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- Cai, Demin, et al.
(author)
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Nuclear Receptors in Hepatic Glucose and Lipid Metabolism During Neonatal and Adult Life
- 2017
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In: Current protein and peptide science. - : BENTHAM SCIENCE PUBL LTD. - 1389-2037 .- 1875-5550. ; 18:6, s. 548-561
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Research review (peer-reviewed)abstract
- Research efforts focusing on metabolic diseases have established a close conjunction between glucolipid abnormalities and nuclear receptors, a large superfamily of receptors including classic peroxisome proliferation-activated receptors (PPARs), liver X receptors (LXRs), farnesoid X receptors (FXRs) and glucocorticoid receptors (GRs) together with burgeoning retinoic acid receptor-related orphan receptors (RORs) and REV-ERBs. Nuclear receptors are identified to control a series of physiological and pathological processes of glucose and lipid metabolism and also implicated to mediate the long-term effects of early environmental and nutritional experiences on the formation of adult chronic metabolic disorders in human and animals. Thus, nuclear receptors play profound roles in fetal programming and adult regulation of glucolipid metabolism. In this review, we provide an overview on the recent advances in the field of nuclear receptors focusing on their roles in lipid and glucose metabolism during early and late life courses. We hope that this knowledge may shed new lights on identifying the novel target molecules or pathways for the prevention and treatment of metabolic disorders involving disrupted glucose and lipid homeostasis in human and animals.
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- Choi, Seong Il
(author)
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A Simple Principle for Understanding the Combined Cellular Protein Folding and Aggregation
- 2020
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In: Current protein and peptide science. - : Bentham Science Publishers Ltd.. - 1389-2037 .- 1875-5550. ; 21:1, s. 3-21
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Research review (peer-reviewed)abstract
- Proteins can undergo kinetic/thermodynamic partitioning between folding and aggregation. Proper protein folding and thermodynamic stability are crucial for aggregation inhibition. Thus, proteinfolding principles have been widely believed to consistently underlie aggregation as a consequence of conformational change. However, this prevailing view appears to be challenged by the ubiquitous phenomena that the intrinsic and extrinsic factors including cellular macromolecules can prevent aggregation, independently of (even with sacrificing) protein folding rate and stability. This conundrum can be definitely resolved by 'a simple principle' based on a rigorous distinction between protein folding and aggregation: aggregation can be controlled by affecting the intermolecular interactions for aggregation, independently of the intramolecular interactions for protein folding. Aggregation is beyond protein folding. A unifying model that can conceptually reconcile and underlie the seemingly contradictory observations is described here. This simple principle highlights, in particular, the importance of intermolecular repulsive forces against aggregation, the magnitude of which can be correlated with the size and surface properties of molecules. The intermolecular repulsive forces generated by the common intrinsic properties of cellular macromolecules including chaperones, such as their large excluded volume and surface charges, can play a key role in preventing the aggregation of their physically connected polypeptides, thus underlying the generic intrinsic chaperone activity of soluble cellular macromolecules. Such intermolecular repulsive forces of bulky cellular macromolecules, distinct from protein conformational change and attractive interactions, could be the puzzle pieces for properly understanding the combined cellular protein folding and aggregation including how proteins can overcome their metastability to amyloid fibrils in vivo.
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