The DOI matches its Crossref record; 179 of the 179 references it cites were found in a registry or an index.
When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again
Open accessAbstract
In the past decade, increasing efforts have been devoted to the study of galectins, a family of evolutionarily conserved glycan-binding proteins with multifunctional properties. Galectins function, either intracellularly or extracellularly, as key biological mediators capable of monitoring changes occurring on the cell surface during fundamental biological processes such as cellular communication, inflammation, development, and differentiation. Their highly conserved structures, exquisite carbohydrate specificity, and ability to modulate a broad spectrum of biological processes have captivated a wide range of scientists from a wide spectrum of disciplines, including biochemistry, biophysics, cell biology, and physiology. However, in spite of enormous efforts to dissect the functions and properties of these glycan-binding proteins, limited information about how structural and biochemical aspects of these proteins can influence biological functions is available. In this review, we aim to integrate structural, biochemical, and functional aspects of this bewildering and ancient family of glycan-binding proteins and discuss their implications in physiologic and pathologic settings.
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Cites
The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity
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Galectins: A family of animal β-galactoside-binding lectins
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Self-citationNegative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation
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Galectin-1: a small protein with major functions
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Glycosylation in cancer: mechanisms and clinical implications
Pinho, S. S., & Reis, C. A. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3982 · Cited by 3,083
Nicolas, J., Magli, S., Rabbachin, L., Sampaolesi, S., Nicotra, F., & Russo, L. (2020) · Biomacromolecules · doi:10.1021/acs.biomac.0c00045 · Cited by 509
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
Freeman, D., Cedillos, R., Choyke, S., Lukic, Z., McGuire, K., Marvin, S., Burrage, A. M., Sudholt, S., Rana, A., O'Connor, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062143 · Cited by 289
Treatment options for alcoholic and non-alcoholic fatty liver disease: A review
Singh, S., Osna, N. A., & Kharbanda, K. K. (2017) · World Journal of Gastroenterology · doi:10.3748/wjg.v23.i36.6549 · Cited by 257
Metadata
- Authors
- Di Lella, S., Sundblad, V., Cerliani, J. P., Guardia, C. M., Estrin, D. A., Vasta, G. R., & Rabinovich, G. A.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-08-26
- Volume
- 50
- Issue
- 37
- Pages
- 7842-7857
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1967989660
- Cited by
- 282
- References
- 179
- FWCI
- 7.00
- Type
- journal article
- Language
- en
- Open access
- green
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- Di Lella, S., Sundblad, V., Cerliani, J. P., Guardia, C. M., Estrin, D. A., Vasta, G. R., & Rabinovich, G. A. (2011). When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again. Biochemistry. https://doi.org/10.1021/bi201121m
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