Structural basis of nucleosome deacetylation and DNA linker tightening by Rpd3S histone deacetylase complex

S Dong, H Li, M Wang, N Rasheed, B Zou, X Gao… - Cell Research, 2023 - nature.com
In Saccharomyces cerevisiae, cryptic transcription at the coding region is prevented by the
activity of Sin3 histone deacetylase (HDAC) complex Rpd3S, which is carried by the …

Structure of the complete Saccharomyces cerevisiae Rpd3S-nucleosome complex

JW Markert, SM Vos, L Farnung - Nature Communications, 2023 - nature.com
Acetylation of histones is a key post-translational modification that guides gene expression
regulation. In yeast, the class I histone deacetylase containing Rpd3S complex plays a …

Epigenetic biomarkers in aging and longevity: Current and future application

M Izadi, N Sadri, A Abdi, S Serajian, D Jalalei… - Life Sciences, 2024 - Elsevier
The aging process has been one of the most necessary research fields in the current
century, and knowing different theories of aging and the role of different genetic, epigenetic …

Nucleosome conformation dictates the histone code

MR Marunde, HA Fuchs, JM Burg, IK Popova, A Vaidya… - Elife, 2024 - elifesciences.org
Histone post-translational modifications (PTMs) play a critical role in chromatin regulation. It
has been proposed that these PTMs form localized 'codes' that are read by specialized …

Deciphering histone H4 lysine acetylation and methylation via sortase-mediated semisynthesis

Y Xiao, K Zou, J Yang, M Wu - Cell Reports Physical Science, 2023 - cell.com
The post-translational modifications of histone H4 play significant roles in regulation of
epigenetic status. Reconstituted nucleosomes that mimic the native chromatin are valuable …

Contemporary Applications of Thioamides and Methods for their Synthesis

TN Hansen, CA Olsen - Chemistry–A European Journal, 2024 - Wiley Online Library
Thioamides are naturally occurring isosteres of amide bonds in which the chalcogen atom of
the carbonyl is changed from oxygen to sulfur. This substitution gives rise to altered …

Deciphering the Allosteric Activation Mechanism of SIRT6 Using Molecular Dynamics Simulations

Z Zhao, J Du, Y Du, Y Gao, M Yu, Y Zhang… - Journal of Chemical …, 2023 - ACS Publications
As a member of the histone deacetylase protein family, the NAD+-dependent SIRT6 plays
an important role in maintaining genomic stability and regulating cell metabolism …

Binding to nucleosome poises human SIRT6 for histone H3 deacetylation

E Smirnova, E Bignon, P Schultz, G Papai, AB Shem - Elife, 2024 - elifesciences.org
Abstract Sirtuin 6 (SIRT6) is an NAD+-dependent histone H3 deacetylase that is prominently
found associated with chromatin, attenuates transcriptionally active promoters and regulates …

Substrates and Cyclic Peptide Inhibitors of the Oligonucleotide‐Activated Sirtuin 7

JE Bolding, AL Nielsen, I Jensen… - Angewandte Chemie …, 2023 - Wiley Online Library
The sirtuins are NAD+‐dependent lysine deacylases, comprising seven isoforms (SIRT1–7)
in humans, which are involved in the regulation of a plethora of biological processes …

Inhibition of SIRT6 aggravates p53-mediated ferroptosis in acute lung injury in mice

Y Cao, T Peng, C Ai, Z Li, X Lei, G Li, T Li, X Wang… - Heliyon, 2023 - cell.com
Although studies have shown that protein 53 (p53)-mediated ferroptosis is involved in acute
lung injury (ALI), the mechanism of its regulation remains unclear. The protective effects of …