Amyloid protein aggregates: new clients for mitochondrial energy production in the brain?-Reference-Cited by-同舟云学术

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Amyloid protein aggregates: new clients for mitochondrial energy production in the brain?

Published:2020-02-13 Issue:16 Volume:287 Page:3386-3395
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Sivanesan Senthilkumar¹^ORCID,Chang Edwin²,Howell Mathew D.³,Rajadas Jayakumar¹⁴

Affiliation:

1. Biomaterials and Advanced Drug Delivery Laboratory Cardiovascular Institute Stanford University School of Medicine Stanford CA USA

2. Department of Radiology Stanford University School of Medicine Stanford CA USA

3. St. Petersburg FL USA

4. Department of Bioengineering and Therapeutic Sciences School of Pharmacy University of California San Francisco San Francisco CA USA

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.15225

Reference72 articles.

1. Ubiquitination of specific mitochondrial matrix proteins

2. Protein trafficking at the crossroads to mitochondria

3. Mitochondrial quality control by the ubiquitin–proteasome system

4. The Ubiquitin-Proteasome System Regulates Mitochondrial Intermembrane Space Proteins

5. Metalloprotease OMA1 Fine-tunes Mitochondrial Bioenergetic Function and Respiratory Supercomplex Stability

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1. Targeting VDAC: A potential therapeutic approach for mitochondrial dysfunction in Alzheimer's disease;Brain Research;2024-07

2. Deciphering mitochondrial dysfunction: Pathophysiological mechanisms in vascular cognitive impairment;Biomedicine & Pharmacotherapy;2024-05

3. Scientific Evidence of Baduanjin Improving Cognitive Function in Patients with Cognitive Impairment;Open Journal of Natural Science;2024

4. Mitochondrial Complex I and β-Amyloid Peptide Interplay in Alzheimer’s Disease: A Critical Review of New and Old Little Regarded Findings;International Journal of Molecular Sciences;2023-11-03

5. Impacts of oxidants and antioxidants on the emergence and progression of Alzheimer's disease;Neurochemistry International;2022-02

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