Novel Structure and Function of Human Sirtuins
Grant Data
Project Title
Novel Structure and Function of Human Sirtuins
Principal Investigator
Professor Hao, Quan
(Project Coordinator (PC))
Co-Investigator(s)
Professor Li Xiang David
(Co-principal investigator)
Professor Huang Jiandong
(Co-principal investigator)
Duration
36
Start Date
2015-03-01
Amount
5400000
Conference Title
Novel Structure and Function of Human Sirtuins
Presentation Title
Keywords
crystal structure, enzymatic function, epigenetics, inhibitor design, sirtuin
Discipline
Structural Biology,Biochemistry
HKU Project Code
C7037-14G
Grant Type
Collaborative Research Fund (CRF) - Group Research Project
Funding Year
2014
Status
Completed
Objectives
1) To solve the crystal structures of SIRT4 and SIRT7 and investigate their potential enzymatic functions in vitro and in vivo. 2) To probe SIRT1-3’s defatty acyl modification activity and structural basis. 3) To develop mechanism-based inhibitors for all human sirtuins (SIRT1-7).
All Publications
Title | Author(s) | Issue Date | |
---|---|---|---|
2018 | |||
SIRT7 Is an RNA-Activated Protein Lysine Deacylase Journal:ACS Chemical Biology | 2016 | ||
SIRT7 Is Activated by DNA and Deacetylates Histone H3 in the Chromatin Context Journal:ACS Chemical Biology | 2016 | ||
Photo-lysine captures proteins that bind lysine post-translational modifications Journal:Nature Chemical Biology | 2016 | ||
Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation Journal:Proceedings of the National Academy of Sciences | 2018 | ||
Histone Ketoamide Adduction by 4-Oxo-2-nonenal Is a Reversible Posttranslational Modification Regulated by Sirt2 Journal:ACS Chemical Biology | 2017 | ||
Efficient Demyristoylase Activity of SIRT2 Revealed by Kinetic and Structural Studies Journal:Scientific Reports | 2015 | ||
Deacylation Mechanism by SIRT2 Revealed in the 1′-SH-2′-O-Myristoyl Intermediate Structure Journal:Cell Chemical Biology | 2017 |