Area of research
Physiology · Molecular Biology
Research interest
Research interests include Alzheimer's disease research and treatments, RNA Research and Splicing, Liver Disease Diagnosis and Treatment, and High Entropy Alloys Studies.
Measurement of Very-High-Energy Diffuse Gamma-Ray Emissions from the Galactic Plane with LHAASO-WCDA
Risk Factors Analysis and Predictive Model Construction for Autoimmune Gastritis: A Nationwide Multicenter Case–Control Study in China
Gut microbiome pattern impacts treatment response in primary biliary cholangitis
Measurement of Ultra-High-Energy Diffuse Gamma-Ray Emission of the Galactic Plane from 10 TeV to 1 PeV with LHAASO-KM2A
Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation
Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation
Conformational change of α-synuclein fibrils in cerebrospinal fluid from different clinical phases of Parkinson’s disease
Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores
Chiral gold nanoparticles enantioselectively rescue memory deficits in a mouse model of Alzheimer’s disease
Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils
CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
Cryo-EM structures of four polymorphic TDP-43 amyloid cores
Comprehensive Analysis of Serum and Fecal Bile Acid Profiles and Interaction with Gut Microbiota in Primary Biliary Cholangitis
Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation
Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation
Author Correction: Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design
Author Correction: Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design
Gut microbial profile is altered in primary biliary cholangitis and partially restored after UDCA therapy