Jayanti Pande - Publications

Affiliations: 
Chemistry State University of New York, Albany, Albany, NY, United States 
Area:
Molecular Chemistry, Biochemistry, General Biophysics

46 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
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
2011 Ghosh KS, Pande A, Pande J. Binding of γ-Crystallin Substrate Prevents the Binding of Copper and Zinc Ions to the Molecular Chaperone α-Crystallin Biochemistry. 50: 3279-3281. PMID 21417258 DOI: 10.1021/bi200091q  0.48
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  0.48
2010 Xie L, Chou SG, Pande A, Pande J, Zhang J, Dresselhaus MS, Kong J, Liu Z. Single-Walled Carbon Nanotubes Probing the Denaturation of Lysozyme. The Journal of Physical Chemistry. C, Nanomaterials and Interfaces. 114: 7717-7720. PMID 29308103 DOI: 10.1021/jp9121497  0.48
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  0.48
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  0.48
2009 Wu Y, Fishkin NE, Pande A, Pande J, Sparrow JR. Novel lipofuscin bisretinoids prominent in human retina and in a model of recessive Stargardt disease. The Journal of Biological Chemistry. 284: 20155-66. PMID 19478335 DOI: 10.1074/jbc.M109.021345  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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  0.48
2003 Pande JN, Pande A, Singh SPN. Acetylator status, drug metabolism and disease National Medical Journal of India. 16: 24-26. PMID 12715953  0.48
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  0.48
2002 Pande J, Hanlon EB, Pande A. A comparison of the environment of thiol groups in bovine and human γ crystallins using Raman spectroscopy [1] Experimental Eye Research. 75: 359-363. PMID 12384098 DOI: 10.1006/exer.2002.2038  0.48
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  0.48
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  0.48
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  0.48
1999 Benedek GB, Pande J, Thurston GM, Clark JI. Theoretical and experimental basis for the inhibition of cataract. Progress in Retinal and Eye Research. 18: 391-402. PMID 10192519 DOI: 10.1016/S1350-9462(98)00023-8  0.48
1998 Asherie N, Pande J, Lomakin A, Ogun O, Hanson SR, Smith JB, Benedek GB. Oligomerization and phase separation in globular protein solutions. Biophysical Chemistry. 75: 213-27. PMID 9894340 DOI: 10.1016/S0301-4622(98)00208-7  0.48
1998 Liu C, Pande J, Lomakin A, Ogun O, Benedek GB. Aggregation in aqueous solutions of bovine lens gamma-crystallins: special role of gamma(s). Investigative Ophthalmology & Visual Science. 39: 1609-19. PMID 9699550  0.48
1997 Pande J, Alexander K. The effect of α, βH, βL and γs crystallins on the inhibition of oxidative dimerization of γβ crystallin Investigative Ophthalmology and Visual Science. 38.  0.48
1997 Alexander K, Pande J, Manoharan R, Ogun O, Benedek G. Oxidative dimerization of yb (or yll) crystallin occurs without significant conformational change: raman spectroscopic evidence Investigative Ophthalmology and Visual Science. 38: S298.  0.48
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  0.48
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  0.48
1996 Pande J, Alexander K, Ogun O, Benedek G. α-Crystallin inhibits the high-Tph protein aggregates formed by the oxidation of αB crystallin Investigative Ophthalmology and Visual Science. 37: S443.  0.48
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.  0.48
1993 Pande J, Ogun O, Nath C, Benedek G. Suppression of phase separation in bovine gamma IV crystallin solutions: effect of modification by charged versus uncharged polar groups. Experimental Eye Research. 57: 257-64. PMID 8224013 DOI: 10.1006/exer.1993.1123  0.48
1991 Pande J, McDermott MJ, Callender RH, Spector A. The calf gamma crystallins--a Raman spectroscopic study. Experimental Eye Research. 52: 193-7. PMID 2013301 DOI: 10.1016/0014-4835(91)90258-G  0.48
1989 Pande J, McDermott MJ, Callender RH, Spector A. Raman spectroscopic evidence for a disulfide bridge in calf gamma II crystallin. Archives of Biochemistry and Biophysics. 269: 250-5. PMID 2916840 DOI: 10.1016/0003-9861(89)90106-9  0.48
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  0.48
1986 Pande J, Pande C, Gilg D, Vasák M, Callender R, Kägi JH. Raman, infrared, and circular dichroism spectroscopic studies on metallothionein: a predominantly "turn"-containing protein. Biochemistry. 25: 5526-32. PMID 3778872  0.48
1985 Pande J, Vašák M, Kägi JHR. Interaction of lysine residues with the metal thiolate clusters in metallothionein Biochemistry. 24: 6717-6722. PMID 3936544  0.48
1982 Druckmann S, Ottolenghi M, Pande A, Pande J, Callender RH. Acid-base equilibrium of the Schiff base in bacteriorhodopsin. Biochemistry. 21: 4953-9. PMID 7138840  0.48
1982 Pande J, Pande A, Callender RH. On the chromophore configuration of metarhodopsin II Photochemistry and Photobiology. 36: 107-109. PMID 7111435  0.48
1981 Pande J, Callender RH, Ebrey TG. Resonance Raman study of the primary photochemistry of bacteriorhodopsin Proceedings of the National Academy of Sciences of the United States of America. 78: 7379-7382. PMID 6950382  0.48
1980 Pande J, Myer JP. The arginines of cytochrome c. The reduction-binding site for 2,3-butanedione and ascorbate. The Journal of Biological Chemistry. 255: 11094-7. PMID 6254959  0.48
1980 Myer YP, Thallum KK, Pande J, Verma BC. Selectivity of oxidase and reductase activity of horse heart cytochrome c Biochemical and Biophysical Research Communications. 94: 1106-1112. PMID 6249297 DOI: 10.1016/0006-291X(80)90533-1  0.48
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