Author [ Title] Type Year
Filters: Author is Udgaonkar, Jayant B [Clear All Filters]
Sengupta I, Udgaonkar JB. 2018. Structural mechanisms of oligomer and amyloid fibril formation by the prion protein.. Chem Commun (Camb).
Singh J, Udgaonkar JB. 2015. Structural effects of multiple pathogenic mutations suggest a model for the initiation of misfolding of the prion protein.. Angew Chem Int Ed Engl. 54(26):7529-33.
Aghera N, Udgaonkar JB. 2017. Stepwise Assembly of β-Sheet Structure during the Folding of an SH3 Domain Revealed by a Pulsed Hydrogen Exchange Mass Spectrometry Study.. Biochemistry.
Bhatia S, Krishnamoorthy G, Udgaonkar JB. 2018. Site-specific time-resolved FRET reveals local variations in the unfolding mechanism in an apparently two-state protein unfolding transition.. Phys Chem Chem Phys. 20(5):3216-3232.
Malhotra P, Udgaonkar JB. 2016. Secondary Structural Change Can Occur Diffusely and Not Modularly during Protein Folding and Unfolding Reactions.. J Am Chem Soc. 138(18):5866-78.
Moulick R, Goluguri RReddy, Udgaonkar JB. 2019. Ruggedness in the Free Energy Landscape Dictates Misfolding of the Prion Protein.. J Mol Biol.
Sabareesan AT, Udgaonkar JB. 2016. Pathogenic mutations within the disordered palindromic region of the prion protein induce structure therein and accelerate the formation of misfolded oligomers.. J Mol Biol.
Singh J, Udgaonkar JB. 2016. The pathogenic mutation T182A converts the prion protein into a molten globule-like conformation whose misfolding to oligomers but not to fibrils is drastically accelerated.. Biochemistry. 55(3):459-69.
Sabareesan AThody, Singh J, Roy S, Udgaonkar JB, Mathew MK. 2016. The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes.. Biophys J. 110(8):1766-76.
Jethva PN, Udgaonkar JB. 2018. The Osmolyte TMAO Modulates Protein Folding Cooperativity by Altering Global Protein Stability.. Biochemistry.
Singh J, Udgaonkar JB. 2015. Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its Implications.. Biochemistry. 54(29):4431-42.
Mondal S, Kallianpur MV, Udgaonkar JB, Krishnamoorthy G. 2016. Molecular crowding causes narrowing of population heterogeneity and restricts internal dynamics in a protein. METHODS AND APPLICATIONS IN FLUORESCENCE. 4(1)
Kumar H, Singh J, Kumari P, Udgaonkar JB. 2017. Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T.. J Biol Chem.
Jethva PN, Udgaonkar JB. 2017. Modulation of the Extent of Cooperative Structural Change During Protein Folding by Chemical Denaturant.. J Phys Chem B. 121(35):8263-8275.
Goluguri RReddy, Udgaonkar JB. 2016. Microsecond rearrangements of hydrophobic clusters in an initially collapsed globule prime structure formation during the folding of a small protein.. J Mol Biol.
Kumar H, Udgaonkar JB. 2019. Mechanistic approaches to understand the prion-like propagation of aggregates of the human tau protein.. Biochim Biophys Acta Proteins Proteom.
Kumar H, Udgaonkar JB. 2018. Mechanistic and Structural Origins of the Asymmetric Barrier to Prion-like Cross-Seeding between Tau-3R and Tau-4R.. J Mol Biol.
Milán-Garcés EA, Thaore P, Udgaonkar JB, Puranik M. 2015. Formation of a CH-π contact in the core of native barstar during folding.. J Phys Chem B. 119(7):2928-32.
Sengupta I, Udgaonkar JB. 2017. Expression and purification of single cysteine-containing mutant variants of the mouse prion protein by oxidative refolding.. Protein Expr Purif.