M
Michael L. Nielsen
Researcher at University of Copenhagen
Publications - 134
Citations - 15189
Michael L. Nielsen is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Proteome & Mass spectrometry. The author has an hindex of 48, co-authored 123 publications receiving 13104 citations. Previous affiliations of Michael L. Nielsen include University of Copenhagen Faculty of Health Sciences & University of Southern Denmark.
Papers
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Journal ArticleDOI
RNA-DNA sequence differences spell genetic code ambiguities.
Thomas Bentin,Michael L. Nielsen +1 more
TL;DR: Widespread sequence differences in the human transcriptome between RNAs and their encoding genes termed RNA-DNA differences (RDDs) are reported and could add a new layer of complexity to gene expression.
Posted ContentDOI
A quantitative and site-specific atlas of the in vivo citrullinome reveals widespread existence of citrullination
A. S. Rebak,Ivo A. Hendriks,Sara C. Buch-Larsen,Jonas D. Elsborg,Rebecca Kirsch,Nadezhda Tsankova Doncheva,Lars Jørn Jensen,Maria A. Christophorou,Michael L. Nielsen +8 more
TL;DR: In this article , the authors employed quantitative mass spectrometry-based proteomics to generate a comprehensive atlas of citrullination sites in a physiologically relevant cell type.
Book ChapterDOI
Characterizing ADP-Ribosylation Sites Using Af1521 Enrichment Coupled to ETD-Based Mass Spectrometry.
Journal ArticleDOI
Transient suppression of SUMOylation in embryonic stem cells generates embryo-like structures
Jack-Christophe Cossec,Tatiana Traboulsi,Sébastien Sart,Yann Loe-Mie,M. Guthmann,Ivo A. Hendriks,Ilan Theurillat,Michael L. Nielsen,Maria-Elena Torres-Padilla,Charles N. Baroud,Anne Dejean +10 more
TL;DR: Recently, the authors showed that mouse embryonic stem cells (ESCs) solely exposed to chemical inhibition of SUMOylation generate embryo-like structures comprising anterior neural and trunk-associated regions.
Journal ArticleDOI
Science Signaling Podcast for 30 August 2016: Human arginine methylome
TL;DR: The human arginine methylome reveals the extent and importance of this posttranslational modification of proteins involved in diverse cellular processes and contributes to a more comprehensive understanding of the extent, function, and regulation of protein arginin methylation.