Evidence map›Paper›PMID 29093720›Full record

ReviewFrontiers in plant science2017

MORC Proteins: Novel Players in Plant and Animal Health.

Aline Koch, Hong-Gu Kang, Jens Steinbrenner, D'Maris A Dempsey, Daniel F Klessig, Karl-Heinz Kogel

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in plant science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
10.1field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  7. Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. ThemSphere · 2024
    Article
  9. Review
  10. AeLife · 2024
    Article
  11. Article
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  13. Morc1 reestablishes H3K9me3 heterochromatin on piRNA-targeted transposons in gonocytes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Review
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  17. DNA polymerase epsilon binds histone H3.1-H4 and recruits MORC1 to mediate meiotic heterochromatin condensation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Review
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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

6 authors at 3 institutions in 2 countries.

Aline KochCentre for BioSystems, Land Use and Nutrition, Institute for Phytopathology, Justus Liebig University Giessen, Giessen, Germany.
Hong-Gu KangDepartment of Biology, Texas State University, San Marcos, TX, United States.
Jens SteinbrennerCentre for BioSystems, Land Use and Nutrition, Institute for Phytopathology, Justus Liebig University Giessen, Giessen, Germany.
D'Maris A DempseyBoyce Thompson Institute for Plant Research, Ithaca, NY, United States.
Daniel F KlessigBoyce Thompson Institute for Plant Research, Ithaca, NY, United States.
Karl-Heinz KogelCentre for BioSystems, Land Use and Nutrition, Institute for Phytopathology, Justus Liebig University Giessen, Giessen, Germany.
University of Giessen · DECornell University · USTexas State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microrchidia (MORC) proteins comprise a family of proteins that have been identified in prokaryotes and eukaryotes. They are defined by two hallmark domains: a GHKL-type ATPase and an S5 fold. MORC proteins in plants were first discovered via a genetic screen for Arabidopsis mutants compromised for resistance to a viral pathogen. Subsequent studies expanded their role in plant immunity and revealed their involvement in gene silencing and transposable element repression. Emerging data suggest that MORC proteins also participate in pathogen-induced chromatin remodeling and epigenetic gene regulation. In addition, biochemical analyses recently demonstrated that plant MORCs have topoisomerase II (topo II)-like DNA modifying activities that may be important for their function. Interestingly, animal MORC proteins exhibit many parallels with their plant counterparts, as they have been implicated in disease development and gene silencing. In addition, human MORCs, like plant MORCs, bind salicylic acid and this inhibits some of their topo II-like activities. In this review, we will focus primarily on plant MORCs, although relevant comparisons with animal MORCs will be provided.

Indexed as

human MORCsimmunitypathogenplant MORCsRNA-directed DNA methylationRNA interference (RNAi)transcriptional gene silencing

Identifiers

PMID29093720
PMCPMC5651269
OpenAlexW2765516885

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.