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Journal of Molecular Biology|October 13, 2022
Evolutionarily Conserved Proline Residues Impede the Misfolding of the Mouse Prion Protein by Destabilizing an Aggregation-competent Partially Unfolded FormSuman Pal, Jayant B UdgaonkarProtein Science : a Publication of the Protein Society|August 5, 2026
Phase separation leads to significant conformational change in the N-terminal region of the prion proteinSuman Pal, Jayant B UdgaonkarJournal of Neurochemistry|November 9, 2023
Mutations of evolutionarily conserved aromatic residues suggest that misfolding of the mouse prion protein may commence in multiple waysSuman Pal, Jayant B UdgaonkarBiochemistry|November 20, 2024
Rigidifying the β2-α2 Loop in the Mouse Prion Protein Slows down Formation of Misfolded OligomersSuman Pal, Jayant B UdgaonkarJournal of Molecular Biology|August 3, 2024
Slow Misfolding of a Molten Globule form of a Mutant Prion Protein Variant into a β-rich DimerSuman Pal, Jayant B UdgaonkarArchives of Biochemistry and Biophysics|October 23, 2012
Polypeptide chain collapse and protein foldingJayant B UdgaonkarAnnual Review of Biophysics|June 25, 2008
Multiple routes and structural heterogeneity in protein foldingJayant B UdgaonkarBiochemistry|January 11, 2011
Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactionsShweta Jain, Jayant B UdgaonkarBiochemistry|August 18, 2010
Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion proteinShweta Jain, Jayant B UdgaonkarBiochemistry|July 15, 2015
Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its ImplicationsJogender Singh, Jayant B UdgaonkarPageof 18