Publications

[OA] - Open Access

2025

28. Narayanan C, Nazarenko Y. 2025. "In Silico Characterization of Molecular Interactions of Aviation-Derived Pollutants with Human Proteins: Implications for Occupational and Public Health." Atmosphere. 16(8), 919.

27. Nazarenko Y†, Narayanan C†. 2025. Energy Recovery Ventilation: What is Needed to Fill the Re-search Gaps. Atmosphere. 16(3), 309.

2024

26. Tran TTQ, Narayanan C, Loes AN, Click TH, Pham NTH, Létourneau M, Harms MJ, Calmettes C, Agarwal PK, Doucet N. "Ancestral sequence reconstruction dissects structural and functional differences among eosinophil ribonucleases." J. Biol. Chem.. 300(5) 2024: 107280.

2023

25. Nazarenko Y*, Narayanan C*, and Ariya PA. 2023. Indoor Air Purifiers in the Fight Against Airborne Pathogens: The Advantage of Circumferential Outflow Diffusers. Atmosphere 15(10): 1520. *Equal Authorship.

24. Bernard DN, Narayanan C, Hempel T, Bafna K, Bhojana PP, Letourneau M, Howell EE, Agarwal PK, Doucet N. 2023. Divergence of conformational motions along the evolutionary pathway in an enzyme superfamily. Structure. 31, 329-342.

2021

23. Nazarenko Y, Narayanan C, Kayium A, Szeptycki H, Ariya PA. 2021. Organic Sorbents for Air Purification: A New Application for Recyclable Hypercrosslinked Polystyrene. Industrial & Engineering Chemistry Research. 60, 10, 3969–3980. doi: 10.1021/acs.iecr.0c05722.

2020

22. Narayanan C, Bernard DN, Létourneau M, Gagnon J, Gagné D, Bafna K, Calmettes C, Couture JF, Agarwal PK & Doucet N. 2020. Insights into structural and dynamical changes experienced by human RNase 6 upon ligand binding. Biochemistry. 59 (6), 755-765.

2019

21. [OA] Bafna K, Narayanan C, Chennubhotla CS, Doucet N, Agarwal PK. 2019. Nucleotide substrate binding characterization in human pancreatic-type ribonucleases. PLoS One. 14(8):e0220037.

2018

20. Debbabi S, Groleau MC, Létourneau M, Narayanan C, Gosselin LL, Gagnon J, Doucet N, Déziel E, Chatenet D. 2018. Antibacterial properties of the pituitary adenylate cyclase-activating polypeptide: A new human antimicrobial peptide. PLoS One. 13(11):e0207366.

19. Gagné D, Narayanan C, Bafna K, Charest LA, Agarwal PK, Doucet N. 2018. Correction to: Sequence-specific backbone resonance assignments and microsecond timescale molecular dynamics simulation of human eosinophil-derived neurotoxin. Biomol NMR Assign. 12(2):365-367.

18. [OA] Narayanan C, Bernard DN, Bafna K, Gagné D, Doucet N, Agarwal PK. 2018. Ligand-induced variations in structural and dynamical properties within an enzyme superfamily. Frontiers in Molecular Biosciences. 5:54.

17. Narayanan C, Bernard DN, Bafna K, Gagné D, Chennubhotla CS, Doucet N, Agarwal PK. 2018. Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily. Structure. 26:426-436.

Article highlighted in Structure Previews ‘Conserved Functional Dynamics: I Like to Move It, Move It’ by Vladimir Uversky.

2017

16. Narayanan C, Bafna K, Roux LD, Agarwal PK, Doucet N. 2017. Applications of NMR and computational methodologies to study protein dynamics. Arch Biochem Biophys. 628:71-80.

15. Gagné D, Narayanan C, Bafna K, Charest LA, Agarwal PK & Doucet N. 2017. Sequence-specific backbone resonance assignments and microsecond timescale molecular dynamics simulation of human eosinophil-derived neurotoxin. Biomol. NMR Assign. 12(2):365-367. 

14. [OA] Narayanan C, Gagné D, Reynolds KA & Doucet N. 2017. Conserved amino acid networks modulate discrete functional properties in an enzyme superfamily. Sci. Rep. 7(1):3207.

2016

13. [OA] Gagné D, Narayanan C, Nguyen-Thi N, Roux L, Bernard DN Brunzelle JS, Couture JF, Agarwal PK, Doucet N. 2016. Ligand binding induces enhanced millisecond conformational exchange in xylanase B2 from Streptomyces lividans. Biochemistry. 55(30), 4184.

12. Agarwal PK, Doucet N, Chennubhotla CS, Ramanathan A & Narayanan C. 2016. Conformational sub-states and populations in enzyme catalysis. Methods Enzymol., 578, 273.

11. [OA] Narayanan C, Bernard DN, Doucet N. 2016. Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies. Catalysts. 6(6), 81.

2015

10. [OA] Gagné D, French RL, Narayanan C, Simonović M, Agarwal PK, Doucet N. 2015. Perturbation of the conformational dynamics of an active-site loop alters enzyme activity. Structure. 23(12), 2256. doi: 10.1016/j.str.2015.10.011

9. [OA] Gagné D, Narayanan C, Doucet N. 2015. Network of long-range concerted chemical shift displacements upon ligand binding to human angiogenin. Prot. Sci. 24(4): 525. doi: 10.1002/pro.2613

2014

8. Narayanan C, Dias CL. 2014. Exploring the free energy landscape of a model b-hairpin peptide and its isoform. Proteins. 82(10): 2394. doi: 10.1002/prot.24601

2013

7. [OA] Narayanan C, Dias CL. 2013. Hydrophobic interactions and hydrogen bonds in b-sheet formation. J. Chem. Phys. 139 (12) 115103. doi: 10.1063/1.4821596

2012

6. [OA] Narayanan C, Weinstock DS, Wu K-P, Baum J, and Levy RM. 2012. Investigation of the polymeric properties of a-synuclein and comparison with NMR experiments: A Replica Exchange Molecular Dynamics Study. J. Chem. Theory Comput. 8(10): 3929. 

2009

5. [OA] Wu KP, Weinstock DS, Narayanan C, Levy RM, Baum J. 2009. Structural Reorganization of alpha-Synuclein at Low pH Observed by NMR and REMD Simulations. J Mol Biol. 391(4): 784. doi: 10.1016/j.jmb.2009.06.063

2008

4. [OA] Weinstock DS, Narayanan C, Baum J, Levy RM. 2008. Correlation between 13C-alpha chemical shifts and helix content of peptide ensembles. Protein Sci. 17(5): 950. doi: 10.1110/ps.073365408

2007

3. [OA] Nanda V, Andrianarijaona A, Narayanan C. 2007. The role of protein homochirality in shaping the energy landscape of folding. Protein Sci.  16(8): 1667.  

2. [OA] Weinstock DS, Narayanan C, Felts AK, Andrec M, Levy RM, Wu KP, Baum J. 2007. Distinguishing among structural ensembles of the GB1 peptide: REMD simulations and NMR experiments. J Am Chem Soc. 129(16): 4858. 

2006

1. Talla V, Narayanan C, Srinivasan N, Balasubramanian D. 2006. Mutation causing self-aggregation in human γ-C crystallin leading to congenital cataract. Invest Ophthalmol Vis Sci. 47(12): 5212.