ReviewLife (Basel, Switzerland)2021
Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases.
Review in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
48 citing papers in PubMed.
- Pyridopyrimidines and Pyridopyrimidinones as Kinase-Targeted Anticancer Agents: Medicinal Chemistry and Mechanistic Insights.Molecules (Basel, Switzerland) · 2026Review
- Targeting FLT3 in Acute Myeloid Leukemia: Structural Insights and Key Challenges.ACS bio & med chem Au · 2026Review
- Are Sulfates of the Hydroxyl Amino Acids Threonine and Serine Truly Extremely Rare or Do They Simply Escape Detection?Life (Basel, Switzerland) · 2026Article
- Beyond Sequence: Posttranslational Remodeling of Antigens in Autoimmunity.Immunological reviews · 2026Review
- Phenotypic Analysis of Mice with Conditional Knockout of PPP2CA in Colonic Tissues.Digestive diseases and sciences · 2026Article
- Protein Phosphorylation: An Essential Role in Shoot Apical Meristem Homeostasis.Plants (Basel, Switzerland) · 2026Review
- Anion-Specific Mechanisms in Fibrinogen Self-Assembly: Contrasting Effects of Phosphates and Chlorides in Nanofiber Formation.Macromolecular bioscience · 2026Article
- Heterologous expression, immunogenic evaluation, and subunit vaccine potential of the σC protein from the Xinjiang avian reovirus (ARV) strain xj-1.1.Poultry science · 2026Article
- SARS-CoV-2 membrane protein recruits PP2A to dephosphorylate the nucleocapsid and promote virion production.Journal of biomedical science · 2026Article
- Exploring the Role of the MAPK Signalling Pathway in Dog Immunity: From Cancer to Parasitic Diseases.Parasite immunology · 2026Review
- Article
- Dephosphorylation at Ser548 regulates hemocyanin-derived antibacterial peptides and immune defense iniScience · 2026Article
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- Interaction between Poly(ADP-ribose) polymerase-1 and α-synuclein pathology in Parkinson's disease.Frontiers in neuroscience · 2026Review
- Microplastics in soil-plant systems: impacts on soil health, plant toxicity, and multiomics insights.Plant cell reports · 2025Review
- Identification and functional evaluation of cyclin-dependent kinase genes reveals that CDKB1;1 and CDKB2;2 contribute to the balance of mitosis and endoreduplication in Medicago truncatula nodule.BMC plant biology · 2025Article
- The multifaceted roles of PP2C phosphatases in plant growth, signaling, and responses to abiotic and biotic stresses.Plant communications · 2025Review
- Absolute Quantitation of Phosphopeptides and Glycopeptides Using Coulometric Mass Spectrometry.ACS measurement science au · 2025Article
- Long noncoding RNAs regulating enzymatic reactions in cancer.Experimental & molecular medicine · 2025Review
- Exploring protein adenylyltransferase as a therapeutic target for combating ESKAPE pathogens in hospital-acquired infections.Molecular biology reports · 2025Review
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
Protein phosphorylation is one of the most widely observed and important post-translational modification (PTM) processes. Protein phosphorylation is regulated by protein kinases, each of which covalently attaches a phosphate group to an amino acid side chain on a serine (Ser), threonine (Thr), or tyrosine (Tyr) residue of a protein, and by protein phosphatases, each of which, conversely, removes a phosphate group from a phosphoprotein. These reversible enzyme activities provide a regulatory mechanism by activating or deactivating many diverse functions of proteins in various cellular processes. In this review, their structures and substrate recognition are described and summarized, focusing on Ser/Thr protein kinases and protein Ser/Thr phosphatases, and the regulation of protein structures by phosphorylation. The studies reviewed here and the resulting information could contribute to further structural, biochemical, and combined studies on the mechanisms of protein phosphorylation and to drug discovery approaches targeting protein kinases or protein phosphatases.
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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.