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From McDonnell et. al. Cell Reports 2016: Cells integrate nutrient sensing and metabolism to coordinate proper cellular responses to a particular nutrient source. For example, glucose drives a gene expression program characterized by activating genes involved in its metabolism, in part, by increasi...
ORGANISM(S): Mus musculus (Mouse) 
2016-12-22 | PXD005040 | Pride
The mechanisms underlying the formation of acyl protein modifications remain poorly understood. By investigating the reactivity of endogenous acyl-CoA metabolites, we found a class of acyl-CoAs that undergoes intramolecular catalysis to form reactive intermediates which non-enzymatically modify prot...
ORGANISM(S): Mus musculus (Mouse) 
2017-04-11 | PXD005895 | Pride
Sirtuins are NAD+-dependent protein deacylases that regulate several aspects of metabolism and aging. In contrast to the other mammalian sirtuins, the primary enzymatic activity of mitochondrial sirtuin 4 (SIRT4) and its overall role in metabolic control has remained enigmatic. Using a combination o...
ORGANISM(S): Mus musculus (Mouse) 
2017-04-05 | PXD005896 | Pride
Mitochondrial Sirtuin 5 (SIRT5) is an NAD+-dependent demalonylase, desuccinylase, and deglutarylase that controls several metabolic pathways. A number of recent studies point to SIRT5 desuccinylase activity being important in maintaining cardiac function and metabolism under stress. Previously, we d...
ORGANISM(S): Mus musculus (Mouse) 
2018-05-16 | PXD008728 | Pride
Nicotinamide riboside supplements (NRS) have been touted as a nutraceutical that promotes cardiometabolic and musculoskeletal health by enhancing nicotinamide adenine dinucleotide (NAD+) biosynthesis, mitochondrial function and/or the activities of NAD-dependent sirtuin deacetylase enzymes. This inv...
ORGANISM(S): Mus musculus (Mouse) 
2022-02-17 | PXD027904 | Pride
From Peterson et. al. 2018: SIRT3 is an NAD+-dependent mitochondrial protein deacetylase purported to influence metabolism through post-translational modification of metabolic enzymes. Fuel-stimulated insulin secretion, which involves mitochondrial metabolism, could be susceptible to SIRT3-mediated...
ORGANISM(S): Rattus norvegicus (Rat) 
2018-06-21 | PXD009509 | Pride
A double knockout (DKO) mouse model harboring muscle-specific deficits in acetyl CoA buffering by carnitine acetyltransferase (CrAT), and lysine deacetylation by SIRT3, resulted in additive hyperacetylation of the mitochondrial proteome, which was augmented exponentially by chronic high fat feeding....
ORGANISM(S): Mus musculus (Mouse) 
2019-11-25 | PXD014586 | Pride
A wide range of protein acyl modifications has been identified on enzymes across various metabolic processes; however, the impact of these modifications remains poorly understood. Protein glutarylation is a recently identified modification that can be non-enzymatically driven by glutaryl-CoA. In mam...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2022-02-21 | PXD018156 | Pride
Strong associations exist between branched chain amino acids (BCAA) and dysregulated glucose and lipid metabolism, but the underlying mechanisms are not well understood. Here we report that inhibition of the kinase (BDK) or overexpression of the phosphatase (PPM1K) that regulate branched-chain keto...
ORGANISM(S): Rattus norvegicus (Rat) 
2018-05-18 | PXD009122 | Pride
Although caloric restriction (CR) was first shown to extend the lifespan of rodents over 75 years ago, the underlying mechanisms remain unclear. Additionally, the majority of published studies have focused on the effects of short-term CR. To better understand cell signaling alterations in a tissue k...
ORGANISM(S): Mus Musculus (mouse) 
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