Evidence map›Paper›PMID 34511335›Full record

ReviewTrends in biochemical sciences2021

The many faces of RNA-based RNase P, an RNA-world relic.

Hong-Duc Phan, Lien B Lai, Walter J Zahurancik, Venkat Gopalan

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

41 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Resurrecting the Activity of the RNA Subunit of Human RNase P.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Article
  4. Article
  5. Coevolution of RNase P and the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  7. Unlocking the role of tRNA-derived fragments in shaping breast cancer signaling.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Roles of tRNA-Derived Fragments in Cancer: Updates and Perspectives.International journal of molecular sciences · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Divergent molecular assembly and catalytic mechanisms between bacterial and archaeal RNase P in pre-tRNA cleavage.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  20. Suppression of theRNA (New York, N.Y.) · 2024
    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

4 authors at 1 institution in 1 country.

Hong-Duc PhanDepartment of Chemistry & Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA; Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA.
Lien B LaiDepartment of Chemistry & Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA. Electronic address: lai.104@osu.edu.
Walter J ZahurancikDepartment of Chemistry & Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Venkat GopalanDepartment of Chemistry & Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA; Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. Electronic address: gopalan.5@osu.edu.
The Ohio State University · US

Funding

Dissecting functional cooperation among subunits in a catalytic ribonucleoproteinR01GM120582 · NIGMS · OHIO STATE UNIVERSITY · PI GOPALAN, VENKAT · 2016 to 2019
$1.9M
NIGMS NIH HHS R01 GM120582
6 · The paper itself

Abstract

RNase P is an essential enzyme that catalyzes removal of the 5' leader from precursor transfer RNAs. The ribonucleoprotein (RNP) form of RNase P is present in all domains of life and comprises a single catalytic RNA (ribozyme) and a variable number of protein cofactors. Recent cryo-electron microscopy structures of representative archaeal and eukaryotic (nuclear) RNase P holoenzymes bound to tRNA substrate/product provide high-resolution detail on subunit organization, topology, and substrate recognition in these large, multisubunit catalytic RNPs. These structures point to the challenges in understanding how proteins modulate the RNA functional repertoire and how the structure of an ancient RNA-based catalyst was reshaped during evolution by new macromolecular associations that were likely necessitated by functional/regulatory coupling.

Indexed as

Ribonuclease PRNA, CatalyticCryoelectron MicroscopyNucleic Acid ConformationRNARNA, TransferRibonuclease PRNARNA, CatalyticRNA, Transfercatalytic ribonucleoproteinprotein-aided RNA catalysisribozymetRNA processing

Identifiers

PMID34511335
PMCPMC8595784
OpenAlexW3200958780

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.