Evidence map›Paper›PMID 15104538›Full record

ReviewThe Biochemical journal2004

Oligomerization of bovine ribonuclease A: structural and functional features of its multimers.

Massimo Libonati, Giovanni Gotte

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Structure of angiogenin dimer bound to double-stranded RNA.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  5. Article
  6. Article
  7. NMR Characterization of Angiogenin Variants and tRNAInternational journal of molecular sciences · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Article
  19. Review
  20. Ribonuclease A suggests how proteins self-chaperone against amyloid fiber formation.Protein science : a publication of the Protein Society · 2012
    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

2 authors.

Massimo LibonatiDipartimento di Scienze Neurologiche e della Visione, Sezione di Chimica Biologica, Facoltà di Medicina e Chirurgia dell'Università di Verona, Strada Le Grazie 8, I-37134 Verona, Italy. massimo.libonati@univr.it
Giovanni Gotte

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bovine pancreatic RNase A (ribonuclease A) aggregates to form various types of catalytically active oligomers during lyophilization from aqueous acetic acid solutions. Each oligomeric species is present in at least two conformational isomers. The structures of two dimers and one of the two trimers have been solved, while plausible models have been proposed for the structures of a second trimer and two tetrameric conformers. In this review, these structures, as well as the general conditions for RNase A oligomerization, based on the well known 3D (three-dimensional) domain-swapping mechanism, are described and discussed. Attention is also focused on some functional properties of the RNase A oligomers. Their enzymic activities, particularly their ability to degrade double-stranded RNAs and polyadenylate, are summarized and discussed. The same is true for the remarkable antitumour activity of the oligomers, displayed in vitro and in vivo, in contrast with monomeric RNase A, which lacks these activities. The RNase A multimers also show an aspermatogenic action, but lack any detectable embryotoxicity. The fact that both activity against double-stranded RNA and the antitumour action increase with the size of the oligomer suggests that these activities may share a common structural requirement, such as a high number or density of positive charges present on the RNase A oligomers.

Indexed as

AnimalsBiopolymersCattleModels, MolecularProtein Structure, QuaternaryProtein Structure, TertiaryRibonuclease, PancreaticStructure-Activity RelationshipBiopolymersRibonuclease, Pancreatic

Identifiers

PMID15104538
PMCPMC1224197

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.