Structural basis of bioenergetic protein complexes in Alzheimer's disease pathogenesis |
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| Institution: | 1. Faculty of Pharmacy, Universiti Teknologi MARA Selangor, Puncak Alam Campus, 42300 Bandar Puncak Alam, Selangor, Malaysia;2. Collaborative Drug Discovery Research, Faculty of Pharmacy, Universiti Teknologi MARA Selangor, Puncak Alam Campus, 42300 Bandar Puncak Alam, Selangor, Malaysia;1. Magnetic Resonance Center (CERM), University of Florence, Via Sacconi 6, Sesto Fiorentino, 50019, Italy;2. Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, 50019, Italy;3. Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (CIRMMP), Via Sacconi 6, Sesto Fiorentino, 50019, Italy;1. Universität Hamburg, ZBH – Center for Bioinformatics, Bundesstr. 43, 20146 Hamburg, Germany;2. insitro, 279 E Grand Ave., CA 94608, South San Francisco, USA;3. BioSolveIT GmbH, An der Ziegelei 79, 53757 Sankt Augustin, Germany;1. Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, Dr. Aiguader 88, Barcelona 08003, Spain;2. Universitat Pompeu Fabra (UPF), Barcelona, Spain;3. Faculty of Automatic Control, Electronics and Computer Science, Silesian University of Technology, Akademicka 16, Gliwice, 44-100, Poland |
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| Abstract: | Alzheimer's disease (AD) is a progressive neurodegenerative disease with no cure where the underlying causes remain elusive. Mitochondrial dysfunction has become a prime suspect in AD pathogenesis since bioenergetic deficits precede the pathology. With advancing structural biology techniques at synchrotrons and cryo-electron microscopes, it is becoming possible to determine the structures of key proteins suspected to contribute to the initiation and propagation of AD, and investigate their interactions. In this review, we provide an overview of the recent developments concerning the structural aspects of mitochondrial protein complexes and their assembly factors involved the production of energy, in pursuit of therapies to halt or even reverse this disease in the early stages when mitochondria are most sensitive to amyloid toxicity. |
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