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Fig. 1 | Molecular Neurodegeneration

Fig. 1

From: Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

Fig. 1

Proteins interconvert between different conformational states in the cell. After its biosynthesis by the ribosome, a protein may fold into its native state and be trafficked to its correct cellular location, assemble into a functional complex, condense into membraneless organelles, or misfold and aggregate. These processes are regulated by the proteostasis network (PN) [1, 140]. Accessing the amyloid state is a process that typically involves the conversion of monomeric proteins into oligomers and ultimately, highly ordered, rigid cross-β sheet fibrillar structures [1]. In addition to being associated with disease, amyloid fibrils can also be functional, and for this reason they have applications in material sciences, biomedical engineering, and drug discovery [1, 2, 141]. Created with biorender.com

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