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Rigo, Frank

https://orcid.org/0000-0001-6467-3309

A5041605141 | I145311948

Mayo Clinic

Johns Hopkins University

Citations 4

Nuclear accumulation of CHMP7 initiates nuclear pore complex injury and subsequent TDP-43 dysfunction in sporadic and familial ALS

Science Translational Medicine | July 28, 2021 | Volume: 13 | Issue: 604 | Pages: No page available

10.1126/scitranslmed.abe1923 | PMID 34321318

Nuclear accumulation of CHMP7 leads to multiple cellular pathologies that can be mitigated via CHMP7 ASOs in familial and sporadic ALS iPSNs.
C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy

Science Translational Medicine | September 2, 2020 | Volume: 12 | Issue: 559 | Pages: No page available

10.1126/scitranslmed.abb3774 | PMID 32878979

G 4 C 2 repeat–derived poly(GR) plays a key role in mediating TDP-43 mislocalization and aggregation in vitro and in vivo.
Poly(GP) proteins are a useful pharmacodynamic marker for C9ORF72 -associated amyotrophic lateral sclerosis

Science Translational Medicine | March 29, 2017 | Volume: 9 | Issue: 383 | Pages: No page available

10.1126/scitranslmed.aai7866 | PMID 28356511

Poly(GP) proteins are a promising pharmacodynamic marker for developing and testing therapeutics for treating C9ORF72 -associated amyotrophic lateral sclerosis.
Targeting RNA Foci in iPSC-Derived Motor Neurons from ALS Patients with a C9ORF72 Repeat Expansion

Science Translational Medicine | October 23, 2013 | Volume: 5 | Issue: 208 | Pages: No page available

10.1126/scitranslmed.3007529 | PMID 24154603

Antisense oligonucleotides can correct disease-specific phenotypes in cultured motor neurons differentiated from iPSCs derived from ALS patients with a C9ORF72 repeat expansion.