ArticleJournal of molecular evolution1996
Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: gene duplication and divergence of a common ancestor rather than convergent evolution.
Article in Journal of molecular evolution, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 99 citations in OpenAlex.
- Article
- Past, Present, and Future of Naturally Occurring Antimicrobials Related to Snake Venoms.Animals : an open access journal from MDPI · 2023Review
- Snakebite drug discovery: high-throughput screening to identify novel snake venom metalloproteinase toxin inhibitors.Frontiers in pharmacology · 2023Article
- Article
- Dynamic genetic differentiation drives the widespread structural and functional convergent evolution of snake venom proteinaceous toxins.BMC biology · 2022Article
- Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction.Frontiers in molecular biosciences · 2021Review
- Size Matters: An Evaluation of the Molecular Basis of Ontogenetic Modifications in the Composition ofToxins · 2020Article
- Article
- The origin and diversification of a novel protein family in venomous snakes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Differential Macrophage Subsets in Muscle Damage Induced by a K49-PLAInflammation · 2019Article
- Article
- Review
- Review
- Article
- Colubrid Venom Composition: An -Omics Perspective.Toxins · 2016Review
- Article
- Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation.Toxins · 2016Review
- ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview.Toxins · 2016Review
- Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage.PLoS neglected tropical diseases · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The evolution of the Metalloproteinase Disintegrin Cysteine-rich (MDC) gene family and that of the mammalian Matrix-degrading Metalloproteinases (MMPs) are compared. The alignment of snake venom and mammalian MDC and MMP precursor sequences generated a phylogenetic tree that grouped these proteins mainly according to their function. Based on this observation, a common ancestry is suggested for mammalian and snake venom MDCs; it is also possible that gene duplication of the already-assembled domain structure, followed by divergence of the copies, may have significantly contributed to the evolution of the functionally diverse MDC proteins. The data also suggest that the structural resemblance of the zinc-binding motif of venom MDCs and MMPs may best be explained by common ancestry and conservation of the proteolytic motifs during the divergence of the proteins rather than through convergent evolution.
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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.