Results 21 to 30 of about 43,794 (228)

Computational Study of Potential Galectin-3 Inhibitors in the Treatment of COVID-19

open access: yesBiomedicines, 2021
Galectin-3 is a carbohydrate-binding protein and the most studied member of the galectin family. It regulates several functions throughout the body, among which are inflammation and post-injury remodelling.
Maral Aminpour   +12 more
doaj   +1 more source

Characterization of Galectin Fusion Proteins with Glycoprotein Affinity Columns and Binding Assays

open access: yesMolecules, 2023
Galectins are β-galactosyl-binding proteins that fulfill essential physiological functions. In the biotechnological field, galectins are versatile tools, such as in the development of biomaterial coatings or the early-stage diagnosis of cancer diseases ...
Carina Dey, Philip Palm, Lothar Elling
doaj   +1 more source

The two endocytic pathways mediated by the carbohydrate recognition domain and regulated by the collagen-like domain of galectin-3 in vascular endothelial cells. [PDF]

open access: yesPLoS ONE, 2012
Galectin-3 plays an important role in endothelial morphogenesis and angiogenesis. We investigated the endocytosis of galectin-3 in human vascular endothelial cells and showed that galectin-3 could associate with and internalized into the cells in a ...
Xiaoge Gao   +7 more
doaj   +1 more source

Binding Characteristics of Galectin-3 Fusion Proteins [PDF]

open access: yesGlycobiology, 2017
Galectin-3 modulates cell adhesion and signaling events by specific binding and cross-linking galactoside containing carbohydrate ligands. Proteolytic cleavage by metalloproteinases yields in vivo N-terminally truncated galectin-3 still bearing the carbohydrate recognition domain.
Sophia, Böcker, Lothar, Elling
openaire   +2 more sources

Galectin-3 Is a Natural Binding Ligand of MCAM (CD146, MUC18) in Melanoma Cells and Their Interaction Promotes Melanoma Progression

open access: yesBiomolecules, 2022
Melanoma cell adhesion molecule (MCAM, CD146, MUC18) is a heavily glycosylated transmembrane protein and a marker of melanoma metastasis. It is expressed in advanced primary melanoma and metastasis but rarely in benign naevi or normal melanocytes.
Yaoyu Pang   +6 more
doaj   +1 more source

TNBC-derived Gal3BP/Gal3 complex induces immunosuppression through CD45 receptor

open access: yesOncoImmunology, 2023
A preliminary study investigating immunotherapy strategies for aggressive triple negative breast cancer (TNBC) revealed an overexpression of genes involved in the release of extracellular vesicles (EVs).
Annat Raiter   +4 more
doaj   +1 more source

A Synthetic Tetramer of Galectin-1 and Galectin-3 Amplifies Pro-apoptotic Signaling by Integrating the Activity of Both Galectins

open access: yesFrontiers in Chemistry, 2020
Galectin-1 (G1) and galectin-3 (G3) are carbohydrate-binding proteins that can signal apoptosis in T cells. We recently reported that a synthetic tetramer with two G1 and two G3 domains (“G1/G3 Zipper”) induces Jurkat T cell death more potently than G1 ...
Shaheen A. Farhadi   +3 more
doaj   +1 more source

Intracellular galectin-3 is a lipopolysaccharide sensor that promotes glycolysis through mTORC1 activation

open access: yesNature Communications, 2022
The carbohydrate binding protein galectin-3 has been linked to diabetes and cancer. Here, authors show that galectin-3 is a sensor of LPS, an important modulator of the mTORC1 signaling, and a critical regulator of glucose metabolism.
Xing Chen   +14 more
doaj   +1 more source

Galectin-3 promotes secretion of proteases that decrease epithelium integrity in human colon cancer cells

open access: yesCell Death and Disease, 2023
Galectin-3 is a galactoside-binding protein that is commonly overexpressed in many epithelial cancers. It is increasingly recognized as a multi-functional, multi-mode promoter in cancer development, progression, and metastasis.
Shun Li   +2 more
doaj   +1 more source

Human T cell glycosylation and implications on immune therapy for cancer [PDF]

open access: yes, 2020
Glycosylation is an important post-translational modification, giving rise to a diverse and abundant repertoire of glycans on the cell surface, collectively known as the glycome.
Callewaert, Nico   +3 more
core   +1 more source

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