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The Role of Protein Glycosylation in Allergy
  • F. Altmann
  • Biology, Medicine
  • International Archives of Allergy and Immunology
  • 9 October 2006
The asparagine-linked carbohydrate moieties of plant and insect glycoproteins are the most abundant environmental immune determinants. They are the structural basis of what is known as cross-reactiveExpand
The Drosophila fused lobes Gene Encodes an N-Acetylglucosaminidase Involved in N-Glycan Processing*
Most processed, e.g. fucosylated, N-glycans on insect glycoproteins terminate in mannose, yet the relevant modifying enzymes require the prior action of N-acetylglucosaminyltransferase I. This led toExpand
Genome, secretome and glucose transport highlight unique features of the protein production host Pichia pastoris
BackgroundPichia pastoris is widely used as a production platform for heterologous proteins and model organism for organelle proliferation. Without a published genome sequence available, strain andExpand
A Unique β1,3-Galactosyltransferase Is Indispensable for the Biosynthesis of N-Glycans Containing Lewis a Structures in Arabidopsis thaliana[W][OA]
In plants, the only known outer-chain elongation of complex N-glycans is the formation of Lewis a [Fucα1-4(Galβ1-3)GlcNAc-R] structures. This process involves the sequential attachment ofExpand
Insect cells as hosts for the expression of recombinant glycoproteins
Baculovirus-mediated expression in insect cells has become well-established for the production of recombinant glycoproteins. Its frequent use arises from the relative ease and speed with which aExpand
Analysis of immunoglobulin glycosylation by LC‐ESI‐MS of glycopeptides and oligosaccharides
Two LC‐ESI‐MS methods for the analysis of antibody glycosylation are presented. In the first approach, tryptic glycopeptides are separated by RP chromatography and analyzed by ESI‐MS. ThisExpand
The effect of temperature on the proteome of recombinant Pichia pastoris.
The impact of environmental factors on the productivity of yeast cells is poorly investigated so far. Therefore, it is a major concern to improve the understanding of cellular physiology of microbialExpand
Peptide‐N4‐(N‐acetyl‐β‐glucosaminyl)asparagine amidase F cannot release glycans with fucose attached α1 → 3 to the asparagine‐linked N‐acetylglucosamine residue
: The ability of peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F (PNGase F) from Flavobacterium meningosepticum and PNGase A from sweet almonds to deglycosylate N-glycopeptides andExpand
Targeted knockouts of Physcomitrella lacking plant-specific immunogenic N-glycans.
Using plants as production factories for therapeutic proteins requires modification of their N-glycosylation pattern because of the immunogenicity of plant-specific sugar residues. In an attemptExpand
Comprehensive glyco‐proteomic analysis of human α1‐antitrypsin and its charge isoforms
Human α1‐antitrypsin (A1PI) is a well‐known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes. The three N‐glycosylation sites of A1PI contain diantennaryExpand