ReviewJournal of molecular evolution2020
Evolutionary Aspects of the Structural Convergence and Functional Diversification of Kunitz-Domain Inhibitors.
Review in Journal of molecular evolution, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 66 citations in OpenAlex.
- Sketching microprotein portraits.Protein science : a publication of the Protein Society · 2026Review
- Conkazal-M1 from the MKAVA family of conotoxins: A dual-function protease inhibitor and neuroactive peptide.Protein science : a publication of the Protein Society · 2026Article
- Insulin Resistance, Anti-inflammatory, and AntioxidantBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- Bannakunin: a dual-target Kunitz inhibitor bridging anticoagulation (FXa/XIIa) and anti-platelet (α2β1/P2Y12) pathways.Cellular & molecular biology letters · 2026Article
- A biochemical difference between HAI-2 variants causing syndromic and non-syndromic Congenital Sodium Diarrhea.PloS one · 2026Article
- Review
- Conkazal-M1 from the MKAVA family of conotoxins - a dual-function protease inhibitor and neuroactive peptide.bioRxiv : the preprint server for biology · 2025Article
- Therapeutic Promise and Biotechnological Prospects ofInternational journal of molecular sciences · 2025Review
- Snake Toxins Affecting Blood Vessel Walls: Mode of Action and Biological Significance.International journal of molecular sciences · 2025Review
- A novel polypeptide from stony coral Goniopora columna inhibits thrombosis by interfering with the contact-kinin pathway.Archives of toxicology · 2025Article
- Article
- Functional characterization of a common XIa inhibitory Kunitz-domain Shp4 from nine schistosoma secreted proteins with diverse C-terminal fragments.PLoS neglected tropical diseases · 2025Article
- Molecular Insights into the Marine GastropodInternational journal of molecular sciences · 2025Article
- The proteotranscriptomic characterization of venom in the white seafanOpen biology · 2025Article
- Guianensin, a Blackfly Salivary Protein, Inhibits the Lectin Pathway of Complement.Journal of medicinal chemistry · 2025Article
- Innate Immunity in Insects: The Lights and Shadows of Phenoloxidase System Activation.International journal of molecular sciences · 2025Review
- Large-scale CRISPR/Cas9 deletions within the WFDC gene cluster uncover gene functionality and critical roles in mammalian reproduction.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Revealing the Diversity of Sequences, Structures, and Targets of Peptides from South China SeaMarine drugs · 2024Article
- The Caenorhabditis elegans cuticle and precuticle: a model for studying dynamic apical extracellular matrices in vivo.Genetics · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kunitz-type domains are ubiquitously found in natural systems as serine protease inhibitors or animal toxins in venomous animals. Kunitz motif is a cysteine-rich peptide chain of ~ 60 amino acid residues with alpha and beta fold, stabilized by three conserved disulfide bridges. An extensive dataset of amino acid variations is found on sequence analysis of various Kunitz peptides. Kunitz peptides show diverse biological activities like inhibition of proteases of other classes and/or adopting a new function of blocking or modulating the ion channels. Based on the amino acid residues at the functional site of various Kunitz-type inhibitors, it is inferred that this 'flexibility within the structural rigidity' is responsible for multiple biological activities. Accelerated evolution of functional sites in response to the co-evolving molecular targets of the hosts of venomous animals or parasites, gene sharing, and gene duplication have been discussed as the most likely mechanisms responsible for the functional heterogeneity of Kunitz-domain inhibitors.
Indexed as
Identifiers
What 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.