Evidence map›Paper›PMID 29311537›Full record

ReviewToxins2017

Secreted Phospholipases A₂ from Animal Venoms in Pain and Analgesia.

Vanessa O Zambelli, Gisele Picolo, Carlos A H Fernandes, Marcos R M Fontes, Yara Cury

Open access · goldAbstract readReview
In one paragraph

Review in Toxins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Quantitative analysis of growth and diversification in venom data using database metrics.Database : the journal of biological databases and curation · 2026
    Article
  6. Article
  7. Article
  8. Phospholipases ABiomolecules · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Crosstalk of Inflammation and Coagulation inInternational journal of molecular sciences · 2023
    Review
  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

5 authors at 2 institutions in 1 country.

Vanessa O ZambelliLaboratory of Pain and Signaling, Butantan Institute, Av. Vital Brasil, 1500, 05503-900 São Paulo, SP, Brazil. vanessa.zambelli@butantan.gov.br.
Gisele PicoloLaboratory of Pain and Signaling, Butantan Institute, Av. Vital Brasil, 1500, 05503-900 São Paulo, SP, Brazil. gisele.picolo@butantan.gov.br.
Carlos A H FernandesDepartment of Physics and Biophysics, São Paulo State University (UNESP), Rua Professor Doutor Antonio Celso Wagner Zanin, s/n, 18618-689 Botucatu, SP, Brazil. fernandes@ibb.unesp.br.
Marcos R M FontesDepartment of Physics and Biophysics, São Paulo State University (UNESP), Rua Professor Doutor Antonio Celso Wagner Zanin, s/n, 18618-689 Botucatu, SP, Brazil. fontes@ibb.unesp.br.ORCID 0000-0002-4634-6221
Yara CuryLaboratory of Pain and Signaling, Butantan Institute, Av. Vital Brasil, 1500, 05503-900 São Paulo, SP, Brazil. yarac57@gmail.com.ORCID 0000-0002-6245-3166
Instituto Butantan · BRUniversidade Estadual Paulista (Unesp) · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Animal venoms comprise a complex mixture of components that affect several biological systems. Based on the high selectivity for their molecular targets, these components are also a rich source of potential therapeutic agents. Among the main components of animal venoms are the secreted phospholipases A₂ (sPLA₂s). These PLA₂ belong to distinct PLA₂s groups. For example, snake venom sPLA₂s from Elapidae and Viperidae families, the most important families when considering envenomation, belong, respectively, to the IA and IIA/IIB groups, whereas bee venom PLA₂ belongs to group III of sPLA₂s. It is well known that PLA₂, due to its hydrolytic activity on phospholipids, takes part in many pathophysiological processes, including inflammation and pain. Therefore, secreted PLA₂s obtained from animal venoms have been widely used as tools to (a) modulate inflammation and pain, uncovering molecular targets that are implicated in the control of inflammatory (including painful) and neurodegenerative diseases; (b) shed light on the pathophysiology of inflammation and pain observed in human envenomation by poisonous animals; and, (c) characterize molecular mechanisms involved in inflammatory diseases. The present review summarizes the knowledge on the nociceptive and antinociceptive actions of sPLA₂s from animal venoms, particularly snake venoms.

Indexed as

AnalgesiaAnalgesicsAnimalsHumansPainPhospholipases A2, SecretoryVenomsAnalgesicsPhospholipases A2, SecretoryVenomsanalgesiaanimal venomscatalytic activitypainsecretory phospholipases A2

Identifiers

PMID29311537
PMCPMC5744126
OpenAlexW2779102044

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.