ReviewACS chemical biology2021
CH-π Interactions in Glycan Recognition.
Review in ACS chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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.
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Who cites it
40 citing papers in PubMed, 85 citations in OpenAlex.
- Structural and functional characterisation of the dextran utilisome fromJournal of structural biology: X · 2026Article
- Development of m6A Readers for Enhanced Recognition In Vitro via Genetic Code Expansion.ACS chemical biology · 2026Article
- Decoding Galectin-Glycan Recognition withJournal of the American Chemical Society · 2026Article
- Structural basis of lipid-linked galactan export by the mycobacterial ABC transporter Wzm-Wzt.Nature communications · 2026Article
- Reduced Processivity in a Chitobiohydrolase Enhances LPMO-Assisted Chitin Depolymerization.Biochemistry · 2026Article
- [Tripeptide polymer-based cell-imprinted hydrogels for high-efficiency circulating tumor cell capture].Se pu = Chinese journal of chromatography · 2026Article
- Conformational Preferences for N-Glycans at the Surface of CEACAM1-Ig1.ACS chemical biology · 2026Article
- Single-Molecule Discrimination of Multisialylated Ganglioside Oligosaccharides Using an Engineered Nanopore.Research (Washington, D.C.) · 2026Article
- Structural Basis for how Sialoglycan-binding Viridans Streptococci Accommodate Ligands that Exceed the Characterized Binding Site.microPublication biology · 2026Article
- Framework-mediated binding of foreign and self-glycans by IGHV4-34 antibodies.Frontiers in immunology · 2026Review
- Phage Display Reveals VLRB-Mediated Recognition of Minimal Tumor Glycan Antigen Sialyl-Tn.Current issues in molecular biology · 2025Article
- Influence of SARA Fractions on the Yield Stress of Heavy Oil.ACS omega · 2025Article
- Human Milk Oligosaccharides Multivalently Presented on Defined Synthetic Neo-Glycoproteins Are Nanomolar Ligands of Tandem-Repeat Galectins.Biomacromolecules · 2025Article
- Ionic Liquid-Modified Resorcinol Formaldehyde Resins: Synthesis and Applications to Methylene Blue Removal.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Molecular architecture and catalytic mechanism of human glycogen debranching enzyme.Nature communications · 2025Article
- Synthetic Mucins as Glycan-Defined Prebiotics.ACS central science · 2025Article
- Article
- The energetic landscape of CH-π interactions in protein-carbohydrate binding.Chemical science · 2025Article
- Epigenetic Regulation Via Electrical Forces.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Tools for structural lectinomics: From structures to lectomes.BBA advances · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Carbohydrate recognition is crucial for biological processes ranging from development to immune system function to host-pathogen interactions. The proteins that bind glycans are faced with a daunting task: to coax these hydrophilic species out of water and into a binding site. Here, we examine the forces underlying glycan recognition by proteins. Our previous bioinformatic study of glycan-binding sites indicated that the most overrepresented side chains are electron-rich aromatic residues, including tyrosine and tryptophan. These findings point to the importance of CH-π interactions for glycan binding. Studies of CH-π interactions show a strong dependence on the presence of an electron-rich π system, and the data indicate binding is enhanced by complementary electronic interactions between the electron-rich aromatic ring and the partial positive charge of the carbohydrate C-H protons. This electronic dependence means that carbohydrate residues with multiple aligned highly polarized C-H bonds, such as β-galactose, form strong CH-π interactions, whereas less polarized residues such as α-mannose do not. This information can guide the design of proteins to recognize sugars and the generation of ligands for proteins, small molecules, or catalysts that bind sugars.
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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.