about
Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitorsBiosynthesis of the tunicamycin antibiotics proceeds via unique exo-glycal intermediatesCovalent assembly of nanoparticles as a peptidase-degradable platform for molecular MRI.Directed evolution of a glycosynthase from Agrobacterium sp. increases its catalytic activity dramatically and expands its substrate repertoire.Uptake of unnatural trehalose analogs as a reporter for Mycobacterium tuberculosis.Detailed dissection of a new mechanism for glycoside cleavage: alpha-1,4-glucan lyase.An ubiquitin-binding molecule can work as an inhibitor of ubiquitin processing enzymes and ubiquitin receptors.Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase.A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase.Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic DesignTotal synthesis of Xanthoangelol B and its various fragments: towards inhibition of virulence factor production of Staphylococcus aureusPalladium-mediated enzyme activation suggests multiphase initiation of glycogenesisSuppression of the Ubiquitin Pathway by Small Molecule Binding to Ubiquitin Enhances Doxorubicin Sensitivity of the Cancer CellsStructural, mechanistic, and computational analysis of the effects of anomeric fluorines on anomeric fluoride departure in 5-fluoroxylosyl fluoridesTargeting Mannitol Metabolism as an Alternative Antimicrobial Strategy Based on the Structure-Function Study of Mannitol-1-Phosphate Dehydrogenase in Staphylococcus aureusEnzymatic glycosylation involving fluorinated carbohydratesSurface display of sialyltransferase on the outer membrane of Escherichia coli and ClearColi
P50
Q27658967-093FE563-CB27-40F8-932E-037DFEA01ABFQ28269258-237B1A8D-F51D-499E-8F61-DE2BC795AF89Q30839205-E2B207B6-4178-4FD6-89CE-121CD82B61FFQ33204723-DD22CA53-E6B4-4D77-B367-B8168A8A9C29Q33838182-613C5602-0249-4C64-9CE4-3E93D89E4D48Q34274203-8CABBBE9-9CC6-4637-94A5-57DB39A62DF8Q38747158-195990CC-C2D2-4EDE-9FFF-C01E6BDBF241Q44997607-0ED25DD2-0540-4BD1-A28C-8439496AE19DQ48027369-4B3B3809-5F7A-42DF-AEE3-63F3D6F6245AQ58547177-D16CFFD1-B622-4D7B-AAC1-BBF31036C31FQ58617033-39D765E3-A2A3-4403-BED1-0D55EB723735Q59056079-8204E8E4-C033-4DF4-9054-AA12DBDC1B11Q64077112-D8EB85F8-CFF7-4627-BB1A-75AF7F509975Q84937613-7C1A9045-D2EE-4B95-AC49-9436B182C8A1Q91753577-EDF20E46-4DB7-467C-88FE-EB5D43F95F03Q92141898-3E7178AF-8BEC-46CF-8839-76A3C263E4C0Q92664881-D5B16B62-34F0-4A97-B416-732863097141
P50
description
researcher ORCID ID = 0000-0002-8598-3303
@en
wetenschapper
@nl
name
Seung Seo Lee
@ast
Seung Seo Lee
@en
Seung Seo Lee
@es
Seung Seo Lee
@nl
type
label
Seung Seo Lee
@ast
Seung Seo Lee
@en
Seung Seo Lee
@es
Seung Seo Lee
@nl
prefLabel
Seung Seo Lee
@ast
Seung Seo Lee
@en
Seung Seo Lee
@es
Seung Seo Lee
@nl
P106
P31
P496
0000-0002-8598-3303