N.  Acharya, Mishra, P., and Jha, S. Kumar, ?Evidence for dry molten globule-like domains in the pH-induced equilibrium folding intermediate of a multidomain protein?, Journal of Physical Chemistry Letters, vol. 7, no. 1, pp. 173-179, 2016.

P.  Mishra and Jha, S. Kumar, ?Alternatively packed dry molten globule-like intermediate in the native state ensemble of a multidomain protein?, Journal of Physical Chemistry B, vol. 121, no. 40, pp. 9336-9347, 2017.

N.  Acharya, Mishra, P., and Jha, S. Kumar, ?Dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein?, Physical Chemistry Chemical Physics, vol. 19, no. 44, pp. 30207-30216, 2017.

N.  Acharya, Mishra, P., and Jha, S. Kumar, ?Dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein (vol 19, pg 20307, 2017)?, Physical Chemistry Chemical Physics, vol. 21, no. 36, pp. 20499-20499, 2019.

M.  Pillai and Jha, S. Kumar, ?Folding and aggregation energy landscapes of tethered RRM domains of human TDP-43 are coupled via a metastable molten globule-like oligomer?, Biochemistry, vol. 58, no. 6, pp. 608-620, 2019.

P.  Mishra and Jha, S. Kumar, ?Slow motion protein dance visualized using red-edge excitation shift of a buried fluorophore?, Journal of Physical Chemistry B, vol. 123, no. 6, pp. 1256-1264, 2019.

M.  Pillai and Jha, S. Kumar, ?Early metastable assembly during the stress-induced formation of worm-like amyloid fibrils of nucleic acid binding domains of TDP-43?, Biochemistry, vol. 59, no. 3, pp. 315-328, 2020.

P.  Mishra, Patni, D., and Jha, S. Kumar, ?pH-dependent protein stability switch coupled to the perturbed pKa of a single ionizable residue?, Biophysical Chemistry, vol. 274, p. 106591, 2021.

D.  Patni and Jha, S. Kumar, ?Protonation-deprotonation switch controls the amyloid-like misfolding of nucleic-acid-binding domains of TDP-43?, Journal of Physical Chemistry B, vol. 125, no. 30, pp. 8383-8394, 2021.

N.  Acharya and Jha, S. Kumar, ?Dry molten globule-like intermediates in protein folding, function, and disease?, Journal of Physical Chemistry B, vol. 126, no. 43, pp. 8614-8622, 2022.

P.  Mishra and Jha, S. Kumar, ?Native state conformational heterogeneity in the energy landscape of protein folding?, Biophysical Chemistry, vol. 283, p. 106761, 2022.

M.  Pillai, Das, A., and Jha, S. Kumar, ?Electrostatic modulation of intramolecular and intermolecular interactions during the formation of an amyloid-like assembly?, Biochemistry, vol. 62, no. 12, pp. 1890-1905, 2023.

M.  Pillai and Jha, S. Kumar, ?Multistep molecular mechanism of amyloid-like aggregation of nucleic acid-binding domain of TDP-43?, Proteins- Structure Function and Bioinformatics, vol. 91, no. 5, pp. 649-664, 2023.

A. A.  Doke and Jha, S. Kumar, ?Shapeshifter TDP-43: molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators?, Biophysical Chemistry, vol. 295, p. 106972, 2023.

D.  Patni and Jha, S. Kumar, ?Thermodynamic modulation of folding and aggregation energy landscape by DNA binding of functional domains of TDP-43?, Biochimica Et Biophysica Acta-Proteins and Proteomics, vol. 1871, no. 4, p. 140916, 2023.

M.  Pillai and Jha, S. Kumar, ?Conformational enigma of TDP-43 misfolding in neurodegenerative disorders?, ACS OMEGA, vol. 9, pp. 40286-40297, 2024.

V.  Tammara, Doke, A. A., Jha, S. Kumar, and Das, A., ?Deciphering the monomeric and dimeric conformational landscapes of the full-length TDP-43 and the impact of the C-terminal domain?, ACS Chemical Neuroscience, vol. 15, pp. 4305-4321, 2024.

D.  Patni, Patil, A. D., Kirmire, M. S., Jha, A., and Jha, S. Kumar, ?DNA-mediated formation of phase-separated coacervates of the nucleic acid-binding domain of TAR DNA-binding protein (TDP-43) prevents its amyloid-like misfolding?, ACS Chemical Neuroscience, vol. 15, no. 22, pp. 4105-4122, 2024.

A. A.  Doke and Jha, S. Kumar, ?Electrostatics choreographs the aggregation dynamics of full-length TDP-43 via a monomeric amyloid precursor?, Biochemistry, vol. 63, no. 12, pp. 1553-1568, 2024.

A. A.  Doke and Jha, S. Kumar, ?Identification of a hidden, highly aggregation-prone intermediate of full-length TDP-43 that triggers its misfolding and amyloid aggregation?, Biochemistry, vol. 63, no. 23, pp. 3100-3113, 2024.

S. R.  More and Jha, S. Kumar, ?Multi-site red-edge excitation shift reveals the residue-specific solvation dynamics during the native to amyloid-like transition of an amyloidogenic protein?, Journal of Physical Chemistry B, 2024.

M.  Pillai, Patil, A. D., Das, A., and Jha, S. Kumar, ?Pathological mutations D169G and P112H electrostatically aggravate the amyloidogenicity of the functional domain of TDP-43?, ACS Chemical Neuroscience, vol. 15, no. 23, pp. 4267-4283, 2024.