K
Katrine T. Schjoldager
Researcher at University of Copenhagen
Publications - 53
Citations - 4251
Katrine T. Schjoldager is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Glycosylation & Glycoprotein. The author has an hindex of 26, co-authored 49 publications receiving 3202 citations.
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Journal ArticleDOI
Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology
Catharina Steentoft,Sergey Y. Vakhrushev,Hiren J. Joshi,Hiren J. Joshi,Yun Kong,Malene Bech Vester-Christensen,Katrine T. Schjoldager,Kirstine Lavrsen,Sally Dabelsteen,Nis Borbye Pedersen,Lara Marcos-Silva,Lara Marcos-Silva,Ramneek Gupta,Eric P. Bennett,Ulla Mandel,Søren Brunak,Søren Brunak,Hans H. Wandall,Steven B. Levery,Henrik Clausen +19 more
TL;DR: A genetic engineering approach using human cell lines to simplify O‐glycosylation (SimpleCells) that enables proteome‐wide discovery of O-glycan sites using ‘bottom‐up’ ETD‐based mass spectrometric analysis and an improved NetOGlyc4.0 model for prediction of O‐ Glycoproteins.
Journal ArticleDOI
Global view of human protein glycosylation pathways and functions
TL;DR: This work predicts that use of (single-cell) transcriptomics, genetic screens, genetic engineering of cellular glycosylation capacities and custom design of glycoprotein therapeutics are advancements that will ignite wider integration of gly cosylation in general cell biology.
Journal ArticleDOI
Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines
Catharina Steentoft,Sergey Y. Vakhrushev,Malene Bech Vester-Christensen,Katrine T. Schjoldager,Yun Kong,Eric P. Bennett,Ulla Mandel,Hans H. Wandall,Steven B. Levery,Henrik Clausen +9 more
TL;DR: Zinc-finger nuclease gene targeting is applied to truncate the O-glycan elongation pathway in human cells, generating stable 'SimpleCell' lines with homogenous O- glycosylation and should facilitate analyses of important functions of protein gly cosylation.
Journal ArticleDOI
Immature truncated O-glycophenotype of cancer directly induces oncogenic features
Prakash Radhakrishnan,Sally Dabelsteen,Frey Brus Madsen,Chiara Francavilla,Katharina L. Kopp,Catharina Steentoft,Sergey Y. Vakhrushev,Jesper V. Olsen,Lars Hansen,Eric P. Bennett,Anders Woetmann,Guangliang Yin,Longyun Chen,Haiyan Song,Mads Bak,Ryan A. Hlady,Staci L. Peters,Rene Opavsky,Christenze Thode,Klaus Qvortrup,Katrine T. Schjoldager,Henrik Clausen,Michael A. Hollingsworth,Hans H. Wandall +23 more
TL;DR: It is demonstrated, with the use of well-defined cell systems generated by precise gene editing, that the aberrant O-glycophenotype by itself induces oncogenic features with enhanced growth and invasion, and further provides support for immunotherapeutic strategies that target aberrant o-glycans.
Journal ArticleDOI
Site-specific protein O-glycosylation modulates proprotein processing - deciphering specific functions of the large polypeptide GalNAc-transferase gene family.
TL;DR: Site-specific O-glycosylation modifies pro-protein processing and other proteolytic events such as ADAM processing and thus emerges as an important co-regulator of limited proteolytics processing events.