Author Title Type [ Year]
Filters: Author is Udgaonkar, Jayant B [Clear All Filters]
Udgaonkar JB. 2019. Introducing the Mechanical Forces in Biochemistry Special Issue.. Biochemistry. 58(47):4655-4656.
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.
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.
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.
Jethva PN, Udgaonkar JB. 2018. The Osmolyte TMAO Modulates Protein Folding Cooperativity by Altering Global Protein Stability.. Biochemistry.
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.
Sengupta I, Udgaonkar JB. 2018. Structural mechanisms of oligomer and amyloid fibril formation by the prion protein.. Chem Commun (Camb).
Sabareesan AThody, Mathew MK, Udgaonkar JB. 2018. Mechanism of aggregation and membrane interactions of mammalian prion protein.. Biochim Biophys Acta.
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.
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.
Malhotra P, Jethva PN, Udgaonkar JB. 2017. Chemical Denaturants Smoothen Ruggedness on the Free Energy Landscape of Protein Folding.. Biochemistry. 56(31):4053-4063.
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, Udgaonkar JB. 2017. Expression and purification of single cysteine-containing mutant variants of the mouse prion protein by oxidative refolding.. Protein Expr Purif.
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.
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.
Nandwani N, Surana P, Udgaonkar JB, Das R, Gosavi S. 2017. Amino-acid composition after loop deletion drives domain swapping.. Protein Sci. 26(10)
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.
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. How cooperative are protein folding and unfolding transitions? Protein Sci.
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)
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.
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.
Singh J, Udgaonkar JB. 2016. Unraveling the Molecular Mechanism of pH-Induced Misfolding and Oligomerization of the Prion Protein.. J Mol Biol. 428(6):1345-55.
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.
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.
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.
Malhotra P, Udgaonkar JB. 2015. Tuning Cooperativity on the Free Energy Landscape of Protein Folding.. Biochemistry. 54(22):3431-41.
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.
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.