On December 31, 2017, Afroz, Tariq; Hock, Eva-Maria; Ernst, Patrick; Foglieni, Chiara; Jambeau, Melanie; Gilhespy, Larissa A. B.; Laferriere, Florent; Maniecka, Zuzanna; Pluckthun, Andreas; Mittl, Peer; Paganetti, Paolo; Allain, Frederic H. T.; Polymenidou, Magdalini published an article.Synthetic Route of 79642-50-5 The title of the article was Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation. And the article contained the following:
TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal phosphorylation and cytoplasmic aggregation characterizes affected neurons in patients with amyotrophic lateral sclerosis and frontotemporal dementia. Here, we report that physiol. nuclear TDP-43 in mouse and human brain forms homo-oligomers that are resistant to cellular stress. Physiol. TDP-43 oligomerization is mediated by its N-terminal domain, which can adopt dynamic, solenoid-like structures, as revealed by a 2.1 Å crystal structure in combination with NMR spectroscopy and electron microscopy. These head-to-tail TDP-43 oligomers are unique among known RNA-binding proteins and represent the functional form of the protein in vivo, since their destabilization results in loss of alternative splicing regulation of known neuronal RNA targets. Our findings indicate that N-terminal domain-driven oligomerization spatially separates the adjoining highly aggregation-prone, C-terminal low-complexity domains of consecutive TDP-43 monomers, thereby preventing low-complexity domain inter-mol. interactions and antagonizing the formation of pathol. aggregates. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Synthetic Route of 79642-50-5
The Article related to tdp43 als rna protein structure brain, General Biochemistry: Proteins and Their Constituents and other aspects.Synthetic Route of 79642-50-5
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