Evidence map›Paper›PMID 25078100›Full record

ArticleThe Journal of biological chemistry2014

Bovine brain ribonuclease is the functional homolog of human ribonuclease 1.

Chelcie H Eller, Jo E Lomax, Ronald T Raines

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Emerging biological functions of ribonuclease 1 and angiogenin.Critical reviews in biochemistry and molecular biology · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Semisynthesis of Human Ribonuclease-S.Bioconjugate chemistry · 2021
    Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Circular zymogens of human ribonuclease 1.Protein science : a publication of the Protein Society · 2019
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  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.

Chelcie H EllerDepartments of Biochemistry and University of Wisconsin, Madison, Wisconsin 53706.
Jo E LomaxGraduate Program in Cellular and Molecular Biology, University of Wisconsin, Madison, Wisconsin 53706.
Ronald T RainesDepartments of Biochemistry and University of Wisconsin, Madison, Wisconsin 53706; Departments of Chemistry, and University of Wisconsin, Madison, Wisconsin 53706. Electronic address: rtraines@wisc.edu.

Funding

RIBONUCLEASES IN CANCER THERAPYR01CA073808 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI RAINES, RONALD T · 1997 to 2024
$7.3M
NCI NIH HHS R01 CA073808
6 · The paper itself

Abstract

Mounting evidence suggests that human pancreatic ribonuclease (RNase 1) plays important roles in vivo, ranging from regulating blood clotting and inflammation to directly counteracting tumorigenic cells. Understanding these putative roles has been pursued with continual comparisons of human RNase 1 to bovine RNase A, an enzyme that appears to function primarily in the ruminant gut. Our results imply a different physiology for human RNase 1. We demonstrate distinct functional differences between human RNase 1 and bovine RNase A. Moreover, we characterize another RNase 1 homolog, bovine brain ribonuclease, and find pronounced similarities between that enzyme and human RNase 1. We report that human RNase 1 and bovine brain ribonuclease share high catalytic activity against double-stranded RNA substrates, a rare quality among ribonucleases. Both human RNase 1 and bovine brain RNase are readily endocytosed by mammalian cells, aided by tight interactions with cell surface glycans. Finally, we show that both human RNase 1 and bovine brain RNase are secreted from endothelial cells in a regulated manner, implying a potential role in vascular homeostasis. Our results suggest that brain ribonuclease, not RNase A, is the true bovine homolog of human RNase 1, and provide fundamental insight into the ancestral roles and functional adaptations of RNase 1 in mammals.

Indexed as

AnimalsBrainCattleCells, CulturedHumansHuman Umbilical Vein Endothelial CellsHydrogen-Ion ConcentrationKineticsLiposomesProtein BindingProtein TransportRibonuclease, PancreaticRNA, Double-StrandedRNA StabilityLiposomesRibonuclease, PancreaticRNA, Double-StrandedDouble-stranded RNA (dsRNA)Enzyme CatalysisHeparin-binding ProteinRibonucleaseRNA

Identifiers

PMID25078100
PMCPMC4176206

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.