{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kubota S"],"funding":["a Grant for Strategic Research Promotion from Yokohama City University","Grants-in-Aid for Scientific Research","a Health and Labor Sciences Research Grant from the Ministry of Health, Labour and Welfare, Japan","Takeda Science Foundation","Grants-in-Aid for Young Scientists"],"pagination":["59"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7986274"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(1)"],"pubmed_abstract":["Intracellular aggregates are a common pathological hallmark of neurodegenerative diseases such as polyglutamine (polyQ) diseases, amyotrophic lateral sclerosis (ALS), Parkinson's disease (PD), and multiple system atrophy (MSA). Aggregates are mainly formed by aberrant disease-specific proteins and are accompanied by accumulation of other aggregate-interacting proteins. Although aggregate-interacting proteins have been considered to modulate the formation of aggregates and to be involved in molecular mechanisms of disease progression, the components of aggregate-interacting proteins remain unknown. In this study, we showed that small glutamine-rich tetratricopeptide repeat-containing protein alfa (SGTA) is an aggregate-interacting protein in neurodegenerative diseases. Immunohistochemistry "],"journal":["Molecular brain"],"pubmed_title":["SGTA associates with intracellular aggregates in neurodegenerative diseases."],"pmcid":["PMC7986274"],"funding_grant_id":["20K16581","#SK2804","#201711060A","18K07531","19K07845","18K07532","18K07503","19K17014","18K07504"],"pubmed_authors":["Tanaka F","Nakamura H","Ikeda S","Kunii M","Kubota S","Tada M","Koyano S","Doi H","Katsumoto A","Fukai R","Takeuchi H","Tanaka K","Komiya H","Takahashi K","Hashiguchi S"],"additional_accession":[]},"is_claimable":false,"name":"SGTA associates with intracellular aggregates in neurodegenerative diseases.","description":"Intracellular aggregates are a common pathological hallmark of neurodegenerative diseases such as polyglutamine (polyQ) diseases, amyotrophic lateral sclerosis (ALS), Parkinson's disease (PD), and multiple system atrophy (MSA). Aggregates are mainly formed by aberrant disease-specific proteins and are accompanied by accumulation of other aggregate-interacting proteins. Although aggregate-interacting proteins have been considered to modulate the formation of aggregates and to be involved in molecular mechanisms of disease progression, the components of aggregate-interacting proteins remain unknown. In this study, we showed that small glutamine-rich tetratricopeptide repeat-containing protein alfa (SGTA) is an aggregate-interacting protein in neurodegenerative diseases. Immunohistochemistry ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2025-04-22T10:47:04.901Z","creation":"2025-04-05T23:40:17.066Z"},"accession":"S-EPMC7986274","cross_references":{"pubmed":["33757575"],"doi":["10.1186/s13041-021-00770-1"]}}