ArticleThe Biochemical journal2018
New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors.
Article in The Biochemical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 72 citations in OpenAlex.
- Probing sulfotransferase binding and inhibition with synthetic PAPS analogs reveals the role of the 3'-phosphate and informs molecular tool design.RSC chemical biology · 2026Article
- Comprehensive analysis of neutrophil extracellular traps-associated inflammatory genes for patients with idiopathic pulmonary fibrosis.Molecular genetics and genomics : MGG · 2026Article
- Structural characterization of metal binding in human tyrosylprotein sulfotransferase 2, TPST2.Scientific reports · 2026Article
- A Bacterial Sulfotransferase Catalyzes an Unusual Di-Sulfation in Natural Products Biosynthesis.Chembiochem : a European journal of chemical biology · 2025Article
- Searching for Sulfotyrosines (sY) in a HA(pY)STACK.Journal of proteome research · 2025Article
- Polysaccharide sulfotransferases: the identification of putative sequences and respective functional characterisation.Essays in biochemistry · 2024Review
- Chemical approaches to the sulfation of small molecules: current progress and future directions.Essays in biochemistry · 2024Review
- Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.Journal of proteome research · 2023Article
- Enhanced tyrosine sulfation is associated with chronic kidney disease-related atherosclerosis.BMC biology · 2023Article
- From Steroid and Drug Metabolism to Glycobiology, Using Sulfotransferase Structures to Understand and Tailor Function.Drug metabolism and disposition: the biological fate of chemicals · 2022Review
- Fluorinated Phosphoadenosine 5'-Phosphosulfate Analogues for Continuous Sulfotransferase Activity Monitoring and Inhibitor Screening byACS chemical biology · 2022Article
- Exploring the Conformational Landscape and Stability of Aurora A Using Ion-Mobility Mass Spectrometry and Molecular Modeling.Journal of the American Society for Mass Spectrometry · 2022Article
- Biochemical Analysis of AKAP-Anchored PKA Signaling Complexes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Mobility shift-based electrophoresis coupled with fluorescent detection enables real-time enzyme analysis of carbohydrate sulfatase activity.The Biochemical journal · 2021Article
- Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification.Biosensors · 2020Article
- Use of the Polo-like kinase 4 (PLK4) inhibitor centrinone to investigate intracellular signalling networks using SILAC-based phosphoproteomics.The Biochemical journal · 2020Article
- Emerging patterns of tyrosine sulfation and O-glycosylation cross-talk and co-localization.Current opinion in structural biology · 2020Review
- Covalent Aurora A regulation by the metabolic integrator coenzyme A.Redox biology · 2020Article
- Structure-based design of nucleoside-derived analogues as sulfotransferase inhibitors.RSC advances · 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
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein tyrosine sulfation is a post-translational modification best known for regulating extracellular protein-protein interactions. Tyrosine sulfation is catalysed by two Golgi-resident enzymes termed tyrosylprotein sulfotransferases (TPSTs) 1 and 2, which transfer sulfate from the cofactor PAPS (3'-phosphoadenosine 5'-phosphosulfate) to a context-dependent tyrosine in a protein substrate. A lack of quantitative tyrosine sulfation assays has hampered the development of chemical biology approaches for the identification of small-molecule inhibitors of tyrosine sulfation. In the present paper, we describe the development of a non-radioactive mobility-based enzymatic assay for TPST1 and TPST2, through which the tyrosine sulfation of synthetic fluorescent peptides can be rapidly quantified. We exploit ligand binding and inhibitor screens to uncover a susceptibility of TPST1 and TPST2 to different classes of small molecules, including the anti-angiogenic compound suramin and the kinase inhibitor rottlerin. By screening the Published Kinase Inhibitor Set, we identified oxindole-based inhibitors of the Ser/Thr kinase RAF (rapidly accelerated fibrosarcoma) as low-micromolar inhibitors of TPST1 and TPST2. Interestingly, unrelated RAF inhibitors, exemplified by the dual BRAF/VEGFR2 inhibitor RAF265, were also TPST inhibitors
Indexed as
Identifiers
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.