Poly-PR and poly-GR interact with importin β, disrupt importin-cargo loading, and inhibit nuclear import in permeabilized cells in a manner that can be rescued by RNA.

The C9orf72 expansion binds and sequesters the splicing factor hnRNP H leading to insoluble G-quadruplex aggregates that functionally reduce hnRNP H, thereby producing splicing defects.

Mutational analysis in cell-based models of C9ORF72 ALS/FTD identifies canonical translation initiation codons (AUG) on the antisense CCCCGG transcript as initiation sites for synthesis of neurotoxic dipeptide repeat proteins.

C9ORF72 antisense repeat expanded RNAs activate PKR/eIF2α dependent integrated stress response and cause neuronal toxicity independent of DPR proteins.

Modulation of insulin signalling could be an effective therapeutic approach against hexanucleotide repeat expansion related to c9ALS/FTD neurodegenerative diseases.

Idiopathic patients along a complex motor neuron disease-dementia spectrum exhibit mRNA splicing changes that are due to multi-protein insolubility.

An image-based multiplex autophagosome RNAi screen targeting all Rab GTPases as well as their GAPs and GEFs identifies the Rab GEF SMCR8 as multifaceted autophagy modulator, which regulates kinase activity and gene expression of ULK1.

An easy-to-implement antibody validation pipeline addresses the reproducibility crisis resulting from the use of non-specific antibodies.

Alteration of the G-quadruplex structure formed by GGGGCC repeat RNA through the direct interaction with RNA-binding proteins can suppress pathogenic repeat-associated non-AUG translation, leading to therapeutic effects on neurodegeneration in C9orf72-linked amyotrophic lateral sclerosis and frontotemporal dementia.

Length-dependent interference of arginine-containing dipeptide repeat proteins with multiple components of the nucleocytoplasmic transport machinery is a potential mechanistic pathway of C9orf72 amyotrophic lateral sclerosis or frontotemporal dementia toxicity.