[HTML][HTML] In situ structure of neuronal C9orf72 poly-GA aggregates reveals proteasome recruitment

Q Guo, C Lehmer, A Martínez-Sánchez, T Rudack… - Cell, 2018 - cell.com
Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of
many neurodegenerative diseases. Here, we address the elusive link between these …

Proximity proteomics of C9orf72 dipeptide repeat proteins identifies molecular chaperones as modifiers of poly-GA aggregation

F Liu, D Morderer, MC Wren… - Acta Neuropathologica …, 2022 - Springer
The most common inherited cause of two genetically and clinico-pathologically overlapping
neurodegenerative diseases, amyotrophic lateral sclerosis (ALS) and frontotemporal …

Cell‐to‐cell transmission of C9orf72 poly‐(Gly‐Ala) triggers key features of ALS/FTD

B Khosravi, KD LaClair, H Riemenschneider… - The EMBO …, 2020 - embopress.org
The C9orf72 repeat expansion causes amyotrophic lateral sclerosis and frontotemporal
dementia, but the poor correlation between C9orf72‐specific pathology and TDP‐43 …

C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration

S May, D Hornburg, MH Schludi, T Arzberger… - Acta …, 2014 - Springer
Hexanucleotide repeat expansion in C9orf72 is the most common pathogenic mutation in
patients with amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration …

Proteomics and C9orf72 neuropathology identify ribosomes as poly-GR/PR interactors driving toxicity

H Hartmann, D Hornburg, M Czuppa… - Life science …, 2018 - life-science-alliance.org
Frontotemporal dementia and amyotrophic lateral sclerosis patients with C9orf72 mutation
show cytoplasmic poly-GR and poly-PR aggregates. Short poly-(Gly-Arg) and poly-(Pro …

Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins

Q Zhou, C Lehmer, M Michaelsen, K Mori… - EMBO molecular …, 2017 - embopress.org
Cell‐to‐cell transmission of protein aggregates is an emerging theme in neurodegenerative
disease. Here, we analyze the dipeptide repeat (DPR) proteins that form neuronal inclusions …

C9ORF72-ALS/FTD-associated poly (GR) binds Atp5a1 and compromises mitochondrial function in vivo

SY Choi, R Lopez-Gonzalez, G Krishnan… - Nature …, 2019 - nature.com
The GGGGCC repeat expansion in C9ORF72 is the most common genetic cause of
amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). However, it is not …

C9orf72 dipeptide repeats impair the assembly, dynamics, and function of membrane-less organelles

KH Lee, P Zhang, HJ Kim, DM Mitrea, M Sarkar… - Cell, 2016 - cell.com
Expansion of a hexanucleotide repeat GGGGCC (G 4 C 2) in C9ORF72 is the most common
cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Transcripts …

PolyGR and polyPR knock-in mice reveal a conserved neuroprotective extracellular matrix signature in C9orf72 ALS/FTD neurons

C Milioto, M Carcolé, A Giblin, R Coneys, O Attrebi… - Nature …, 2024 - nature.com
Dipeptide repeat proteins are a major pathogenic feature of C9orf72 amyotrophic lateral
sclerosis (C9ALS)/frontotemporal dementia (FTD) pathology, but their physiological impact …

C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins

YJ Zhang, TF Gendron, JC Grima, H Sasaguri… - Nature …, 2016 - nature.com
Neuronal inclusions of poly (GA), a protein unconventionally translated from G4C2 repeat
expansions in C9ORF72, are abundant in patients with frontotemporal dementia (FTD) and …