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Steffen Goletz

Researcher at Max Delbrück Center for Molecular Medicine

Publications -  117
Citations -  2015

Steffen Goletz is an academic researcher from Max Delbrück Center for Molecular Medicine. The author has contributed to research in topics: Antigen & Antibody. The author has an hindex of 23, co-authored 114 publications receiving 1902 citations. Previous affiliations of Steffen Goletz include Humboldt State University & Charité.

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Localization of O-Glycosylation Sites on Glycopeptide Fragments from Lactation-associated MUC1 ALL PUTATIVE SITES WITHIN THE TANDEM REPEAT ARE GLYCOSYLATION TARGETS IN VIVO

TL;DR: In this article, a mass spectrometric sequencing strategy was developed to identify in vivo O-glycosylation sites on mucin-derived glycopeptides, where the mass of C- or N-terminal fragments registered for the mono-to pentasubstituted PAP20 indicated that GalNAc was linked to the peptide at Ser5,Thr6 (GSTA) and Thr14(VTSA) but contrary to previous in vitro glycosylations studies also at Thr19 and Ser15 located within the PDTR or
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Selection of large diversities of antiidiotypic antibody fragments by phage display.

TL;DR: In this article, the authors describe a fast and reliable technique for generating large diversities of anti-iotypic single chain antibody fragments from non-immunized phagemid libraries using phage display.
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PankoMab: a potent new generation anti-tumour MUC1 antibody

TL;DR: PankoMab is a novel antibody, which binds specifically to this epitope and was designed to show the highest glycosylation dependency and the strongest additive binding effect when compared to other MUC1 antibodies, which renders it a superior antibody for in vivo diagnostics and various immunotherapeutic approaches.
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What makes cancer stem cell markers different

Uwe Karsten, +1 more
- 04 Jul 2013 - 
TL;DR: A hypothesis is proposed which might help to solve the problem of tumor specificity in at least a subgroup of stem cell markers, and Glycosylation may provide the key.
Journal Article

Enhanced Binding of Antibodies to the DTR Motif of MUC1 Tandem Repeat Peptide Is Mediated by Site-specific Glycosylation

TL;DR: Evidence is presented that the antigenicity of the single repeat toward a considerable number of antibodies to the DTR motif is greatly enhanced if it is glycosylated within this motif, and only in this position, and several lines of evidence suggest that Glycosylation with N-acetylgalactosamine is sufficient for the observed enhancement effect.