Results 61 to 70 of about 63,826 (347)

Nanoscale Mapping of the Subcellular Glycosylation Landscape

open access: yesAdvanced Science, EarlyView.
Using multiplexed super‐resolution imaging with fluorophore‐labeled lectins, this study reports intracellular glycosylation at the nanoscale across organelles and synaptic specializations. Extending glycan analysis beyond the cell surface, Glyco‐STORM reveals distinct glycosylation nanodomains in the ER, Golgi, lysosomes, and synaptic sites.
Helene Gregoria Schroeter   +4 more
wiley   +1 more source

Enzymatic synthesis of l-fucose from l-fuculose using a fucose isomerase from Raoultella sp. and the biochemical and structural analyses of the enzyme

open access: yesBiotechnology for Biofuels, 2019
Background l-Fucose is a rare sugar with potential uses in the pharmaceutical, cosmetic, and food industries. The enzymatic approach using l-fucose isomerase, which interconverts l-fucose and l-fuculose, can be an efficient way of producing l-fucose for ...
In Jung Kim   +3 more
doaj   +1 more source

Advances in the study of core fucosylation in mammals

open access: yes浙江大学学报. 农业与生命科学版, 2021
Glycosylation is a major posttranslational modification, which involves in the regulation of important physiological functions. Among them, core fucosylation is an α1, 6-linked fucose to N-glycans, which catalyzes by only one glycosyltransferase.
TIAN Yinping, YI Wen
doaj   +1 more source

Characterization of Fut10 and Fut11, Putative Alpha-1-3/4 Fucosyltransferase Genes Important for Vertebrate Development [PDF]

open access: yes, 2007
Two new, putative alpha-1-3/4 fucosyltransferases ([alpha]1-3/4 Fuc-Ts), Fuc-TX and Fuc-TXI, were identified in the vertebrate genome and transcriptome sequence databases through sequence homology-based queries. These proteins have a significant sequence
Santosh K. Patnaik
core   +1 more source

Studying Lactoferrin N-Glycosylation. [PDF]

open access: yes, 2017
Lactoferrin is a multifunctional glycoprotein found in the milk of most mammals. In addition to its well-known role of binding iron, lactoferrin carries many important biological functions, including the promotion of cell proliferation and ...
Barile, Daniela   +4 more
core   +3 more sources

GlycoChat Uncovers Glycan–Lectin Circuits in the Tumor Microenvironment of Pancreatic Cancer

open access: yesAdvanced Science, EarlyView.
Aberrant glycosylation drives cancer progression, yet its role in the tumor microenvironment remains unclear. We developed GlycoChat to map glycan–lectin circuits at single‐cell resolution. We discovered that cancer cells induce immunosuppressive macrophage differentiation and impair phagocytosis through interactions with CLEC10A and SIGLEC3 ...
Dinh Xuan Tuan Anh   +8 more
wiley   +1 more source

Carbohydrate specificity of sea urchin sperm bindin: a cell surface lectin mediating sperm-egg adhesion. [PDF]

open access: yes, 1982
We have examined the carbohydrate specificity of bindin, a sperm protein responsible for the adhesion of sea urchin sperm to eggs, by investigating the interaction of a number of polysaccharides and glycoconjugates with isolated bindin.
Glabe, CG   +3 more
core  

A novel mechanism for binding of galactose-terminated glycans by the C-type carbohydrate recognition domain in blood dendritic cell antigen 2 [PDF]

open access: yes, 2015
Blood dendritic cell antigen 2 (BDCA-2; also designated CLEC4C or CD303) is uniquely expressed on plasmacytoid dendritic cells. Stimulation of BDCA-2 with antibodies leads to an anti-inflammatory response in these cells, but the natural ligands for the ...
Drickamer, K   +5 more
core   +1 more source

Protein oxidation of fucose environments (POFE) reveals fucose–protein interactions

open access: yesChemical Science
POFE (Protein Oxidation of Fucose Environments) method utilizes proximity-based oxidative proteomics to decipher cellular fucosylated glycoprotein interactions.
Yixuan Xie   +6 more
openaire   +4 more sources

L-Fucose treatment of FUT8-CDG

open access: yesMolecular Genetics and Metabolism Reports, 2020
FUT8-CDG is a severe multisystem disorder caused by mutations in FUT8, encoding the α-1,6-fucosyltransferase. We report on dizygotic twins with FUT8-CDG presenting with dysmorphisms, failure to thrive, and respiratory abnormalities. Due to the severe phenotype, oral L-fucose supplementation was started.
Park, Julien H.   +10 more
openaire   +4 more sources

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