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1-5 of 5
Keywords: Galectin
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Journal Articles
Journal:
Journal of Cell Science
J Cell Sci (2018) 131 (9): jcs208884.
Published: 1 May 2018
...Ludger Johannes; Ralf Jacob; Hakon Leffler ABSTRACT Galectins are carbohydrate-binding proteins that are involved in many physiological functions, such as inflammation, immune responses, cell migration, autophagy and signalling. They are also linked to diseases such as fibrosis, cancer and heart...
Includes: Supplementary data
Journal Articles
Sarah E. Stewart, Sam A. Menzies, Stephanie J. Popa, Natalia Savinykh, Anna Petrunkina Harrison, Paul J. Lehner, Kevin Moreau
Journal:
Journal of Cell Science
J Cell Sci (2017) 130 (19): 3234–3247.
Published: 1 October 2017
...Sarah E. Stewart; Sam A. Menzies; Stephanie J. Popa; Natalia Savinykh; Anna Petrunkina Harrison; Paul J. Lehner; Kevin Moreau ABSTRACT Galectins are a family of lectin binding proteins expressed both intracellularly and extracellularly. Galectin-3 (Gal-3, also known as LGALS3) is expressed...
Includes: Supplementary data
Journal Articles
Journal:
Journal of Cell Science
J Cell Sci (2015) 128 (13): 2213–2219.
Published: 1 July 2015
...Ivan R. Nabi; Jay Shankar; James W. Dennis 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...
Includes: Supplementary data
Journal Articles
Journal:
Journal of Cell Science
J Cell Sci (2014) 127 (20): 4457–4469.
Published: 15 October 2014
... membrane through a transcytotic pathway mediated by the plus-end kinesin KIF16B. Here, we demonstrate that this apical transcytotic pathway requires apical sorting of basolateral proteins, which is mediated by apical signals and galectin-4. Using RPE and KPT cell lines, and AP-1B-knockdown MDCK cells, we...
Includes: Supplementary data
Journal Articles
Journal:
Journal of Cell Science
J Cell Sci (2003) 116 (7): 1305–1318.
Published: 1 April 2003
... receptor for galectin-1, as both soluble and membrane-associated fragments of CA125 derived from HeLa cell lysates are shown to bind specifically to human galectin-1 with high efficiency. This interaction is demonstrated (1) to depend on β-galactose-terminated, O-linked oligosaccharide chains of CA125, (2...