Nitin Pandey
Assistant Professor of Physiology and Neuroscience, University of Southern California
Research Interests
Publications
Fibrillation in Human Serum Albumin Is Enhanced in the Presence of Copper(II)
The Journal of Physical Chemistry B / Jul 20, 2010
Pandey, N. K., Ghosh, S., & Dasgupta, S. (2010). Fibrillation in Human Serum Albumin Is Enhanced in the Presence of Copper(II). The Journal of Physical Chemistry B, 114(31), 10228–10233. https://doi.org/10.1021/jp103876p
The 17-residue-long N terminus in huntingtin controls stepwise aggregation in solution and on membranes via different mechanisms
Journal of Biological Chemistry / Feb 01, 2018
Pandey, N. K., Isas, J. M., Rawat, A., Lee, R. V., Langen, J., Pandey, P., & Langen, R. (2018). The 17-residue-long N terminus in huntingtin controls stepwise aggregation in solution and on membranes via different mechanisms. Journal of Biological Chemistry, 293(7), 2597–2605. https://doi.org/10.1074/jbc.m117.813667
(−)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme
International Journal of Biological Macromolecules / Mar 01, 2013
Ghosh, S., Pandey, N. K., & Dasgupta, S. (2013). (−)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme. International Journal of Biological Macromolecules, 54, 90–98. https://doi.org/10.1016/j.ijbiomac.2012.11.031
Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures
PLoS ONE / Sep 16, 2013
Ghosh, S., Pandey, N. K., Singha Roy, A., Tripathy, D. R., Dinda, A. K., & Dasgupta, S. (2013). Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures. PLoS ONE, 8(9), e74336. https://doi.org/10.1371/journal.pone.0074336
The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract
Journal of Biological Chemistry / Dec 01, 2018
Bravo-Arredondo, J. M., Kegulian, N. C., Schmidt, T., Pandey, N. K., Situ, A. J., Ulmer, T. S., & Langen, R. (2018). The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract. Journal of Biological Chemistry, 293(51), 19613–19623. https://doi.org/10.1074/jbc.ra118.004808
Fructose restrains fibrillogenesis in human serum albumin
International Journal of Biological Macromolecules / Oct 01, 2013
Pandey, N. K., Ghosh, S., & Dasgupta, S. (2013). Fructose restrains fibrillogenesis in human serum albumin. International Journal of Biological Macromolecules, 61, 424–432. https://doi.org/10.1016/j.ijbiomac.2013.08.006
Effect of surfactants on preformed fibrils of human serum albumin
International Journal of Biological Macromolecules / Aug 01, 2013
Pandey, N. K., Ghosh, S., & Dasgupta, S. (2013). Effect of surfactants on preformed fibrils of human serum albumin. International Journal of Biological Macromolecules, 59, 39–45. https://doi.org/10.1016/j.ijbiomac.2013.04.014
Preferential binding of fisetin to the native state of bovine serum albumin: spectroscopic and docking studies
Molecular Biology Reports / Jan 01, 2013
Singha Roy, A., Pandey, N. K., & Dasgupta, S. (2013). Preferential binding of fisetin to the native state of bovine serum albumin: spectroscopic and docking studies. Molecular Biology Reports, 40(4), 3239–3253. https://doi.org/10.1007/s11033-012-2399-9
Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils
Biochemistry / Jul 07, 2017
Isas, J. M., Langen, A., Isas, M. C., Pandey, N. K., & Siemer, A. B. (2017). Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils. Biochemistry, 56(28), 3579–3586. https://doi.org/10.1021/acs.biochem.7b00138
Effect of (−)-epigallocatechin gallate on the fibrillation of human serum albumin
International Journal of Biological Macromolecules / Sep 01, 2014
Bhattacharya, S., Pandey, N. K., Roy, A., & Dasgupta, S. (2014). Effect of (−)-epigallocatechin gallate on the fibrillation of human serum albumin. International Journal of Biological Macromolecules, 70, 312–319. https://doi.org/10.1016/j.ijbiomac.2014.07.003
Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions
Journal of Biomolecular Structure and Dynamics / May 28, 2014
Ghosh, S., Pandey, N. K., Banerjee, P., Chaudhury, K., Nagy, N. V., & Dasgupta, S. (2014). Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions. Journal of Biomolecular Structure and Dynamics, 33(5), 991–1007. https://doi.org/10.1080/07391102.2014.921864
Identification of distinct conformations associated with monomers and fibril assemblies of mutant huntingtin
Human Molecular Genetics / Apr 18, 2018
Ko, J., Isas, J. M., Sabbaugh, A., Yoo, J. H., Pandey, N. K., Chongtham, A., Ladinsky, M., Wu, W.-L., Rohweder, H., Weiss, A., Macdonald, D., Munoz-Sanjuan, I., Langen, R., Patterson, P. H., & Khoshnan, A. (2018). Identification of distinct conformations associated with monomers and fibril assemblies of mutant huntingtin. Human Molecular Genetics, 27(13), 2330–2343. https://doi.org/10.1093/hmg/ddy141
Fibrillation of hen egg white lysozyme triggers reduction of copper(II)
International Journal of Biological Macromolecules / Jul 01, 2012
Ghosh, S., Pandey, N. K., Bhattacharya, S., Roy, A., & Dasgupta, S. (2012). Fibrillation of hen egg white lysozyme triggers reduction of copper(II). International Journal of Biological Macromolecules, 51(1–2), 1–6. https://doi.org/10.1016/j.ijbiomac.2012.04.024
Structure of Membrane-Bound Huntingtin Exon 1 Reveals Membrane Interaction and Aggregation Mechanisms
Structure / Oct 01, 2019
Tao, M., Pandey, N. K., Barnes, R., Han, S., & Langen, R. (2019). Structure of Membrane-Bound Huntingtin Exon 1 Reveals Membrane Interaction and Aggregation Mechanisms. Structure, 27(10), 1570-1580.e4. https://doi.org/10.1016/j.str.2019.08.003
Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II)
Journal of Biomolecular Structure and Dynamics / Jul 22, 2013
Pandey, N. K., Ghosh, S., Nagy, N. V., & Dasgupta, S. (2013). Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II). Journal of Biomolecular Structure and Dynamics, 32(9), 1366–1378. https://doi.org/10.1080/07391102.2013.819300
Discovery of Small Molecule Inhibitors of Huntingtin Exon 1 Aggregation by FRET-Based High-Throughput Screening in Living Cells
ACS Chemical Neuroscience / Jun 22, 2020
Lo, C. H., Pandey, N. K., Lim, C. K.-W., Ding, Z., Tao, M., Thomas, D. D., Langen, R., & Sachs, J. N. (2020). Discovery of Small Molecule Inhibitors of Huntingtin Exon 1 Aggregation by FRET-Based High-Throughput Screening in Living Cells. ACS Chemical Neuroscience, 11(15), 2286–2295. https://doi.org/10.1021/acschemneuro.0c00226
Effects of urea, metal ions and surfactants on the binding of baicalein with bovine serum albumin
Journal of Pharmaceutical Analysis / Aug 01, 2016
Roy, A. S., Dinda, A. K., Pandey, N. K., & Dasgupta, S. (2016). Effects of urea, metal ions and surfactants on the binding of baicalein with bovine serum albumin. Journal of Pharmaceutical Analysis, 6(4), 256–267. https://doi.org/10.1016/j.jpha.2016.04.001
Lipid-modulation of membrane insertion and refolding of the apoptotic inhibitor Bcl-xL
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics / Jul 01, 2019
Vasquez-Montes, V., Vargas-Uribe, M., Pandey, N. K., Rodnin, M. V., Langen, R., & Ladokhin, A. S. (2019). Lipid-modulation of membrane insertion and refolding of the apoptotic inhibitor Bcl-xL. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1867(7–8), 691–700. https://doi.org/10.1016/j.bbapap.2019.04.006
Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
Nature Communications / Jul 13, 2021
Mario Isas, J., Pandey, N. K., Xu, H., Teranishi, K., Okada, A. K., Fultz, E. K., Rawat, A., Applebaum, A., Meier, F., Chen, J., Langen, R., & Siemer, A. B. (2021). Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted. Nature Communications, 12(1). https://doi.org/10.1038/s41467-021-24411-2
Crowded milieu prevents fibrillation of hen egg white lysozyme with retention of enzymatic activity
Journal of Photochemistry and Photobiology B: Biology / Sep 01, 2014
Ghosh, S., Pandey, N. K., & Dasgupta, S. (2014). Crowded milieu prevents fibrillation of hen egg white lysozyme with retention of enzymatic activity. Journal of Photochemistry and Photobiology B: Biology, 138, 8–16. https://doi.org/10.1016/j.jphotobiol.2014.04.021
Disruption of human serum albumin fibrils by a static electric field
Journal of Physics D: Applied Physics / Jul 03, 2014
Pandey, N. K., Mitra, S., Chakraborty, M., Ghosh, S., Sen, S., Dasgupta, S., & DasGupta, S. (2014). Disruption of human serum albumin fibrils by a static electric field. Journal of Physics D: Applied Physics, 47(30), 305401. https://doi.org/10.1088/0022-3727/47/30/305401
Binding of hen egg white lysozyme fibrils with nucleic acids
Journal of Photochemistry and Photobiology B: Biology / Oct 01, 2013
Ghosh, S., Pandey, N. K., Sen, S., Tripathy, D. R., & Dasgupta, S. (2013). Binding of hen egg white lysozyme fibrils with nucleic acids. Journal of Photochemistry and Photobiology B: Biology, 127, 52–60. https://doi.org/10.1016/j.jphotobiol.2013.07.015
Evidence of two oxidation states of copper during aggregation of hen egg white lysozyme (HEWL)
International Journal of Biological Macromolecules / May 01, 2015
Ghosh, S., Pandey, N. K., Bhattacharya, S., Roy, A., Nagy, N. V., & Dasgupta, S. (2015). Evidence of two oxidation states of copper during aggregation of hen egg white lysozyme (HEWL). International Journal of Biological Macromolecules, 76, 1–9. https://doi.org/10.1016/j.ijbiomac.2015.02.014
Effect of Temperature and Solvent on Fibrillation of Human Serum Albumin
Protein & Peptide Letters / Jan 28, 2015
Pandey, N., Ghosh, S., Tripathy, D., & Dasgupta, S. (2015). Effect of Temperature and Solvent on Fibrillation of Human Serum Albumin. Protein & Peptide Letters, 22(2), 112–118. https://doi.org/10.2174/0929866521666140320104409
Amplification of neurotoxic HTTex1 assemblies in human neurons
Neurobiology of Disease / Nov 01, 2021
Chongtham, A., Isas, J. M., Pandey, N. K., Rawat, A., Yoo, J. H., Mastro, T., Kennedy, M. B., Langen, R., & Khoshnan, A. (2021). Amplification of neurotoxic HTTex1 assemblies in human neurons. Neurobiology of Disease, 159, 105517. https://doi.org/10.1016/j.nbd.2021.105517
Distribution of Protein Ramachandran Psi (ψ) Angle Using Non-Resonance Visible Raman Scattering Measurements
The Journal of Physical Chemistry B / Nov 01, 2013
Bhattacharya, S., Ghosh, S., Pandey, N. K., Chaudhury, S., Dasgupta, S., & Roy, A. (2013). Distribution of Protein Ramachandran Psi (ψ) Angle Using Non-Resonance Visible Raman Scattering Measurements. The Journal of Physical Chemistry B, 117(45), 13993–14000. https://doi.org/10.1021/jp408009y
An insight into the ribonucleolytic and antiangiogenic activity of buffalo lactoferrin
Journal of Biomolecular Structure and Dynamics / Dec 10, 2013
Tripathy, D. R., Pandey, N. K., Dinda, A. K., Ghosh, S., Singha Roy, A., & Dasgupta, S. (2013). An insight into the ribonucleolytic and antiangiogenic activity of buffalo lactoferrin. Journal of Biomolecular Structure and Dynamics, 33(1), 184–195. https://doi.org/10.1080/07391102.2013.865564
Education
IIT Kharagpur
PhD, Chemistry / July, 2014
Banaras Hindu University
MS, Chemistry
Experience
University of Southern California
Postdoctoral research Associate / June, 2014 — May, 2019
Research Associate / June, 2019 — June, 2021
Assistant Professor of Research / July, 2021 — Present
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