Jayanti Pande
Affiliations: | Chemistry | State University of New York, Albany, Albany, NY, United States |
Area:
Molecular Chemistry, Biochemistry, General BiophysicsGoogle:
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Publications
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| Hou W, Pande A, Pande J. (2022) Oxidation of active cysteines mediates protein aggregation of S10R, the cataract-associated mutant of mouse GammaB-crystallin. Proteins |
| Ramirez LMS, Shekhtman A, Pande J. (2019) Hydrophobic residues of melittin mediate its binding to αA-crystallin. Protein Science : a Publication of the Protein Society |
| Ramirez LS, Pande J, Shekhtman A. (2018) Helical Structure of Recombinant Melittin. The Journal of Physical Chemistry. B |
| Ramirez L, Shekhtman A, Pande J. (2018) Solution NMR Structure and Backbone Dynamics of Recombinant Bee Venom Melittin. Biochemistry |
| Mallik PK, Shi H, Pande J. (2017) RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain. Biochemical and Biophysical Research Communications |
| Dixit K, Pande A, Pande J, et al. (2016) NMR structure of a major lens protein, Human γC-Crystallin: Role of dipole moment in protein solubility. Biochemistry |
| Pande A, Mokhor N, Pande J. (2015) Deamidation of Human γs-Crystallin Increases Attractive Protein Interactions: Implications for Cataract Biochemistry. 54: 4890-4899 |
| Banerjee PR, Pande A, Shekhtman A, et al. (2015) Molecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin. Biochemistry. 54: 505-15 |
| Bharat SV, Shekhtman A, Pande J. (2014) The cataract-associated V41M mutant of human γS-crystallin shows specific structural changes that directly enhance local surface hydrophobicity. Biochemical and Biophysical Research Communications. 443: 110-4 |
| Banerjee PR, Puttamadappa SS, Pande A, et al. (2011) Increased hydrophobicity and decreased backbone flexibility explain the lower solubility of a cataract-linked mutant of γD-crystallin. Journal of Molecular Biology. 412: 647-59 |