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Jayanti Pande - Publications

Affiliations: 
Chemistry State University of New York, Albany, Albany, NY, United States 
Area:
Molecular Chemistry, Biochemistry, General Biophysics
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32 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2022 Hou W, Pande A, Pande J. Oxidation of active cysteines mediates protein aggregation of S10R, the cataract-associated mutant of mouse GammaB-crystallin. Proteins. PMID 35726360 DOI: 10.1002/prot.26391  0.368
2019 Ramirez LMS, Shekhtman A, Pande J. Hydrophobic residues of melittin mediate its binding to αA-crystallin. Protein Science : a Publication of the Protein Society. PMID 31762096 DOI: 10.1002/Pro.3792  0.412
2018 Ramirez LS, Pande J, Shekhtman A. Helical Structure of Recombinant Melittin. The Journal of Physical Chemistry. B. PMID 30570258 DOI: 10.1021/Acs.Jpcb.8B08424  0.377
2018 Ramirez L, Shekhtman A, Pande J. Solution NMR Structure and Backbone Dynamics of Recombinant Bee Venom Melittin. Biochemistry. PMID 29668274 DOI: 10.1021/Acs.Biochem.8B00156  0.38
2017 Mallik PK, Shi H, Pande J. RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain. Biochemical and Biophysical Research Communications. PMID 28720498 DOI: 10.1016/J.Bbrc.2017.07.085  0.331
2016 Dixit K, Pande A, Pande J, Sarma SP. NMR structure of a major lens protein, Human γC-Crystallin: Role of dipole moment in protein solubility. Biochemistry. PMID 27187112 DOI: 10.1021/Acs.Biochem.6B00359  0.463
2015 Pande A, Mokhor N, Pande J. Deamidation of Human γs-Crystallin Increases Attractive Protein Interactions: Implications for Cataract Biochemistry. 54: 4890-4899. PMID 26158710 DOI: 10.1021/Acs.Biochem.5B00185  0.463
2015 Banerjee PR, Pande A, Shekhtman A, Pande J. Molecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin. Biochemistry. 54: 505-15. PMID 25478825 DOI: 10.1021/Bi5014479  0.649
2014 Bharat SV, Shekhtman A, Pande J. 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. PMID 24287181 DOI: 10.1016/J.Bbrc.2013.11.073  0.51
2011 Banerjee PR, Puttamadappa SS, Pande A, Shekhtman A, Pande J. 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. PMID 21827768 DOI: 10.1016/J.Jmb.2011.07.058  0.698
2011 Banerjee PR, Pande A, Patrosz J, Thurston GM, Pande J. Cataract-associated mutant E107A of human gammaD-crystallin shows increased attraction to alpha-crystallin and enhanced light scattering. Proceedings of the National Academy of Sciences of the United States of America. 108: 574-9. PMID 21173272 DOI: 10.1073/Pnas.1014653107  0.668
2011 Banerjee PR, Puttamadappa S, Pande A, Shekhtman A, Pande J. Structure, Dynamics and Surface Hydrophobicity of the Cataract-Associated Mutant, Pro23Thr of Human Gamma D-crystallin: Molecular Basis of Cataract Formation Biophysical Journal. 100: 539a. DOI: 10.1016/J.Bpj.2010.12.3144  0.673
2010 Pande A, Ghosh KS, Banerjee PR, Pande J. Increase in surface hydrophobicity of the cataract-associated P23T mutant of human gammaD-crystallin is responsible for its dramatically lower, retrograde solubility. Biochemistry. 49: 6122-9. PMID 20553008 DOI: 10.1021/Bi100664S  0.687
2010 Danysh BP, Patel TP, Czymmek KJ, Edwards DA, Wang L, Pande J, Duncan MK. Characterizing molecular diffusion in the lens capsule. Matrix Biology : Journal of the International Society For Matrix Biology. 29: 228-36. PMID 20026402 DOI: 10.1016/J.Matbio.2009.12.004  0.388
2010 Banerjee PR, Pande A, Thurston G, Pande J. Thermodynamic Studies on the Cataract-Associated Mutant, E107a, of Human Gamma-D Crystallin: Molecular Basis for Cataract Formation Biophysical Journal. 98: 44a. DOI: 10.1016/J.Bpj.2009.12.254  0.651
2009 Pande A, Gillot D, Pande J. The cataract-associated R14C mutant of human γD-crystallin shows a variety of intermolecular disulfide cross-links: A raman spectroscopic study Biochemistry. 48: 4937-4945. PMID 19382745 DOI: 10.1021/Bi9004182  0.404
2009 Pande A, Zhang J, Banerjee PR, Puttamadappa SS, Shekhtman A, Pande J. NMR study of the cataract-linked P23T mutant of human gammaD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility. Biochemical and Biophysical Research Communications. 382: 196-9. PMID 19275895 DOI: 10.1016/J.Bbrc.2009.03.007  0.669
2007 McManus JJ, Lomakin A, Ogun O, Pande A, Basan M, Pande J, Benedek GB. Altered phase diagram due to a single point mutation in human gammaD-crystallin. Proceedings of the National Academy of Sciences of the United States of America. 104: 16856-61. PMID 17923670 DOI: 10.1073/Pnas.0707412104  0.462
2005 Pande A, Annunziata O, Asherie N, Ogun O, Benedek GB, Pande J. Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin. Biochemistry. 44: 2491-500. PMID 15709761 DOI: 10.1021/Bi0479611  0.503
2005 Annunziata O, Pande A, Pande J, Ogun O, Lubsen NH, Benedek GB. Oligomerization and phase transitions in aqueous solutions of native and truncated human beta B1-crystallin. Biochemistry. 44: 1316-28. PMID 15667225 DOI: 10.1021/Bi048419F  0.394
2003 Basak A, Bateman O, Slingsby C, Pande A, Asherie N, Ogun O, Benedek GB, Pande J. High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract. Journal of Molecular Biology. 328: 1137-47. PMID 12729747 DOI: 10.1016/S0022-2836(03)00375-9  0.359
2002 Annunziata O, Asherie N, Lomakin A, Pande J, Ogun O, Benedek GB. Effect of polyethylene glycol on the liquid-liquid phase transition in aqueous protein solutions. Proceedings of the National Academy of Sciences of the United States of America. 99: 14165-70. PMID 12391331 DOI: 10.1073/Pnas.212507199  0.369
2001 Asherie N, Pande J, Pande A, Zarutskie JA, Lomakin J, Lomakin A, Ogun O, Stern LJ, King J, Benedek GB. Enhanced crystallization of the Cys18 to Ser mutant of bovine gammaB crystallin. Journal of Molecular Biology. 314: 663-9. PMID 11733987 DOI: 10.1006/Jmbi.2001.5155  0.307
2001 Pande A, Pande J, Asherie N, Lomakin A, Ogun O, King J, Benedek GB. Crystal cataracts: human genetic cataract caused by protein crystallization. Proceedings of the National Academy of Sciences of the United States of America. 98: 6116-20. PMID 11371638 DOI: 10.1073/Pnas.101124798  0.43
2000 Pande A, Pande J, Asherie N, Lomakin A, Ogun O, King JA, Lubsen NH, Walton D, Benedek GB. Molecular basis of a progressive juvenile-onset hereditary cataract. Proceedings of the National Academy of Sciences of the United States of America. 97: 1993-8. PMID 10688888 DOI: 10.1073/Pnas.040554397  0.479
1999 Zastavker YV, Asherie N, Lomakin A, Pande J, Donovan JM, Schnur JM, Benedek GB. Self-assembly of helical ribbons. Proceedings of the National Academy of Sciences of the United States of America. 96: 7883-7. PMID 10393916 DOI: 10.1073/Pnas.96.14.7883  0.306
1996 Friberg G, Pande J, Ogun O, Benedek GB. Pantethine inhibits the formation of high-Tc protein aggregates in gamma B crystallin solutions. Current Eye Research. 15: 1182-90. PMID 9018433 DOI: 10.3109/02713689608995154  0.31
1996 Liu C, Asherie N, Lomakin A, Pande J, Ogun O, Benedek GB. Phase separation in aqueous solutions of lens gamma-crystallins: special role of gamma s. Proceedings of the National Academy of Sciences of the United States of America. 93: 377-82. PMID 8552642 DOI: 10.1073/Pnas.93.1.377  0.33
1995 Fine BM, Pande J, Lomakin A, Ogun OO, Benedek GB. Dynamic critical phenomena in aqueous protein solutions. Physical Review Letters. 74: 198-201. PMID 10057733 DOI: 10.1103/Physrevlett.74.198  0.358
1995 Liu C, Lomakin A, Thurston GM, Hayden D, Pande A, Pande J, Ogun O, Asherie N, Benedek GB. Phase separation in multicomponent aqueous-protein solutions Journal of Physical Chemistry®. 99: 454-461. DOI: 10.1021/J100001A067  0.355
1987 Myer YP, Kumar S, Kinnally K, Pande J. Methionine-oxidized horse heart cytochromes c. II. Conformation and heme configuration Journal of Protein Chemistry. 6: 321-342. DOI: 10.1007/Bf00248052  0.314
1981 Myer YP, Pande A, Pande J, Thallam KK, Saturno AF, Verma BC. Cytochromec: Ascorbate reduction site and possible electron-transfer path International Journal of Quantum Chemistry. 20: 513-521. DOI: 10.1002/Qua.560200223  0.374
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