Corrigendum to “Anti-α-synuclein ASO delivered to monoamine neurons prevents α-synuclein accumulation in a Parkinson's disease-like mouse model and in monkeys” [EBioMedicine 2020; 59:102944]
Year: 2021
Type: erratum
Abstract: The authors have recently noticed that the published version of this article contained errors in the accession code and in the antisense oligonucleotide sequence for detecting human α-synuclein mRNA using in situ hybridization. The correct sequence complementary to bases 669-709 corresponds to GenBank accession https://www.ncbi.nlm.nih.gov/nuccore/NM_000345.4. Moreover, unlike IND-1233-ASO, the IND-1337-ASO sequence is not 100% complementary to human α-synuclein mRNA. IND-1337-ASO sequence was optimized for the AAV5-CBA construct that encodes the human-α-synuclein provided by Michael J. Fox Foundation. The sequence was modified to fully match that inserted in this model including mouse codon optimization.These corrections do not change the description, interpretation, or the original conclusions of the manuscript. The authors apologize for any inconvenience caused by these unintentional errors. The authors have recently noticed that the published version of this article contained errors in the accession code and in the antisense oligonucleotide sequence for detecting human α-synuclein mRNA using in situ hybridization. The correct sequence complementary to bases 669-709 corresponds to GenBank accession https://www.ncbi.nlm.nih.gov/nuccore/NM_000345.4. Moreover, unlike IND-1233-ASO, the IND-1337-ASO sequence is not 100% complementary to human α-synuclein mRNA. IND-1337-ASO sequence was optimized for the AAV5-CBA construct that encodes the human-α-synuclein provided by Michael J. Fox Foundation. The sequence was modified to fully match that inserted in this model including mouse codon optimization. These corrections do not change the description, interpretation, or the original conclusions of the manuscript. The authors apologize for any inconvenience caused by these unintentional errors. Anti-α-synuclein ASO delivered to monoamine neurons prevents α-synuclein accumulation in a Parkinson's disease-like mouse model and in monkeysProgressive neuronal death in monoaminergic nuclei and widespread accumulation of α-synuclein are neuropathological hallmarks of Parkinson's disease (PD). Given that α-synuclein may be an early mediator of the pathological cascade that ultimately leads to neurodegeneration, decreased α-synuclein synthesis will abate neurotoxicity if delivered to the key affected neurons. Full-Text PDF Open Access
Source: EBioMedicine
Institutions: Consejo Superior de Investigaciones Científicas, Institut d'Investigacions Biomèdiques de Barcelona, Consorci Institut D'Investigacions Biomediques August Pi I Sunyer, Instituto de Salud Carlos III, Centro de Investigación Biomédica en Red de Salud Mental, Universidade Federal do Paraná, Rush University Medical Center, Institució Catalana de Recerca i Estudis Avançats, Biomedical Research Networking Center on Neurodegenerative Diseases, Vall d'Hebron Institut de Recerca, Centro de Investigación Biomédica en Red
Language: English
Subfield: Neurology
Field: Medicine
Domain: Health Sciences
Open Access status: gold
Estimated APC paid: $3,500
OpenAlex ID: W3216035595