{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["27(7)"],"submitter":["Patra M"],"pubmed_abstract":["Here, we describe a single patient from a consanguineous family, who suffers from developmental delay, intellectual disability, hypermetropia, moderate alternating esotropia, unsteady gait, and peripheral polyneuropathy. Brain MRI revealed basal ganglia disease. Exome analysis disclosed a homozygous variant, c.452G>C (p.(Arg151Thr)), in TID1, encoding a mitochondrial J-protein chaperone that is known for its function in assisting the Hsp70 chaperone, mortalin, in mediating the refolding of denatured protein and dissolving protein aggregates. Results from in vitro import assays showed that both wild type and c.452G>C (p.(Arg151Thr)) are efficiently imported into isolated mitochondria. However, the import rate of the c.452G>C (p.(Arg151Thr)) variant was less than that of the wild-type protei"],"journal":["European journal of human genetics : EJHG"],"pagination":["1072-1080"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6777446"],"repository":["biostudies-literature"],"pubmed_title":["A novel variant of the human mitochondrial DnaJ protein, Tid1, associates with a human disease exhibiting developmental delay and polyneuropathy."],"pmcid":["PMC6777446"],"pubmed_authors":["Azem A","Elpeleg O","Ashhab M","Abuzer S","Weiss C","Mahajnah M","Kessel A","Patra M","Abu-Libdeh B"],"additional_accession":[]},"is_claimable":false,"name":"A novel variant of the human mitochondrial DnaJ protein, Tid1, associates with a human disease exhibiting developmental delay and polyneuropathy.","description":"Here, we describe a single patient from a consanguineous family, who suffers from developmental delay, intellectual disability, hypermetropia, moderate alternating esotropia, unsteady gait, and peripheral polyneuropathy. Brain MRI revealed basal ganglia disease. Exome analysis disclosed a homozygous variant, c.452G>C (p.(Arg151Thr)), in TID1, encoding a mitochondrial J-protein chaperone that is known for its function in assisting the Hsp70 chaperone, mortalin, in mediating the refolding of denatured protein and dissolving protein aggregates. Results from in vitro import assays showed that both wild type and c.452G>C (p.(Arg151Thr)) are efficiently imported into isolated mitochondria. However, the import rate of the c.452G>C (p.(Arg151Thr)) variant was less than that of the wild-type protei","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jul","modification":"2026-04-15T11:25:18.464Z","creation":"2020-07-04T07:18:13Z"},"accession":"S-EPMC6777446","cross_references":{"pubmed":["30770860"],"doi":["10.1038/s41431-019-0358-9"]}}