ReviewBritish journal of pharmacology2014
The structural role of receptor tyrosine sulfation in chemokine recognition.
Review in British journal of pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
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Who cites it
67 citing papers in PubMed.
- Evasins: Biology and Therapeutic Potential of Broad-Spectrum Chemokine Inhibitors.Basic & clinical pharmacology & toxicology · 2026Review
- Discovery of a sulfotyrosine-motif in the human TrkB extracellular domain required for agonist activation.bioRxiv : the preprint server for biology · 2026Article
- Biomechanical signaling of cytoskeleton and membrane reorganization in tumor immune chemotactic migration.Theranostics · 2026Review
- Deciphering the Interlinked CXCR4-Mediated Feedback Loop Among Signaling Pathways in Diabetic Wound Healing.Current diabetes reviews · 2026Review
- Filamentous chemokine CCL5 structure and the functional aspects.Scientific reports · 2025Article
- Selection Pressure Regulates the Evolution-Structure-Function Paradigm of Monocyte Chemoattractant Protein Family.Journal of molecular evolution · 2025Article
- Chemokine Receptor N-Terminus Charge Dictates Reliance on Post-Translational Modifications for Effective Ligand Capture and Following Boosting by Defense Peptides.International journal of molecular sciences · 2024Article
- Leveraging Tunable Nanoparticle Surface Functionalization to Alter Cellular Migration.ACS nanoscience Au · 2024Article
- CX3CL1 (Fractalkine)-CX3CR1 Axis in Inflammation-Induced Angiogenesis and Tumorigenesis.International journal of molecular sciences · 2024Review
- Sulfated CXCR3 Peptide Trap Use as a Promising Therapeutic Approach for Age-Related Macular Degeneration.Biomedicines · 2024Article
- Arylsulfatases and neuraminidases modulate engagement of CCR5 by chemokines by removing key electrostatic interactions.Scientific reports · 2024Article
- Structural basis of antibody inhibition and chemokine activation of the human CC chemokine receptor 8.Nature communications · 2023Article
- Fluorosulfate as a Latent Sulfate in Peptides and Proteins.Journal of the American Chemical Society · 2023Article
- NMR indicates the N-termini of PSGL1 and CCR7 bind competitively to the chemokine CCL21.Biochemistry and biophysics reports · 2023Article
- Chemokine binding to PSGL-1 is controlled by O-glycosylation and tyrosine sulfation.Cell chemical biology · 2023Article
- A lentiviral vector B cell gene therapy platform for the delivery of the anti-HIV-1 eCD4-Ig-knob-in-hole-reversed immunoadhesin.Molecular therapy. Methods & clinical development · 2023Article
- "Glyco-sulfo barcodes" regulate chemokine receptor function.Cellular and molecular life sciences : CMLS · 2023Article
- Emerging roles of a chemoattractant receptor GPR15 and ligands in pathophysiology.Frontiers in immunology · 2023Review
- TPST2-mediated receptor tyrosine sulfation enhances leukocidin cytotoxicity andFrontiers in immunology · 2023Article
- Unleashing the potential of noncanonical amino acid biosynthesis to create cells with precision tyrosine sulfation.Nature communications · 2022Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosine sulfation is a post-translational modification of secreted and transmembrane proteins, including many GPCRs such as chemokine receptors. Most chemokine receptors contain several potentially sulfated tyrosine residues in their extracellular N-terminal regions, the initial binding site for chemokine ligands. Sulfation of these receptors increases chemokine binding affinity and potency. Although receptor sulfation is heterogeneous, insights into the molecular basis of sulfotyrosine (sTyr) recognition have been obtained using purified, homogeneous sulfopeptides corresponding to the N-termini of chemokine receptors. Receptor sTyr residues bind to a shallow cleft defined by the N-loop and β3-strand elements of cognate chemokines. Tyrosine sulfation enhances the affinity of receptor peptides for cognate chemokines in a manner dependent on the position of sulfation. Moreover, tyrosine sulfation can alter the selectivity of receptor peptides among several cognate chemokines for the same receptor. Finally, binding to receptor sulfopeptides can modulate the oligomerization state of chemokines, thereby influencing the ability of a chemokine to activate its receptor. These results increase the motivation to investigate the structural basis by which tyrosine sulfation modulates chemokine receptor activity and the biological consequences of this functional modulation.
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