Evidence map›Paper›PMID 31197198›Full record

ArticleScientific reports2019

Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities.

Hisao Masai, Rino Fukatsu, Naoko Kakusho, Yutaka Kanoh, Kenji Moriyama, Yue Ma, Keisuke Iida, Kazuo Nagasawa

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Chronic RNA G-quadruplex Accumulation in Aging and Alzheimer's Disease.bioRxiv : the preprint server for biology · 2025
    Article
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  7. Article
  8. Article
  9. Review
  10. 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

8 authors at 3 institutions in 1 country.

Hisao MasaiDepartment of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, 156-8506, Japan. masai-hs@igakuken.or.jp.
Rino FukatsuDepartment of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, 156-8506, Japan.
Naoko KakushoDepartment of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, 156-8506, Japan.
Yutaka KanohDepartment of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, 156-8506, Japan.
Kenji MoriyamaDepartment of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, 156-8506, Japan.
Yue MaDepartment of Biotechnology and Life Science, Faculty of Technology, Tokyo University of Agriculture and Technology, Tokyo, 184-8588, Japan.
Keisuke IidaMolecular Chirality Research Center, Synthetic Organic Chemistry, Department of Chemistry, Graduate School of Science, Chiba University, Chiba, 263-8522, Japan.
Kazuo NagasawaDepartment of Biotechnology and Life Science, Faculty of Technology, Tokyo University of Agriculture and Technology, Tokyo, 184-8588, Japan.
Tokyo Metropolitan Institute of Medical Science · JPTokyo University of Agriculture and Technology · JPChiba University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rif1 is a conserved protein regulating replication timing and binds preferentially to the vicinity of late-firing/dormant origins in fission yeast. The Rif1 binding sites on the fission yeast genome have an intrinsic potential to generate G-quadruplex (G4) structures to which purified Rif1 preferentially binds. We previously proposed that Rif1 generates chromatin architecture that may determine replication timing by facilitating the chromatin loop formation. Here, we conducted detailed biochemical analyses on Rif1 and its G4 binding. Rif1 prefers sequences containing long stretches of guanines and binds preferentially to the multimeric G4 of parallel or hybrid/mix topology. Rif1 forms oligomers and binds simultaneously to multiple G4. We present a model on how Rif1 may facilitate the formation of chromatin architecture through its G4 binding and oligomerization properties.

Indexed as

G-QuadruplexesProtein MultimerizationBase SequenceChromatinDNA, FungalModels, BiologicalOligonucleotidesPeptidesProtein BindingSchizosaccharomycesSchizosaccharomyces pombe ProteinsTelomereTelomere-Binding ProteinsChromatinDNA, FungalOligonucleotidesPeptidesRif1 protein, S pombeSchizosaccharomyces pombe ProteinsTelomere-Binding Proteins

Identifiers

PMID31197198
PMCPMC6565636
OpenAlexW2951051592

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.