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Kumar H, Udgaonkar JB. 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 properties.. Protein Sci.
Bhatia S, Krishnamoorthy G, Udgaonkar JB. 2021. Mapping Distinct Sequences of Structure Formation Differentiating Multiple Folding Pathways of a Small Protein.. J Am Chem Soc.
Sen S, Udgaonkar JB. 2019. Binding-induced folding under unfolding conditions: Switching between induced fit and conformational selection mechanisms.. J Biol Chem. 294(45):16942-16952.
Nandwani N, Surana P, Negi H, Mascarenhas NM, Udgaonkar JB, Das R, Gosavi S. 2019. A five-residue motif for the design of domain swapping in proteins.. Nat Commun. 10(1):452.
Udgaonkar JB. 2019. Introducing the Mechanical Forces in Biochemistry Special Issue.. Biochemistry. 58(47):4655-4656.
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. 1867(10):922-932.
Bhatia S, Krishnamoorthy G, Dhar D, Udgaonkar JB. 2019. Observation of Continuous Contraction and a Metastable Misfolded State during the Collapse and Folding of a Small Protein.. J Mol Biol.
Sabareesan AThody, Mathew MK, Udgaonkar JB. 2018. Mechanism of aggregation and membrane interactions of mammalian prion protein.. Biochim Biophys Acta.
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.
Jethva PN, Udgaonkar JB. 2018. The Osmolyte TMAO Modulates Protein Folding Cooperativity by Altering Global Protein Stability.. 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.
Nandwani N, Surana P, Udgaonkar JB, Das R, Gosavi S. 2017. Amino-acid composition after loop deletion drives domain swapping.. Protein Sci. 26(10)
Malhotra P, Jethva PN, Udgaonkar JB. 2017. Chemical Denaturants Smoothen Ruggedness on the Free Energy Landscape of Protein Folding.. Biochemistry. 56(31):4053-4063.
Sen S, Goluguri RReddy, Udgaonkar JB. 2017. A Dry Transition State More Compact Than the Native State Is Stabilized by Non-Native Interactions during the Unfolding of a Small Protein.. Biochemistry.
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.
Sabareesan AThody, Udgaonkar JB. 2017. The G126V Mutation in the Mouse Prion Protein Hinders Nucleation-Dependent Fibril Formation by Slowing Initial Fibril Growth and by Increasing the Critical Concentration.. Biochemistry. 56(44):5931-5942.
Moulick R, Udgaonkar JB. 2017. Identification and structural characterization of the precursor conformation of the prion protein which directly initiates misfolding and oligomerization.. J Mol Biol.
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.
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.
Sengupta I, Bhate SH, Das R, Udgaonkar JB. 2017. Salt-mediated oligomerization of the mouse prion protein monitored by real time NMR.. J Mol Biol.
Nussinov R, Udgaonkar JB. 2016. Editorial overview: Folding and binding: Dynamic conformational heterogeneity is pivotal to cell life.. Curr Opin Struct Biol. 36:iv-vi.
Malhotra P, Udgaonkar JB. 2016. How cooperative are protein folding and unfolding transitions? Protein Sci.
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.
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)
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.
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 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.
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.
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.
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.
Moulick R, Das R, Udgaonkar JB. 2015. Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.. J Biol Chem. 290(42):25227-40.
Goluguri RReddy, Udgaonkar JB. 2015. Rise of the Helix from a Collapsed Globule during the Folding of Monellin.. Biochemistry. 54(34):5356-65.
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.