Publications by authors named "Chi-Li Lin"
Article Synopsis
- Diabetes is closely associated with Alzheimer’s Disease (AD), characterized by neurotoxic proteins and brain damage, particularly affecting the hippocampus, which is crucial for memory and emotions.
- Type 2 diabetes involves insulin resistance, and recent studies showed that certain subfractions from okra can inhibit the enzyme DPP-4, improving insulin sensitivity and neuron health in the hippocampus by enhancing autophagy.
- This research suggests that treatment with okra extract could potentially mitigate the cognitive and emotional issues linked to insulin resistance in Alzheimer’s patients, highlighting the need for further human trials to confirm these findings.
This study reveals an uncovered mechanism for the regulation of polyamine homeostasis through protein arginyl citrullination of antizyme (AZ), a natural inhibitor of ornithine decarboxylase (ODC). ODC is critical for the cellular production of polyamines. AZ binds to ODC dimers and promotes the degradation of ODC via the 26S proteasome.
View Article and Find Full Text PDFBackground: Human ornithine decarboxylase (ODC) is a well-known oncogene, and the discovery of ODC enzyme inhibitors is a beneficial strategy for cancer therapy and prevention.
Methods: We examined the inhibitory effects of a variety of flavone and flavonol derivatives on ODC enzymatic activity, and performed in silico molecular docking of baicalein, 7,8-dihydroxyflavone and myricetin to the whole dimer of human ODC to investigate the possible binding site of these compounds on ODC. We also examined the cytotoxic effects of these compounds with cell-based studies.
Ornithine decarboxylase (ODC), cyclin D1 (CCND1) and antizyme inhibitor (AZI) promote cell growth. ODC and CCND1 can be degraded through antizyme (AZ)-mediated 26S proteasomal degradation. This paper describes a mechanistic study of the molecular interactions between AZ and its interacting proteins.
View Article and Find Full Text PDFHuman mitochondrial NAD(P)+-dependent malic enzyme (m-NAD(P)-ME) is allosterically activated by the four-carbon trans dicarboxylic acid, fumarate. Previous studies have suggested that the dicarboxylic acid in a trans conformation around the carbon-carbon double bond is required for the allosteric activation of the enzyme. In this paper, the allosteric effects of fumarate analogs on m-NAD(P)-ME are investigated.
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