ArticleInternational journal of biological sciences2015
Evolutionary History of Cathepsin L (L-like) Family Genes in Vertebrates.
Article in International journal of biological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Distinct Evolutionary Trajectories of Major Intracellular Proteolytic Systems in Gilthead Seabream and European Seabass.Biology · 2026Article
- Calibrating T cell responsiveness through interactions with self.Nature reviews. Immunology · 2026Review
- Psyllid Cysteine Cathepsins Directly Cleave the Outer Membrane Protein BamD of Citrus Huanglongbing Pathogen.Plant biotechnology journal · 2026Article
- Evolutionary diversification and immunoprofiling of cathepsin L toolkit in common carp.Frontiers in cellular and infection microbiology · 2026Article
- Organic matter degradation by oceanic fungi differs between polar and non-polar waters.Nature communications · 2025Article
- Origin and Early Diversification of the Papain Family of Cysteine Peptidases.International journal of molecular sciences · 2023Article
- Molecular mechanism of interaction between SARS-CoV-2 and host cells and interventional therapy.Signal transduction and targeted therapy · 2021Review
- An integrated transcriptomic and proteomic approach to identify the main Torymus sinensis venom components.Scientific reports · 2021Article
- Homocysteine in Neurology: A Possible Contributing Factor to Small Vessel Disease.International journal of molecular sciences · 2021Review
- Cathepsin V suppresses GATA3 protein expression in luminal A breast cancer.Breast cancer research : BCR · 2020Article
- Structure of the Plasmodium falciparum PfSERA5 pseudo-zymogen.Protein science : a publication of the Protein Society · 2020Article
- Cathepsin L in COVID-19: From Pharmacological Evidences to Genetics.Frontiers in cellular and infection microbiology · 2020Review
- Article
- Diversity of Neuropeptide Cell-Cell Signaling Molecules Generated by Proteolytic Processing Revealed by Neuropeptidomics Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Review
- l-Homocysteine-induced cathepsin V mediates the vascular endothelial inflammation in hyperhomocysteinaemia.British journal of pharmacology · 2018Article
- The Effect of Estradiol on the Growth Plate Chondrocytes of Limb and Spine from Postnatal MiceInternational journal of biological sciences · 2017Article
- Gene Expression Profiling Reveals Functional Specialization along the Intestinal Tract of a Carnivorous Teleostean Fish (Dicentrarchus labrax).Frontiers in physiology · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cathepsin L family, an important cysteine protease found in lysosomes, is categorized into cathepsins B, F, H, K, L, S, and W in vertebrates. This categorization is based on their sequence alignment and traditional functional classification, but the evolutionary relationship of family members is unclear. This study determined the evolutionary relationship of cathepsin L family genes in vertebrates through phylogenetic construction. Results showed that cathepsins F, H, S and K, and L and V were chronologically diverged. Tandem-repeat duplication was found to occur in the evolutionary history of cathepsin L family. Cathepsin L in zebrafish, cathepsins S and K in xenopus, and cathepsin L in mice and rats underwent evident tandem-repeat events. Positive selection was detected in cathepsin L-like members in mice and rats, and amino acid sites under positive selection pressure were calculated. Most of these sites appeared at the connection of secondary structures, suggesting that the sites may slightly change spatial structure. Severe positive selection was also observed in cathepsin V (L2) of primates, indicating that this enzyme had some special functions. Our work provided a brief evolutionary history of cathepsin L family and differentiated cathepsins S and K from cathepsin L based on vertebrate appearance. Positive selection was the specific cause of differentiation of cathepsin L family genes, confirming that gene function variation after expansion events was related to interactions with the environment and adaptability.
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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.