Evidence map›Paper›PMID 19844921›Full record

ReviewJournal of cellular biochemistry2009

Broadening the mission of an RNA enzyme.

Michael C Marvin, David R Engelke

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 41 citations in OpenAlex.

  1. Coevolution of RNase P and the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Molecular recognition of pre-tRNA byRNA (New York, N.Y.) · 2017
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Michael C MarvinDepartment of Biological Chemistry, University of Michigan School of Medicine, Ann Arbor, Michigan 48109-0606, USA.
David R Engelke
University of Michigan–Ann Arbor · US

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
EUKARYOTIC TRNA MATURATIONR01GM034869 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ENGELKE, DAVID R · 1985 to 2006
$2.3M
Nuclear Organization of RNA Polymerase III TranscriptionR01GM082875 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ENGELKE, DAVID R · 2008 to 2011
$1.4M
NIGMS NIH HHS GM034869NIGMS NIH HHS R01 GM034869NIGMS NIH HHS R01 GM082875NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32-GM08353NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

The "RNA World" hypothesis suggests that life developed from RNA enzymes termed ribozymes, which carry out reactions without assistance from proteins. Ribonuclease (RNase) P is one ribozyme that appears to have adapted these origins to modern cellular life by adding protein to the RNA core in order to broaden the potential functions. This RNA-protein complex plays diverse roles in processing RNA, but its best-understood reaction is pre-tRNA maturation, resulting in mature 5' ends of tRNAs. The core catalytic activity resides in the RNA subunit of almost all RNase P enzymes but broader substrate tolerance is required for recognizing not only the diverse sequences of tRNAs, but also additional cellular RNA substrates. This broader substrate tolerance is provided by the addition of protein to the RNA core and allows RNase P to selectively recognize different RNAs, and possibly ribonucleoprotein (RNP) substrates. Thus, increased protein content correlated with evolution from bacteria to eukaryotes has further enhanced substrate potential enabling the enzyme to function in a complex cellular environment.

Indexed as

Base SequenceBinding SitesEukaryotaKineticsModels, MolecularMolecular Sequence DataNucleic Acid ConformationRibonuclease PRNARNA, BacterialRNA, CatalyticRNA, TransferSubstrate SpecificityRibonuclease PRNARNA, BacterialRNA, CatalyticRNA, Transfer

Identifiers

PMID19844921
PMCPMC2800852
OpenAlexW1996784759

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.