Exploring the acceptor substrate recognition of the human beta-galactoside alpha 2,6-sialyltransferase.
about
Structure-function analysis of the human sialyltransferase ST3Gal I: role of n-glycosylation and a novel conserved sialylmotifUniversal phosphatase-coupled glycosyltransferase assayThe structure of human α-2,6-sialyltransferase reveals the binding mode of complex glycansMolecular phylogeny and functional genomics of beta-galactoside alpha2,6-sialyltransferases that explain ubiquitous expression of st6gal1 gene in amniotes.C-terminal amino acids of Helicobacter pylori alpha1,3/4 fucosyltransferases determine type I and type II transfer.The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of substrate specificity.Recent development in the design of sialyltransferase inhibitors.Synthesis of sialoglycopolypeptide for potentially blocking influenza virus infection using a rat alpha2,6-sialyltransferase expressed in BmNPV bacmid-injected silkworm larvaeIdentification of a novel protein binding motif within the T-synthase for the molecular chaperone Cosmc.Functional organization of Golgi N- and O-glycosylation pathways involves pH-dependent complex formation that is impaired in cancer cells.Probing the CMP-Sialic Acid Donor Specificity of Two Human β-d-Galactoside Sialyltransferases (ST3Gal I and ST6Gal I) Selectively Acting on O- and N-Glycosylproteins.Variability among TSH Measurements Can Be Reduced by Combining a Glycoengineered Calibrator to Epitope-Defined Immunoassays.High-quality production of human α-2,6-sialyltransferase in Pichia pastoris requires control over N-terminal truncations by host-inherent protease activities.Molecular dissection of the ST8Sia IV polysialyltransferase. Distinct domains are required for neural cell adhesion molecule recognition and polysialylation.Two N-terminally truncated variants of human β-galactoside α2,6 sialyltransferase I with distinct properties for in vitro protein glycosylation.Computational characterisation of the interactions between human ST6Gal I and transition-state analogue inhibitors: insights for inhibitor design
P2860
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P2860
Exploring the acceptor substrate recognition of the human beta-galactoside alpha 2,6-sialyltransferase.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Exploring the acceptor substra ...... e alpha 2,6-sialyltransferase.
@en
type
label
Exploring the acceptor substra ...... e alpha 2,6-sialyltransferase.
@en
prefLabel
Exploring the acceptor substra ...... e alpha 2,6-sialyltransferase.
@en
P2093
P2860
P356
P1476
Exploring the acceptor substra ...... e alpha 2,6-sialyltransferase.
@en
P2093
El Battari A
Guillemot JC
Legaigneur P
Malissard M
P2860
P304
21608-21617
P356
10.1074/JBC.M100860200
P407
P577
2001-02-20T00:00:00Z