<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Scharf A</submitter><funding>NIH HHS</funding><pagination>426-35</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4819850</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10(4)</volume><pubmed_abstract>Identifying nanomaterial-bio-interactions are imperative due to the broad introduction of nanoparticle (NP) applications and their distribution. Here, we demonstrate that silica NPs effect widespread protein aggregation in the soil nematode Caenorhabditis elegans ranging from induction of amyloid in nucleoli of intestinal cells to facilitation of protein aggregation in body wall muscles and axons of neural cells. Proteomic screening revealed that exposure of adult C. elegans with silica NPs promotes segregation of proteins belonging to the gene ontology (GO) group of "protein folding, proteolysis and stress response" to an SDS-resistant aggregome network. Candidate proteins in this group include chaperones, heat shock proteins and subunits of the 26S proteasome which are all decisively inv</pubmed_abstract><journal>Nanotoxicology</journal><pubmed_title>Anti-amyloid compounds protect from silica nanoparticle-induced neurotoxicity in the nematode C. elegans.</pubmed_title><pmcid>PMC4819850</pmcid><funding_grant_id>P40 OD010440</funding_grant_id><funding_grant_id>P40   OD010440</funding_grant_id><pubmed_authors>Scharf A</pubmed_authors><pubmed_authors>von Mikecz A</pubmed_authors><pubmed_authors>Guhrs KH</pubmed_authors></additional><is_claimable>false</is_claimable><name>Anti-amyloid compounds protect from silica nanoparticle-induced neurotoxicity in the nematode C. elegans.</name><description>Identifying nanomaterial-bio-interactions are imperative due to the broad introduction of nanoparticle (NP) applications and their distribution. Here, we demonstrate that silica NPs effect widespread protein aggregation in the soil nematode Caenorhabditis elegans ranging from induction of amyloid in nucleoli of intestinal cells to facilitation of protein aggregation in body wall muscles and axons of neural cells. Proteomic screening revealed that exposure of adult C. elegans with silica NPs promotes segregation of proteins belonging to the gene ontology (GO) group of "protein folding, proteolysis and stress response" to an SDS-resistant aggregome network. Candidate proteins in this group include chaperones, heat shock proteins and subunits of the 26S proteasome which are all decisively inv</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016</publication><modification>2025-04-22T08:11:52.365Z</modification><creation>2019-03-27T03:11:09Z</creation></dates><accession>S-EPMC4819850</accession><cross_references><pubmed>26444998</pubmed><doi>10.3109/17435390.2015.1073399</doi></cross_references></HashMap>