The neurodegenerative disorder-associated proteins prions, α-synuclein, and tau were undetectable in the mutant COs.

<p>(A) A western blot analysis of PrP in DD, DN, and NN COs as well as in mouse brain homogenate infected with 22L scrapie (PrP<sup>Sc</sup>) after digesting with proteinase-K (PK). (B) A western blot analysis of PrP in DD, DN, and NN COs as well as in mouse brain homogenate infect...

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Main Author:	Simote T. Foliaki (11548933) (author)
Other Authors:	Anna Smith (3175848) (author), Benjamin Schwarz (1527106) (author), Eric Bohrnsen (12206821) (author), Catharine M. Bosio (178161) (author), Katie Williams (6166097) (author), Christina D. Orrú (14474985) (author), Hailey Lachenauer (14474988) (author), Bradley R. Groveman (11548936) (author), Cathryn L. Haigh (781205) (author)
Published:	2023
Subjects:	Biochemistry Medicine Cell Biology Genetics Molecular Biology Neuroscience Physiology Evolutionary Biology Chemical Sciences not elsewhere classified shifting biosynthetic intermediates krebs cycle intermediates greater mitochondrial activity data strongly suggests cellular energy homeostasis substantially increased glycolytic neuronal electrophysiological function cellular lipid composition isotype control organoids prp molecules lacking folded prp isoforms compromised neuronal activity cellular oxidative stress altered energy metabolism increased energy demand disease associated changes oxidative stress energy supply prp function increased mitophagy lipid droplets prp ). turn resulting translational processing tissue deposition still unknown prion protein particularly acetylcholine damaging effect could confirm brain cells abnormal post
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The neurodegenerative disorder-associated proteins prions, α-synuclein, and tau were undetectable in the mutant COs.

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