proteinaceous zipper-like structure known as the synaptonemal complex (SC), which forms between pairs of homologous chromosomes during meiosis from yeast to humans, plays important roles in promoting interhomolog crossover formation, regulating cessation of DNA double-strand break (DSB) formation following crossover designation, and ensuring accurate meiotic chromosome segregation. Recent studies are starting to reveal critical roles for different protein modifications in regulating SC dynamics. Protein SUMOylation, N-terminal acetylation, and phosphorylation have been shown to be essential for the regulated assembly and disassembly of the SC. Moreover, phosphorylation of specific SC components has been found to link changes in SC dynamics with meiotic recombination. This review highlights the latest findings on how protein modifications regulate SC dynamics and functions.

Indexed as

DNA Breaks, Double-StrandedProtein Processing, Post-TranslationalAnimalsChromosome SegregationCrossing Over, GeneticHumansModels, GeneticSaccharomyces cerevisiaeSynaptonemal Complexmeiosismeiotic recombinationN-terminal acetylationphosphorylationSUMOylationsynaptonemal complex

Identifiers

PMID29290403
PMCPMC5834363
OpenAlexW2778308097

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.