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Molecular Mechanisms of Alzheimer's Disease Induced by Amyloid-β and Tau Phosphorylation Along with RhoA Activity: Perspective of RhoA/Rho-Associated Protein Kinase Inhibitors for Neuronal Therapy.
Cells
January 2025
Department of Biochemistry, Hallym University College of Medicine, Chuncheon 24252, Kangwon-do, Republic of Korea.
Amyloid-β peptide (Aβ) is a critical cause of Alzheimer's disease (AD). It is generated from amyloid precursor protein (APP) through cleavages by β-secretase and γ-secretase. γ-Secretase, which includes presenilin, is regulated by several stimuli.
View Article and Find Full Text PDFSynergetic role of TRPV4 inhibitor and mechanical loading on reducing inflammation.
Front Immunol
January 2025
Department of Bioengineering, College of Engineering, University of Toledo, Toledo, OH, United States.
Resolution of inflammation is essential for normal tissue healing and regeneration, with macrophages playing a key role in regulating this process through phenotypic changes from a pro-inflammatory to an anti-inflammatory state. Pharmacological and mechanical (mechanotherapy) techniques can be employed to polarize macrophages toward an anti-inflammatory phenotype, thereby diminishing inflammation. One clinically relevant pharmacological approach is the inhibition of Transient Receptor Potential Vanilloid 4 (TRPV4).
View Article and Find Full Text PDFStructural insights into actin filament turnover.
Trends Cell Biol
January 2025
Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany. Electronic address:
The dynamic turnover of actin filaments drives the morphogenesis and migration of all eukaryotic cells. This review summarizes recent insights into the molecular mechanisms of actin polymerization and disassembly obtained through high-resolution structures of actin filament assemblies. We first describe how, upon polymerization, actin subunits age within the filament through changes in their associated adenine nucleotide.
View Article and Find Full Text PDFTMT-labelled quantitative proteomics reveals the mechanism of Rhodotorula mucilaginosa on proteolysis of dry-cured ham: Structural protein degradation, amino acid release and taste improvement.
Food Chem
January 2025
Zhejiang Key Laboratory of Intelligent Food Logistic and Processing; Zhejiang-Malaysia Joint Research Laboratory for Agricultural Product Processing and Nutrition; College of Food Science and Engineering, Ningbo University, Ningbo 315211, China. Electronic address:
To investigate the mechanism of Rhodotorula mucilaginosa on structural protein degradation and taste development of Jinhua ham, the effects of Rhodotorula mucilaginosa and Pichia kudriavzevii on proteolytic enzyme activities, surface hydrophobicity, myofibril microstructure, protein degradation, free amino acids and sensory attributes were investigated during the dry-ripening of Jinhua ham. The inoculation of Rhodotorula mucilaginosa EIODSF019 (RE) and Rhodotorula mucilaginosa XZY63-3 (RX) consistently exhibited higher proteolytic enzyme activities compared with Pichia kudriavzevii XS-5 (PK). The decrease of α-helix exposing more internal hydrophobic groups of myofibrillar proteins, contributed to higher surface hydrophobicity of RE compared with PK and RX.
View Article and Find Full Text PDFInvestigation the antioxidant mechanisms of Capsaicinoids on myofibrillar protein based on multispectral and molecular docking.
Food Chem
January 2025
School of Food and Bioengineering, Xihua University, Chengdu 610039, China. Electronic address:
This study investigated the interactions between Capsaicinoids (CAPs) and beef myofibrillar proteins (MPs) in a peroxyl radical system and elucidated the antioxidant mechanisms of CAPs by multispectral and molecular docking. Results showed that low concentration CAPs prevented the oxidative changes of protein structure caused by the attack of AAPH radicals on MPs, while high concentration of CAPs changed the structure of the proteins to form more small molecule aggregates, and reduce the binding of actin-myosin, which was conducive to the tenderization of the meats. CAPs bound to the MPs through hydrophobic interaction, hydrogen bonding and electrostatic interaction, altering the secondary and tertiary structure of MPs, increasing the α-helix content of MPs, and improving the antioxidant structural stability of MPs.
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