title: Cellular strategies to cope with protein aggregation.
abstract: Nature has evolved several mechanisms to detoxify intracellular protein aggregates that arise upon proteotoxic challenges. These include the controlled deposition of misfolded proteins at distinct cellular sites, the protein disaggregation and refolding by molecular chaperones and/or degradation of misfolded and aggregated protein species by cellular clearance pathways. In this article, we discuss cellular the strategies of prokaroytes and eukaryotes to control protein aggregation.
authors.affiliation: Leibniz-Institute for Molecular Pharmacology (FMP) im Forschungsverbunbd Berlin e.V., Robert-Roessle-Straße 10, 13125 Berlin, Germany.
authors.forename: Annika
authors.initials: A
authors.lastname: Scior
authors.affiliation: Leibniz-Institute for Molecular Pharmacology (FMP) im Forschungsverbunbd Berlin e.V., Robert-Roessle-Straße 10, 13125 Berlin, Germany Academic Medical Center Amsterdam, Department of Cell Biology and Histology, Meibergdreef 9, 1105 AZ, Amsterdam, The Netherlands.
authors.forename: Katrin
authors.initials: K
authors.lastname: Juenemann
authors.affiliation: Leibniz-Institute for Molecular Pharmacology (FMP) im Forschungsverbunbd Berlin e.V., Robert-Roessle-Straße 10, 13125 Berlin, Germany Kirstein@fmp-berlin.de.
authors.forename: Janine
authors.initials: J
authors.lastname: Kirstein
mesh_terms: D000682:Amyloid / Q000378:metabolism; D000818:Animals; D002477:Cells / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism; D066329:Protein Aggregates; D066263:Protein Aggregation, Pathological / Q000378:metabolism* / Q000473:pathology / Q000628:therapy
chemical_list: D000682:Amyloid; D018832:Molecular Chaperones; D066329:Protein Aggregates
keywords: aggresome; amyloid; autophagy; chaperones; degradation; deposition; disaggregase; misfolding; polyQ; proteasome; protein quality control; proteostasis