Area of research
Physiology · Hardware and Architecture
Research interest
Research interests include Alzheimer's disease research and treatments, Parallel Computing and Optimization Techniques, Distributed and Parallel Computing Systems, and Cholinesterase and Neurodegenerative Diseases.
Small molecules disaggregate alpha-synuclein and prevent seeding from patient brain-derived fibrils
Structure-based design of nanobodies that inhibit seeding of Alzheimer’s patient–extracted tau fibrils
Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils
Structure-based discovery of small molecules that disaggregate Alzheimer’s disease tissue derived tau fibrils in vitro
De novo designed protein inhibitors of amyloid aggregation and seeding
Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies
Extended β-Strands Contribute to Reversible Amyloid Formation
Bioinformatic identification of previously unrecognized amyloidogenic proteins
Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores
Inhibition of synucleinopathic seeding by rationally designed inhibitors
Structure-based inhibitors of amyloid beta core suggest a common interface with tau
Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation
Structure-based inhibitors halt prion-like seeding by Alzheimer’s disease–and tauopathy–derived brain tissue samples
Role of the extent of prophylactic regional lymph node radiotherapy on survival in high‐risk neuroblastoma: A report from the COG A3973 study
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design
Atomic structures of corkscrew‐forming segments of SOD1 reveal varied oligomer conformations
Author Correction: Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design
Structure-based inhibitors of tau aggregation
Common fibrillar spines of amyloid-β and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors