Sujoy Mukherjee, Ph.D.

Affiliations: 
2008 University of Illinois, Urbana-Champaign, Urbana-Champaign, IL 
Area:
biomolecular NMR
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"Sujoy Mukherjee"
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Eric Oldfield grad student 2008 UIUC
 (Applications of solid state nuclear magnetic resonance spectroscopy as a tool for structure based drug design.)
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Publications

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Bej A, Rasquinha JA, Mukherjee S. (2018) Conformational entropy as a determinant of thermodynamic stability in p53 core domain. Biochemistry
Mukherjee S, Pondaven SP, Hand K, et al. (2017) Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study. Scientific Reports. 7: 10339
Rasquinha JA, Bej A, Dutta S, et al. (2017) Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy. Biochemistry
Goswami R, Wohlfahrt G, Törmäkangas O, et al. (2015) Structure-guided discovery of 2-aryl/pyridin-2-yl-1H-indole derivatives as potent and selective hepsin inhibitors. Bioorganic & Medicinal Chemistry Letters
Bej A, Das JK, Mall SS, et al. (2015) Backbone Dynamics Modulates the Amyloidogenic Propensity of Transthyretin through Non-Native Intermediates Biophysical Journal. 108: 45a
Das JK, Mall SS, Bej A, et al. (2014) Conformational flexibility tunes the propensity of transthyretin to form fibrils through non-native intermediate states. Angewandte Chemie (International Ed. in English). 53: 12781-4
Mukherjee S, Pondaven SP, Jaroniec CP. (2011) Conformational flexibility of a human immunoglobulin light chain variable domain by relaxation dispersion nuclear magnetic resonance spectroscopy: implications for protein misfolding and amyloid assembly. Biochemistry. 50: 5845-57
Jedidi I, Zhang F, Qiu H, et al. (2010) Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX domain, to recruit mediator to target genes in vivo. The Journal of Biological Chemistry. 285: 2438-55
Mukherjee S, Pondaven SP, Höfer N, et al. (2009) Backbone and side-chain (1)H, (13)C and (15)N resonance assignments of LEN, a human immunoglobulin kappaIV light-chain variable domain. Biomolecular Nmr Assignments. 3: 255-9
Mukherjee S, Huang C, Guerra F, et al. (2009) Thermodynamics of bisphosphonates binding to human bone: a two-site model. Journal of the American Chemical Society. 131: 8374-5
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