ArticleBeilstein journal of organic chemistry2015
Glycodendrimers: tools to explore multivalent galectin-1 interactions.
Article in Beilstein journal of organic chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 24 citations in OpenAlex.
- Disaccharide-Presenting Iron(II) Complexes as Synthetic Mimics of Natural Glycan Epitopes for Lectin Recognition.Inorganic chemistry · 2026Article
- Lactose-Functionalized Carbosilane Glycodendrimers Are Highly Potent Multivalent Ligands for Galectin-9 Binding: Increased Glycan Affinity to Galectins Correlates with Aggregation Behavior.Biomacromolecules · 2023Article
- Synthesis, binding affinity, and inhibitory capacity of cyclodextrin-based multivalent glycan ligands for human galectin-3.Bioorganic & medicinal chemistry · 2022Article
- Homo- and Heterogeneous Glycoconjugates on the Basis ofMolecules (Basel, Switzerland) · 2022Review
- Nanoparticles To Study Lectins inBiomacromolecules · 2021Article
- Synthesis of Galectin Inhibitors by Regioselective 3'-Molecules (Basel, Switzerland) · 2020Article
- Protein Aggregation Nucleated by Functionalized Dendritic Polyglycerols.Polymer chemistry · 2020Article
- The Role of Galectin-1 in Cancer Progression, and Synthetic Multivalent Systems for the Study of Galectin-1.International journal of molecular sciences · 2016Review
- Engineering galectin-glycan interactions for immunotherapy and immunomodulation.Experimental biology and medicine (Maywood, N.J.) · 2016Review
- Multivalency as a chemical organization and action principle.Beilstein journal of organic chemistry · 2015Article
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
Four generations of lactose-functionalized polyamidoamine (PAMAM) were employed to further the understanding of multivalent galectin-1 mediated interactions. Dynamic light scattering and fluorescence microscopy were used to study the multivalent interaction of galectin-1 with the glycodendrimers in solution, and glycodendrimers were observed to organize galectin-1 into nanoparticles. In the presence of a large excess of galectin-1, glycodendrimers nucleated galectin-1 into nanoparticles that were remarkably homologous in size (400-500 nm). To understand augmentation of oncologic cellular aggregation by galectin-1, glycodendrimers were used in cell-based assays with human prostate carcinoma cells (DU145). The results revealed that glycodendrimers provided competitive binding sites for galectin-1, which diverted galectin-1 from its typical function in cellular aggregation of DU145 cells.
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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.