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Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson’s disease
Hajung Yoo 1 (Graduate student), Jeongmin Lee 1 (Graduate student), Bokwang Kim 1 (Graduate student), Heechang Moon 1 (Graduate student), Huisu Jeong 1 (Graduate student), Kyungmi Lee1 (Undergraduate student), Woo Jeung Song 1 (Graduate student), Junho K. Hur 1 (Associate professor), Yohan Oh 1,* (Associate professor)
1Department of Biomedical Science, Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Republic of Korea,
2Department of Medicine and 3Department of Medical Genetics, College of Medicine, Hanyang University, Seoul 04763, Republic of Korea,
4Hanyang Institute of Bioscience and Biotechnology, Hanyang University, Seoul 04763, Republic of Korea,
5Department of Biochemistry and Molecular Biology, College of Medicine, Hanyang University, Seoul 04763, Republic of Korea
Together with neuronal loss, the existence of insoluble inclusions of alpha-synuclein (メ-syn) in the brain is widely accepted as a hallmark of synucleinopathies including Parkinson’s disease (PD), multiple system atrophy, and dementia with Lewy body. Because the メ-syn aggregates are deeply involved in the pathogenesis, there have been many attempts to demonstrate the mechanism of the aggregation and its potential causative factors including post-translational modifications (PTMs). Although no concrete conclusions have been made based on the previous study results, growing evidence suggests that modifications such as phosphorylation and ubiquitination can alter メ-syn characteristics to have certain effects on the aggregation process in PD; either facilitating or inhibiting fibrillization. In the present work, we reviewed studies showing the significant impacts of PTMs on メ-syn aggregation. Furthermore, the PTMs modulating メ-syn aggregation-induced cell death have been discussed.
Abstract, Accepted Manuscript [Submitted on April 21, 2022, Accepted on June 22, 2022]
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