Drupal-Biblio17<style face="normal" font="default" size="100%">Evidence for dry molten globule-like domains in the pH-induced equilibrium folding intermediate of a multidomain protein</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Alternatively packed dry molten globule-like intermediate in the native state ensemble of a multidomain protein</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein (vol 19, pg 20307, 2017)</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Folding and aggregation energy landscapes of tethered RRM domains of human TDP-43 are coupled via a metastable molten globule-like oligomer</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Slow motion protein dance visualized using red-edge excitation shift of a buried fluorophore</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Early metastable assembly during the stress-induced formation of worm-like amyloid fibrils of nucleic acid binding domains of TDP-43</style>Drupal-Biblio17<style face="normal" font="default" size="100%">pH-dependent protein stability switch coupled to the perturbed pKa of a single ionizable residue</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Protonation-deprotonation switch controls the amyloid-like misfolding of nucleic-acid-binding domains of TDP-43</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Dry molten globule-like intermediates in protein folding, function, and disease</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Native state conformational heterogeneity in the energy landscape of protein folding</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Electrostatic modulation of intramolecular and intermolecular interactions during the formation of an amyloid-like assembly</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Multistep molecular mechanism of amyloid-like aggregation of nucleic acid-binding domain of TDP-43</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Shapeshifter TDP-43: molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Thermodynamic modulation of folding and aggregation energy landscape by DNA binding of functional domains of TDP-43</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Conformational enigma of TDP-43 misfolding in neurodegenerative disorders</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Deciphering the monomeric and dimeric conformational landscapes of the full-length TDP-43 and the impact of the C-terminal domain</style>Drupal-Biblio17<style face="normal" font="default" size="100%">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</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Electrostatics choreographs the aggregation dynamics of full-length TDP-43 via a monomeric amyloid precursor</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Identification of a hidden, highly aggregation-prone intermediate of full-length TDP-43 that triggers its misfolding and amyloid aggregation</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Multi-site red-edge excitation shift reveals the residue-specific solvation dynamics during the native to amyloid-like transition of an amyloidogenic protein</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Pathological mutations D169G and P112H electrostatically aggravate the amyloidogenicity of the functional domain of TDP-43</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Structural and mechanistic heterogeneity of the phase separation and aggregation of full-length TDP-43 is governed by environmental conditions</style>