BETA: Related publications


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Sabareesan AT, Singh J, Roy S, et al. (2016) The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes. Biophysical Journal. 110: 1766-76
Nussinov R, Udgaonkar JB. (2016) Editorial overview: Folding and binding: Dynamic conformational heterogeneity is pivotal to cell life. Current Opinion in Structural Biology
Singh J, Udgaonkar JB. (2016) Unraveling the molecular mechanism of pH-induced misfolding and oligomerization of the prion protein. Journal of Molecular Biology
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. The Journal of Biological Chemistry. 290: 25227-40
Goluguri RR, Udgaonkar JB. (2015) Rise of the Helix from a Collapsed Globule during the Folding of Monellin. Biochemistry. 54: 5356-65
Malhotra P, Udgaonkar JB. (2015) Tuning Cooperativity on the Free Energy Landscape of Protein Folding. Biochemistry. 54: 3431-41
Singh J, Udgaonkar JB. (2015) Structural Effects of Multiple Pathogenic Mutations Suggest a Model for the Initiation of Misfolding of the Prion Protein. Angewandte Chemie (International Ed. in English). 54: 7529-33
Milán-Garcés EA, Thaore P, Udgaonkar JB, et al. (2015) Formation of a CH-π contact in the core of native barstar during folding. The Journal of Physical Chemistry. B. 119: 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: 4431-4442
Singh J, Kumar H, Sabareesan AT, et al. (2014) Rational stabilization of helix 2 of the prion protein prevents its misfolding and oligomerization. Journal of the American Chemical Society. 136: 16704-7
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