ReviewToxins2020
Cysteine-Rich Secretory Proteins (CRISPs) From Venomous Snakes: An Overview of the Functional Diversity in A Large and Underappreciated Superfamily.
Review in Toxins, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 96 citations in OpenAlex.
- BrazilianToxins · 2026Article
- Diversity and Bioprospection of Functional Proteins from Sea AnemoneMarine drugs · 2026Article
- Venom variation and the future of antivenom design: Integrating population venomics, evolutionary toxinology, and precision therapeutics.Toxicon: X · 2026Review
- Article
- Inter- and Intraspecific Venom Variation in the Reclusive Rear-Fanged Black-Striped Snakes (Toxins · 2026Article
- Venom Variation as a Window into the Ecology and Evolution of Snakes.Integrative and comparative biology · 2026Review
- Comparative Proteomics, Functional Characterization and Immunological Cross-Reactivity Studies on Russell's Viper Venom from Two Distinct Geographical Regions in South India.International journal of molecular sciences · 2025Article
- Article
- Proteome Analysis of the Six-Eyed Sand-SpiderToxins · 2025Article
- Snake Toxins Affecting Blood Vessel Walls: Mode of Action and Biological Significance.International journal of molecular sciences · 2025Review
- Article
- An insight into the salivary gland content of the human body louse, Pediculus humanus.Scientific reports · 2025Article
- Article
- Snake Venom Compounds: A New Frontier in the Battle Against Antibiotic-Resistant Infections.Toxins · 2025Review
- Categorization and Characterization of Snake Venom Variability through Intact Toxin Analysis by Mass Spectrometry.Journal of proteome research · 2025Article
- A deep insight into the sialome of the house fly, Musca domestica, infected with the salivary gland hypertrophy virus (MdSGHV).Scientific reports · 2025Article
- Article
- Article
- Exploring the Venom Gland Transcriptome ofToxins · 2024Article
- CAP superfamily proteins in human: a new target for cancer therapy.Medical oncology (Northwood, London, England) · 2024Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The CAP protein superfamily (Cysteine-rich secretory proteins (CRISPs), Antigen 5 (Ag5), and Pathogenesis-related 1 (PR-1) proteins) is widely distributed, but for toxinologists, snake venom CRISPs are the most familiar members. Although CRISPs are found in the majority of venoms, very few of these proteins have been functionally characterized, but those that have been exhibit diverse activities. Snake venom CRISPs (svCRISPs) inhibit ion channels and the growth of new blood vessels (angiogenesis). They also increase vascular permeability and promote inflammatory responses (leukocyte and neutrophil infiltration). Interestingly, CRISPs in lamprey buccal gland secretions also manifest some of these activities, suggesting an evolutionarily conserved function. As we strive to better understand the functions that CRISPs serve in venoms, it is worth considering the broad range of CRISP physiological activities throughout the animal kingdom. In this review, we summarize those activities, known crystal structures and sequence alignments, and we discuss predicted functional sites. CRISPs may not be lethal or major components of venoms, but given their almost ubiquitous occurrence in venoms and the accelerated evolution of svCRISP genes, these venom proteins are likely to have functions worth investigating.
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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.