<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kern U</submitter><funding>Deutsche Forschungsgemeinschaft</funding><pagination>404</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7920061</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10(2)</volume><pubmed_abstract>DJ-1 is an abundant and ubiquitous component of cellular proteomes. DJ-1 supposedly exerts a wide variety of molecular functions, ranging from enzymatic activities as a deglycase, protease, and esterase to chaperone functions. However, a consensus perspective on its molecular function in the cellular context has not yet been reached. Structurally, the C-terminal helix 8 of DJ-1 has been proposed to constitute a propeptide whose proteolytic removal transforms a DJ-1 zymogen to an active hydrolase with potential proteolytic activity. To better understand the cell-contextual functionality of DJ-1 and the role of helix 8, we employed post-mitotically differentiated, neuron-like SH-SY5Y neuroblastoma cells with stable over-expression of full length DJ-1 or DJ-1 lacking helix 8 (ΔH8), either wit</pubmed_abstract><journal>Cells</journal><pubmed_title>Impact of DJ-1 and Helix 8 on the Proteome and Degradome of Neuron-Like Cells.</pubmed_title><pmcid>PMC7920061</pmcid><funding_grant_id>SCHI 871/11-1; PA 2807/3-1; SCHI 871/9-1; SCHI 871/8-1;GR 1748/6-1;</funding_grant_id><funding_grant_id>SFB850</funding_grant_id><pubmed_authors>Schmidt N</pubmed_authors><pubmed_authors>Gensch N</pubmed_authors><pubmed_authors>Frohlich K</pubmed_authors><pubmed_authors>Biniossek ML</pubmed_authors><pubmed_authors>Kern U</pubmed_authors><pubmed_authors>Baerenfaller K</pubmed_authors><pubmed_authors>Schilling O</pubmed_authors><pubmed_authors>Bedacht J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Impact of DJ-1 and Helix 8 on the Proteome and Degradome of Neuron-Like Cells.</name><description>DJ-1 is an abundant and ubiquitous component of cellular proteomes. DJ-1 supposedly exerts a wide variety of molecular functions, ranging from enzymatic activities as a deglycase, protease, and esterase to chaperone functions. However, a consensus perspective on its molecular function in the cellular context has not yet been reached. Structurally, the C-terminal helix 8 of DJ-1 has been proposed to constitute a propeptide whose proteolytic removal transforms a DJ-1 zymogen to an active hydrolase with potential proteolytic activity. To better understand the cell-contextual functionality of DJ-1 and the role of helix 8, we employed post-mitotically differentiated, neuron-like SH-SY5Y neuroblastoma cells with stable over-expression of full length DJ-1 or DJ-1 lacking helix 8 (ΔH8), either wit</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Feb</publication><modification>2026-04-07T22:43:59.176Z</modification><creation>2025-05-29T20:31:52.74Z</creation></dates><accession>S-EPMC7920061</accession><cross_references><pubmed>33669258</pubmed><doi>10.3390/cells10020404</doi></cross_references></HashMap>