Erdmann Rapp
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View article: Immunoglobulin A carries sulfated and O-acetylated N-glycans primarily at the tailpiece site – strategies for site-specific N-glycan identification
Immunoglobulin A carries sulfated and O-acetylated N-glycans primarily at the tailpiece site – strategies for site-specific N-glycan identification Open
Sulfated N- glycans from human immunoglobulin A (IgA) were recently discovered via glycomic approaches. However, their site-specific description is still pending. Certain N- glycan structures at specific N- glycosylation sites in IgA are c…
View article: Raider of the lost N-glycans – Localizing rare and frequently overlooked IgG N-glycans with sulfation or bisecting LacNAc
Raider of the lost N-glycans – Localizing rare and frequently overlooked IgG N-glycans with sulfation or bisecting LacNAc Open
Immunoglobulin G (IgG) is the most abundant immunoglobulin in human blood. Here it plays a central role in the immune system by recognizing antigens and mediating effector functions of the humoral immune defense. The role of IgG N- glycosy…
View article: Maternal Dietary Fiber Intake During Lactation and Human Milk Oligosaccharide Fucosylation: a PRIMA Birth Cohort Study
Maternal Dietary Fiber Intake During Lactation and Human Milk Oligosaccharide Fucosylation: a PRIMA Birth Cohort Study Open
Human milk oligosaccharides (HMOs) have an important role in the microbiome and immune system development of breastfed infants. Previous explorative studies indicated an association between maternal carbohydrate intake, including dietary f…
View article: New Avenues for Human Blood Plasma Biomarker Discovery via Improved In-Depth Analysis of the Low-Abundant N-glycoproteome
New Avenues for Human Blood Plasma Biomarker Discovery via Improved In-Depth Analysis of the Low-Abundant N-glycoproteome Open
View article: In-depth N-glycoproteomic analysis of human blood plasma proteins
In-depth N-glycoproteomic analysis of human blood plasma proteins Open
One of the most common post-translational modifications of proteins is glycosylation. This modification enzymatically attaches a sugar chain, called glycan, to a protein. Glycosylated proteins represent around 45% of the proteins in the eu…
View article: A hierarchical structure in the N-glycosylation process governs the N-glycosylation output: prolonged cultivation induces glycoenzymes expression variations that are reflected in the cellular N-glycome but not in the protein and site-specific glycoprofile of CHO cells
A hierarchical structure in the N-glycosylation process governs the N-glycosylation output: prolonged cultivation induces glycoenzymes expression variations that are reflected in the cellular N-glycome but not in the protein and site-specific glycoprofile of CHO cells Open
N-glycosylation is a central component in the modification of secretory proteins. One characteristic of this process is a heterogeneous output. The heterogeneity is the result of both structural constraints of the glycoprotein as well as t…
View article: Immunoglobulin A Carries Sulfated<i>N-</i>glycans Primarily at the Tailpiece Site – An Oxonium-Ion-Guided Approach for Site-Specific<i>N</i>-glycan Identification
Immunoglobulin A Carries Sulfated<i>N-</i>glycans Primarily at the Tailpiece Site – An Oxonium-Ion-Guided Approach for Site-Specific<i>N</i>-glycan Identification Open
Sulfated N- glycans from human immunoglobulin A (IgA) were recently discovered via glycomic approaches. However, their site-specific description is still pending. Certain N- glycan structures at specific N- glycosylation sites in IgA are c…
View article: Macrophage- and CD4+ T cell-derived SIV differ in glycosylation, infectivity and neutralization sensitivity
Macrophage- and CD4+ T cell-derived SIV differ in glycosylation, infectivity and neutralization sensitivity Open
The human immunodeficiency virus (HIV) envelope protein (Env) mediates viral entry into host cells and is the primary target for the humoral immune response. Env is extensively glycosylated, and these glycans shield underlying epitopes fro…
View article: “Small is beautiful” – Examining reliable determination of low-abundant therapeutic antibody glycovariants
“Small is beautiful” – Examining reliable determination of low-abundant therapeutic antibody glycovariants Open
Glycans associated with biopharmaceutical drugs play crucial roles in drug safety and efficacy, and therefore, their reliable detection and quantification is essential. Our study introduces a multi-level quantification approach for glycosy…
View article: “Small is beautiful” – the significance of reliable determination of low- abundant therapeutic antibody glycovariants
“Small is beautiful” – the significance of reliable determination of low- abundant therapeutic antibody glycovariants Open
Glycans associated with biopharmaceutical drugs play crucial roles in drug safety and efficacy, and therefore, their reliable detection and quantification is essential. Our study introduces a multi-level quantification approach for glycosy…
View article: Macrophage- and CD4 <sup>+</sup> T cell-derived SIV differ in glycosylation, infectivity and neutralization sensitivity
Macrophage- and CD4 <sup>+</sup> T cell-derived SIV differ in glycosylation, infectivity and neutralization sensitivity Open
The human immunodeficiency virus (HIV) envelope protein (Env) mediates viral entry into host cells and is the primary target for the humoral immune response. Env is extensively glycosylated, and these glycans shield underlying epitopes fro…
View article: New avenues for human blood plasma biomarker discovery via improved in-depth analysis of the low-abundant<i>N-</i>glycoproteome
New avenues for human blood plasma biomarker discovery via improved in-depth analysis of the low-abundant<i>N-</i>glycoproteome Open
To understand implications of protein glycosylation for clinical diagnostic and biopharmaceuticals, innovative glycoproteomic technologies are required. Recently, significant advances were made, particularly toward structure-focused N- gly…
View article: Cell-free N-glycosylation of peptides using synthetic lipid-linked hybrid and complex N-glycans
Cell-free N-glycosylation of peptides using synthetic lipid-linked hybrid and complex N-glycans Open
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Issue Information Open
View article: Removable Dyes—The Missing Link for In-Depth N-Glycan Analysis via Multi-Method Approaches
Removable Dyes—The Missing Link for In-Depth N-Glycan Analysis via Multi-Method Approaches Open
As the roles of glycans in health and disease continue to be unraveled, it is becoming apparent that glycans’ immense complexity cannot be ignored. To fully delineate glycan structures, we developed an integrative approach combining a set …
View article: Genetic knockout of porcine <i>GGTA1</i> or <i>CMAH</i>/<i>GGTA1</i> is associated with the emergence of neo‐glycans
Genetic knockout of porcine <i>GGTA1</i> or <i>CMAH</i>/<i>GGTA1</i> is associated with the emergence of neo‐glycans Open
Background Pig‐derived tissues could overcome the shortage of human donor organs in transplantation. However, the glycans with terminal α‐Gal and Neu5Gc, which are synthesized by enzymes, encoded by the genes GGTA1 and CMAH , are known to …
View article: Comparative analysis of transferrin and IgG N-glycosylation in two human populations
Comparative analysis of transferrin and IgG N-glycosylation in two human populations Open
Human plasma transferrin (Tf) N-glycosylation has been mostly studied as a marker for congenital disorders of glycosylation, alcohol abuse, and hepatocellular carcinoma. However, inter-individual variability of Tf N-glycosylation is not kn…
View article: Reliable N-Glycan Analysis–Removal of Frequently Occurring Oligosaccharide Impurities by Enzymatic Degradation
Reliable N-Glycan Analysis–Removal of Frequently Occurring Oligosaccharide Impurities by Enzymatic Degradation Open
Glycosylation, especially N-glycosylation, is one of the most common protein modifications, with immense importance at the molecular, cellular, and organismal level. Thus, accurate and reliable N-glycan analysis is essential in many areas …
View article: Unambiguous identification of α-Gal epitopes in intact monoclonal antibodies by NMR spectroscopy
Unambiguous identification of α-Gal epitopes in intact monoclonal antibodies by NMR spectroscopy Open
The α-Gal epitope consisting of the terminal trisaccharide Galα1,3Galβ1,4GlcNAc exposed on cell or protein surfaces can cause severe immune reactions, such as hypersensitivity reactions, in humans. This epitope is also called the xenotrans…
View article: Editorial: Immunoglobulin Glycosylation Analysis: State-of-the-Art Methods and Applications in Immunology
Editorial: Immunoglobulin Glycosylation Analysis: State-of-the-Art Methods and Applications in Immunology Open
EDITORIAL article Front. Immunol., 20 May 2022Sec. B Cell Biology Volume 13 - 2022 | https://doi.org/10.3389/fimmu.2022.923393
View article: A Bacterial Mannose Binding Lectin as a Tool for the Enrichment of C- and O-Mannosylated Peptides
A Bacterial Mannose Binding Lectin as a Tool for the Enrichment of C- and O-Mannosylated Peptides Open
Mass spectrometry (MS) easily detects C-mannosylated peptides from purified proteins but not from complex biological samples. Enrichment of specific glycopeptides by lectin affinity prior to MS analysis has been widely applied to support g…
View article: The minimum information required for a glycomics experiment (MIRAGE): reporting guidelines for capillary electrophoresis
The minimum information required for a glycomics experiment (MIRAGE): reporting guidelines for capillary electrophoresis Open
The Minimum Information Required for a Glycomics Experiment (MIRAGE) is an initiative to standardize the reporting of glycoanalytical methods and to assess their reproducibility. To date, the MIRAGE Commission has published several reporti…
View article: Synthetic glycans control gut microbiome structure and mitigate colitis in mice
Synthetic glycans control gut microbiome structure and mitigate colitis in mice Open
View article: Serum <i>N</i>-glycomics of a novel CDG-IIb patient reveals aberrant IgG glycosylation
Serum <i>N</i>-glycomics of a novel CDG-IIb patient reveals aberrant IgG glycosylation Open
Rare genetic mutations of the mannosyl-oligosaccharide glucosidase (MOGS) gene affecting the function of the mannosyl-oligosaccharide glucosidase (glucosidase I) are the cause of the congenital disorder of glycosylation IIb (CDG-IIb). Gluc…
View article: Synthetic glycans that control gut microbiome structure mitigate colitis in mice
Synthetic glycans that control gut microbiome structure mitigate colitis in mice Open
Relative abundances of bacterial species in the gut microbiome have been linked to many diseases. Species of gut bacteria are ecologically differentiated by their abilities to metabolize different glycans, making glycan delivery a powerful…
View article: Author Correction: Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis
Author Correction: Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis Open
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View article: Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis
Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis Open
View article: A spoonful of L‐fucose—an efficient therapy for GFUS‐CDG, a new glycosylation disorder
A spoonful of L‐fucose—an efficient therapy for GFUS‐CDG, a new glycosylation disorder Open
Congenital disorders of glycosylation are a genetically and phenotypically heterogeneous family of diseases affecting the co- and posttranslational modification of proteins. Using exome sequencing, we detected biallelic variants in GFUS (N…
View article: Simultaneous Monitoring of Monoclonal Antibody Variants by Strong Cation-Exchange Chromatography Hyphenated to Mass Spectrometry to Assess Quality Attributes of Rituximab-Based Biotherapeutics
Simultaneous Monitoring of Monoclonal Antibody Variants by Strong Cation-Exchange Chromatography Hyphenated to Mass Spectrometry to Assess Quality Attributes of Rituximab-Based Biotherapeutics Open
Different manufacturing processes and storage conditions of biotherapeutics can lead to a significant variability in drug products arising from chemical and enzymatic post-translational modifications (PTMs), resulting in the co-existence o…
View article: Simultaneous monitoring of monoclonal antibody variants by strong cation-exchange chromatography hyphenated to mass spectrometry to assess quality attributes of rituximab-based biotherapeutics
Simultaneous monitoring of monoclonal antibody variants by strong cation-exchange chromatography hyphenated to mass spectrometry to assess quality attributes of rituximab-based biotherapeutics Open
This deposit contains 43 files (.raw) refered to the publication "Simultaneous monitoring of monoclonal antibody variants by strong cation exchange chromatography hyphenated to mass spectrometry to assess quality attributes of rituximab-ba…