References
- Burchell VS, Gandhi S, Deas E, Wood NW, Abramov AY. Targeting mitochondrial dysfunction in neurodegenerative disease : Part II. Expert Opin Ther Targets. 2010:497–511.
- Ashrafi G, Schwarz TL. The pathways of mitophagy for quality control and clearance of mitochondria. Cell Death Differ. 2012;20(1):31–42.
- McWilliams TG, Muqit MM. PINK1 and Parkin: emerging themes in mitochondrial homeostasis. Curr Opin Cell Biol. 2017;45:83–91.
- Um JH, Yun J. Emerging role of mitophagy in human diseases and physiology. BMB Rep. 2017;50:299–307.
- Esteban‐Martínez L, Sierra‐Filardi E, McGreal RS, et al. Programmed mitophagy is essential for the glycolytic switch during cell differentiation. Embo J. [Internet]. 2017;36:1688–1706. Available from: http://emboj.embopress.org/lookup/doi/10.15252/embj.201695916
- Rodolfo C, Campello S, Cecconi F. Mitophagy in neurodegenerative diseases. Neurochem Int. [Internet]. 2018;117:156–166.
- Chen L, Ma K, Han J, et al. Monitoring mitophagy in mammalian cells. Methods Enzymol. 2017;588:187–208.
- Katayama H, Kogure T, Mizushima N, et al. A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery. Chem Biol. [Internet]. 2011;18:1042–1052.
- Kasianowicz J, Benz R, McLaughlin S. The kinetic mechanism by which CCCP (carbonyl cyanide m-Chlorophenylhydrazone) transports protons across membranes. J Membr Biol. 1984;82:179–190.
- Narendra DP, Jin SM, Tanaka A, et al. PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol. 2010;8:e1000298.
- Ettinger A, Wittmann T. Flourescence live cell imaging. Methods Cell Biol. 2015;123:77–94.
- McLelland G-L, Goiran T, Yi W, et al. Mfn2 ubiquitination by PINK1/parkin gates the p97-dependent release of ER from mitochondria to drive mitophagy. Elife. [Internet]. 2018;7:e32866. Available from: https://elifesciences.org/articles/32866
- Soutar MPM, Kempthorne L, Miyakawa S, et al. AKT signalling selectively regulates PINK1 mitophagy in SHSY5Y cells and human iPSC-derived neurons. Sci Rep. 2018:1–11. Available from: https://www.nature.com/articles/s41598-018-26949-6.pdf
- Francis GL. Albumin and mammalian cell culture: implications for biotechnology applications. Cytotechnology. 2010;62:1–16.
- Diolez P, Moreau F. Effect of bovine serum albumin on membrane potential in plant mitochondria. Physiol Plant. 1983;59:177–182.
- Tretter L, Mayer-Takacs D, Adam-Vizi V. The effect of bovine serum albumin on the membrane potential and reactive oxygen species generation in succinate-supported isolated brain mitochondria. Neurochem Int. 2007;50:139–147.
- Dairaku N, Kato K, Honda K, et al. Oligomycin and antimycin A prevent nitric. J Lab Clin Med. 2004;143(3):143–151. .
- Cutting WC, Mehrtens HG, Tainter ML. Actions and uses of dinitrophenol: promising metabolic applications. J Am Med Assoc. 1933;101:193.
- Tainter ML, Wood DA. A case of fatal dinitrophenol poisoning. J Am Med Assoc. 1934;102:1147.
- Lou P-H, Hansen BS, Olsen PH, et al. Mitochondrial uncouplers with an extraordinary dynamic range. Biochem J. [Internet]. 2007; 407:129–140. Available from: http://biochemj.org/lookup/doi/10.1042/BJ20070606
- Georgakopoulos ND, Wells G, Campanella M. The pharmacological regulation of cellular mitophagy. Nat Chem Biol. [Internet]. 2017; 13:136–146. Available from: http://www.nature.com/doifinder/10.1038/nchembio.2287
- Mailloux RJ, McBride SL, Harper ME. Unearthing the secrets of mitochondrial ROS and glutathione in bioenergetics. Trends Biochem Sci. [Internet]. 2013;38:592–602.
- Cantin AM, Paquette B, Richter M, et al. Albumin-mediated regulation of cellular glutathione and nuclear factor kappa B activation. Am J Respir Crit Care Med. 2000;162:1539–1546.
- Mlejnek P, Dolezel P. Loss of mitochondrial transmembrane potential and glutathione depletion are not sufficient to account for induction of apoptosis by carbonyl cyanide 4-(trifluoromethoxy)phenylhydrazone in human leukemia K562 cells. Chem Biol Interact. [Internet]. 2015;239:100–110.
- Yamasaki K, Chuang VTG, Maruyama T, et al. Albumin-drug interaction and its clinical implication. Biochim Biophys Acta Gen Subj. [Internet]. 2013;1830:5435–5443.
- Kane MS, Paris A, Codron P, et al. Current mechanistic insights into the CCCP-induced cell survival response. Biochem Pharmacol. [Internet]. 2018;148:100–110.
- McCoy MK, Kaganovich A, Rudenko IN, et al. Hexokinase activity is required for recruitment of parkin to depolarized mitochondria. Hum Mol Genet. [Internet]. 2014;23:145–156. [ cited 2014 May 1]. Available from: http://www.ncbi.nlm.nih.gov/pubmed/23962723
- Ardley HC, Scott GB, Rose SA, et al. Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin. Mol Biol Cell. 2003;14:4541–4556.
- Plun-Favreau H, Klupsch K, Moisoi N, et al. The mitochondrial protease HtrA2 is regulated by Parkinson’s disease-associated kinase PINK1. Nat Cell Biol. 2007;9:1243–1252.