ArticleProceedings of the National Academy of Sciences of the United States of America2008
Congenital disease SNPs target lineage specific structural elements in protein kinases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 69 citations in OpenAlex.
- Critical role of the CMGC insert sequence for tyrosine autophosphorylation in the protein kinase DYRK1B.Scientific reports · 2025Article
- Molecular insights into TP53 mutation (p. Arg267Trp) and its connection to Choroid Plexus Carcinomas and Li-Fraumeni Syndrome.Genes & genomics · 2024Article
- Biochemical and hydrogen-deuterium exchange studies of the single nucleotide polymorphism Y649C in human platelet 12-lipoxygenase linked to a bleeding disorder.Archives of biochemistry and biophysics · 2023Article
- Calculation of centralities in protein kinase A.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A walk-through MAPK structure and functionality with the 30-year-old yeast MAPK Slt2.International microbiology : the official journal of the Spanish Society for Microbiology · 2021Review
- A Comprehensive Phylogenetic Analysis of the MAP4K Family in the Green Lineage.Frontiers in plant science · 2021Article
- The functional landscape of the human phosphoproteome.Nature biotechnology · 2020Article
- Kinase Domain Is a Dynamic Hub for Driving LRRK2 Allostery.Frontiers in molecular neuroscience · 2020Article
- The dynamic switch mechanism that leads to activation of LRRK2 is embedded in the DFGψ motif in the kinase domain.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- LF4/MOK and a CDK-related kinase regulate the number and length of cilia in Tetrahymena.PLoS genetics · 2019Article
- Orange is the new black: Kinases are the new master regulators of tumor suppression.IUBMB life · 2019Review
- Evolution of protein kinase substrate recognition at the active site.PLoS biology · 2019Article
- De Novo Missense Substitutions in the Gene Encoding CDK8, a Regulator of the Mediator Complex, Cause a Syndromic Developmental Disorder.American journal of human genetics · 2019Article
- Post-translational modifications at the ATP-positioning G-loop that regulate protein kinase activity.Pharmacological research · 2018Review
- Functional characterization of DYRK1A missense variants associated with a syndromic form of intellectual deficiency and autism.Biology open · 2018Article
- Protein kinase C: perfectly balanced.Critical reviews in biochemistry and molecular biology · 2018Review
- The Molecular Basis for Specificity at the Level of the Protein Kinase a Catalytic Subunit.Frontiers in endocrinology · 2018Review
- Cleavage Alters the Molecular Determinants of Protein Kinase C-δ Catalytic Activity.Molecular and cellular biology · 2017Article
- Analysis of somatic mutations across the kinome reveals loss-of-function mutations in multiple cancer types.Scientific reports · 2017Article
- Dynamics-Driven Allostery in Protein Kinases.Trends in biochemical sciences · 2015Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The catalytic domain of protein kinases harbors a large number of disease-causing single nucleotide polymorphisms (SNPs) and common or neutral SNPs that are not known or hypothesized to be associated with any disease. Distinguishing these two types of polymorphisms is critical in accurately predicting the causative role of SNPs in both candidate gene and genome-wide association studies. In this study, we have analyzed the structural location of common and disease-associated SNPs in the catalytic domain of protein kinases and find that, although common SNPs are randomly distributed within the catalytic core, known disease SNPs consistently map to regulatory and substrate binding regions. In particular, a buried side-chain network that anchors the flexible activation loop to the catalytic core is frequently mutated in disease patients. This network was recently shown to be absent in distantly related eukaryotic-like kinases, which lack an exaggerated activation loop and, presumably, are not regulated by phosphorylation.
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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.