ArticleJournal of venom research2011
Purification of a phospholipase A(2) from Daboia russelii siamensis venom with anticancer effects.
Article in Journal of venom research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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.
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.
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Who cites it
14 citing papers in PubMed.
- Biological Effects of Secretory Phospholipase ABulletin of experimental biology and medicine · 2026Article
- Unraveling snake venom phospholipase APharmacological reports : PR · 2023Review
- Functional Characterization and Anti-Tumor Effect of a Novel Group II Secreted Phospholipase AMolecules (Basel, Switzerland) · 2023Article
- Article
- Purification, Characterization and Evaluation of the Antitumoral Activity of a Phospholipase A2 from the SnakePharmaceuticals (Basel, Switzerland) · 2022Article
- Qualitative Analysis of Proteins in Two Snake Venoms, Gloydius Blomhoffii and Agkistrodon Acutus.Journal of pharmacopuncture · 2022Article
- Article
- Cytotoxicity of snake venom enzymatic toxins: phospholipase A2 and l-amino acid oxidase.Biochemical Society transactions · 2020Review
- Review
- First Look at the Venom of Naja ashei.Molecules (Basel, Switzerland) · 2018Article
- Anticancer properties of phospholipase A2 from Daboia siamensis venom on human skin melanoma cells.The journal of venomous animals and toxins including tropical diseases · 2016Article
- Antitumoral activity of snake venom proteins: new trends in cancer therapy.BioMed research international · 2014Review
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- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
Venom phospholipases A2 (PLA(2)) are associated with neurotoxic, myotoxic, cardiotoxic, platelet aggregation, and edema activities. A PLA(2) (Drs-PLA(2)) was purified from Daboia russelii siamensis venom by a two-step purification procedure consisting of size-exclusion, followed by anion exchange high performance liquid chromatography (HPLC). The molecular weight of the Drs-PLA(2) was 13,679Da, which was determined by MALDI-TOF mass spectrometry. Its N-terminal amino acid sequence was homologous to basic PLA(2)s of viperid snake venoms. The Drs-PLA(2) had indirect hemolytic and anticoagulant activities, cytotoxic activity with a CC(50) of 65.8nM, and inhibited SK-MEL-28 cell migration with an IC(50) of 25.6nM. In addition, the Drs-PLA(2) inhibited the colonization of B16F10 cells in lungs of BALB/c mice by ∼65%.
Indexed as
Identifiers
22091349PMC3210966What OpenQuestion holds
Registered trials
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.