ArticleProceedings of the National Academy of Sciences of the United States of America2017
Predicting glycosaminoglycan surface protein interactions and implications for studying axonal growth.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. 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, 35 citations in OpenAlex.
- The p.(Leu97Ile) variant expands the genetic landscape of NEFL-associated Charcot-Marie-tooth neuropathies.Human molecular genetics · 2026Article
- Unraveling the Potential of Small Molecule Heparin Glycomimetics in Neuroregenerative Therapeutics.Journal of the American Chemical Society · 2025Article
- Structural Insights into Endostatin-Heparan Sulfate Interactions Using Modeling Approaches.Molecules (Basel, Switzerland) · 2024Article
- Hindbrain boundaries as niches of neural progenitor and stem cells regulated by the extracellular matrix proteoglycan chondroitin sulphate.Development (Cambridge, England) · 2024Article
- Novel Genetic and Biochemical Insights into the Spectrum of NEFL-Associated Phenotypes.Journal of neuromuscular diseases · 2024Review
- Assessing Genetic Algorithm-Based Docking Protocols for Prediction of Heparin Oligosaccharide Binding Geometries onto Proteins.Biomolecules · 2023Article
- Tools for mammalian glycoscience research.Cell · 2022Review
- Article
- A Bittersweet Computational Journey among Glycosaminoglycans.Biomolecules · 2021Review
- Sulfated glycans engage the Ang-Tie pathway to regulate vascular development.Nature chemical biology · 2021Article
- Chondroitin Sulfate/Dermatan Sulfate-Protein Interactions and Their Biological Functions in Human Diseases: Implications and Analytical Tools.Frontiers in cell and developmental biology · 2021Review
- Glycosaminoglycan-Protein Interactions and Their Roles in Human Disease.Frontiers in molecular biosciences · 2021Review
- Three-Dimensional Structures of Carbohydrates and Where to Find Them.International journal of molecular sciences · 2020Review
- Photoaffinity Probes for the Identification of Sequence-Specific Glycosaminoglycan-Binding Proteins.Journal of the American Chemical Society · 2020Article
- Operation spinal cord regeneration: Patterning information residing in extracellular matrix glycosaminoglycans.Brain and behavior · 2020Review
- Age-related functional changes of total thyroid hormones and glycosaminoglycans in growing calves.Veterinary world · 2019Article
- Glycosaminoglycan-Protein Interactions by Nuclear Magnetic Resonance (NMR) Spectroscopy.Molecules (Basel, Switzerland) · 2018Review
- Perspectives on "the biology of spinal cord regeneration success and failure".Neural regeneration research · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cell-surface carbohydrates play important roles in numerous biological processes through their interactions with various protein-binding partners. These interactions are made possible by the vast structural diversity of carbohydrates and the diverse array of carbohydrate presentations on the cell surface. Among the most complex and important carbohydrates are glycosaminoglycans (GAGs), which display varied stereochemistry, chain lengths, and patterns of sulfation. GAG-protein interactions participate in neuronal development, angiogenesis, spinal cord injury, viral invasion, and immune response. Unfortunately, little structural information is available for these complexes; indeed, for the highly sulfated chondroitin sulfate motifs, CS-E and CS-D, there are no structural data. We describe here the development and validation of the GAG-Dock computational method to predict accurately the binding poses of protein-bound GAGs. We validate that GAG-Dock reproduces accurately (<1-Å rmsd) the crystal structure poses for four known heparin-protein structures. Further, we predict the pose of heparin and chondroitin sulfate derivatives bound to the axon guidance proteins, protein tyrosine phosphatase σ (RPTPσ), and Nogo receptors 1-3 (NgR1-3). Such predictions should be useful in understanding and interpreting the role of GAGs in neural development and axonal regeneration after CNS injury.
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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.