ArticleMolecules (Basel, Switzerland)2017
Lactose Binding Induces Opposing Dynamics Changes in Human Galectins Revealed by NMR-Based Hydrogen-Deuterium Exchange.
Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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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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
9 citing papers in PubMed, 15 citations in OpenAlex.
- Discovery ofACS medicinal chemistry letters · 2023Article
- Design and synthesis of novel 3-triazolyl-1-thiogalactosides as galectin-1, -3 and -8 inhibitors.RSC advances · 2022Article
- Chemokines modulate glycan binding and the immunoregulatory activity of galectins.Communications biology · 2021Article
- Site-Specific Cross-Linking of Galectin-1 Homodimers via Poly(ethylene glycol) Bismaleimide.Cellular and molecular bioengineering · 2021Article
- Unravelling the Time Scale of Conformational Plasticity and Allostery in Glycan Recognition by Human Galectin-1.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Enzyme dynamics: Looking beyond a single structure.ChemCatChem · 2020Article
- Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Exploring functional pairing between surface glycoconjugates and human galectins using programmable glycodendrimersomes.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Dissecting the Structure-Activity Relationship of Galectin-Ligand Interactions.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Galectins are β-galactoside-binding proteins implicated in a myriad of biological functions. Despite their highly conserved carbohydrate binding motifs with essentially identical structures, their affinities for lactose, a common galectin inhibitor, vary significantly. Here, we aimed to examine the molecular basis of differential lactose affinities amongst galectins using solution-based techniques. Consistent dissociation constants of lactose binding were derived from nuclear magnetic resonance (NMR) spectroscopy, intrinsic tryptophan fluorescence, isothermal titration calorimetry and bio-layer interferometry for human galectin-1 (hGal1), galectin-7 (hGal7), and the N-terminal and C-terminal domains of galectin-8 (hGal8
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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.