ReviewFrontiers in molecular biosciences2021
Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction.
Review in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Structural basis for the differential recognition of integrin αvβ3 by rhodostomin and trimucrin.Communications biology · 2026Article
- Lowly Expressed Toxin Transcripts in Poorly Characterized Myanmar Russell's Viper Venom Gland.Biotech (Basel (Switzerland)) · 2025Article
- Surface Acoustic Waves-Based Molecular Recognition of a Collagen Receptor on Human Erythrocytes.International journal of molecular sciences · 2025Article
- Targets Involved in the Pharmacology of Bothrops Snakebite:Current drug targets · 2025Review
- Venomics and Peptidomics of Palearctic Vipers: A Clade-Wide Analysis of Seven Taxa of the GeneraJournal of proteome research · 2024Article
- Purification, and characterization of a new pro-coagulant protein from IranianBiochemistry and biophysics reports · 2024Article
- Dabsylated Bradykinin Is Cleaved by Snake Venom Proteases fromBiomedicines · 2024Article
- Review
- Venom-derived peptides for breaking through the glass ceiling of drug development.Frontiers in chemistry · 2024Review
- CC5 and CC8, Two Disintegrin Isoforms fromInternational journal of molecular sciences · 2023Article
- Disintegrin-like Protein Strategy to Inhibit Aggressive Triple-Negative Breast Cancer.International journal of molecular sciences · 2023Article
- Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation.Molecules (Basel, Switzerland) · 2023Article
- The Role of Integrins for Mediating Nanodrugs to Improve Performance in Tumor Diagnosis and Treatment.Nanomaterials (Basel, Switzerland) · 2023Review
- Exploring Toxin Genes of Myanmar Russell's Viper,Toxins · 2023Article
- Snake venom disintegrins update: insights about new findings.The journal of venomous animals and toxins including tropical diseases · 2023Review
- The First Snake Venom KTS/Disintegrins-Integrin Interactions Using Bioinformatics Approaches.Molecules (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disintegrins are small cysteine-rich proteins found in a variety of snake venom. These proteins selectively modulate integrin function, heterodimeric receptors involved in cell-cell and cell-matrix interaction that are widely studied as therapeutic targets. Snake venom disintegrins emerged from the snake venom metalloproteinase and are classified according to the sequence size and number of disulfide bonds. Evolutive structure and function diversification of disintegrin family involves a stepwise decrease in the polypeptide chain, loss of cysteine residues, and selectivity. Since the structure elucidation of echistatin, the description of the structural properties of disintegrins has allowed the investigation of the mechanisms involved in integrin-cell-extracellular matrix interaction. This review provides an analysis of the structures of all family groups enabling the description of an expanded classification of the disintegrin family in seven groups. Each group presents a particular disulfide pattern and sequence signatures, facilitating the identification of new disintegrins. The classification was based on the disintegrin-like domain of the human metalloproteinase (ADAM-10). We also present the sequence and structural signatures important for disintegrin-integrin interaction, unveiling the relationship between the structure and function of these proteins.
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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.