Role of succinylation modification in central nervous system diseases

Wang, Chao; Cui, Weigang; Yu, Bing; Zhou, Han; Cui, Zhenwen; Guo, Pin; Yu, Tao; Feng, Yugong

doi:10.1016/j.arr.2024.102242

Ageing Research Reviews

2024

DOI: 10.1016/j.arr.2024.102242

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Role of succinylation modification in central nervous system diseases

Chao Wang,

Weigang Cui,

Bing Yu

et al.

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2024

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Cited by 2 publications

References 107 publications

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Protein modification in neurodegenerative diseases

Ramazi,

Dadzadi,

Darvazi

et al. 2024

MedComm

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Posttranslational modifications play a crucial role in governing cellular functions and protein behavior. Researchers have implicated dysregulated posttranslational modifications in protein misfolding, which results in cytotoxicity, particularly in neurodegenerative diseases such as Alzheimer disease, Parkinson disease, and Huntington disease. These aberrant posttranslational modifications cause proteins to gather in certain parts of the brain that are linked to the development of the diseases. This leads to neuronal dysfunction and the start of neurodegenerative disease symptoms. Cognitive decline and neurological impairments commonly manifest in neurodegenerative disease patients, underscoring the urgency of comprehending the posttranslational modifications’ impact on protein function for targeted therapeutic interventions. This review elucidates the critical link between neurodegenerative diseases and specific posttranslational modifications, focusing on Tau, APP, α‐synuclein, Huntingtin protein, Parkin, DJ‐1, and Drp1. By delineating the prominent aberrant posttranslational modifications within Alzheimer disease, Parkinson disease, and Huntington disease, the review underscores the significance of understanding the interplay among these modifications. Emphasizing 10 key abnormal posttranslational modifications, this study aims to provide a comprehensive framework for investigating neurodegenerative diseases holistically. The insights presented herein shed light on potential therapeutic avenues aimed at modulating posttranslational modifications to mitigate protein aggregation and retard neurodegenerative disease progression.

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Protein modification in neurodegenerative diseases

Ramazi,

Dadzadi,

Darvazi

et al. 2024

MedComm

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PTMD 2.0: an updated database of disease-associated post-translational modifications

Huang,

Feng,

Liu

et al. 2024

Nucleic Acids Research

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Various post-translational modifications (PTMs) participate in nearly all aspects of biological processes by regulating protein functions, and aberrant states of PTMs are frequently associated with human diseases. Here, we present a comprehensive database of PTMs associated with diseases (PTMD 2.0), including 342 624 PTM–disease associations (PDAs) in 15 105 proteins for 93 types of PTMs and 2083 diseases. Based on the distinct PTM states in diseases, we classified all PDAs into six categories: upregulation (U) or downregulation (D) of PTM levels, absence (A) or presence (P) of PTMs, and creation (C) or disruption (N) of PTM sites. We provided detailed annotations for each PDA and carefully annotated disease-associated proteins by integrating the knowledge from 101 additional resources that covered 13 aspects, including disease-associated information, variation and mutation, protein–protein interaction, protein functional annotation, DNA and RNA element, protein structure, chemical–target relationship, mRNA expression, protein expression/proteomics, subcellular localization, biological pathway annotation, functional domain annotation and physicochemical property. With a data volume of ∼8 GB, we anticipate that PTMD 2.0 will serve as a fundamental resource for further analysing the relationships between PTMs and diseases. The online service of PTMD 2.0 is freely available at https://ptmd.biocuckoo.cn/.

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Role of succinylation modification in central nervous system diseases

Cited by 2 publications

References 107 publications

Protein modification in neurodegenerative diseases

Protein modification in neurodegenerative diseases

PTMD 2.0: an updated database of disease-associated post-translational modifications

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