Evidence map›Paper›PMID 35769869›Full record

ReviewToxicon: X2022

Biochemistry and toxicology of proteins and peptides purified from the venom of

Jüri Siigur, Ene Siigur

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Toxicon: X, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. International journal of molecular sciences · 2025
    Article
  2. Article
  3. Cytogenetic Analysis of the Bimodal Karyotype of the Common European Adder,Animals : an open access journal from MDPI · 2022
    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.

Jüri SiigurLaboratory of Environmental Toxicology, National Institute of Chemical Physics and Biophysics, Akadeemia Tee 23, 12618, Tallinn, Estonia.
Ene SiigurLaboratory of Environmental Toxicology, National Institute of Chemical Physics and Biophysics, Akadeemia Tee 23, 12618, Tallinn, Estonia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The isolation and characterization of individual snake venom components is important for a deeper understanding of the pathophysiology of envenomation and for improving the therapeutic procedures of patients. It also opens possibilities for the discovery of novel toxins that might be useful as tools for understanding cellular and molecular processes. The variable venom composition, toxicological and immunological properties of the common vipers (

Indexed as

5′-NT, 5′- nucleotidaseACE, angiotensin converting enzymeAspP, aspartic proteaseBAEE, benzoylarginine ethyl esterBNP, B-type natriuretic peptideBPP, bradykinin potentiating peptidesCNP, C-type natriuretic peptideCRISP, cysteine rich secretory proteinCTL, C-type lectin/snaclecHyal, hyaluronidaseKUN, Kunitz type proteinase inhibitorLAAO, L-amino acid oxidaseMALDI-TOF MS, matrix-assisted laser desorption ionization/time of flight mass spectrometryNGF, nerve growth factorNP, natriuretic peptidePDE, phosphodiesterasePLA2, phospholipase A2PLB, phospholipase BPro-Phe-Arg-MCA, Pro-Phe-Arg-4-methylcoumarinyl-7-amideQC, glutaminyl-peptide cyclotransferaseSnake venomSVMP, snake venom metalloproteinaseSVSP, snake venom serine proteinaseTAME, tosylarginine methyl esterVBFXAE, V. berus factor X activating enzymeVEGF, vascular endothelial growth factorVipera berus baraniVipera berus berus (Common viper)Vipera berus bosniensisVipera berus marassoVipera berus sachalinensis

Identifiers

PMID35769869
PMCPMC9234072

What OpenQuestion holds

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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.