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000282332 0247_ $$2doi$$a10.1007/s12035-025-05359-6
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000282332 037__ $$aDZNE-2025-01293
000282332 041__ $$aEnglish
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000282332 1001_ $$aZahra, Fatima Tu$$b0
000282332 245__ $$aSynuclein Proteoforms: Role in Health and Disease.
000282332 260__ $$aTotowa, NJ$$bHumana Press$$c2025
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000282332 520__ $$aSynucleins α, β, and γ are inherently disordered proteins that play essential roles in neuronal physiology and are increasingly recognized as key players in neurodegenerative disease mechanisms. The molecular basis of synucleinopathies, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy, is the pathological aggregation and misfolding of synucleins. However, the biological significance of the diverse synuclein proteoforms that result from alternative splicing, extensive post-translational modifications, and conformational heterogeneity is still not fully understood. This review systematically incorporates current knowledge of the structural and functional diversity of synuclein proteoforms, highlighting their molecular interactions and aggregation pathways. We investigate the regulatory effects of β and γ-synucleins (β-syn and γ-syn), which have different physiological functions and clinical applications in addition to influencing α-synuclein (α-syn) aggregation. In addition to synucleins' involvement in the central nervous system, recent findings show their role in immune regulation and functions in peripheral tissues, highlighting their systemic relevance. Controversial aspects, such as the mechanisms of prion-like propagation, proteoform-specific toxicity, and differential cellular vulnerability, are thoroughly analyzed. Synuclein proteoforms have been thoroughly characterized due to developments in molecular imaging and proteomic techniques, opening the door for targeted treatment approaches. Developing novel treatments for mitigating the progression of synucleinopathies and enhancing patient outcomes requires an understanding of the complex biology of synuclein proteoforms. The goal of this study is to present a thorough framework that connects translational research and molecular neurobiology in disorders related to synuclein.
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000282332 650_7 $$2Other$$aPTMs
000282332 650_7 $$2Other$$aProtein misfolding
000282332 650_7 $$2Other$$aProteoforms
000282332 650_7 $$2Other$$aSynuclein
000282332 650_7 $$2Other$$aSynucleinopathies
000282332 650_7 $$2NLM Chemicals$$aSynucleins
000282332 650_7 $$2NLM Chemicals$$aalpha-Synuclein
000282332 650_7 $$2NLM Chemicals$$aProtein Isoforms
000282332 650_2 $$2MeSH$$aHumans
000282332 650_2 $$2MeSH$$aAnimals
000282332 650_2 $$2MeSH$$aSynucleins: metabolism
000282332 650_2 $$2MeSH$$aSynucleins: chemistry
000282332 650_2 $$2MeSH$$aHealth
000282332 650_2 $$2MeSH$$aSynucleinopathies: metabolism
000282332 650_2 $$2MeSH$$aalpha-Synuclein: metabolism
000282332 650_2 $$2MeSH$$aNeurodegenerative Diseases: metabolism
000282332 650_2 $$2MeSH$$aProtein Isoforms: metabolism
000282332 7001_ $$aKayani, Hooreen$$b1
000282332 7001_ $$aNoreen, Samra$$b2
000282332 7001_ $$0P:(DE-2719)9001208$$aNoor, Aneeqa$$b3
000282332 7001_ $$0P:(DE-2719)9000358$$aZafar, Saima$$b4$$eLast author$$udzne
000282332 773__ $$0PERI:(DE-600)2079384-4$$a10.1007/s12035-025-05359-6$$gVol. 63, no. 1, p. 87$$n1$$p87$$tMolecular neurobiology$$v63$$x0893-7648$$y2025
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