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The Journal of Physical Chemistry. B|May 3, 2022
Elongation of Fibrils Formed by a Tau Fragment is Inhibited by a Transient Dimeric IntermediateHarish Kumar, Jayant B UdgaonkarProtein Science : a Publication of the Protein Society|January 26, 2021
The Lys 280 → Gln mutation mimicking disease-linked acetylation of Lys 280 in tau extends the structural core of fibrils and modulates their catalytic propertiesHarish Kumar, Jayant B UdgaonkarJournal of Molecular Biology|September 30, 2018
Mechanistic and Structural Origins of the Asymmetric Barrier to Prion-like Cross-Seeding between Tau-3R and Tau-4RHarish Kumar, Jayant B UdgaonkarBiochimica Et Biophysica Acta. Proteins and Proteomics|April 16, 2019
Mechanistic approaches to understand the prion-like propagation of aggregates of the human tau proteinHarish Kumar, Jayant B UdgaonkarJournal of Molecular Biology|September 19, 2021
Microsecond Dynamics During the Binding-induced Folding of an Intrinsically Disordered ProteinSreemantee Sen, Harish Kumar, Jayant B UdgaonkarThe Journal of Biological Chemistry|August 2, 2017
Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin THarish Kumar, Jogender Singh, Pratibha Kumari, et al.Journal of the American Chemical Society|November 20, 2014
Rational stabilization of helix 2 of the prion protein prevents its misfolding and oligomerizationJogender Singh, Harish Kumar, Ambadi T Sabareesan, et al.Archives 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 UdgaonkarPageof 77