Author

C. A. Olsen

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 6 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:drug response / drug discovery· 3 Organism:human· 3 Organism:bacteria (other)· 2 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Assay:ChIP-seq· 1

Frequent Co-Authors

C. Moreno-Yruela· 4 shared A. L. Nielsen· 3 shared A. S. Madsen· 3 shared B. H. Gless· 2 shared B. S. Bejder· 2 shared H. Ingmer· 2 shared J. E. Bolding· 2 shared M. Baek· 2 shared

Activity by Year

2017-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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4 shared papersBiochemistry

C. Moreno-Yruela

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Author profile →

8 papers

Recent·Most cited

A short-lived peptide signal regulates cell-to-cell communication in Listeria monocytogenes

B. S. Bejder, F. Monda, B. H. Gless, M. S. Bojer, H. Ingmer, C. A. Olsen

The paper develops stabilized AIP analogues to study QS in L. monocytogenes, finding that the short-lived thiolactone-containing pentamer is the most potent AIP.

bioRxiv · Jul 4, 2023 · PreprintMicrobiology

Fluorogenic Substrates and Cyclic Peptide Inhibitors of the Oligonucleotide Activated SIRT7

J. E. Bolding, A. L. Nielsen, I. Jensen, T. N. Hansen, L. A. Ryberg, S. T. Jameson, P. Harris, G. H. Peters, J. Denu, J. M. Rogers, C. A. Olsen

This study develops fluorogenic assays and cyclic peptide inhibitors to probe SIRT7 activity and selectivity, revealing its monomeric structure and substrate preferences.

bioRxiv · Jun 16, 2023 · PreprintBiochemistry

Determination of Slow-binding HDAC Inhibitor Potency and Subclass Selectivity

C. Moreno-Yruela, C. A. Olsen

The paper compares the potency and selectivity of slow-binding HDAC inhibitors using discontinuous and continuous assays, finding lower potencies for entinostat and confirming RGFP966's selectivity.

bioRxiv · Dec 18, 2021Biochemistry

Chemical phylogenetics of the staphylococcal quorum sensing landscape

B. H. Gless, B. S. Bejder, L. Vitolo, L. Marques, P. S. Andersen, M. S. Bojer, H. Ingmer, C. A. Olsen

The paper maps staphylococcal quorum sensing interactions by testing over 200 AIPs against reporter strains, identifying a pan-inhibitory AIP that reduces MRSA skin infection in mice.

bioRxiv · Apr 18, 2021 · PreprintMicrobiology

Class I Histone Deacetylases (HDAC1-3) are Histone Lysine Delactylases

C. Moreno-Yruela, D. Zhang, W. Wei, M. Baek, J. Gao, A. L. Nielsen, J. E. Bolding, L. Yang, S. T. Jameson, J. Wong, C. A. Olsen, Y. Zhao

This study identifies HDAC1-3 and SIRT1-3 as enzymes that remove histone lactylation marks, contrasting with the known role of acetylation.

bioRxiv · Mar 24, 2021Biochemistry

Mechanism-based inhibitors of SIRT2: structure-activity relationship, X-ray structures, target engagement, regulation of alpha-tubulin acetylation and inhibition of breast cancer cell migration

A. L. Nielsen, N. Rajabi, N. Kudo, K. L. Larsen, C. Moreno-Yruela, M. Baek, M. Fontenas, A. Lucidi, A. S. Madsen, M. Yoshida, C. A. Olsen

The paper develops potent, selective SIRT2 inhibitors with features suitable for cell culture and therapeutic development.

bioRxiv · Mar 20, 2020 · PreprintBiochemistry

An NAD+-dependent sirtuin depropionylase and deacetylase (Sir2La) from the probiotic bacterium Lactobacillus acidophilus NCFM

S. V. Olesen, N. Rajabi, B. Svensson, C. A. Olsen, A. S. Madsen

This paper identifies and characterizes Sir2La, a NAD+-dependent sirtuin from Lactobacillus acidophilus NCFM, showing it deacetylates and depropionylates lysine residues.

bioRxiv · Jan 23, 2018Biochemistry

Histone Deacetylase 11 is an ε-N-Myristoyllysine Hydrolase

C. Moreno-Yruela, I. Galleano, A. S. Madsen, C. A. Olsen

This study identifies HDAC11 as an ε-N-myristoyllysine hydrolase, showing it efficiently cleaves long-chain acyl modifications and is insensitive to common HDAC inhibitors but inhibited by macrocyclic hydroxamic acid peptides.

bioRxiv · Nov 1, 2017Biochemistry