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Archives of Biochemistry and Biophysics|May 3, 2017
Hyperthermophilic l-asparaginase bypasses monomeric intermediates during folding to retain cooperativity and avoid amyloid assemblyDushyant K Garg, Bishwajit KunduBiochimica Et Biophysica Acta. Proteins and Proteomics|April 6, 2025
Green tea polyphenol EGCG acts differentially on end-stage amyloid polymorphs of α-synuclein formed in different polyol osmolytesSantosh Devi, Dushyant K Garg, Rajiv BhatBiochemistry|November 7, 2025
A30P and A30G Mutations in α-Synuclein Promote Metastable Long-Lived Aggregates with Distinct Structural Responses to EGCGSantosh Devi, Dushyant K Garg, Rajiv BhatInternational Journal of Biological Macromolecules|October 19, 2017
Heterologous expression of an engineered protein domain acts as chaperone and enhances thermotolerance of Escherichia coliRajender Jena, Dushyant K Garg, Lipsa Choudhury, et al.The FEBS Journal|April 5, 2013
N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperoneRachana Tomar, Dushyant K Garg, Rahul Mishra, et al.Extremophiles : Life Under Extreme Conditions|April 12, 2015
Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forcesDushyant K Garg, Rachana Tomar, Reema R Dhoke, et al.International Journal of Biological Macromolecules|May 29, 2020
In-silico and biophysical investigation of biomolecular interaction between naringin and nsP2 of the chikungunya virusPraveen Kumar Tripathi, Jasdeep Singh, Nitika Gaurav, et al.Journal of Biotechnology|February 5, 2020
Application of a protein domain as chaperone for enhancing biological activity and stability of other proteinsRajender Jena, Dushyant K Garg, Mohan Murali V Achary, et al.Pageof 1