ReviewPharmacological research2018
Post-translational modifications at the ATP-positioning G-loop that regulate protein kinase activity.
Review in Pharmacological research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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
20 citing papers in PubMed, 40 citations in OpenAlex.
- Machine Learning and Virtual Screening Methods to Discover Potential Cyclin-Dependent Kinase 2 (CDK2) Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Proximity-Induced Rewiring of Oncogenic Kinase Triggers Apoptosis.ACS central science · 2026Article
- Virus-Mediated Overexpression of Two Allelic Protein Fragments Elicits Drastically Different Responses in Soybean.Viruses · 2026Article
- Dynamic acetylation of a conserved lysine impacts glycerol kinase activity and abundance in the haloarchaeon Haloferax volcanii.The Journal of biological chemistry · 2026Article
- Kinase Inhibitors for Targeted Cancer Therapy.Current topics in medicinal chemistry · 2026Review
- Regulatory mimicry of cyclin-dependent kinases by a conserved herpesvirus protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Research on the regulation mechanism of drought tolerance in wheat.Plant cell reports · 2025Review
- A missense variant effect map for the human tumor-suppressor protein CHK2.American journal of human genetics · 2024Article
- The fitness cost of spurious phosphorylation.The EMBO journal · 2024Article
- DEAD box RNA helicases are pervasive protein kinase interactors and activators.Genome research · 2024Article
- Protein kinase PfPK2 mediated signalling is critical for host erythrocyte invasion by malaria parasite.PLoS pathogens · 2023Article
- Article
- The fitness cost of spurious phosphorylation.bioRxiv : the preprint server for biology · 2023Article
- Modulation of IRAK enzymes as a therapeutic strategy against SARS-CoV-2 induced cytokine storm.Clinical and experimental medicine · 2023Review
- Genome-wide identification, evolutionary and expression analysis of the cyclin-dependent kinase gene family in peanut.BMC plant biology · 2023Article
- Deciphering the conformational transitions of LIMK2 active and inactive states to ponder specific druggable states through microsecond scale molecular dynamics simulation.Journal of computer-aided molecular design · 2022Article
- Decoding the Cardiac Actions of Protein Kinase D Isoforms.Molecular pharmacology · 2021Review
- Crystal structure of the human PRPK-TPRKB complex.Communications biology · 2021Article
- A Comprehensive Phylogenetic Analysis of the MAP4K Family in the Green Lineage.Frontiers in plant science · 2021Article
- SMYD2 promotes cervical cancer growth by stimulating cell proliferation.Cell & bioscience · 2019Article
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
Abstract
Protein kinases are a superfamily of enzymes that control a wide range of cellular functions. These enzymes share a highly conserved catalytic core that folds into a similar bilobar three-dimensional structure. One highly conserved region in the protein kinase core is the glycine-rich loop (or G-loop), a highly flexible loop that is characterized by a consensus GxGxxG sequence. The G-loop points toward the catalytic cleft and functions to bind and position ATP for phosphotransfer. Of note, in many protein kinases, the second and third glycine residues in the G-loop triad flank residues that can be targets for phosphorylation (Ser, Thr, or Tyr) or other post-translational modifications (ubiquitination, acetylation, O-GlcNAcylation, oxidation). There is considerable evidence that cyclin-dependent kinases are held inactive through inhibitory phosphorylation of the conserved Thr/Tyr residues in this position of the G-loop and that dephosphorylation by cellular phosphatases is required for CDK activation and progression through the cell cycle. This review summarizes literature that identifies residues in or adjacent to the G-loop in other protein kinases that are targets for functionally important post-translational modifications.
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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.