ReviewFrontiers in molecular biosciences2021
NMR Characterization of the Interactions Between Glycosaminoglycans and Proteins.
Review in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Comparison of Protein-Glycosaminoglycan Interactions in ff14sb/GLYCAM06j-1 and CHARMM36m Force Fields.Journal of chemical information and modeling · 2026Article
- Structure-Encoded Location Biased Signaling in a Class B GPCR: Focus on the PTH Type 1 Receptor.Handbook of experimental pharmacology · 2026Review
- Group A Streptococcus interacts with glycosaminoglycans via M proteins to modulate bacterial adherence in vitro.The FEBS journal · 2025Article
- Fast-diffusing receptor collisions with slow-diffusing peptide ligand assemble the ternary parathyroid hormone-GPCR-arrestin complex.Nature communications · 2024Article
- Identification of heparin-binding amino acid residues in antibody HS4C3 with the potential to design antibodies against heparan sulfate domains.Glycobiology · 2024Article
- Deciphering the role of glycosaminoglycans in GPCR signaling.Cellular signalling · 2024Review
- Heparin Oligosaccharides as Vasoactive Intestinal Peptide Inhibitors via their Binding Process Characterization.Current protein & peptide science · 2024Article
- Solvent Model Benchmark for Molecular Dynamics of Glycosaminoglycans.Journal of chemical information and modeling · 2023Article
- Glycosaminoglycans: What Remains To Be Deciphered?JACS Au · 2023Review
- Studying specificity in protein-glycosaminoglycan recognition with umbrella sampling.Beilstein journal of organic chemistry · 2023Article
- Modeling Protein-Glycosaminoglycan Complexes: Does the Size Matter?Journal of chemical information and modeling · 2021Article
- Advanced Molecular Dynamics Approaches to Model a Tertiary Complex APRIL/TACI with Long Glycosaminoglycans.Biomolecules · 2021Article
- Semaphorin 3A-Glycosaminoglycans Interaction as Therapeutic Target for Axonal Regeneration.Pharmaceuticals (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosaminoglycans (GAGs) constitute a considerable fraction of the glycoconjugates found on cellular membranes and in the extracellular matrix of virtually all mammalian tissues. The essential role of GAG-protein interactions in the regulation of physiological processes has been recognized for decades. However, the underlying molecular basis of these interactions has only emerged since 1990s. The binding specificity of GAGs is encoded in their primary structures, but ultimately depends on how their functional groups are presented to a protein in the three-dimensional space. This review focuses on the application of NMR spectroscopy on the characterization of the GAG-protein interactions. Examples of interpretation of the complex mechanism and characterization of structural motifs involved in the GAG-protein interactions are given. Selected families of GAG-binding proteins investigated using NMR are also described.
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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 Socratic graph.