ReviewChemical Society reviews2023
Exploring multivalent carbohydrate-protein interactions by NMR.
Review in Chemical Society reviews, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 43 citations in OpenAlex.
- Targeting virus-glycan recognition in influenza viruses and coronaviruses: from the molecular principles to glycomimetic antivirals strategies.RSC chemical biology · 2026Review
- Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026Review
- Immune implications and therapeutic opportunities of tumor glycosylation.Nature cancer · 2026Review
- Fluorinated Glycan Frameshifts: Automated Synthesis Expedites the Study of Glycan-Protein Interactions byAngewandte Chemie (International ed. in English) · 2026Article
- The Impact of Methanol Concentration on Recombinant Protein Glycosylation in Pichia pastoris SuperMan5.Microbial biotechnology · 2025Article
- Deciphering the intermolecular interactions between G-quadruplex (G4)-forming sequences.Nucleic acids research · 2025Article
- Elucidation of the Synergistic Interaction Between Bilirubin and Casein Protein: An Integrated Spectroscopy and Computational Approach.Biomacromolecules · 2025Article
- Human Milk Oligosaccharides Multivalently Presented on Defined Synthetic Neo-Glycoproteins Are Nanomolar Ligands of Tandem-Repeat Galectins.Biomacromolecules · 2025Article
- Revisiting Proteus 2.0: Two Decades of Pioneering Lectin Crystallography at BioMol-Lab in Northeast Brazil.ACS omega · 2025Review
- Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Expression and immobilization of novel N-glycan-binding protein for highly efficient purification and enrichment of N-glycans, N-glycopeptides, and N-glycoproteins.Analytical and bioanalytical chemistry · 2024Article
- Quantifying Siglec-sialylated ligand interactions: a versatileChemical science · 2024Article
- Biophysical Assays for Investigating Modulators of Macromolecular Complexes: An Overview.ACS omega · 2024Review
- Dissecting the Conformational Stability of a Glycan Hairpin.Journal of the American Chemical Society · 2024Article
- A consensus structural motif for the capsular polysaccharide ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Speeding-up the Determination of Protein-Ligand Affinities by STD NMR: The Reduced Data Set STD NMR Approach (rd-STD NMR).Analytical chemistry · 2024Article
- Fluorinated ManJournal of the American Chemical Society · 2023Article
- Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection.Cellular & molecular immunology · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear Magnetic Resonance (NMR) has been widely employed to assess diverse features of glycan-protein molecular recognition events. Different types of qualitative and quantitative information at different degrees of resolution and complexity can be extracted from the proper application of the available NMR-techniques. In fact, affinity, structural, kinetic, conformational, and dynamic characteristics of the binding process are available. Nevertheless, except in particular cases, the affinity of lectin-sugar interactions is weak, mostly at the low mM range. This feature is overcome in biological processes by using multivalency, thus augmenting the strength of the binding. However, the application of NMR methods to monitor multivalent lectin-glycan interactions is intrinsically challenging. It is well known that when large macromolecular complexes are formed, the NMR signals disappear from the NMR spectrum, due to the existence of fast transverse relaxation, related to the large size and exchange features. Indeed, at the heart of the molecular recognition event, the associated free-bound chemical exchange process for both partners takes place in a particular timescale. Thus, these factors have to be considered and overcome. In this review article, we have distinguished, in a subjective manner, the existence of multivalent presentations in the glycan or in the lectin. From the glycan perspective, we have also considered whether multiple epitopes of a given ligand are presented in the same linear chain of a saccharide (
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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.