Evidence map›Paper›PMID 18211964›Full record

ReviewJournal of leukocyte biology2008

RNase A ribonucleases and host defense: an evolving story.

Helene F Rosenberg

Open access · greenAbstract readReview
In one paragraph

Review in Journal of leukocyte biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing 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

99 citing papers in PubMed, 179 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. The Contribution of Human Antimicrobial Peptides to Fungi.International journal of molecular sciences · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Eosinophilia in cancer and its regulation by sex hormones.Trends in endocrinology and metabolism: TEM · 2023
    Review
  16. Review
  17. Emerging biological functions of ribonuclease 1 and angiogenin.Critical reviews in biochemistry and molecular biology · 2022
    Review
  18. Article
  19. Review
  20. Article

39 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

1 author at 1 institution in 1 country.

Helene F RosenbergLaboratory of Allergic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892, USA. hrosenberg@niaid.nih.gov
National Institutes of Health · US

Funding

Eosinophils, Inflammation and ImmunityZIAAI000941 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ROSENBERG, HELENE · 2009 to 2020
$8.0M
Inflammation and Therapy for Respiratory Virus InfectionZ01AI000943 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI ROSENBERG, HELENE · 2004 to 2008
$1.6M
Biology of the Eosinophilic LeukocyteZ01AI000941 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI ROSENBERG, HELENE · 2004 to 2008
$1.6M
Ribonucleases A in Health and DiseaseZIAAI000942 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ROSENBERG, HELENE · 2009 to 2018
$1.5M
Molecular Biology of the Ribonuclease A Gene SuperfamilyZ01AI000942 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI ROSENBERG, HELENE · 2004 to 2008
$1.4M
Intramural NIH HHS Z01 AI000941Intramural NIH HHS Z01 AI000942Intramural NIH HHS Z01 AI000943
6 · The paper itself

Abstract

RNase A (bovine pancreatic RNase) is the founding member an extensive family of divergent proteins that share specific elements of sequence homology, a unique disulfide-bonded tertiary structure, and the ability to hydrolyze polymeric RNA. Among the more intriguing and perhaps counterintuitive findings, at the current state of the art, the connection between RNase activity and characterized host defense functions is quite weak; whether this is a scientific reality or more a reflection of what has been chosen for study remains to be determined. Several of the RNase A family RNases are highly cationic and have cytotoxic and bactericidal properties that are clearly (eosinophil cationic protein, leukocyte RNase A-2) or are probably (RNase 7) unrelated to their enzymatic activity. Interestingly, peptides derived from the leukocyte RNase A-2 sequence are nearly as bactericidal as the entire protein, suggesting that among other functions, the RNase A superfamily may be serving as a source of gene scaffolds for the generation of novel cytotoxic peptides. Other RNase A ribonucleases are somewhat less cationic (mouse angiogenin 4, zebrafish RNases) and have moderate bactericidal activities that have not yet been explored mechanistically. Additional host defense functions characterized specifically for the RNase eosinophil-derived neurotoxin include reducing infectivity of RNA viruses for target cells in culture, which does require RNase activity, chemoattraction of immature human dendritic cells via a G-protein-coupled receptor-dependent mechanism, and activation of TLR2. The properties of individual RNase A ribonucleases, recent experimental findings, and important questions for the near and distant future will be reviewed.

Indexed as

AnimalsCattleChickensEosinophil Cationic ProteinEosinophilsLeukocytesMammalsPancreasRana catesbeianaRibonuclease, PancreaticRibonucleasesZebrafishangiogeninEosinophil Cationic ProteinRibonuclease 7Ribonuclease, PancreaticRibonucleases

Identifiers

PMID18211964
PMCPMC2692241
OpenAlexW2056782021

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.