Evidence map›Paper›PMID 16595295›Full record

ArticleCritical reviews in biochemistry and molecular biology

Ribonuclease P: the evolution of an ancient RNA enzyme.

Scott C Walker, David R Engelke

Open access · greenAbstract read
In one paragraph

Article in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
8.3field-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

100 citing papers in PubMed, 185 citations in OpenAlex.

  1. Article
  2. Article
  3. Coevolution of RNase P and the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. From peptides to DNA: All required steps can be catalyzed.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Therapeutic promise of engineered nonsense suppressor tRNAs.Wiley interdisciplinary reviews. RNA · 2021
    Review
  17. Article
  18. Article
  19. Article
  20. Article

40 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

2 authors at 1 institution in 1 country.

Scott C WalkerDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA.
David R Engelke
University of Michigan · US

Funding

EUKARYOTIC TRNA MATURATIONR01GM034869 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ENGELKE, DAVID R · 1985 to 2006
$2.3M
NIGMS NIH HHS GM 34869NIGMS NIH HHS R01 GM034869
6 · The paper itself

Abstract

Ribonuclease P (RNase P) is an ancient and essential endonuclease that catalyses the cleavage of the 5' leader sequence from precursor tRNAs (pre-tRNAs). The enzyme is one of only two ribozymes which can be found in all kingdoms of life (Bacteria, Archaea, and Eukarya). Most forms of RNase P are ribonucleoproteins; the bacterial enzyme possesses a single catalytic RNA and one small protein. However, in archaea and eukarya the enzyme has evolved an increasingly more complex protein composition, whilst retaining a structurally related RNA subunit. The reasons for this additional complexity are not currently understood. Furthermore, the eukaryotic RNase P has evolved into several different enzymes including a nuclear activity, organellar activities, and the evolution of a distinct but closely related enzyme, RNase MRP, which has different substrate specificities, primarily involved in ribosomal RNA biogenesis. Here we examine the relationship between the bacterial and archaeal RNase P with the eukaryotic enzyme, and summarize recent progress in characterizing the archaeal enzyme. We review current information regarding the nuclear RNase P and RNase MRP enzymes in the eukaryotes, focusing on the relationship between these enzymes by examining their composition, structure and functions.

Indexed as

Evolution, MolecularAnimalsBase SequenceHumansModels, BiologicalMolecular Sequence DataNucleic Acid ConformationProtein BindingRibonuclease PRibonucleoproteinsRNA PrecursorsSubstrate SpecificityRibonuclease PRibonucleoproteinsRNA Precursors

Identifiers

PMID16595295
PMCPMC2803672
OpenAlexW2133173870

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.