Evidence map›Paper›PMID 19931535›Full record

ReviewFEBS letters2010

Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects.

Lien B Lai, Agustín Vioque, Leif A Kirsebom, Venkat Gopalan

Open access · bronzeAbstract readComparative StudyReview
In one paragraph

Review in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
5.1field-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

84 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Article
  3. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Suppression of theRNA (New York, N.Y.) · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structural basis for impaired 5' processing of a mutant tRNA associated with defects in neuronal homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. The many faces of RNA-based RNase P, an RNA-world relic.Trends in biochemical sciences · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

24 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

4 authors at 3 institutions in 3 countries.

Lien B LaiDepartment of Biochemistry and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Agustín Vioque
Leif A Kirsebom
Venkat Gopalan
The Ohio State University · USInstituto de Bioquímica Vegetal y Fotosíntesis · ESUppsala University · SE

Funding

Structure and Function in Catalytic RNP AssemblyR01GM067807 · NIGMS · OHIO STATE UNIVERSITY · PI FOSTER, MARK P. · 2004 to 2009
$1.7M
Catalytic inactivation of miRNA function by customized RNase P-based ribozymesR21AI082242 · NIAID · OHIO STATE UNIVERSITY · PI GOPALAN, VENKAT, SCHOENBERG, DANIEL R. · 2009 to 2010
$495k
Spatiotemporal Regulation of Brain RNase P as a Basis for Neurological DisordersR21NS096600 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ACKERMAN, SUSAN L, GOPALAN, VENKAT · 2016 to 2017
$439k
NIAID NIH HHS AI082242NIAID NIH HHS R21 AI082242NIGMS NIH HHS GM067807NIGMS NIH HHS R01 GM067807
6 · The paper itself

Abstract

For an enzyme functioning predominantly in a seemingly housekeeping role of 5' tRNA maturation, RNase P displays a remarkable diversity in subunit make-up across the three domains of life. Despite the protein complexity of this ribonucleoprotein enzyme increasing dramatically from bacteria to eukarya, the catalytic function rests with the RNA subunit during evolution. However, the recent demonstration of a protein-only human mitochondrial RNase P has added further intrigue to the compositional variability of this enzyme. In this review, we discuss some possible reasons underlying the structural diversity of the active sites, and use them as thematic bases for elaborating new directions to understand how functional variations might have contributed to the complex evolution of RNase P.

Indexed as

ArchaeaBacteriaCatalysisEukaryotaOrganellesRibonuclease PSubstrate SpecificityRibonuclease P

Identifiers

PMID19931535
PMCPMC2799185
OpenAlexW2013039688

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.