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Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity.
Moretti M, Marzi I, Cantarutti C, Vivoli Vega M, Mandaliti W, Mimmi MC, Bemporad F, Corazza A, Chiti F. Moretti M, et al. Molecules. 2022 Jul 5;27(13):4309. doi: 10.3390/molecules27134309. Molecules. 2022. PMID: 35807552 Free PMC article.
TAR DNA-binding protein 43 (TDP-43) forms intraneuronal cytoplasmic inclusions associated with amyotrophic lateral sclerosis and ubiquitin-positive frontotemporal lobar degeneration. ...This was attributed to protein monomerization and oligomeric seeds disruption by the co …
TAR DNA-binding protein 43 (TDP-43) forms intraneuronal cytoplasmic inclusions associated with amyotrophic lateral sclerosis and ubiq …
Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43.
Vivoli-Vega M, Guri P, Chiti F, Bemporad F. Vivoli-Vega M, et al. Int J Mol Sci. 2020 Aug 29;21(17):6259. doi: 10.3390/ijms21176259. Int J Mol Sci. 2020. PMID: 32872449 Free PMC article.
TAR DNA-binding protein 43 (TDP-43) is a 414-residue long nuclear protein whose deposition into intraneuronal insoluble inclusions has been associated with the onset of amyotrophic lateral sclerosis (ALS) and other diseases. ...Taken together, our results indicate that NTD …
TAR DNA-binding protein 43 (TDP-43) is a 414-residue long nuclear protein whose deposition into intraneuronal insoluble inclusions ha …