Evidence map›Paper›PMID 38393149›Full record

ArticleToxins2024

Viper Venom Phospholipase A2 Database: The Structural and Functional Anatomy of a Primary Toxin in Envenomation.

Ana L Novo de Oliveira, Miguel T Lacerda, Maria J Ramos, Pedro A Fernandes

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Toxins, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
9.9field-weighted citation impact, top 2% 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

20 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Crystal structure and functional characterization of an Asp49 phospholipase AActa crystallographica. Section F, Structural biology communications · 2026
    Article
  5. Article
  6. Article
  7. Snake Venom PLAToxins · 2025
    Review
  8. Phospholipases ABiomolecules · 2025
    Review
  9. Article
  10. Article
  11. Computational Strategies for Broad Spectrum Venom Phospholipase AJournal of chemical information and modeling · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Epitope-based antibody development against metalloproteinases and phospholipases AThe journal of venomous animals and toxins including tropical diseases · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Ana L Novo de OliveiraRequimte-Faculty of Sciences, University of Porto, Rua do Campo Alegre s/n, 4169-000 Porto, Portugal.ORCID 0000-0001-6594-6022
Miguel T LacerdaRequimte-Faculty of Sciences, University of Porto, Rua do Campo Alegre s/n, 4169-000 Porto, Portugal.
Maria J RamosRequimte-Faculty of Sciences, University of Porto, Rua do Campo Alegre s/n, 4169-000 Porto, Portugal.
Pedro A FernandesRequimte-Faculty of Sciences, University of Porto, Rua do Campo Alegre s/n, 4169-000 Porto, Portugal.ORCID 0000-0003-2748-4722
Universidade do Porto · PT

Funding

Fundação para a Ciência e Tecnologia PTDC/QUI-OUT/1401/202
6 · The paper itself

Abstract

Viper venom phospholipase A2 enzymes (vvPLA2s) and phospholipase A2-like (PLA2-like) proteins are two of the principal toxins in viper venom that are responsible for the severe myotoxic and neurotoxic effects caused by snakebite envenoming, among other pathologies. As snakebite envenoming is the deadliest neglected tropical disease, a complete understanding of these proteins' properties and their mechanisms of action is urgently needed. Therefore, we created a database comprising information on the holo-form, cofactor-bound 3D structure of 217 vvPLA2 and PLA2-like proteins in their physiologic environment, as well as 79 membrane-bound viper species from 24 genera, which we have made available to the scientific community to accelerate the development of new anti-snakebite drugs. In addition, the analysis of the sequenced, 3D structure of the database proteins reveals essential aspects of the anatomy of the proteins, their toxicity mechanisms, and the conserved binding site areas that may anchor universal interspecific inhibitors. Moreover, it pinpoints hypotheses for the molecular origin of the myotoxicity of the PLA2-like proteins. Altogether, this study provides an understanding of the diversity of these toxins and how they are conserved, and it indicates how to develop broad, interspecies, efficient small-molecule inhibitors to target the toxin's many mechanisms of action.

Indexed as

Snake BitesViper VenomsBinding SitesHumansMyotoxicityPhospholipases A2Phospholipases A2Viper Venomsmyotoxicityphospholipase A2snakebite envenomingsnake venom viperstructure–activity relationshiptoxin

Identifiers

PMID38393149
PMCPMC10893444
OpenAlexW4391432271

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.