Results 1 to 10 of about 11,605 (209)
Molecules, 2021 Potent, cell-permeable, and subtype-selective sialyltransferase inhibitors represent an attractive family of substances that can potentially be used for the clinical treatment of cancer metastasis.
Chih-Wei Fu +2 more
exaly +4 more sources
Sulfonylurea Bioisosteres of Sulfonic Acid in JFD 00458-Based ST6GAL1 Inhibitors Enhance Membrane Permeability. [PDF]
ChemMedChemST6GAL1 sialylates glycoconjugates in the Golgi, modulating immune recognition and enabling tumor immune evasion. To effectively reach ST6GAL1, inhibitors should demonstrate good membrane permeability. Based on nonpermeable hit JFD 00458, we developed sulfonylurea analogs achieving increased membrane permeability and potency.
Koraj N +9 more
europepmc +2 more sources
Protein O-Glycosylation Shapes Lymphatic Endothelia and Lymph Node Macrophage Populations. [PDF]
FASEB JTo study the functional roles of O‐glycans on lymphatic endothelia, we deleted Cosmc, the chaperone required for core‐1 O‐glycan synthesis. Loss of core‐1 O‐glycans entailed major changes in glycoprotein composition of lymphatic endothelial cells (LEC), including reduced podoplanin (Pdpn), CD44, and Lyve‐1, and increased ICAM‐1; reduced CD44 was caused
Frey J +11 more
europepmc +2 more sources
ST6Gal1: Oncogenic signaling pathways and targets
Frontiers in Molecular Biosciences, 2022 The Golgi-sialyltransferase ST6Gal1 (βgalactosidase α2,6 sialyltransferase 1), adds the negatively charged sugar, sialic acid, to the terminal galactose of N-glycosylated proteins.
Sajina GC +2 more
doaj +1 more source
Multi-Faceted Effects of ST6Gal1 Expression on Precursor B-Lineage Acute Lymphoblastic Leukemia
Frontiers in Oncology, 2022 Normal early human B-cell development from lymphoid progenitors in the bone marrow depends on instructions from elements in that microenvironment that include stromal cells and factors secreted by these cells including the extracellular matrix ...
Mingfeng Zhang +5 more
doaj +1 more source
An efficient and robust HPLC method to determine the sialylation levels of human epithelial cells.
PLoS ONE, 2022 Sialyltransferase, an enzyme responsible for attaching sialic acid to the cell surface, is reported to play a key role in cancer, making sialyltransferase a potential therapeutic target in drug development. Several methods have been developed to quantify
Hyo Jeong Kim +3 more
doaj +1 more source
A glyco-engineering approach for site-specific conjugation to Fab glycans
mAbs, 2023 Effective processes for synthesizing antibody-drug conjugates (ADCs) require: 1) site-specific incorporation of the payload to avoid interference with binding to the target epitope, 2) optimal drug/antibody ratio to achieve sufficient potency while ...
Maria L. Jaramillo +10 more
doaj +1 more source
Molecules, 2021 Mammalian cell surfaces are modified with complex arrays of glycans that play major roles in health and disease. Abnormal glycosylation is a hallmark of cancer; terminal sialic acid and fucose in particular have high levels in tumor cells, with positive ...
Ravneet Kaur Grewal +6 more
doaj +1 more source
Frontiers in Cell and Developmental Biology, 2022 Sialylation aberration has been implicated in lung cancer development by altering signaling pathways. Hence, it is urgent to identify key sialyltransferases in the development of lung adenocarcinoma (LUAD), which is a common malignant subtype of non ...
Jiaxuan Li +16 more
doaj +1 more source
Lipoprotein sialylation in atherosclerosis: Lessons from mice
Frontiers in Endocrinology, 2022 Sialylation is a dynamically regulated modification, which commonly occurs at the terminal of glycan chains in glycoproteins and glycolipids in eukaryotic cells.
Liming Yu +3 more
doaj +1 more source