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Evolutionarily Conserved Proline Residues Impede the Misfolding of the Mouse Prion Protein by Destabilizing an Aggregation-competent Partially Unfolded Form

PAL, SUMAN; UDGAONKAR, JAYANT B (Elsevier B.V., 2022-12)

The misfolding of the prion protein has been linked to several neurodegenerative diseases. Despite extensive studies, the mechanism of the misfolding process remains poorly understood. The present study structurally ...
Mutations of evolutionarily conserved aromatic residues suggest that misfolding of the mouse prion protein may commence in multiple ways

PAL, SUMAN; UDGAONKAR, JAYANT B. (Wiley, 2023-12)

The misfolding of the mammalian prion protein from its α-helix rich cellular isoform to its β-sheet rich infectious isoform is associated with several neurodegenerative diseases. The determination of the structural mechanism ...
Slow Misfolding of a Molten Globule form of a Mutant Prion Protein Variant into a β-rich Dimer

PAL, SUMAN; UDGAONKAR, JAYANT B. (Elsevier B.V., 2024-10)

Misfolding of the prion protein is linked to multiple neurodegenerative diseases. A better understanding of the process requires the identification and structural characterization of intermediate conformations via which ...
Rigidifying the β2−α2 Loop in the Mouse Prion Protein Slows down Formation of Misfolded Oligomers

PAL, SUMAN; UDGAONKAR, JAYANT B. (American Chemical Society, 2024-12)

Transmissible Spongiform Encephalopathies are fatal neurodegenerative diseases caused by the misfolding of the cellular prion protein (PrPC) into its pathological isoform (PrPSc). Efficient transmission of PrPSc occurs ...

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