Back to search

Article

Mechanism of activation for the sirtuin 6 protein deacylase

2020-01-01

Abstract excerpt

The histone deacetylase sirtuin 6 (SIRT6) regulates numerous biological functions, including transcriptional repression, DNA repair, and telomere maintenance. Recombinant SIRT6 displays catalytic efficiencies 2 orders of magnitude greater for long-chain deacylation than deacetylation against peptide substrates; however, deacetylation can be enhanced by allosteric small-molecule activators. Here, we investigated th...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
3a88a9d9-79f7-5547-b4d7-d188235439ed
DOI
10.1016/s0021-9258(17)49896-6
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Mechanism of activation for the sirtuin 6 protein deacylaseDOI 10.1016/s0021-9258(17)49896-6
Mechanism of activation for the sirtuin 6 protein deacylase.Semantic proximity
Biological and catalytic functions of sirtuin 6 as targets for small-molecule modulatorsSemantic proximity
Evolved, Selective Erasers of Distinct Lysine AcylationsSemantic proximity
Identifying the functional contribution of the defatty-acylase activity of SIRT6.Semantic proximity
SIRT7 Is an RNA-Activated Protein Lysine Deacylase.Semantic proximity
Role of the Substrate Specificity-Defining Residues of Human SIRT5 in Modulating the Structural Stability and Inhibitory Features of the Enzyme.Semantic proximity
Substrates and Cyclic Peptide Inhibitors of the Oligonucleotide Activated SIRT7Semantic proximity
DNA stimulates SIRT6 to mono-ADP-ribosylate proteins within histidine repeatsSemantic proximity
The Two-Faced Role of SIRT6 in CancerSemantic proximity
Nonallosteric Sirtuin Enzyme Activation: Characterization of Hit CompoundsSemantic proximity
Integrative computational simulations and functional assays decode allosteric dysregulation in a pathogenic SIRT6 variant.Semantic proximity
The Substrate Specificity of SirtuinsSemantic proximity
Select a neighboring publication to make it the new centre.