ArticleProtein science : a publication of the Protein Society2023
Pathogenic mutation hotspots in protein kinase domain structure.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Stable simulations do not guarantee functional engagement: a case study of off-target prediction for Seladelpar and Zanamivir.Journal of computer-aided molecular design · 2026Article
- Integrating evidence from protein domains to identify cancer driver mutations.Protein science : a publication of the Protein Society · 2026Article
- Uncovering the molecular basis of kinase activity and substrate recognition with phospho-PCA.bioRxiv : the preprint server for biology · 2025Article
- Proteomic analysis and functional characterization of excretory-secretory products from adult Toxocara canis: insights into parasite-host interactions.BMC genomics · 2025Article
- DrugDomain 2.0: comprehensive database of protein domains-ligands/drugs interactions across the whole Protein Data Bank.bioRxiv : the preprint server for biology · 2025Article
- Article
- Decoding the functional impact of the cancer genome through protein-protein interactions.Nature reviews. Cancer · 2025Review
- DrugDomain 2.0: Comprehensive database of protein domains-ligands/drugs interactions across the whole Protein Data Bank.Computational and structural biotechnology journal · 2025Article
- Proteomics analysis reveals the differential protein expression of female and male adult Toxocara canis using Orbitrap Astral analyzer.Infectious diseases of poverty · 2024Article
- DrugDomain: The evolutionary context of drugs and small molecules bound to domains.Protein science : a publication of the Protein Society · 2024Article
- Pathogenic mutation hotspots in protein kinase domain structure.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Control of eukaryotic cellular function is heavily reliant on the phosphorylation of proteins at specific amino acid residues, such as serine, threonine, tyrosine, and histidine. Protein kinases that are responsible for this process comprise one of the largest families of evolutionarily related proteins. Dysregulation of protein kinase signaling pathways is a frequent cause of a large variety of human diseases including cancer, autoimmune, neurodegenerative, and cardiovascular disorders. In this study, we mapped all pathogenic mutations in 497 human protein kinase domains from the ClinVar database to the reference structure of Aurora kinase A (AURKA) and grouped them by the relevance to the disease type. Our study revealed that the majority of mutation hotspots associated with cancer are situated within the catalytic and activation loops of the kinase domain, whereas non-cancer-related hotspots tend to be located outside of these regions. Additionally, we identified a hotspot at residue R371 of the AURKA structure that has the highest number of exclusively non-cancer-related pathogenic mutations (21) and has not been previously discussed.
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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.