Evidence map›Paper›PMID 31017792›Full record

ArticleJournal of proteome research2019

Comprehensive Study of the Proteome and Transcriptome of the Venom of the Most Venomous European Viper: Discovery of a New Subclass of Ancestral Snake Venom Metalloproteinase Precursor-Derived Proteins.

Adrijana Leonardi, Tamara Sajevic, Jože Pungerčar, Igor Križaj

Open access · hybridAbstract read
In one paragraph

Article in Journal of proteome research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.9field-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

29 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The Venom ofVeterinary sciences · 2024
    Article
  11. Tiny but Mighty:Toxins · 2024
    Article
  12. Review
  13. Article
  14. Comparison of cytotoxicity methods for studyingCentral-European journal of immunology · 2024
    Article
  15. Venom Proteomics ofToxins · 2023
    Article
  16. Article
  17. Article
  18. Article
  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

4 authors at 1 institution in 1 country.

Adrijana LeonardiDepartment of Molecular and Biomedical Sciences , Jožef Stefan Institute , Jamova cesta 39 , SI-1000 Ljubljana , Slovenia.ORCID 0000-0001-9854-9955
Tamara SajevicDepartment of Molecular and Biomedical Sciences , Jožef Stefan Institute , Jamova cesta 39 , SI-1000 Ljubljana , Slovenia.
Jože PungerčarDepartment of Molecular and Biomedical Sciences , Jožef Stefan Institute , Jamova cesta 39 , SI-1000 Ljubljana , Slovenia.ORCID 0000-0001-7228-336X
Igor KrižajDepartment of Molecular and Biomedical Sciences , Jožef Stefan Institute , Jamova cesta 39 , SI-1000 Ljubljana , Slovenia.ORCID 0000-0003-0203-0708
Jožef Stefan Institute · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nose-horned viper, its nominotypical subspecies Vipera ammodytes ammodytes ( Vaa), in particular, is, medically, one of the most relevant snakes in Europe. The local and systemic clinical manifestations of poisoning by the venom of this snake are the result of the pathophysiological effects inflicted by enzymatic and nonenzymatic venom components acting, most prominently, on the blood, cardiovascular, and nerve systems. This venom is a very complex mixture of pharmacologically active proteins and peptides. To help improve the current antivenom therapy toward higher specificity and efficiency and to assist drug discovery, we have constructed, by combining transcriptomic and proteomic analyses, the most comprehensive library yet of the Vaa venom proteins and peptides. Sequence analysis of the venom gland cDNA library has revealed the presence of messages encoding 12 types of polypeptide precursors. The most abundant are those for metalloproteinase inhibitors (MPis), bradykinin-potentiating peptides (BPPs), and natriuretic peptides (NPs) (all three on a single precursor), snake C-type lectin-like proteins (snaclecs), serine proteases (SVSPs), P-II and P-III metalloproteinases (SVMPs), secreted phospholipases A

Indexed as

TranscriptomeAmino Acid SequenceAngiotensin-Converting Enzyme InhibitorsAnimalsAntiveninsDisintegrinsGene LibraryGene OntologyLectins, C-TypeMetalloproteasesMolecular Sequence AnnotationNatriuretic PeptidesPhospholipases A2, SecretoryProtease InhibitorsProteomeProteomicsAngiotensin-Converting Enzyme InhibitorsAntiveninsDisintegrinsLectins, C-TypeMetalloproteasesNatriuretic PeptidesPhospholipases A2, SecretoryProtease InhibitorsProteomeRNA, MessengerSerine ProteasesViper Venomsmetalloproteinasenew subclassproteomicssnaketranscriptomicsvenom compositionVipera ammodytes ammodytesViperidae

Identifiers

PMID31017792
PMCPMC6727599
OpenAlexW2941462697

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.