Pub. Date : 2017 May 15
PMID : 28504272
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins. | Adenosine Triphosphate | sirtuin 1 | Homo sapiens |
| 2 | Here, we report that Sirt1 is negatively regulated by ATP, which binds to the C-terminal domain (CTD) of Sirt1. | Adenosine Triphosphate | sirtuin 1 | Homo sapiens |
| 3 | Here, we report that Sirt1 is negatively regulated by ATP, which binds to the C-terminal domain (CTD) of Sirt1. | Adenosine Triphosphate | sirtuin 1 | Homo sapiens |
| 4 | ATP suppresses Sirt1 activity by impairing the CTD"s ability to bind to the deacetylase domain as well as its ability to function as the substrate recruitment site. | Adenosine Triphosphate | sirtuin 1 | Homo sapiens |
| 5 | Mutations that prevent ATP binding increase Sirt1"s ability to promote stress resistance and inhibit adipogenesis under high-ATP conditions. | Adenosine Triphosphate | sirtuin 1 | Homo sapiens |
| 6 | Mutations that prevent ATP binding increase Sirt1"s ability to promote stress resistance and inhibit adipogenesis under high-ATP conditions. | Adenosine Triphosphate | sirtuin 1 | Homo sapiens |