biblio
, “Conformational enigma of TDP-43 misfolding in neurodegenerative disorders”, ACS OMEGA, vol. 9, pp. 40286-40297, 2024.
, “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.
, “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.
, “Electrostatics choreographs the aggregation dynamics of full-length TDP-43 via a monomeric amyloid precursor”, Biochemistry, vol. 63, no. 12, pp. 1553-1568, 2024.
, “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.
, “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.
, “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.
, “Electrostatic modulation of intramolecular and intermolecular interactions during the formation of an amyloid-like assembly”, Biochemistry, vol. 62, no. 12, pp. 1890-1905, 2023.
, “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.
, “Shapeshifter TDP-43: molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators”, Biophysical Chemistry, vol. 295, p. 106972, 2023.
, “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.
, “Dry molten globule-like intermediates in protein folding, function, and disease”, Journal of Physical Chemistry B, vol. 126, no. 43, pp. 8614-8622, 2022.
, “Native state conformational heterogeneity in the energy landscape of protein folding”, Biophysical Chemistry, vol. 283, p. 106761, 2022.
, “pH-dependent protein stability switch coupled to the perturbed pKa of a single ionizable residue”, Biophysical Chemistry, vol. 274, p. 106591, 2021.
, “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.
, “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.
, “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.
, “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.
, “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.
, “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.
, “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.
, “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.