ReviewToxins2016
Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation.
Review in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
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Who cites it
24 citing papers in PubMed, 57 citations in OpenAlex.
- Article
- Cross-continental venom narratives: proteo-transcriptomic insights into Hydrophis cyanocinctus of India and China.Archives of toxicology · 2026Article
- Nephroprotective Effects of Wedelolactone against Snake Venom-Induced Acute Kidney Injury: Insights into Experimental Envenomation.ACS omega · 2026Article
- Genome of venomous caterpillarProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Maggot Kinase and Natural Thrombolytic Proteins.ACS omega · 2024Review
- Toxicological analyses of the venoms of Nigerian vipers Echis ocellatus and Bitis arietans.Tropical medicine and health · 2024Article
- Pictolysin-III, a Hemorrhagic Type-III Metalloproteinase Isolated fromPharmaceutics · 2023Article
- Venom-gland transcriptomics of the Malayan pit viper (Heliyon · 2023Article
- Article
- Snake venom disintegrins update: insights about new findings.The journal of venomous animals and toxins including tropical diseases · 2023Review
- Extracellular Vesicles fromToxins · 2022Article
- Poly-Gly Region Regulates the Accessibility of Metal Binding Sites in Snake Venom Peptides.Inorganic chemistry · 2022Article
- The rise of genomics in snake venom research: recent advances and future perspectives.GigaScience · 2022Article
- Venom proteomic analysis of medically important Nigerian viperBiochemistry and biophysics reports · 2021Article
- Proteomic Identification and Quantification of Snake Venom Biomarkers in Venom and Plasma Extracellular Vesicles.Toxins · 2021Article
- Article
- Proteomic Investigations of Two PakistaniToxins · 2020Article
- Fast venomic analysis ofToxicon: X · 2020Article
- 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
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Snake venom metalloproteinases (SVMPs) are abundant in the venoms of vipers and rattlesnakes, playing important roles for the snake adaptation to different environments, and are related to most of the pathological effects of these venoms in human victims. The effectiveness of SVMPs is greatly due to their functional diversity, targeting important physiological proteins or receptors in different tissues and in the coagulation system. Functional diversity is often related to the genetic diversification of the snake venom. In this review, we discuss some published evidence that posit that processing and post-translational modifications are great contributors for the generation of functional diversity and for maintaining latency or inactivation of enzymes belonging to this relevant family of venom toxins.
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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.