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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.

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Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

TL;DR: A proteomic-scale analysis of protein acetylation suggests that it is an important biological regulatory mechanism and the regulatory scope of lysine acetylations is broad and comparable with that of other major posttranslational modifications.
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Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast.

TL;DR: Comparison of protein levels of essentially all endogenous proteins in haploid yeast cells to their diploid counterparts spans more than four orders of magnitude in protein abundance with no discrimination against membrane or low level regulatory proteins.
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A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles

TL;DR: This work combines single-step immunoenrichment of ubiquitylated peptides with peptide fractionation and high-resolution mass spectrometry to investigate endogenous ubiquitylation sites, and for the first time demonstrates proteome-wide, site-specific quantification of endogenous putative ubiquitylations sites.
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A Dual Pressure Linear Ion Trap Orbitrap Instrument with Very High Sequencing Speed

TL;DR: A next generation LTQ Orbitrap system termed Velos is described, with significantly increased sensitivity and scan speed, and an improved higher-energy collisional dissociation cell with increased ion extraction capabilities was implemented.
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Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose).

TL;DR: In vitro and in vivo, it is shown that the nucleic acid-mimicking biopolymer poly(ADP-ribose) (PAR) nucleates intracellular liquid demixing, which is a general mechanism to dynamically reorganize the soluble nuclear space with implications for pathological protein aggregation caused by derailed phase separation.