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-Reference-Cited by-同舟云学术

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

Published:2021 Issue:2 Volume:2 Page:612-626
ISSN:2633-0679
Container-title:RSC Chemical Biology
language:en
Short-container-title:RSC Chem. Biol.

Author:

Nielsen Alexander L.¹²³⁴⁵^ORCID,Rajabi Nima¹²³⁴⁵,Kudo Norio⁶⁷⁸,Lundø Kathrine⁹²³⁴⁵^ORCID,Moreno-Yruela Carlos¹²³⁴⁵^ORCID,Bæk Michael¹²³⁴⁵^ORCID,Fontenas Martin¹²³⁴⁵,Lucidi Alessia¹²³⁴⁵,Madsen Andreas S.¹²³⁴⁵,Yoshida Minoru⁶⁷⁸,Olsen Christian A.¹²³⁴⁵^ORCID

Affiliation:

1. Center for Biopharmaceuticals & Department of Drug Design and Pharmacology

2. Faculty of Health and Medical Sciences

3. University of Copenhagen

4. Copenhagen

5. Denmark

6. RIKEN Center for Sustainable Resource Science (S13)

7. Wako

8. Japan

9. Novo Nordisk Foundation Center for Basic Metabolic Research

Abstract

Sirtuin 2 (SIRT2) is a protein deacylase enzyme that removes acetyl groups and longer chain acyl groups from post-translationally modified lysine residues. Here, we developed small peptide-based inhibitors of its activity in living cells in culture.

Funder

H2020 European Research Council

Novo Nordisk Fonden

Carlsbergfondet

Lundbeckfonden

Japan Society for the Promotion of Science

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2021/CB/D0CB00036A

Reference100 articles.

1. The Substrate Specificity of Sirtuins