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Nitin Pandey

Title(s)Postdoctoral Scholar - Research Associate
SchoolKeck School of Medicine of USC
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    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Researchers can login to make corrections and additions, or contact us for help.
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    1. Bravo-Arredondo JM, Kegulian NC, Schmidt T, Pandey NK, Situ AJ, Ulmer TS, Langen R. The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract. J Biol Chem. 2018 Dec 21; 293(51):19613-19623. PMID: 30315108.
      View in: PubMed
    2. Ko J, Isas JM, Sabbaugh A, Yoo JH, Pandey NK, Chongtham A, Ladinsky M, Wu WL, Rohweder H, Weiss A, Macdonald D, Munoz-Sanjuan I, Langen R, Patterson PH, Khoshnan A. Identification of distinct conformations associated with monomers and fibril assemblies of mutant huntingtin. Hum Mol Genet. 2018 Apr 18. PMID: 29912367.
      View in: PubMed
    3. Pandey NK, Isas JM, Rawat A, Lee RV, Langen J, Pandey P, Langen R. The 17-residue-long N terminus in huntingtin controls stepwise aggregation in solution and on membranes via different mechanisms. J Biol Chem. 2018 02 16; 293(7):2597-2605. PMID: 29282287.
      View in: PubMed
    4. Isas JM, Langen A, Isas MC, Pandey NK, Siemer AB. Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils. Biochemistry. 2017 07 18; 56(28):3579-3586. PMID: 28621522.
      View in: PubMed
    5. Ghosh S, Pandey NK, Bhattacharya S, Roy A, Nagy NV, Dasgupta S. Evidence of two oxidation states of copper during aggregation of hen egg white lysozyme (HEWL). Int J Biol Macromol. 2015 May; 76:1-9. PMID: 25709020.
      View in: PubMed
    6. Ghosh S, Pandey NK, Banerjee P, Chaudhury K, Nagy NV, Dasgupta S. Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions. J Biomol Struct Dyn. 2015; 33(5):991-1007. PMID: 24806136.
      View in: PubMed