ArticleBioconjugate chemistry2019
Multivalent Cluster Nanomolecules for Inhibiting Protein-Protein Interactions.
Article in Bioconjugate chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Utilizing Light to Control Glycopolymer-DC-SIGN Interactions via Molecular Motors.Journal of the American Chemical Society · 2026Article
- Atomically Precise Polyanionic Boron Cluster Agents with Broad-Spectrum Antiviral Activity.Precision chemistry · 2026Article
- Emerging drug design strategies in anti-influenza drug discovery.Acta pharmaceutica Sinica. B · 2023Review
- Single─Not Double─3D-Aromaticity in an OxidizedJournal of the American Chemical Society · 2023Article
- Identification of hot regions in hub protein-protein interactions by clustering and PPRA optimization.BMC medical informatics and decision making · 2021Article
- Gold(III) Aryl Complexes as Reagents for Constructing Hybrid Peptide-Based Assemblies via CysteineInorganic chemistry · 2021Article
- Sulfoglycodendrimer Therapeutics for HIV-1 and SARS-CoV-2.Advanced therapeutics · 2021Article
- An Organometallic Strategy for Assembling Atomically Precise Hybrid Nanomaterials.Journal of the American Chemical Society · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Multivalent protein-protein interactions serve central roles in many essential biological processes, ranging from cell signaling and adhesion to pathogen recognition. Uncovering the rules that govern these intricate interactions is important not only to basic biology and chemistry but also to the applied sciences where researchers are interested in developing molecules to promote or inhibit these interactions. Here we report the synthesis and application of atomically precise inorganic cluster nanomolecules consisting of an inorganic core and a covalently linked densely packed layer of saccharides. These hybrid agents are stable under biologically relevant conditions and exhibit multivalent binding capabilities, which enable us to study the complex interactions between glycosylated structures and a dendritic cell lectin receptor. Importantly, we find that subtle changes in the molecular structure lead to significant differences in the nanomolecule's protein-binding properties. Furthermore, we demonstrate an example of using these hybrid nanomolecules to effectively inhibit protein-protein interactions in a human cell line. Ultimately, this work reveals an intricate interplay between the structural design of multivalent agents and their biological activities toward protein surfaces.
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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.