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Christian Schölz

Researcher at Ludwig Maximilian University of Munich

Publications -  14
Citations -  2079

Christian Schölz is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Acetylation & Lysine. The author has an hindex of 9, co-authored 13 publications receiving 1653 citations. Previous affiliations of Christian Schölz include University of Copenhagen.

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Journal ArticleDOI

Lysine Succinylation Is a Frequently Occurring Modification in Prokaryotes and Eukaryotes and Extensively Overlaps with Acetylation

TL;DR: A systems-wide view of succinylation and its dynamic regulation is provided and its extensive overlap with acetylation is shown, indicating that succinylated levels are globally affected by succinyl-CoA concentration.
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Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli

TL;DR: It is found that most acetylation occurred at a low level and accumulated in growth-arrested cells in a manner that depended on the formation of acetyl-phosphate (AcP) through glycolysis, suggesting that AcP may acetylate proteins nonenzymatically in cells.
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Time-Resolved Analysis Reveals Rapid Dynamics and Broad Scope of the CBP/p300 Acetylome

TL;DR: This work combined quantitative proteomics with CBP/p300-specific catalytic inhibitors, bromodomain inhibitor, and gene knockout to reveal a comprehensive map of regulated acetylation sites and their dynamic turnover rates, revealing a dynamic balance between acetylations and deacetylation.
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Proteomic Analyses Reveal Divergent Ubiquitylation Site Patterns in Murine Tissues

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.
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Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae.

TL;DR: Qualitative mass spectrometry data show that a majority of acetylation occurs at very low levels in exponentially growing yeast and is uniformly affected by exposure to acetyl‐CoA.