Evidence map›Paper›PMID 19228196›Full record

ReviewThe FEBS journal2009

Ribonuclease H: the enzymes in eukaryotes.

Susana M Cerritelli, Robert J Crouch

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 500 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
500citing papers in PubMed, 1 pooled it
11.4field-weighted citation impact, top 1% 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

500 citing papers in PubMed, 1 synthesis or guideline pooled it, 821 citations in OpenAlex.

  1. Synthetic lethal mutants inJournal of bacteriology · 2023
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Ribonucleotide errors, RNase HII, and ribonucleotide excision repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. RNA-Based Therapies for Inherited Metabolic Disorders.Journal of inherited metabolic disease · 2026
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. NAR molecular medicine · 2026
    Article

440 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.

Susana M CerritelliProgram in Genomics of Differentiation, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Robert J Crouch
Eunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Factors Influencing Genetic Transcription Initiation And TerminationZIAHD000068 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI CROUCH, ROBERT J · 2009 to 2025
$22.0M
FACTORS INFLUENCING GENETIC TRANSCRIPTION-INITIATION AND TERMINATIONZ01HD000068 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI CROUCH, ROBERT J · 1985 to 2008
$2.2M
Intramural NIH HHS Z01 HD000068
6 · The paper itself

Abstract

Ribonucleases H are enzymes that cleave the RNA of RNA/DNA hybrids that form during replication and repair and which could lead to DNA instability if they were not processed. There are two main types of RNase H, and at least one of them is present in most organisms. Eukaryotic RNases H are larger and more complex than their prokaryotic counterparts. Eukaryotic RNase H1 has acquired a hybrid binding domain that confers processivity and affinity for the substrate, whereas eukaryotic RNase H2 is composed of three different proteins: the catalytic subunit (2A), similar to the monomeric prokaryotic RNase HII, and two other subunits (2B and 2C) that have no prokaryotic counterparts and as yet unknown functions, but that are necessary for catalysis. In this minireview, we discuss some of the most recent findings on eukaryotic RNases H1 and H2, focusing on the structural data on complexes between human RNase H1 and RNA/DNA hybrids that had provided great detail of how the hybrid binding- and RNase H-domains recognize and cleave the RNA strand of the hybrid substrates. We also describe the progress made in understanding the in vivo function of eukaryotic RNases H. Although prokayotes and some single-cell eukaryotes do not require RNases H for viability, in higher eukaryotes RNases H are essential. Rnaseh1 null mice arrest development around E8.5 because RNase H1 is necessary during embryogenesis for mitochondrial DNA replication. Mutations in any of the three subunits of human RNase H2 cause Aicardi-Goutières syndrome, a human neurological disorder with devastating consequences.

Indexed as

Amino Acid SequenceAnimalsHumansMiceMitochondriaMolecular Sequence DataProtein ConformationRibonuclease HSaccharomyces cerevisiaeSequence Homology, Amino AcidSubstrate SpecificityRibonuclease H

Identifiers

PMID19228196
PMCPMC2746905
OpenAlexW1557728494

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.