about
Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodiesIncrease in sialylation and branching in the mouse serum N-glycome correlates with inflammation and ovarian tumour progressionOptimal Synthetic Glycosylation of a Therapeutic AntibodyOptimal Synthetic Glycosylation of a Therapeutic AntibodyUniCarb-DB: a database resource for glycomic discoveryGlycosylation of liver acute-phase proteins in pancreatic cancer and chronic pancreatitis.Mass Spectrometric Quantification of N-Linked Glycans by Reference to Exogenous Standards.Reducing V3 Antigenicity and Immunogenicity on Soluble, Native-Like HIV-1 Env SOSIP TrimersPresence of terminal N-acetylgalactosamineβ1-4N-acetylglucosamine residues on O-linked oligosaccharides from gastric MUC5AC: involvement in Helicobacter pylori colonization?MIRAGE: the minimum information required for a glycomics experimentCharacterization of fibrinogen glycosylation and its importance for serum/plasma N-glycome analysis.The minimum information required for a glycomics experiment (MIRAGE) project: improving the standards for reporting mass-spectrometry-based glycoanalytic dataGalactosyltransferase 4 is a major control point for glycan branching in N-linked glycosylation.EndoE from Enterococcus faecalis hydrolyzes the glycans of the biofilm inhibiting protein lactoferrin and mediates growth.Identification of O-glycan Structures from Chicken Intestinal Mucins Provides Insight into Campylobactor jejuni Pathogenicity.High-resolution mass spectrometry of small molecules bound to membrane proteinsDistinguishing N-acetylneuraminic acid linkage isomers on glycopeptides by ion mobility-mass spectrometry.Travelling-wave ion mobility and negative ion fragmentation of high-mannose N-glycans.Exploring the glycosylation of serum CA125.Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals.EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and α1-acid glycoprotein.High-throughput RNAi screening for N-glycosylation dependent loci in Caenorhabditis elegans.Glycosylation and Fc receptors.Molecular Architecture of the Cleavage-Dependent Mannose Patch on a Soluble HIV-1 Envelope Glycoprotein Trimer.Method for milk oligosaccharide profiling by 2-aminobenzamide labeling and hydrophilic interaction chromatography.UniCarbKB: putting the pieces together for glycomics research.Convergent immunological solutions to Argentine hemorrhagic fever virus neutralization.Structural characterization and biological implications of sulfated N-glycans in a serine protease from the neotropical moth Hylesia metabus (Cramer [1775]) (Lepidoptera: Saturniidae).N-linked glycan structures of the human Fcγ receptors produced in NS0 cells.Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1.The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans.Global N-Glycan Site Occupancy of HIV-1 gp120 by Metabolic Engineering and High-Resolution Intact Mass Spectrometry.Travelling-wave ion mobility mass spectrometry and negative ion fragmentation of hybrid and complex N-glycansThe role of interfacial lipids in stabilizing membrane protein oligomers.Native mass spectrometry: towards high-throughput structural proteomics.The conserved oligomeric Golgi complex is required for fucosylation of N-glycans in Caenorhabditis elegans.Modeling a congenital disorder of glycosylation type I in C. elegans: a genome-wide RNAi screen for N-glycosylation-dependent loci.Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure deAntibody production using a ciliate generates unusual antibody glycoforms displaying enhanced cell-killing activity.The minimum information required for a glycomics experiment (MIRAGE) project: improving the standards for reporting glycan microarray-based data.
P50
Q28069362-DBE50BD2-E20D-45CC-A314-D0D83F794ABEQ28536329-55AEEE63-C13D-4C2A-BD2D-A254578F26AEQ28831266-3964CCB8-7F78-44E4-AC8C-5D994C874301Q28831364-71BB8ADF-FB7A-4794-B474-66805F448478Q30050750-7665D285-CCFB-4554-8797-597E9C87E2EEQ33764483-886892AE-491F-49EA-AF3F-2CF5E4BA47C2Q33885373-155CCA79-2734-41CA-8109-93517EBCBBD0Q33907694-57EFD068-9E0C-4D3F-97F4-57C37A19DDE9Q34250321-0F7B4955-E5E0-4522-A005-CC41A7A6392FQ34411320-DE7C0D7B-2774-404B-8847-CEA6FF4EDF6BQ34476817-58A5D29B-C832-4BB4-BE80-B521F8CE1D2AQ34573489-3ADA9AD3-4842-49F5-8B8D-387AB3669C1CQ34589283-683A031F-C807-490D-9300-C49F6C9B3029Q35114449-1EF06F4C-E450-41AC-8C3E-EA22B0D677CBQ35692089-34CC5509-E4C9-4902-952E-A9D22ECF822DQ35931284-694D9210-1484-415C-9CF1-0A7565776AF9Q35939622-4B6D8F66-DEDE-491C-911E-6071B5AD1541Q36767085-230BAA5B-3344-4C32-9B15-BAB54E6C0514Q37139074-3CC95462-D3CA-4CD5-BD27-76196DA61463Q37181828-3558F95B-3890-447F-AD08-C0F5D533FCB6Q37186877-5681D335-2A40-4338-8B2E-3CED93694055Q37785145-2D40E643-C26E-4924-BAD1-1D840CBB5377Q38239277-78644563-65D6-47C4-8ED9-EA3A61F72338Q38290294-BA160AFE-FB2A-408D-963D-8250AE1BEFDEQ38335224-1745DF7E-7439-47FA-A60C-70AF469B984AQ38421228-25C2132B-A3E8-4781-8DCC-9089D9F118B7Q38718346-8624822F-F3E6-4822-975D-E36371594AF3Q38928377-A9CCF7D0-65A4-4BB4-A2D7-7018F9CE176FQ39137999-A63B9E6E-6B96-433B-A22A-C6062BFFFC83Q40058876-E778D3B6-0AD1-4E70-B2E5-3103CF079949Q40231057-2A5398BC-E928-461F-922A-3A360EE7AD75Q40406623-3BAC17E1-F857-4962-8CBF-D9D99BAC7C89Q40495731-A7E0C9BA-BB80-4323-A8AA-9CA8C4FB8EE2Q40958729-59F37077-472E-4CB0-BE21-2AF6E2C20F7DQ41696638-65CD24F0-05D4-416A-B082-AF92CF73EC16Q41854051-F3A34382-4EC6-49E5-97EF-F747DC182471Q41971316-D30196DA-312C-40AA-B6B5-1EDDB445DC10Q42103741-B69621DE-48C0-44F0-A57F-A74AD0D58A57Q42129626-35CB7341-FE1F-412D-BC18-4E42046B6659Q42346544-5FF0BC52-64BA-4CC1-B1C3-8B432D1244A0
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Weston B Struwe
@ast
Weston B Struwe
@en
Weston B Struwe
@es
Weston B Struwe
@sl
type
label
Weston B Struwe
@ast
Weston B Struwe
@en
Weston B Struwe
@es
Weston B Struwe
@sl
prefLabel
Weston B Struwe
@ast
Weston B Struwe
@en
Weston B Struwe
@es
Weston B Struwe
@sl
P1053
D-6180-2018
P106
P21
P31
P3829
P496
0000-0003-0594-226X
P569
2000-01-01T00:00:00Z