Surabhi Mehra

The paper identifies an alternatively misfolded PrP species, PrPAM, generated by PRNP mutations that may initially protect against prion replication, explaining delayed disease onset.

This study investigates whether distinct α-synuclein strains contribute to clinical subtypes of multiple system atrophy (MSA) and finds no differences in strain properties between MSA-C and MSA-P.

This study compares four methods of purifying α-synuclein for seed amplification assays, finding that osmotic shock-purified monomer has the lowest aggregation propensity and best inter-batch reproducibility.

The paper compares the interactomes of mouse and bank vole prion proteins in brain tissue to determine if differences in protein interactions explain the bank vole's susceptibility to prions.

The paper identifies key amino acid residues in bank vole prion protein (BVPrP) that enable it to act as a universal prion acceptor, revealing molecular mechanisms for cross-species prion replication.

This study shows that knock-in mice with specific prion protein mutations spontaneously develop prion disease, producing atypical prion strains with similar properties regardless of mutation type.

This study identifies two distinct α-synuclein fibril polymorphs with different structural and functional properties linked to prion-like behavior in Parkinson's disease.

This study investigates how the size of α-synuclein fibril seeds affects their amplification, cellular uptake, and toxicity, revealing distinct mechanisms for small and large seeds.

This study shows that α-synuclein undergoes liquid-liquid phase separation, which transitions to solid amyloid fibrils, contributing to Parkinson's disease pathogenesis.