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Computational insights into mechanism of AIM4-mediated inhibition of aggregation of TDP-43 protein implicated in ALS and evidence for in vitro inhibition of liquid-liquid phase separation (LLPS) of TDP-43 2C -A315T by AIM4

2019-10-08

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TDP-43 is an RNA/DNA-binding protein of versatile physiological functions and it is also implicated in the pathogenesis of amyotrophic lateral sclerosis (ALS) disease in addition to several other implicated proteins such as mutant SOD1 and FUS etc. Cytoplasmic mis-localization, liquid-liquid phase separation (LLPS) due to RNA depletion and aggregation of TDP-43 are suggested to be important TDP-43-toxicity causing...

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Literature Corpus work: a2caf0ff-875d-5674-9d66-bcb4ba10f44a
DOI: 10.1101/797613

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Computational insights into mechanism of AIM4-mediated inhibition of aggregation of TDP-43 protein implicated in ALS and evidence for in vitro inhibition of liquid-liquid phase separation (LLPS) of TDP-43 2C -A315T by AIM4DOI 10.1101/797613Read

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Aggresome Formation and Liquid-liquid Phase Separation Independently Induce Cytoplasmic Aggregation of TAR DNA-binding protein 43Semantic proximity Read

Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregationSemantic proximity Read

TDP-43 oligomers detected as initial intermediate species during aggregate formationSemantic proximity Read

Influence of ALS-linked M337V mutation on the conformational ensembles of TDP-43321-340 peptide monomer and dimer.Semantic proximity Read

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.Semantic proximity Read

Computational insights into mechanism of AIM4-mediated inhibition of aggregation of TDP-43 protein implicated in ALS and evidence for <i>in vitro</i> inhibition of liquid-liquid phase separation (LLPS) of TDP-43 <sup>2C</sup> -A315T by AIM4

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