Author

C. Moreno-Yruela

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:drug response / drug discovery· 2 Assay:ChIP-seq· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

C. A. Olsen· 4 shared A. L. Nielsen· 2 shared A. S. Madsen· 2 shared M. Baek· 2 shared A. Lucidi· 1 shared D. Zhang· 1 shared I. Galleano· 1 shared J. E. Bolding· 1 shared

Activity by Year

2017-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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4 shared papersBiochemistry

C. A. Olsen

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4 papers

Recent·Most cited

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

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

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