ArticleACS chemical biology2012
Noncarbohydrate glycomimetics and glycoprotein surrogates as DC-SIGN antagonists and agonists.
Article in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
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Who cites it
21 citing papers in PubMed, 52 citations in OpenAlex.
- Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026Review
- Lewis-X-Containing Triterpenoid Saponins Inhibit DC-SIGN- and L-SIGN-Mediated Transfer of HIV-1 Infection.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Glycomimetics for the inhibition and modulation of lectins.Chemical Society reviews · 2023Review
- The multiple roles of C-type lectin receptors in cancer.Frontiers in oncology · 2023Review
- Review
- A Remote Secondary Binding Pocket Promotes Heteromultivalent Targeting of DC-SIGN.Journal of the American Chemical Society · 2021Article
- Glycan Epitopes and Potential Glycoside Antagonists of DC-SIGN Involved in COVID-19: In Silico Study.Biomolecules · 2021Article
- Article
- Molecular Recognition in C-Type Lectins: The Cases of DC-SIGN, Langerin, MGL, and L-Sectin.Chembiochem : a European journal of chemical biology · 2020Review
- A mimetic peptide of α2,6-sialyllactose promotes neuritogenesis.Neural regeneration research · 2020Article
- Enhancing Potency and Selectivity of a DC-SIGN Glycomimetic Ligand by Fragment-Based Design: Structural Basis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Antigen structure affects cellular routing through DC-SIGN.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The polysialic acid mimetics idarubicin and irinotecan stimulate neuronal survival and neurite outgrowth and signal via protein kinase C.Journal of neurochemistry · 2017Article
- Pseudo-Mannosylated DC-SIGN Ligands as Immunomodulants.Scientific reports · 2016Article
- "Rules of Engagement" of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling.ChemistryOpen · 2016Review
- Biomimetic and synthetic interfaces to tune immune responses.Biointerphases · 2015Review
- Chemical Lectinology: Tools for Probing the Ligands and Dynamics of Mammalian Lectins In Vivo.Chemistry & biology · 2015Review
- Simultaneous dual protein labeling using a triorthogonal reagent.Journal of the American Chemical Society · 2013Article
- Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR protein reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.The Journal of biological chemistry · 2013Article
- Glycopolymer probes of signal transduction.Chemical Society reviews · 2013Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
An understanding of the biological roles of lectins will be advanced by ligands that can inhibit or even recruit lectin function. To this end, glycomimetics, noncarbohydrate ligands that function analogously to endogenous carbohydrates, are being sought. The advantage of having such ligands is illustrated by the many roles of the protein DC-SIGN. DC-SIGN is a C-type lectin displayed on dendritic cells, where it binds to mannosides and fucosides to mediate interactions with other host cells or bacterial or viral pathogens. DC-SIGN engagement can modulate host immune responses (e.g., suppress autoimmunity) or benefit pathogens (e.g., promote HIV dissemination). DC-SIGN can bind to glycoconjugates, internalize glycosylated cargo for antigen processing, and transduce signals. DC-SIGN ligands can serve as inhibitors as well as probes of the lectin's function, so they are especially valuable for elucidating and controlling DC-SIGN's roles in immunity. We previously reported a small molecule that embodies key features of the carbohydrates that bind DC-SIGN. Here, we demonstrate that this noncarbohydrate ligand acts as a true glycomimetic. Using NMR HSQC experiments, we found that the compound mimics saccharide ligands: It occupies the same carbohydrate-binding site and interacts with the same amino acid residues on DC-SIGN. The glycomimetic also is functional. It had been shown previously to antagonize DC-SIGN function, but here we use it to generate DC-SIGN agonists. Specifically, appending this glycomimetic to a protein scaffold affords a conjugate that elicits key cellular signaling responses. Thus, the glycomimetic can give rise to functional glycoprotein surrogates that elicit lectin-mediated signaling.
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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.