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%">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%">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%">Structural and mechanistic heterogeneity of the phase separation and aggregation of full-length TDP-43 is governed by environmental conditions</style>