01942nas a2200229   4500008004100000022001400041245012400055210006900179260000800248300001100256490000800267520108800275653003101363653001701394653002901411653002301440653002901463653004001492100002401532700002401556856013201580       2023                        eng d  a0301-462200aShapeshifter TDP-43: molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators0 aShapeshifter TDP43 molecular mechanism of structural polymorphis  cAPR  a1069720 v2953 a<p>
	TDP-43 is a nucleic acid-binding protein that performs physiologically essential functions and is known to un-dergo phase separation and aggregation during stress. Initial observations have shown that TDP-43 forms het-erogeneous assemblies, including monomer, dimer, oligomers, aggregates, phase-separated assemblies, etc. However, the significance of each assembly of TDP-43 concerning its function, phase separation, and aggregation is poorly known. Furthermore, how different assemblies of TDP-43 are related to each other is unclear. In this review, we focus on the various assemblies of TDP-43 and discuss the plausible origin of the structural het-erogeneity of TDP-43. TDP-43 is involved in multiple physiological processes like phase separation, aggregation, prion-like seeding, and performing physiological functions. However, the molecular mechanism behind the physiological process performed by TDP-43 is not well understood. The current review discusses the plausible molecular mechanism of phase separation, aggregation, and prion-like propagation of TDP-43.</p>
10aAmyloid versus non-amyloid10aCoacervation10aEnvironmental conditions10aPrion-like seeding10aStructural heterogeneity10aThermodynamic and kinetic mechanism1 aDoke, Abhilasha, A.1 aJha, Santosh, Kumar  uhttps://library.ncl.res.in/content/shapeshifter-tdp-43-molecular-mechanism-structural-polymorphism-aggregation-phase-separation