Evidence map›Paper›PMID 28495858›Full record

ArticleThe Biochemical journal2017

Comparative functional analysis of ribonuclease 1 homologs: molecular insights into evolving vertebrate physiology.

Jo E Lomax, Chelcie H Eller, Ronald T Raines

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

  1. Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Ribonuclease 1 Induces T-Cell Dysfunction and Impairs CD8Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Emerging biological functions of ribonuclease 1 and angiogenin.Critical reviews in biochemistry and molecular biology · 2022
    Review
  11. Structure-Based Design of an RNase Chimera for Antimicrobial Therapy.International journal of molecular sciences · 2021
    Article
  12. Article
  13. Semisynthesis of Human Ribonuclease-S.Bioconjugate chemistry · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Endothelial Ribonuclease 1 in Cardiovascular and Systemic Inflammation.Frontiers in cell and developmental biology · 2020
    Review
  18. Review
  19. Article
  20. Article
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

3 authors at 2 institutions in 1 country.

Jo E LomaxGraduate Program in Cell and Molecular Biology, University of Wisconsin-Madison, 1525 Linden Drive, Madison, WI, U.S.A.
Chelcie H EllerDepartment of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI, U.S.A.
Ronald T RainesDepartment of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI, U.S.A. rtraines@wisc.edu.
University of Wisconsin–Madison · USUniversity of Wisconsin System · US

Funding

TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
RIBONUCLEASES IN CANCER THERAPYR01CA073808 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI RAINES, RONALD T · 1997 to 2024
$7.3M
NCI NIH HHS R01 CA073808NIGMS NIH HHS P41 GM103399
6 · The paper itself

Abstract

Pancreatic-type ribonucleases (ptRNases) comprise a class of highly conserved secretory endoribonucleases in vertebrates. The prototype of this enzyme family is ribonuclease 1 (RNase 1). Understanding the physiological roles of RNase 1 is becoming increasingly important, as engineered forms of the enzyme progress through clinical trials as chemotherapeutic agents for cancer. Here, we present an in-depth biochemical characterization of RNase 1 homologs from a broad range of mammals (human, bat, squirrel, horse, cat, mouse, and cow) and nonmammalian species (chicken, lizard, and frog). We discover that the human homolog of RNase 1 has a pH optimum for catalysis, ability to degrade double-stranded RNA, and affinity for cell-surface glycans that are distinctly higher than those of its homologs. These attributes have relevance for human health. Moreover, the functional diversification of the 10 RNase 1 homologs illuminates the regulation of extracellular RNA and other aspects of vertebrate evolution.

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsCatsCattleChickensHorsesHumansMicePhylogenyRanidaeRibonucleasesRNASequence Homology, Amino AcidVertebratesRibonucleasesRNAenzyme activityenzymologymolecular evolutionprotein structureribonucleaseRNA

Identifiers

PMID28495858
PMCPMC5660862
OpenAlexW2612978844

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.