about
Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylationStructural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogStructural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound formsStructural and Kinetic Characterizations of the Polysialic Acid O-Acetyltransferase OatWY from Neisseria meningitidisNMR spectroscopic characterization of the sialyltransferase CstII from Campylobacter jejuni: histidine 188 is the general baseStructural and Kinetic Analysis of Substrate Binding to the Sialyltransferase Cst-II from Campylobacter jejuniStructure and Mechanism of the Lipooligosaccharide Sialyltransferase from Neisseria meningitidisNovel biosynthetic functions of lipopolysaccharide rfaJ homologs from Helicobacter pylori.Identification of a lipopolysaccharide alpha-2,3-sialyltransferase from Haemophilus influenzae.High-throughput screening methodology for the directed evolution of glycosyltransferases.Variants of the beta 1,3-galactosyltransferase CgtB from the bacterium Campylobacter jejuni have distinct acceptor specificities.Fluorescence activated cell sorting as a general ultra-high-throughput screening method for directed evolution of glycosyltransferases.X-ray crystallographic structure of a bacterial polysialyltransferase provides insight into the biosynthesis of capsular polysialic acid.A sensitive fluorescence-based assay for monitoring GM2 ganglioside hydrolysis in live patient cells and their lysatesIncorporation of N-acetylneuraminic acid into Haemophilus somnus lipooligosaccharide (LOS): enhancement of resistance to serum and reduction of LOS antibody binding.Mechanistic investigation of the endo-alpha-N-acetylgalactosaminidase from Streptococcus pneumoniae R6.Identification and characterization of NeuB3 from Campylobacter jejuni as a pseudaminic acid synthase.Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways.Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori.Characterization of five β-glycoside hydrolases from Cellulomonas fimi ATCC 484.In cellulo examination of a beta-alpha hybrid construct of beta-hexosaminidase A subunits, reported to interact with the GM2 activator protein and hydrolyze GM2 gangliosideBiochemical characterization of a polysialyltransferase from Mannheimia haemolytica A2 and comparison to other bacterial polysialyltransferases.Site-specific enzymatic polysialylation of therapeutic proteins using bacterial enzymesOne step closer to a sweet conclusion.Evidence for acquisition of the lipooligosaccharide biosynthesis locus in Campylobacter jejuni GB11, a strain isolated from a patient with Guillain-Barré syndrome, by horizontal exchangeIdentification and characterization of a lipopolysaccharide α,2,3-sialyltransferase from the human pathogen Helicobacter bizzozeroniiProteomic Analysis of the Secretome of Cellulomonas fimi ATCC 484 and Cellulomonas flavigena ATCC 482.Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange.Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases.Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigensRecognition of sialylated poly-N-acetyllactosamine chains on N- and O-linked glycans by human and avian influenza A virus hemagglutinins.A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidaseReview of phosphocholine substituents on bacterial pathogen glycans: synthesis, structures and interactions with host proteins.A beta-1,4-galactosyltransferase from Helicobacter pylori is an efficient and versatile biocatalyst displaying a novel activity for thioglycoside synthesis.A single bifunctional UDP-GlcNAc/Glc 4-epimerase supports the synthesis of three cell surface glycoconjugates in Campylobacter jejuni.Intermediate trapping on a mutant retaining alpha-galactosyltransferase identifies an unexpected aspartate residue.Effects of both shortening and lengthening the active site nucleophile of Bacillus circulans xylanase on catalytic activity.Construction of a hybrid β-hexosaminidase subunit capable of forming stable homodimers that hydrolyze GM2 ganglioside in vivo.Analysis of Campylobacter jejuni capsular loci reveals multiple mechanisms for the generation of structural diversity and the ability to form complex heptoses.Overexpression of the Bacillus subtilis and circulans xylanases in Escherichia coli.
P50
Q24338493-BB5C8FF2-6512-4655-BD93-004DCBE0A89DQ27642976-A4AA930D-2C22-4D05-A83F-17B22363A2D6Q27644849-06AEFFC0-AFD7-44CA-B808-6E6A3FE3B272Q27655942-DD99B5FA-1BC9-450B-B316-36AF42A147B6Q27657766-F2E0E837-6EE1-49BE-9C1F-EF9A93792ED1Q27671666-C76DD86A-8CEF-41B8-B9BB-3AF7B0DC50F7Q27672663-D99ED649-47DA-4EBE-8BE5-84F2FAA19069Q31158199-F0382D0E-273C-4CB0-AE96-D86E30F4F033Q31795714-FF918D0C-B9D6-44BE-B7A6-91B80296BF6FQ33251463-CC87A11D-8588-4944-AEE3-83A29E6AD9F5Q33296424-646B30A7-B82E-439C-8265-ED617E32DF2FQ33641991-901C9969-D760-47A1-A0EA-4C80594996A9Q33918635-1DC6343A-DCCB-4F02-B99E-DFE548354286Q33961400-A3424E5A-97AF-40D0-A52F-773CB764F34FQ34129976-E2182136-72A8-4B85-9ABC-79D48063C59EQ34192022-AC4B5958-60E0-468B-8324-6B0C20644B14Q34445426-9D7BAEDE-59CA-410B-8D6C-F8FAA377FCA7Q34467309-CD4CF88E-7D70-4BF1-8F3E-C2F0910DA586Q34485821-70D9E1B5-3AC4-4A92-895F-29E3881D2AE8Q34593552-D97D8D58-1ADE-41CF-A64B-45ADEE2F081CQ34618426-6B672012-2441-4ED0-AD76-3E25D89DA657Q34904580-60F840E9-802C-49E6-B334-D15A76E2C5CFQ34938414-571B40A5-D738-4DD5-B2C5-292510745DBCQ35033325-6BA1FFCD-5C63-43D7-8838-4B0C406FEC15Q35549851-9C66516C-3227-40D3-8AE6-5DEBA4C82381Q35943153-6E1A5ECA-FE47-49B3-B57A-7631CC7C4E21Q35948003-BCD1CA58-4E08-4C02-BF16-8DB7D5D7FD55Q36279549-314A22B4-E999-440D-BC7A-A187FF374C45Q36318867-FC5D9A86-B87B-469E-9962-86FC00A2AD2BQ36368302-4FEB28CD-18DC-4280-B603-6092BAE3AE41Q36452947-9B395836-241F-4830-9B5E-0B8D41B563B2Q37285195-38F944C4-9F47-47CA-8D26-1996BB0B6E49Q38126260-8EA249D2-2F03-424A-8F31-21A59F4E8F84Q38290792-B215F87C-CE33-43CB-8EB3-DA3467650B8FQ38334961-E373C046-E845-4776-8F7A-890202FBAAB9Q38342603-D53F1A04-885C-447E-8045-0D7C9A4D1034Q38354246-CC7F37EE-A198-44E4-B7D6-DF6285F33411Q38721702-0FA84A0E-51ED-4656-9002-97C4B3C6A437Q39121875-542D6DE7-1785-4DD9-801A-78EFF5B604D8Q41076551-1E51F3D9-0D1F-4A3E-9F95-BD1084453F1D
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Warren Wakarchuk
@ast
Warren Wakarchuk
@en
Warren Wakarchuk
@es
Warren Wakarchuk
@nl
Warren Wakarchuk
@sl
type
label
Warren Wakarchuk
@ast
Warren Wakarchuk
@en
Warren Wakarchuk
@es
Warren Wakarchuk
@nl
Warren Wakarchuk
@sl
prefLabel
Warren Wakarchuk
@ast
Warren Wakarchuk
@en
Warren Wakarchuk
@es
Warren Wakarchuk
@nl
Warren Wakarchuk
@sl
P1053
Q-9514-2017
P106
P1153
7005205838
P1960
cWMBiM4AAAAJ
P21
P31
P3829
P496
0000-0002-1539-1679
P569
2000-01-01T00:00:00Z