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.

Stem-cell-based neural replacement, in combination with optogenetic stimulation, could represent a translationally viable therapeutic strategy to overcome atrophy and paralysis of targeted muscles in people living with amyotrophic lateral sclerosis.

In the SOD1^G93A mouse model of amyotrophic lateral sclerosis (ALS), expression of transmembrane signaling molecule ephrinB2 in spinal cord astrocytes contributes to motor neuron damage and loss of diaphragm function.

Self-assembly of bacterial ice nucleation proteins is required for efficient activity and is mediated by electrostatic interactions, creating long and thin fibres.

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.

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.

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