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Year: 2024
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Document type: Review article
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Author: N/A
Target audience: Researchers, scientists in neurobiology, biochemistry, and Parkinson’s disease studies
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Post-Translational Modifications of α-Synuclein and Their Role in Synucleinopathy Pathogenesis: Systematic Review 2010–2024
Year: 2010–2024
Region / Location: International
Subject: Neurodegenerative Diseases / Protein Aggregation
Document Type: Systematic Review
Institution / Organization: Not specified
Authors: Multiple peer-reviewed studies
Target Audience: Researchers and clinicians in neurology and molecular biology
Date of Publication: June 2024
Research Focus: Effects of post-translational modifications on α-synuclein aggregation, structure, and toxicity
Methods: Literature review of PubMed, Scopus, Web of Science using PRISMA framework
Key Findings: Phosphorylation at Ser129 promotes aggregation; N-terminal acetylation and Ser87 phosphorylation reduce aggregation; C-terminal truncation and tyrosine nitration enhance neurotoxicity; PTM crosstalk affects aggregation and degradation pathways
Potential Applications: PTM-specific α-synuclein species as biomarkers for diagnosis and disease staging
Document Type Classification: Scientific review article
Post-Translational Modifications of α-Synuclein and Their Role in Synucleinopathy Pathogenesis: Systematic Review 2010–2024
Year: 2010–2024
Region / Location: International
Subject: Neurodegenerative Diseases / Protein Aggregation
Document Type: Systematic Review
Institution / Organization: Not specified
Authors: Multiple peer-reviewed studies
Target Audience: Researchers and clinicians in neurology and molecular biology
Date of Publication: June 2024
Research Focus: Effects of post-translational modifications on α-synuclein aggregation, structure, and toxicity
Methods: Literature review of PubMed, Scopus, Web of Science using PRISMA framework
Key Findings: Phosphorylation at Ser129 promotes aggregation; N-terminal acetylation and Ser87 phosphorylation reduce aggregation; C-terminal truncation and tyrosine nitration enhance neurotoxicity; PTM crosstalk affects aggregation and degradation pathways
Potential Applications: PTM-specific α-synuclein species as biomarkers for diagnosis and disease staging
Document Type Classification: Scientific review article
Methods and Experimental Model Details for SMCxPRO pUb Assay and α-Synuclein PFF Studies in Mice, Rats, and Primary Neuronal Cultures
Document type: Materials and Methods section
Species: C57Bl6/J mice; Sprague Dawley rats
Animal source: The Jackson Laboratories (Bar Harbor, Maine); Zhejiang Vital River Laboratory Animal Technology Co., Ltd.
Experimental facilities: BioDuro-Sundia (Shanghai, China)
Ethics approval: IACUC approved protocols
Regulatory compliance: Animal Welfare Act (9 CFR Parts 1–3); Guide for the Care and Use of Laboratory Animals (8th Edition); AAALAC accreditation (001516)
Cell lines: YPMK; YPMK PINK1 KO; EPF1; HEK293 PINK1 KO; SK-OV-3; ΔOTC
Primary cultures: Mouse hippocampal and cortical neurons (E16, A53T α-synuclein M83 mice)
Key assay: SMCxPRO pUb assay
Key reagents: Rabbit anti-pS65-Ub antibody (CST E2J6T); Mouse anti-Ub antibody (CST P4D1); K48 pUb tetramers (RnD Systems UC-250)
Instrumentation: SMCxPRO system; Agilent Seahorse XFe96 analyzer; ImageXpress Micro Confocal High-Content Imaging System
Experimental focus: α-synuclein preformed fibrils (PFFs); mitochondrial respiration; mitophagy measurement (MT-mKeima)
Data availability: Available from corresponding author upon reasonable request under Material Transfer Agreement
Code availability: No original code reported
Post-Translational Modifications of α-Synuclein and Their Role in Synucleinopathy Pathogenesis: Systematic Review 2010–2024
Year: 2010–2024
Region / Location: International
Subject: Neurodegenerative Diseases / Protein Aggregation
Document Type: Systematic Review
Institution / Organization: Not specified
Authors: Multiple peer-reviewed studies
Target Audience: Researchers and clinicians in neurology and molecular biology
Date of Publication: June 2024
Research Focus: Effects of post-translational modifications on α-synuclein aggregation, structure, and toxicity
Methods: Literature review of PubMed, Scopus, Web of Science using PRISMA framework
Key Findings: Phosphorylation at Ser129 promotes aggregation; N-terminal acetylation and Ser87 phosphorylation reduce aggregation; C-terminal truncation and tyrosine nitration enhance neurotoxicity; PTM crosstalk affects aggregation and degradation pathways
Potential Applications: PTM-specific α-synuclein species as biomarkers for diagnosis and disease staging
Document Type Classification: Scientific review article
Topics: Post-Translational Synucleinopathy -Synuclein