Sulfur(VI) Fluoride Exchange Chemistry in Solid-Phase Synthesis of Compound Arrays: Discovery of Histone Deacetylase Inhibitors

Autor: Tobias N. Hansen, Daniela Danková, Michael Bæk, Linda Grlaš, Christian A. Olsen

Publikováno v: JACS Au, Vol 4, Iss 5, Pp 1854-1862 (2024)

Externí odkaz: https://doaj.org/article/7c34f47ddeab411d9d8c6102b3e57d53

Chiral Posttranslational Modification to Lysine epsilon-Amino Groups

Autor: Carlos Moreno–Yruela, Michael Bæk, Fabrizio Monda, Christian Adam Olsen

The sophistication of proteomic analysis has revealed that protein lysine residues are posttranslationally modified by a variety of acyl groups. Protein lysine acetylation regulates metabolism, gene expression, and microtubule formation and has been

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8ca7f51996fb7b06d515304a907348cd
https://doi.org/10.26434/chemrxiv-2022-s3xls

Investigation of Carboxylic Acid Isosteres for Inhibition of the Human SIRT5 Lysine Deacylase Enzyme

Autor: Sylvester E. G. Petersen, Michael Bæk, Huy T. Nguyen, Christian R. O. Bartling, Nima Rajabi, Christian A. Olsen, Julie E. Bolding, Alexander L. Nielsen, Tobias Nikolaj Gress Hansen, Kristian Strømgaard, Oskar Ørts Bahlke

Sirtuin 5 (SIRT5) is a protein lysine deacylase enzyme that regulates diverse biology by hydrolyzing -N-carboxyacyllysine posttranslational modifications in the cell. Inhibition of SIRT5 has been linked to potential treatment of several cancers bu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5c0ba5190480559a31c8e30d497899af
https://doi.org/10.26434/chemrxiv-2021-29rtf

Hydroxamic acid-modified peptide microarrays for profiling isozyme-selective interactions and inhibition of histone deacetylases

Autor: Hans Michael Maric, Carlos Moreno-Yruela, Christian A. Olsen, Michael Bæk, Clemens Schulte, Adela-Eugenie Vrsanova

Publikováno v: Nature Communications
Moreno-Yruela, C, Bæk, M, Vrsanova, A, Schulte, C, Maric, H M & Olsen, C A 2021, ' Hydroxamic acid-modified peptide microarrays for profiling isozyme-selective interactions and inhibition of histone deacetylases ', Nature Communications, vol. 12, no. 1 . https://doi.org/10.1038/s41467-020-20250-9
Nature Communications, 12 (1), Art.-Nr.: 62
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)

Histones control gene expression by regulating chromatin structure and function. The posttranslational modifications (PTMs) on the side chains of histones form the epigenetic landscape, which is tightly controlled by epigenetic modulator enzymes and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42e9da135e93a75ce21cf6b045ddcf5d
https://doi.org/10.1038/s41467-020-20250-9

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

Autor: Alexander L. Nielsen, Andreas Stahl Madsen, Nima Rajabi, Kathrine Lundø, Minoru Yoshida, Norio Kudo, Michael Bæk, Christian A. Olsen, Carlos Moreno-Yruela, Alessia Lucidi, Martin Fontenas

Publikováno v: Nielsen, A L, Rajabi, N, Kudo, N, Lundø, K, Moreno-Yruela, C, Bæk, M, Fontenas, M, Lucidi, A, Madsen, A S, Yoshida, M & Olsen, C A 2021, ' Mechanism-based inhibitors of SIRT2: structure–activity relationship, X-ray structures, target engagement, regulation of α-tubulin acetylation and inhibition of breast cancer cell migration ', RSC Chemical Biology, vol. 2, pp. 612-626 . https://doi.org/10.1039/D0CB00036A
RSC Chemical Biology

Sirtuin 2 (SIRT2) is a protein deacylase enzyme that removes acetyl groups and longer chain acyl groups from post-translationally modified lysine residues. It affects diverse biological functions in the cell and has been considered a drug target in r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5286e36b7d84447506d7380fe9a23ce3
https://doi.org/10.1101/2020.03.20.000380