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Intramitochondrial proteostasis is directly coupled to α-synuclein and amyloid β1-42 pathologies

Janin Lautenschläger, Sara Wagner-Valladolid, Amberley D. Stephens, Ana Fernández‐Villegas, Colin Hockings, Ajay Mishra, James D. Manton, Marcus Fantham, Meng Lü, Eric J. Rees, Clemens F. Kaminski, Gabriele S. Kaminski Schierle

2020Journal of Biological Chemistry34 citationsDOIOpen Access PDF

Abstract

can influence protein homeostasis of cytosolic aggregation-prone proteins. We propose that approaches that seek to maintain mitochondrial fitness, rather than target downstream mitochondrial dysfunction, may aid in the search for therapeutic strategies to manage PD and related neuropathologies.

Topics & Concepts

ProteostasisMitochondrionCell biologyProteasomeReactive oxygen speciesBiologyProtein aggregationProteasesAmyloid (mycology)BiochemistryChemistryEnzymeBotanyParkinson's Disease Mechanisms and TreatmentsAlzheimer's disease research and treatmentsNeurological diseases and metabolism
Intramitochondrial proteostasis is directly coupled to α-synuclein and amyloid β1-42 pathologies | Litcius