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.
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Journal ArticleDOI
Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry.
TL;DR: NPG Nature Asia-Pacific, 2-37 Ichigayatamachi, Shinjuku-ku, Tokyo 162-0843, Tel: 81 (03) 3267 8751, Fax: 81-03- 3267 8746.
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Direct neuronal glucose uptake heralds activity-dependent increases in cerebral metabolism
Iben Lundgaard,Baoman Li,Lulu Xie,Hongyi Kang,Simon Sanggaard,John Douglas R Haswell,Wei Sun,Siri Goldman,Solomiya Blekot,Michael L. Nielsen,Takahiro Takano,Rashid Deane +11 more
TL;DR: It is shown, using 2-photon imaging of a near-infrared 2-deoxyglucose analogue (2DG-IR), that glucose is taken up preferentially by neurons in awake behaving mice, and the neuron is identified as the principal locus of glucose uptake as visualized by functional brain imaging.
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Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole orbitrap mass spectrometer.
TL;DR: It is demonstrated that peptide identification on a quadrupole Orbitrap is dependent on sample amounts, acquisition speed, and data quality, which emphasizes the need for acquisition methods tailored for different sample loads and analytical preferences.
Journal ArticleDOI
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation
Ivo A. Hendriks,David Lyon,Clifford Young,Lars Juhl Jensen,Alfred C.O. Vertegaal,Michael L. Nielsen +5 more
TL;DR: An augmented K0–SUMO proteomics strategy is used to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins, providing system-wide evidence for a remarkable degree of cross-talk between SUMOylation and other major PTMs.
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Proteomic Analyses Reveal Divergent Ubiquitylation Site Patterns in Murine Tissues
Sebastian Wagner,Sebastian Wagner,Petra Beli,Brian T. Weinert,Christian Schölz,Christian D. Kelstrup,Clifford Young,Michael L. Nielsen,Jesper V. Olsen,Cord Brakebusch,Chunaram Choudhary +10 more
TL;DR: It is demonstrated that different di-glycine-lysine-specific monoclonal antibodies exhibit sequence preferences, and that their complementary use increases the depth of ubiquitylation site analysis, thereby providing a more unbiased view of protein ubiquitylated.