The DOI matches its Crossref record; 162 of the 162 references it cites were found in a registry or an index.
Galectin-1: a small protein with major functions
Open accessAbstract
Galectins are a family of carbohydrate-binding proteins with an affinity for beta-galactosides. Galectin-1 (Gal-1) is differentially expressed by various normal and pathological tissues and appears to be functionally polyvalent, with a wide range of biological activity. The intracellular and extracellular activity of Gal-1 has been described. Evidence points to Gal-1 and its ligands as one of the master regulators of such immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host-pathogen interactions. Gal-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Gal-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Gal-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Gal-1 expression is what should be developed for therapeutic applications against cancer progression. Gal-1 is thus a promising molecular target for the development of new and original therapeutic tools.
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Cites
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Cited by
Hatori, M., Vollmers, C., Zarrinpar, A., DiTacchio, L., Bushong, E. A., Gill, S., Leblanc, M., Chaix, A., Joens, M., Fitzpatrick, J. A. J., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.019 · Cited by 1,986
Inside, outside, upside down: damage-associated molecular-pattern molecules (DAMPs) and redox
Rubartelli, A., & Lotze, M. T. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.08.004 · Cited by 614
Glycomimetics versus Multivalent Glycoconjugates for the Design of High Affinity Lectin Ligands
Cecioni, S., Imberty, A., & Vidal, S. (2015) · Chemical Reviews · doi:10.1021/cr500303t · Cited by 544
A novel microglial subset plays a key role in myelinogenesis in developing brain
Wlodarczyk, A., Holtman, I. R., Krueger, M., Yogev, N., Bruttger, J., Khorooshi, R., Benmamar‐Badel, A., de Boer‐Bergsma, J. J., Martin, N. A., Karram, K., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201696056 · Cited by 535
Sato, S., St‐Pierre, C., Bhaumik, P., & Nieminen, J. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2009.00790.x · Cited by 299
Metadata
- Authors
- Camby, I., Le Mercier, M., Lefranc, F., & Kiss, R.
- Venue
- Glycobiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-07-13
- Volume
- 16
- Issue
- 11
- Pages
- 137R-157R
- ISSN
- 0959-6658 (ISSN-L)
- 1460-2423
- OpenAlex
- W2157672076
- Cited by
- 893
- References
- 162
- FWCI
- 14.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
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