More SR and Jha SK, Multi-Site Red-Edge Excitation Shift Reveals the Residue-Specific Solvation Dynamics During the Native to Amyloid-like Transition of an Amyloidogenic Protein, J. Phys. Chem. B., IN PRESS, (2024).
Tamara V, Doke AA And Jha SK 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 Chem. Neurosci., 15, 4305 - 4321 (2024), DOI:10.1021/acschemneuro.4c00557.
Pillai M, Patil AD And Das A and Jha SK, Pathological mutations D169G and P112H electrostatically aggravate the amyloidogenicity of the functional domain of TDP-43, ACS Chem. Neurosci., 15, 4267 - 4283 (2024), DOI:10.1021/acschemneuro.4c00372.
Doke AA and Jha SK, Identification of a Hidden, Highly Aggregation-prone Intermediate of Full-length TDP-43 that Triggers its Misfolding and Amyloid Aggregation, Biochemistry., 63, 63, 3100?3 - 3113 (2024), DOI:10.1021/acs.biochem.4c00389.
Patni D, Patil AD, Kirmire MS And Jha A and Jha SK, 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 Chem. Neurosci., 15, 4105 - 4122 (2024), DOI:10.1021/acschemneuro.4c00117.
Pillai M and Jha SK, Conformational Enigma of TDP-43 Misfolding in Neurodegenerative Disorders, ACS Omega., 9, 40286 - 40297 (2024), DOI:doi.org/10.1021/acsomega.4c04119.
Doke AA And Jha SK, Electrostatics choreograph the aggregation dynamics of full-length TDP-43 via a monomeric amyloid precursor, Biochemistry., , (2024), DOI:10.1021/acs.biochem.4c00060.
Pillai M And Das A And Jha SK, Electrostatic modulation of intramolecular and intermolecular interactions during the formation of an amyloid-like assembly, Biochemistry., 62, 1890 - 1905 (2023), DOI:10.1021/acs.biochem.3c00014.
Patni D And Jha SK, Thermodynamic modulation of folding and aggregation energy landscape by DNA binding of functional domains of TDP-43, BBA - Proteins and Proteomics., 1871, 140916 (2023), DOI:10.1016/j.bbapap.2023.140916.
Doke AA And Jha SK, Shapeshifter TDP-43: Molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators, Biophys. Chem., 295, 106972 (2023).
Pillai M And Jha SK, Multi-step molecular mechanism of amyloid-like aggregation of nucleic acid-binding domain of TDP-43, Proteins: Struct. Funct. Genet., 91, 649 - 664 (2023), DOI:10.1002/prot.26455.
Acharya N And Jha SK, Dry molten globule-like intermediates in protein folding, function and disease, J. Phys. Chem. B., 126, 8614 - 8622 (2022).
Doke AA And Jha SK, Effect of in-vitro solvation condition on inter and intra-molecular assembly of full-length TDP-43, J. Phys. Chem. B., 126, 4799 - 4813 (2022).
Mishra P And Jha SK, The native state conformational heterogeneity in the energy landscape of protein folding, Biophys. Chem., 283, 106761 (2022).
Patni D And Jha SK, Protonation-deprotonation switch controls the amyloid-like misfolding of nucleic acid binding domains of TDP-43, J. Phys. Chem. B., 125, 30, 8383 - 8394 (2021).
Mishra P, Patni D And Jha SK, A pH-dependent protein stability switch coupled to the perturbed pKa of a single ionizable residue, Biophys. Chem., 274, 106591 (2021).
Pillai M And Jha SK, Early metastable assembly during the stress-induced formation of worm-like amyloid fibrils of nucleic acid binding domains of TDP-43, Biochemistry., 59 (2), 315 - 328 (2020).
Mishra P And Jha SK, Slow motion protein dance visualized using red edge excitation shift of a buried fluorophore, J. Phys. Chem. B., 123, 1256 - 1264 (2019).
Pillai M And Jha SK, The folding and aggregation energy landscapes of tethered RRM domains of human TDP-43 are coupled via a metastable molten globule-like oligomer, Biochemistry., 58, 608 - 620 (2019).
Mishra P And Jha SK, An alternatively packed dry molten globule-like intermediate in the native state ensemble of a multi-domain protein, J. Phys. Chem. B., 121, 9336 - 9347 (2017).
Acharya N, Mishra P And Jha SK, A dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein, Phys. Chem. Chem. Phys., 19, 30207 - 30216 (2017).
Acharya N, Mishra P And Jha SK, Evidence for dry molten globule-like domains in the pH-induced equilibrium folding intermediate of a multi-domain protein, J. Phys. Chem. Lett., 7, 173 - 179 (2016).
Jha SK And Marqusee S, Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride, Proc. Natl. Acad. Sci. USA., 111, 4856 - 4861 (2014).
Recommended by Faculty of 1000 Biology http://f1000.com/prime/718313266
Jha SK, Deepalakshmi PD And Udgaonkar JB , Characterization of deamidation of barstar using electrospray ionization quadrupole time-of-flight mass spectrometry, which stabilizes an equilibrium unfolding intermediate, Protein Sci., 21, 633 - 646 (2012).
Jha SK, Ji M, Gaffney KJ And Boxer SG, Site-specific measurement of water dynamics in the substrate pocket of ketosteroid isomerase using time-resolved vibrational spectroscopy, J. Phys. Chem. B., 116, 11414 - 11421 (2012).
Jha SK, Ji M, Gaffney KJ And Boxer SG, Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase, Proc. Natl. Acad. Sci. USA., 108, 16612 - 16617 (2011).
Jha SK And Udgaonkar JB , Free energy barriers in protein folding and unfolding reactions, Curr. Sci., 99, 457 - 475 (2010).
Jha SK, Dasgupta A, Malhotra P And Udgaonkar JB, Identification of multiple folding pathways of monellin using pulsed thiol labeling and mass spectrometry, Biochemistry., 50, 3062 - 3074 (2010).
Jha SK And Udgaonkar JB, Direct evidence for a dry molten globule intermediate during the unfolding of a small protein, Proc. Natl. Acad. Sci. USA., 106, 12289 - 12294 (2009), DOI:(Recommended by Faculty of 1000 Biology http://f1000.com/14021991).
Recommended by Faculty of 1000 Biology http://f1000.com/14021991
Jha SK, Dhar D, Krishnamoorthy G And Udgaonkar JB , Continuous dissolution of structure during the unfolding of a small protein, Proc. Natl. Acad. Sci. USA., 106, 11113 - 11118 (2009).
Jha SK And Udgaonkar JB , Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry, J. Biol. Chem., 282, 37479 - 37491 (2007).
