<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kubota S</submitter><funding>a Grant for Strategic Research Promotion from Yokohama City University</funding><funding>Grants-in-Aid for Scientific Research</funding><funding>a Health and Labor Sciences Research Grant from the Ministry of Health, Labour and Welfare, Japan</funding><funding>Takeda Science Foundation</funding><funding>Grants-in-Aid for Young Scientists</funding><pagination>59</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7986274</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14(1)</volume><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 </pubmed_abstract><journal>Molecular brain</journal><pubmed_title>SGTA associates with intracellular aggregates in neurodegenerative diseases.</pubmed_title><pmcid>PMC7986274</pmcid><funding_grant_id>20K16581</funding_grant_id><funding_grant_id>#SK2804</funding_grant_id><funding_grant_id>#201711060A</funding_grant_id><funding_grant_id>18K07531</funding_grant_id><funding_grant_id>19K07845</funding_grant_id><funding_grant_id>18K07532</funding_grant_id><funding_grant_id>18K07503</funding_grant_id><funding_grant_id>19K17014</funding_grant_id><funding_grant_id>18K07504</funding_grant_id><pubmed_authors>Tanaka F</pubmed_authors><pubmed_authors>Nakamura H</pubmed_authors><pubmed_authors>Ikeda S</pubmed_authors><pubmed_authors>Kunii M</pubmed_authors><pubmed_authors>Kubota S</pubmed_authors><pubmed_authors>Tada M</pubmed_authors><pubmed_authors>Koyano S</pubmed_authors><pubmed_authors>Doi H</pubmed_authors><pubmed_authors>Katsumoto A</pubmed_authors><pubmed_authors>Fukai R</pubmed_authors><pubmed_authors>Takeuchi H</pubmed_authors><pubmed_authors>Tanaka K</pubmed_authors><pubmed_authors>Komiya H</pubmed_authors><pubmed_authors>Takahashi K</pubmed_authors><pubmed_authors>Hashiguchi S</pubmed_authors></additional><is_claimable>false</is_claimable><name>SGTA associates with intracellular aggregates in neurodegenerative diseases.</name><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 </description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Mar</publication><modification>2025-04-22T10:47:04.901Z</modification><creation>2025-04-05T23:40:17.066Z</creation></dates><accession>S-EPMC7986274</accession><cross_references><pubmed>33757575</pubmed><doi>10.1186/s13041-021-00770-1</doi></cross_references></HashMap>