A5014460828- Alzheimer's disease research and treatments
- Drug Transport and Resistance Mechanisms
- Lipid Membrane Structure and Behavior
- Prion Diseases and Protein Misfolding
- Cholinesterase and Neurodegenerative Diseases
- Autophagy in Disease and Therapy
- Nanopore and Nanochannel Transport Studies
- Trace Elements in Health
- X-ray Diffraction in Crystallography
- Supramolecular Self-Assembly in Materials
- Malaria Research and Control
- Crystallization and Solubility Studies
- Computational Drug Discovery Methods
- Porphyrin and Phthalocyanine Chemistry
- Crystallography and molecular interactions
- Advanced Glycation End Products research
- Enzyme-mediated dye degradation
- Microbial Metabolic Engineering and Bioproduction
- Protein Interaction Studies and Fluorescence Analysis
- Adipose Tissue and Metabolism
- Biochemical effects in animals
- Fish Biology and Ecology Studies
- Cancer, Lipids, and Metabolism
- Enzyme Catalysis and Immobilization
- Metal-Catalyzed Oxygenation Mechanisms
Huazhong University of Science and Technology
2017-2025
Chinese Academy of Fishery Sciences
2024
Ministry of Agriculture and Rural Affairs
2024
Lund University
2024
Paul Scherrer Institute
2019-2023
Wenzhou Medical University
2023
First Affiliated Hospital of Wenzhou Medical University
2023
Shanghai Jiao Tong University
2020
Nantong University
2014-2020
Sichuan University
2006-2013
We analyzed aging parameters using a mechanistic target of rapamycin (mTOR) hypomorphic mouse model. Mice with two (mTOR(Δ/Δ)) alleles are viable but express mTOR at approximately 25% wild-type levels. These animals demonstrate reduced mTORC1 and mTORC2 activity exhibit an 20% increase in median survival. While mTOR(Δ/Δ) mice smaller than mice, these do not any alterations normalized food intake, glucose homeostasis, or metabolic rate. Consistent their increased lifespan, exhibited reduction...
Impaired or deficient autophagy is believed to cause contribute aging, as well a number of age-related pathologies. The exact mechanism through which alterations in induce these various pathologies not understood. Here we describe the creation two vivo mouse models that allow for characterization alteration mitochondrial function and contribution corresponding oxidative stress following deletion Atg7. Using demonstrate isolated mitochondria obtained from Atg7-/- skeletal muscle exhibit...
Amyloid-β peptide (Aβ) oligomers are pathogenic species of amyloid aggregates in Alzheimer's disease. Like certain protein toxins, Aβ permeabilize cellular membranes, presumably through a pore formation mechanism. Owing to their structural and stoichiometric heterogeneity, the structure these pores remains be characterized. We studied functional Aβ42-pore equivalent, created by fusing Aβ42 oligomerizing, soluble domain α-hemolysin (αHL) toxin. Our data reveal Aβ42-αHL share major structural,...
FeTPPS binds to the His20 residue of hCT, delaying switch its α-helix bundles into β-sheet-rich fibrils.
In search of water-soluble artemisinin derivatives that are more stable than sodium artesunate, over 30 containing an amino group (compounds 3−5) were synthesized and tested in mice. All products (except 5a 5b) the β isomers. These basic compounds combined with organic acids (oxalic acid, maleic etc.) to yield corresponding salts. Generally, maleates have better solubility water oxalates. The aqueous solutions these salts can be kept at room temperature for several weeks without any...
Abstract Amyloid-β (Aβ) peptide aggregation plays a central role in the progress of Alzheimer’s disease (AD), which Aβ-deposited extracellular amyloid plaques are major hallmark. The brain micro-environmental variation AD patients, like local acidification, increased ionic strength, or changed metal ion levels, cooperatively modulates Aβ peptides. Here, we investigate multivariate effects varied pH, strength and Zn 2+ on 40 fibrillation kinetics. Our results reveal that kinetics strongly...
The lipid-α-Synuclein (α-Syn) interaction plays a crucial role in the pathogenesis of Parkinson's disease. Here, we investigate lipid-binding and -unbinding kinetics α-Syn an α-hemolysin (αHL) single nanopore. Under applied voltage, engineered sequence can be trapped at nanopore due to dielectrophoretic force. conformational switch events observed pore-membrane junction through interpretation blockade current amplitudes dwell time. This allows further analysis dynamics. We study how...
Amyloid-β plaques and oxidative stress are the major hallmarks of Alzheimer's disease. Our previous study found that heme-Aβ complex enhanced catalytic effect free heme on protein tyrosine nitration in presence hydrogen peroxide (H2O2) nitrite (NO2-). Y10 Aβ could be first target to nitrated. We also Aβ1-40 significantly decreased its aggregation. However, a contrary report showed Aβ1-42 by peroxynitrite To rule out interference caused oxidation, we used synthetic nitrated influence Aβ1-42's...
Oligomerization of antimicrobial peptides (AMPs) is critical in their effects on pathogens. LL-37 and its truncated fragments are widely investigated regarding structures, activities, application, such as developing new antibiotics. Due to the small size weak intermolecular interactions fragments, it still elusive establish relationship between oligomeric states activities. Here, an α-hemolysin nanopore, mass spectrometry (MS), molecular dynamic (MD) simulations used characterize two...
The deposition of human islet amyloid polypeptide (hIAPP) within β-cells is implicated in the etiology type 2 diabetes mellitus (T2Dm). It was reported that heme could bind to hIAPP. We speculate binding may affect aggregation In this study, UV-vis spectroscopy used detect interaction pattern between and ThT Bis-ANS fluorescence assay, circular dichroism spectroscopy, gel electrophoresis transmission electron microscopy were employed study effect on found dramatically inhibited hIAPP...
Protein homeostasis collapse typically leads to protein aggregation into amyloid fibrils and diffuse amorphous aggregates, which both occur in Alzheimer's other neurodegenerative diseases, but their relationship remains be clarified. Here we examine the interactions between amorphously aggregated non-chaperone proteins (albumin, β-lactoglobulin, superoxide dismutase 1) amyloid-β (Aβ) peptides. Amorphous aggregates suppress primary nucleation elongation of Aβ fibrillation modulate toxicity....
If the tetraphenylporphyrin of a metalloporphyrin and an amyloid protein have opposite charge properties, will be effective inhibitor this protein.