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Dushyant Kumar Garg

Postdoctoral Fellow
  • E-maildushyant.garg@uib.no
  • Visitor Address
    Jonas Lies vei 91
    5009 Bergen
  • Postal Address
    Postboks 7804
    5020 Bergen

1. Devi S*, Garg DK*, Bhat R. Kinetic control in amyloid polymorphism: Different agitation and solution conditions promote     distinct amyloid polymorphs of alpha-synuclein. BBA Proteins & Proteomics. 1871: 140917. 2023

*contributed equally

2. Garg DK, Bhat R. Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils. Biophysical Journal. 121, 2568-2582. 2022

3. Tripathi PK, Singh J, Gaurav N, Garg DK, Patel AK. In-silico and biophysical investigation of biomolecular interaction between naringin and nsP2 of the chikungunya virus. International Journal of Biological Macromolecules. 160, 1061-1065. 2020

4. Jena R*, Garg DK*, Achary MMV, Singh J, Tomar R, Choudhury L, Bansal R, KunduB.Application of protein domain as chaperone for enhancing biological activity and stability of other proteins. Journal of Biotechnology. 310, 68-79. 2020

*contributed equally

5. Kumar S, Karmakar R, Garg DK, Gupta I, Patel AK. Elucidating the functional aspects of different domains of bean common mosaic virus coat protein. Virus Research. 277,197755. 2019

6. Jena R, Garg DK, Choudhuri L, Saini S, Kundu B. Heterologous expression of an engineered protein domain acts as chaperone and enhances thermotolerance of Escherichia coli. International Journal of Biological Macromolecules. 107, 2086-2093. 2018

7. Garg DK, Kundu B. Hyperthermophilic l-asparaginase bypasses monomericintermediates during folding to retain cooperativity and avoid amyloid assembly. Archives of Biochemistry and Biophysics. 622, 36-46. 2017

8. Garg DK, Kundu B. Clues for divergent, polymorphic amyloidogenesis through dissection of amyloid forming steps of bovine carbonic anhydrase and its critical amyloid-forming stretch. BBA Proteins & Proteomics. 1864: 794-804. 2016

9. Garg DK, Tomar R, Dhoke R, Srivastava A, and Kundu B. Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through unusually strong intersubunit associative forces. Extremophiles. 19: 681-91. 2015

10. Tomar R, Garg DK, Mishra R, Thakur AK, Kundu B*. N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. FEBS Journal. 280 (11): 2688-99. 2013