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http://dx.doi.org/10.1007/0-387-34132-3_14 | DOI Listing |
Immunol Res
January 2025
Department of Otolaryngology, Qingdao Traditional Chinese Medicine Hospital (Qingdao Hiser Hospital), Qingdao Hiser Hospital Affiliated of Qingdao University, Qingdao, 266033, Shandong, People's Republic of China.
Baicalein, one of the major active flavonoids found in Scutellaria baicalensis, has been revealed to exhibit potent anti-inflammatory properties in allergic airway inflammation. This study aimed to explore the role of baicalein and its relevant mechanism in the treatment of allergic rhinitis (AR). The bioinformatics tools were used to predict the targets of baicalein and AR-related genes.
View Article and Find Full Text PDFPoult Sci
January 2025
Feedworks Pty Ltd, Romsey, VIC, Australia.
The effectiveness of guanidinoacetic acid (GAA) in reduced protein (RP) diets on performance and gut health of broilers under heat stress is largely unknown. A 35-d experiment was conducted using four dietary treatments: a standard protein diet (SP, 22.1 and 20.
View Article and Find Full Text PDFCell Rep
January 2025
Institute of Chemistry, Academia Sinica, Taipei 115, Taiwan; Sustainable Chemical Science and Technology, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan; Department of Applied Chemistry, National Chiayi University, Chiayi City 600, Taiwan; Neuroscience Program of Academia Sinica, Academia Sinica, Taipei 115, Taiwan. Electronic address:
The toxicity of C9ORF72-encoded polyproline-arginine (poly-PR) dipeptide is associated with its ability to disrupt the liquid-liquid phase separation of intrinsically disordered proteins participating in the formation of membraneless organelles, such as the nucleolus and paraspeckles. Amyotrophic lateral sclerosis (ALS)-related TAR DNA-binding protein 43 (TDP-43) also undergoes phase separation to form nuclear condensates (NCs) in response to stress. However, whether poly-PR alters the nuclear condensation of TDP-43 in ALS remains unclear.
View Article and Find Full Text PDFInsulin degrading enzyme (IDE) is a dimeric 110 kDa M16A zinc metalloprotease that degrades amyloidogenic peptides diverse in shape and sequence, including insulin, amylin, and amyloid-β, to prevent toxic amyloid fibril formation. IDE has a hollow catalytic chamber formed by four homologous subdomains organized into two ∼55 kDa N- and C-domains (IDE-N and IDE-C, respectively), in which peptides bind, unfold, and are repositioned for proteolysis. IDE is known to transition between a closed state, poised for catalysis, and an open state, able to release cleavage products and bind new substrate.
View Article and Find Full Text PDFEuroasian J Hepatogastroenterol
December 2024
Department of Gastroenterology and Metabology, Ehime University Graduate School of Medicine, Ehime, Japan.
Objectives: To predict and characterize the three-dimensional (3D) structure of protein arginine methyltransferase 2 (PRMT2) using homology modeling, besides, the identification of potent inhibitors for enhanced comprehension of the biological function of this protein arginine methyltransferase (PRMT) family protein in carcinogenesis.
Materials And Methods: An method was employed to predict and characterize the three-dimensional structure. The bulk of PRMTs in the PDB shares just a structurally conserved catalytic core domain.
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