The DOI matches its Crossref record; 178 of the 178 references it cites were found in a registry or an index.
The galectin lattice at a glance
Abstract
Galectins are a family of widely expressed β-galactoside-binding lectins in metazoans. The 15 mammalian galectins have either one or two conserved carbohydrate recognition domains (CRDs), with galectin-3 being able to pentamerize; they form complexes that crosslink glycosylated ligands to form a dynamic lattice. The galectin lattice regulates the diffusion, compartmentalization and endocytosis of plasma membrane glycoproteins and glycolipids. The galectin lattice also regulates the selection, activation and arrest of T cells, receptor kinase signaling and the functionality of membrane receptors, including the glucagon receptor, glucose and amino acid transporters, cadherins and integrins. The affinity of transmembrane glycoproteins to the galectin lattice is proportional to the number and branching of their N-glycans; with branching being mediated by Golgi N-acetylglucosaminyltransferase-branching enzymes and the supply of UDP-GlcNAc through metabolite flux through the hexosamine biosynthesis pathway. The relative affinities of glycoproteins for the galectin lattice depend on the activities of the Golgi enzymes that generate the epitopes of their ligands and, thus, provide a means to analyze biological function of lectins and of the ‘glycome’ more broadly.
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1 retracted
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Self-citation
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Schjoldager, K. T., Narimatsu, Y., Joshi, H. J., & Clausen, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00294-x · Cited by 1,309
Galectin-3 Coordinates a Cellular System for Lysosomal Repair and Removal
Jia, J., Claude-Taupin, A., Gu, Y., Choi, S. W., Peters, R., Bissa, B., Mudd, M. H., Allers, L., Pallikkuth, S., Lidke, K. A., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2019.10.025 · Cited by 434
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Regulation of Transmembrane Signaling by Phase Separation
Case, L. B., Ditlev, J. A., & Rosen, M. K. (2019) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115534 · Cited by 303
The therapeutic potential of galectin-3 inhibition in fibrotic disease
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Metadata
- Authors
- Nabi, I. R., Shankar, J., & Dennis, J. W.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2015-07-01
- Volume
- 128
- Issue
- 13
- Pages
- 2213-2219
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2097954680
- Cited by
- 329
- References
- 178
- FWCI
- 11.27
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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