ReviewThe journal of venomous animals and toxins including tropical diseases2023
Snake venom disintegrins update: insights about new findings.
Review in The journal of venomous animals and toxins including tropical diseases, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Sea nettle jellyfish venom targets proteoglycans to cause cell death and pain.Science advances · 2026Article
- Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy.Toxins · 2026Review
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- Venom variation and the future of antivenom design: Integrating population venomics, evolutionary toxinology, and precision therapeutics.Toxicon: X · 2026Review
- Early vascular toxicity induced by Bothrops atrox venom in the chorioallantoic membrane assay: Kinetic profile and translational insights.PLoS neglected tropical diseases · 2026Article
- Venom Variation as a Window into the Ecology and Evolution of Snakes.Integrative and comparative biology · 2026Review
- Snake Toxins Affecting Blood Vessel Walls: Mode of Action and Biological Significance.International journal of molecular sciences · 2025Review
- Review
- Article
- Peptide Fraction fromAntioxidants (Basel, Switzerland) · 2025Article
- Diagnosis of human envenoming by terrestrial venomous animals: Routine, advances, and perspectives.Toxicon: X · 2024Article
- Extracellular Matrix as a Target in Melanoma Therapy: From Hypothesis to Clinical Trials.Cells · 2024Review
- Comparative Analysis of Tentacle Extract and Nematocyst Venom: Toxicity, Mechanism, and Potential Intervention in the Giant JellyfishMarine drugs · 2024Article
- Expression, Purification and Characterization of Recombinant Disintegrin from Gloydius Brevicaudus Venom in Escherichia Coli.The protein journal · 2024Article
- Dabsylated Bradykinin Is Cleaved by Snake Venom Proteases fromBiomedicines · 2024Article
- Review
- Differential effects of the venoms of Russell's viper and Indian cobra on human myoblasts.Scientific reports · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Snake venom disintegrins are low molecular weight, non-enzymatic proteins rich in cysteine, present in the venom of snakes from the families Viperidae, Crotalidae, Atractaspididae, Elapidae, and Colubridae. This family of proteins originated in venom through the proteolytic processing of metalloproteinases (SVMPs), which, in turn, evolved from a gene encoding an A Disintegrin And Metalloprotease (ADAM) molecule. Disintegrins have a recognition motif for integrins in their structure, allowing interaction with these transmembrane adhesion receptors and preventing their binding to proteins in the extracellular matrix and other cells. This interaction gives disintegrins their wide range of biological functions, including inhibition of platelet aggregation and antitumor activity. As a result, many studies have been conducted in an attempt to use these natural compounds as a basis for developing therapies for the treatment of various diseases. Furthermore, the FDA has approved Tirofiban and Eptifibatide as antiplatelet compounds, and they are synthesized from the structure of echistatin and barbourin, respectively. In this review, we discuss some of the main functional and structural characteristics of this class of proteins and their potential for therapeutic use.
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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.