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Dr. SUMAN NAG
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Address 1
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Address 2
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Title
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Dr.
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First Name
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SUMAN
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Last Name
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NAG
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University/Institution
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Stanford University
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Phone #
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6502834375
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Email ID
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sumannag@stanford.edu
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City
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Stanford
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Country
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United States
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State
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California
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Zipcode
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94035
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Department
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Biochemistry
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Company Name
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Area of Research
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Human cardiomyopathy and cardiac protein function
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Brief Description of Research Interest :
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I am generally interested in understanding protein function and mechanisms of protein related disorders (proteopathy). My current interest lies in understanding the function of human cardiac sarcomeric proteins and the role of missense cardiomyopathic mutations in these proteins. More specifically, I am interested in knowing how the human cardiac myosin, the force generator of the heart, interact with the regulated actin filaments to generate contractile force and how this interaction is affected by these disease causing mutations. I employ several biochemical and biophysical tools such as protein purification, single molecule optical techniques, protein binding assays, steady state and time resolved fluorescence spectroscopy, stopped flow kinetics, in vitro motility and many more to address these questions. I received my PhD from the Tata Institute of Fundamental Research, in India, working on the biophysics of aggregation and misfolding of the Alzheimer's amyloid beta peptide. I am currently a post doctoral researcher in Stanford University, School of Medicine with Prof. James Spudich.
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Representative Publications :
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Publications [Citations]
1. JongminSung, Nag. S, Kim IMortensen, Christian L Vestergaard, Shirley Sutton, Kathleen Ruppel and JamesA. Spudich. Single-molecule harmonicforce-spectroscopy: Load-dependent kinetics of human β-cardiac myosin. Submitted 2014
2. RuthSommese*, Pan S*, Sallam KI, Nag. S,Shirley Sutton, Susan Miller, James A. Spudich, Kathleen Ruppel and AshleyEA. Establishingdisease causality for a novel sarcomeric gene variant using a functional invitro assay of human troponin. Submitted2014
*Equal contribution
3. TejasM. Gupte*, Farah Haque*, Binnu Gangadharan, Margaret S. Sunitha, Deepa SelviRani, Namita Mukundan, Amruta Jambekar, Kumarasamy Thangaraj, RamanathanSowdhamini, Ruth F. Sommese, Nag. S,James A Spudich and John A. Mercer. Mechanisticheterogeneity in contractile properties of TPM1 mutants associated withinherent cardiomyopathies J. Biol. Chem.2014, 290 (11), 7003-15
*Equalcontribution
4. BidyutSarkar*, Arkarup Bandyopadhyay*, Anand Kant Das, Nag. S, Sanjeev Kumar Kaushalya, Umakant Tripathy, MohammedShameem, Shubha Shukla and Sudipta Maiti. Label -free dopamine imaging inlive rat slices ACS Chem. Neurosci. 2014,5(5), 329-334 [1]
*Equalcontribution
5. RuthSommese*, Nag. S*,Shirley Sutton, Susan Miller, James A. Spudich and Kathleen Ruppel. Effectsof troponinT hypertrophic and dilated cardiomyopathy mutations on the calciumsensitivity of the regulated thin filament and its interaction with humanβ-cardiac myosin. Plos One 2013 8(12), e83403 1-10.[5]
*Equal contribution
6. Nag. S*, BidyutSarkar*, Muralidharan Chandrakesan, Debanjan Bhowmik, MamataKombrabail, Sucheta Dandekar, Eitan Lerner, Elisha Haas, and Sudipta Maiti. A folding transition underlies the emergenceof membrane affinity in amyloid-β. Phys.Chem. Chem. Phys 2013, 15, 19129-19133 [4]
*Equal contribution
7. RuthSommese*, Jongmin Sung*, Nag. S*,Shirley Sutton, John Deacon, Elizabeth Choe, Leslie Leinwand, Kathleen Ruppeland James A. Spudich. Molecular consequences of the R453Chypertrophic cardiomyopathy mutation on human β-cardiac myosin motor function.Proc.Natl. Acad. Sci. 2013,110 (13), 12607-12612 [24]
*Equal contribution.
Highlighted by Murreta and David Thomas in Proc.Natl. Acad. Sci. Commentary 2013,110 (13), 12507-12508
8. C.Muralidharan, Bidyut Sarkar, Venus Singh Mithu, Rajiv Abhyankar, DebanjanBhowmik, Nag S., BankanidhiSahoo, Riddhi Shah, Sushma Gurav, Raja Banerjee, Sucheta Dandekar, Jaya C.Jose, Neelanjana Sengupta, Perunthiruthy K. Madhu and Sudipta Maiti. The basic structural motif and majorbiophysical properties of Amyloid-b are encoded in thefragment 18-35. Chem. Phys2013, 422, 80-87[2]
9. Rajiv Abhyankar, Banakanidhi Sahoo, Niraj K.Singh, Linda M. Meijer, Bidyut Sarkar, Anand K. Das, Nag. S, Muralidharan Chandrakesan, Debanjan Bhowmik, Sucheta Dandekar and SudiptaMaiti. Amyloiddiagnostics: Probing protein aggregation and conformation with ultrasensitivefluorescence detection. Proceedings of SPIE 2012, Vol. 8233, (1), 8233B0 1-8
10. Nag. S, BidyutSarkar, Arkarup Bandyopadhyay, Bankanidhi Sahoo, Varun K. A. Sreenivasan,Mamata Kombrabail, C Muralidharan, and Sudipta Maiti. The nature of the amyloid-b monomer andthe monomer-oligomer equilibrium. J. Biol. Chem. 2011, 286 (16),13827-13833. [41]
11. NirajKumar Singh, Jenu V. Chacko, Varun K. A.Sreenivasan, Nag S., and Sudipta Maiti. Anultra-compact alignment-free single molecule fluorescence device with afoldable light path. J. Biomed. Opt. 2011, 16(2),025004 1-4.[4]
12. Jiji Chen, Nag S, Pierre-AlexandreVidi, Joseph Irudayaraj. Singlemolecule in vivo analysis of toll-like receptor- 9 and CpG DNA interaction.PlosOne.2011, 6(4), e17991, 1-8. [20]
13. Nag S, Jiji Chen, Joseph Irudayaraj, and Sudipta Maiti. Direct Measurementof the attachment and assembly of small amyloid-β oligomers on live cellmembranes at physiological concentrations. Biophys. J. 2010,99(6), 1969-1975. [32]
14. Bankanidhi Sahoo, Nag, S., Parijat Sengupta,Sudipta Maiti. On the stability of the solubleamyloid aggregates. Biophys.J. 2009,97(5), 1454-1460. [20]
15. Nag S., Bandyopadhyay, Arkarup, SudiptaMaiti. Spatial pH-jump measures chemicalkinetics in a steady state system. J.Phys. Chem. A. 2009,113(18):5269-5272. [4]
16. BankanidhiSahoo, J Balaji, Nag S.,Sanjeev K. Kaushalya, Sudipta Maiti. Proteinaggregation probed by two-photon fluorescence correlation spectroscopy ofnative tryptophan. J. Chem. Phys. 2008, 129, 075103. [21]
17. KaushalyaSK , Nag S , Ghosh H ,Arumugam S , Maiti S. A high-resolutionlarge area serotonin map of a live rat brain section. Neuroreport.2008 May 7, 19(7):717-21. [6]
18. Kaushalya,SK*, Nag, S*, and Maiti S, Serotonin: Multiphoton imaging and relevant spectral data. Proceedingsof SPIE 2008, Vol. 6860, (1), 68601C 1-8. [2]
*Equal contribution
19. Nag S , Balaji J , Madhu PK , Maiti S. Intermolecular association provides specificoptical and NMR signatures for serotonin at intravesicular concentrations. BiophysJ. 2008 May 15, 94(10):4145-53. [6]
20. BankanidhiSahoo, Mithun Goswami, Nag S,and Sudipta Maiti, Spontaneous formationof a protein corona prevents the loss of quantum dot fluorescence inphysiological buffer. Chem. Phys. Lett.(2007), 445, 217-220. [26]
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