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Deletion of FgAtg27 decreases the pathogenicity of Fusarium graminearum through influence autophagic process.
Int J Biol Macromol
January 2025
Engineering Research Center of Ecology and Agricultural Use of Wetland, Ministry of Education, MARA Key Laboratory of Sustainable Crop Production in the Middle Reaches of the Yangtze River (Co-construction by Ministry and Province), Hubei Engineering Research Center for Pest Forewarning and Management, College of Agriculture, Yangtze University, Jingzhou 434025, Hubei, China. Electronic address:
Autophagy is a conserved and unique degradation system in eukaryotic cells, which plays crucial roles in the growth, development and pathogenesis of Fungi. Despite that, it is poorly understood in Fusarium graminearum currently. Here, we identified an autophagy gene FgAtg27 from F.
View Article and Find Full Text PDFTau destabilization in a familial deletion mutant K280 accelerates its fibrillization and enhances the seeding effect.
J Biol Chem
January 2025
Genomics Research Center, Academia Sinica, Taipei, Taiwan; Taiwan International Graduate Program in Interdisciplinary Neuroscience, National Yang Ming Chiao Tung University and Academia Sinica, Taipei, Taiwan; Department of Biochemical Science and Technology, National Taiwan University, Taipei, Taiwan; Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Institute of Biological Chemistry, Academia Sinica; Institute of Biochemical Sciences, National Taiwan University; Taiwan International Graduate Program in Interdisciplinary Neuroscience, National Taiwan University and Academia Sinica, Taipei, Taiwan. Electronic address:
Tauopathies cover a range of neurodegenerative diseases in which natively unfolded tau protein aggregates and spreads in the brain during disease progression. To gain insights into the mechanism of tau structure and spreading, here, we examined the biochemical and cellular properties of human full-length wild-type and familial mutant tau, ΔK280, with a deletion at lysine 280. Our results showed that both wild-type and mutant tau are predominantly monomeric by analytical ultracentrifugation.
View Article and Find Full Text PDFINTERACTION OF SMALL HEAT SHOCK PROTEINS WITH BAG3.
Biochimie
January 2025
Department of Biochemistry, School of Biology, M.V. Lomonosov Moscow State University; Department of Biochemistry and Regenerative Biomedicine Faculty of Basic Medicine, M.V. Lomonosov Moscow State University. Electronic address:
BAG3 is a universal adapter protein involved in various cellular processes, including the regulation of apoptosis, chaperone-assisted selective autophagy, and heat shock protein function. The interaction between small heat shock proteins (sHsps) and their α-crystallin domains (Acds) with full-length BAG3 protein and its IPV domain was analyzed using size-exclusion chromatography, native gel electrophoresis, and chemical cross-linking. HspB7 and the 3D mutant of HspB1 (which mimics phosphorylation) showed no interaction, HspB6 weakly interacted, and HspB8 strongly interacted with full-length BAG3.
View Article and Find Full Text PDFStructure-based discovery of novel diarylpyrimidines as potent and selective Non-Nucleoside reverse transcriptase inhibitors: From CH(CN)-Biphenyl-Diarylpyrimidines to CNNH-Biphenyl-Diarylpyrimidines.
Eur J Med Chem
January 2025
Sichuan Research Center for Drug Precision Industrial Technology, West China School of Pharmacy, Sichuan University, Chengdu, 610041, China; Engineering Center of Catalysis and Synthesis for Chiral Molecules, Department of Chemistry, Fudan University, Shanghai, 200433, China; Shanghai Engineering Center of Industrial Asymmetric Catalysis for Chiral Drugs, Shanghai, 200433, China; Institute of Flow Chemistry and Engineering, School of Chemistry and Materials, Jiangxi Normal University, Nanchang, 330022, China. Electronic address:
In order to enhance the anti-HIV-1 potency and selectivity of the previously reported compound 3 (EC = 27 nM, SI = 1361), a series of novel biphenyl-diarylpyrimidine derivatives were developed by employing structure-based drug design strategy. Among these derivatives, compound M44 demonstrated the most potent inhibitory activity against wild-type (WT) HIV-1 as well as five drug-resistant mutants (EC = 5-148 nM), which were 5-173 times more potent than that of 3 (EC = 27-9810 nM). Furthermore, this analogue exhibited approximately 11-fold lower cytotoxicity (CC = 54 μM) than that of etravirine and rilpivirine.
View Article and Find Full Text PDFEngineering dimer mutants of human geranylgeranyl pyrophosphate synthase.
PLoS One
January 2025
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland and Labrador, Canada.
Geranylgeranyl pyrophosphate synthase (GGPPS), a key enzyme in protein prenylation, plays a critical role in cellular signal transduction and is a promising target for cancer therapy. However, the enzyme's native hexameric quaternary structure presents challenges for crystallographic studies. The primary objective of this study was to engineer dimeric forms of human GGPPS to facilitate high-resolution crystallographic analysis of its ligand binding interactions.
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