Evidence map›Paper›PMID 27571103›Full record

ReviewToxins2016

Natural Inhibitors of Snake Venom Metalloendopeptidases: History and Current Challenges.

Viviane A Bastos, Francisco Gomes-Neto, Jonas Perales, Ana Gisele C Neves-Ferreira, Richard H Valente

Abstract readHistorical ArticleReview
In one paragraph

Review in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. A novel broad spectrum venom metalloproteinase autoinhibitor in the rattlesnakeProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
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.

Viviane A BastosLaboratory of Toxinology, Oswaldo Cruz Foundation (FIOCRUZ), Rio de Janeiro 21040-900, Brazil. vivika.bastos@gmail.com.
Francisco Gomes-NetoLaboratory of Toxinology, Oswaldo Cruz Foundation (FIOCRUZ), Rio de Janeiro 21040-900, Brazil. gomes.netof@gmail.com.
Jonas PeralesLaboratory of Toxinology, Oswaldo Cruz Foundation (FIOCRUZ), Rio de Janeiro 21040-900, Brazil. jperales@ioc.fiocruz.br.
Ana Gisele C Neves-FerreiraLaboratory of Toxinology, Oswaldo Cruz Foundation (FIOCRUZ), Rio de Janeiro 21040-900, Brazil. jonasperales@gmail.com.
Richard H ValenteLaboratory of Toxinology, Oswaldo Cruz Foundation (FIOCRUZ), Rio de Janeiro 21040-900, Brazil. richardhemmi@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The research on natural snake venom metalloendopeptidase inhibitors (SVMPIs) began in the 18th century with the pioneering work of Fontana on the resistance that vipers exhibited to their own venom. During the past 40 years, SVMPIs have been isolated mainly from the sera of resistant animals, and characterized to different extents. They are acidic oligomeric glycoproteins that remain biologically active over a wide range of pH and temperature values. Based on primary structure determination, mammalian plasmatic SVMPIs are classified as members of the immunoglobulin (Ig) supergene protein family, while the one isolated from muscle belongs to the ficolin/opsonin P35 family. On the other hand, SVMPIs from snake plasma have been placed in the cystatin superfamily. These natural antitoxins constitute the first line of defense against snake venoms, inhibiting the catalytic activities of snake venom metalloendopeptidases through the establishment of high-affinity, non-covalent interactions. This review presents a historical account of the field of natural resistance, summarizing its main discoveries and current challenges, which are mostly related to the limitations that preclude three-dimensional structural determinations of these inhibitors using "gold-standard" methods; perspectives on how to circumvent such limitations are presented. Potential applications of these SVMPIs in medicine are also highlighted.

Indexed as

AnimalsAntidotesHistory, 18th CenturyHistory, 19th CenturyHistory, 20th CenturyHistory, 21st CenturyHumansMetalloendopeptidasesProtease InhibitorsProtein ConformationReptilian ProteinsSnake BitesSnake VenomsStructure-Activity RelationshipAntidotesMetalloendopeptidasesProtease InhibitorsReptilian ProteinsSnake Venomscross-linkinghydrogen/deuterium exchangemass spectrometrymetalloendopeptidase inhibitormodelingnatural immunitynatural resistancesnake venomstructuretherapeutic application

Identifiers

PMID27571103
PMCPMC5037476

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Registered trials

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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.