Dushyant Kumar Garg

Affiliations: 
Jawaharlal Nehru University (JNU), New Delhi 
Area:
Protein folding, protein aggregation
Google:
"Dushyant Garg"
Mean distance: (not calculated yet)
 
BETA: Related publications

Publications

You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect.

Devi S, Garg DK, Bhat R. (2023) Kinetic control in amyloid polymorphism: Different agitation and solution conditions promote distinct amyloid polymorphs of alpha-synuclein. Biochimica Et Biophysica Acta. Proteins and Proteomics. 1871: 140917
Garg DK, Bhat R. (2022) Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils. Biophysical Journal
Tripathi PK, Singh J, Gaurav N, et al. (2020) In-silico and biophysical investigation of biomolecular interaction between naringin and nsP2 of the chikungunya virus. International Journal of Biological Macromolecules
Jena R, Garg DK, Achary MMV, et al. (2020) Application of a protein domain as chaperone for enhancing biological activity and stability of other proteins. Journal of Biotechnology
Kumar S, Karmakar R, Garg DK, et al. (2019) Elucidating the functional aspects of different domains of bean common mosaic virus coat protein. Virus Research. 197755
Jena R, Garg DK, Choudhury L, et al. (2017) Heterologous expression of an engineered protein domain acts as chaperone and enhances thermotolerance of Escherichia coli. International Journal of Biological Macromolecules
Garg DK, Kundu B. (2017) Hyperthermophilic L-asparaginase bypasses monomeric intermediates during folding to retain cooperativity and avoid amyloid assembly. Archives of Biochemistry and Biophysics
Garg DK, Kundu B. (2016) Clues for divergent, polymorphic amyloidogenesis through dissection of amyloid forming steps of bovine carbonic anhydrase and its critical amyloid forming stretch. Biochimica Et Biophysica Acta. 1864: 794-804
Garg DK, Tomar R, Dhoke RR, et al. (2015) Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forces. Extremophiles : Life Under Extreme Conditions. 19: 681-91
Tomar R, Garg DK, Mishra R, et al. (2013) N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. The Febs Journal. 280: 2688-99
See more...