@article {48492,
	title = {Shapeshifter TDP-43: molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators},
	journal = {Biophysical Chemistry},
	volume = {295},
	year = {2023},
	month = {APR},
	pages = {106972},
	type = {Review},
	abstract = {<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>
},
	keywords = {Amyloid versus non-amyloid, Coacervation, Environmental conditions, Prion-like seeding, Structural heterogeneity, Thermodynamic and kinetic mechanism},
	issn = {0301-4622},
	doi = {10.1016/j.bpc.2023.106972},
	author = {Doke, Abhilasha A. and Jha, Santosh Kumar}
}
