Evidence map›Paper›PMID 32586950›Full record

ArticleScience (New York, N.Y.)2020

Structural insight into precursor ribosomal RNA processing by ribonuclease MRP.

Pengfei Lan, Bin Zhou, Ming Tan, Shaobai Li, Mi Cao, Jian Wu, Ming Lei

Abstract read
PubMed Publisher
In one paragraph

Article in Science (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Human lncRNAProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. RNase MRP subunit composition and role in 40S ribosome biogenesis.Nature structural & molecular biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. VIRMA-mediated mScience advances · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Molecular determinants of RNase MRP specificity and function.bioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Article
  17. RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024
    Review
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Pengfei LanState Key Laboratory of Oncogenes and Related Genes, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China.ORCID 0000-0002-7654-2717
Bin ZhouState Key Laboratory of Oncogenes and Related Genes, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China.ORCID 0000-0001-5760-6298
Ming TanState Key Laboratory of Oncogenes and Related Genes, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China.
Shaobai LiState Key Laboratory of Oncogenes and Related Genes, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China.
Mi CaoState Key Laboratory of Oncogenes and Related Genes, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China.
Jian WuState Key Laboratory of Oncogenes and Related Genes, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China. leim@shsmu.edu.cn wujian@shsmu.edu.cn.ORCID 0000-0002-2072-0967
Ming LeiState Key Laboratory of Oncogenes and Related Genes, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China. leim@shsmu.edu.cn wujian@shsmu.edu.cn.ORCID 0000-0002-1153-4791
State Key Laboratory of Oncogene and Related Genes · CNShanghai Jiao Tong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribonuclease (RNase) MRP is a conserved eukaryotic ribonucleoprotein complex that plays essential roles in precursor ribosomal RNA (pre-rRNA) processing and cell cycle regulation. In contrast to RNase P, which selectively cleaves transfer RNA-like substrates, it has remained a mystery how RNase MRP recognizes its diverse substrates. To address this question, we determined cryo-electron microscopy structures of

Indexed as

Cryoelectron MicroscopyEndoribonucleasesHoloenzymesProtein ConformationRibonucleasesRibonucleoproteinsRNA, CatalyticRNA PrecursorsRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityEndoribonucleasesHoloenzymesmitochondrial RNA-processing endoribonucleasePOP4 protein, S cerevisiaeRibonucleasesRibonucleoproteinsRNA, CatalyticRNA PrecursorsRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID32586950
OpenAlexW3037095441

What OpenQuestion holds

Textmetadata
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.