MVN University Palwal Haryana
The aggregation of ?-synuclein is widely recognised as a central molecular event in the development of Parkinson’s disease. These aggregates are thought to form initially at synaptic terminals, potentially arising from abnormal interactions between ?-synuclein and lipid membranes or from failures in cellular protein quality control systems. Such interactions may promote the formation of structurally distinct conformations, often referred to as strains, which could contribute to the variability observed in clinical manifestations of Parkinson’s disease and other ?-synuclein-related disorders. For neuronal damage to occur, ?-synuclein aggregates must possess two key properties: the capacity to act as seeds that drive further protein aggregation, and the ability to induce cellular toxicity. This toxicity is believed to result, at least in part, from disruption of synaptic vesicle dynamics and impairment of organelle function. Given the highly flexible and dynamic nature of ?-synuclein, different aggregate species along its conformational spectrum may differentially contribute to seeding activity and toxic effects. Despite significant progress, it remains unclear which specific forms of ?-synuclein are most relevant in human disease. However, recent developments in cryo-electron microscopy have enabled detailed structural analysis of fibrils derived directly from brain tissue. When combined with studies in stem cell-based systems and animal models, these advances are expected to improve our understanding of disease mechanisms and support the identification of targeted therapeutic strategies and reliable biomarkers. This review outlines the key mechanisms underlying the initiation and spread of ?-synuclein aggregation in experimental models and discusses their implications for clinical applications. flexible and dynamic nature of ?-synuclein, different aggregate species along its conformational spectrum may differentially contribute to seeding activity and toxic effects. Despite significant progress, it remains unclear which specific forms of ?-synuclein are most relevant in human disease. However, recent developments in cryo-electron microscopy have enabled detailed structural analysis of fibrils derived directly from brain tissue. When combined with studies in stem cell-based systems and animal models, these advances are expected to improve our understanding of disease mechanisms and support the identification of targeted therapeutic strategies and reliable biomarkers. This review outlines the key mechanisms underlying the initiation and spread of ?-synuclein aggregation in experimental models and discusses their implications for clinical application.
Parkinson’s disease (PD) is the second most common neurodegenerative condition worldwide. It is characterised by a combination of motor disturbances—such as tremor, muscle rigidity, slowness of movement (bradykinesia), and impaired balance—alongside a broad spectrum of non-motor symptoms including constipation, orthostatic hypotension, REM sleep behaviour disorder, apathy, and progressive cognitive impairment. The way PD presents can differ markedly from one individual to another. Nevertheless, it is generally classified into three main clinical subtypes: a tremor-predominant form with unilateral onset and slow progression; a more severe form marked by symmetrical motor involvement, early cognitive decline, autonomic dysfunction, REM sleep behaviour disorder, and faster progression; and a third category that exhibits features intermediate between these two extremes [1, 2]. A notable feature of PD is its prolonged prodromal phase, during which non-motor symptoms—particularly REM sleep behaviour disorder—may be evident long before classical motor signs become apparent. Despite this variability in clinical presentation, a shared molecular hallmark of PD is the abnormal accumulation and aggregation of α-synuclein within neuronal networks, especially in regions of the autonomic nervous system, brainstem, and cortex. This common pathogenic pathway has become a central focus for the development of disease-modifying therapies [3]. The pathological involvement of α-synuclein extends beyond PD. In Multiple System Atrophy (MSA), a more aggressive parkinsonian disorder, α-synuclein aggregates predominantly accumulate in oligodendrocytes rather than neurons [4]. In Lewy body dementia, widespread α-synuclein inclusions are observed throughout cortical and brainstem regions, forming the defining neuropathological feature of the disease [5]. Moreover, α-synuclein aggregation has also been reported in certain cases of Alzheimer’s disease as well as in a range of rare inherited neurodegenerative disorders [6–8]. Several lines of evidence strongly support a causative role for α-synuclein in neurodegeneration. Genetic studies have identified mutations and multiplications in the SNCA gene in familial forms of PD, while common variants within this locus represent a major susceptibility factor in sporadic cases [9]. In addition, α-synuclein monomers have an intrinsic ability to assemble into fibrillar structures that closely resemble those isolated from diseased brain tissue when examined using electron microscopy [4, 5]. Experimental models further demonstrate that increased expression or aggregation of α-synuclein can lead to neuronal dysfunction and eventual cell loss [10]. The neurotoxic effects associated with PD are thought to arise from particular α-synuclein assemblies that combine two critical properties: the ability to seed and propagate further aggregation, and the capacity to disrupt normal cellular function. These toxic species interfere with essential processes such as synaptic vesicle trafficking and the maintenance of organelle integrity, ultimately contributing to neuronal damage. Although Lewy bodies and Lewy neurites are regarded as the defining pathological features of PD at post-mortem examination, they likely represent only a fraction of the underlying pathology. Importantly, their presence does not consistently correlate with disease severity [11, 12]. Advances in detection methods have revealed that α-synuclein aggregates are far more extensively distributed than previously recognised, particularly within presynaptic terminals [13]. This observation suggests that early-stage aggregates, which are smaller and more soluble, may play a more direct role in driving neurodegeneration, whereas larger inclusions could reflect a later cellular response aimed at sequestering misfolded proteins. Improved understanding of these molecular and cellular mechanisms, together with the development of experimental models that replicate key aspects of the disease, has opened new avenues for therapeutic intervention and biomarker discovery. While previous reviews have comprehensively addressed the structural diversity and pathogenic potential of α-synuclein [14, 15], the present work focuses on key findings related to the initiation and propagation of α-synuclein aggregation in model systems, the underlying molecular mechanisms, and their relevance for clinical translation.
Initiation of α-synuclein aggregation via disrupted membrane interactions
α-Synuclein is among the most abundant proteins in neurons, accounting for roughly 0.5–1% of total brain protein. It is primarily concentrated at presynaptic terminals, where it gives rise to the characteristic punctate distribution pattern seen within the neuropil of healthy brain tissue [16, 17]. Despite its high expression, its normal physiological role appears to be limited, as studies involving genetic knockout in animal models reveal only modest functional consequences. These include minor, activity-dependent effects on neurotransmitter release [18] and alterations in the expansion of the exocytic fusion pore during vesicle release [19]. The pathological role of α-synuclein is therefore not linked to loss of function but rather to a toxic gain of function, particularly under conditions of mutation or elevated expression. Experimental evidence indicates that even relatively small increases in α-synuclein levels—comparable to those observed in individuals with SNCA gene multiplication—can disrupt synaptic organisation. Specifically, such increases reduce synaptic vesicle density at active zones and impair the normal reclustering of vesicles after endocytosis, even in the absence of overt neurodegenerative changes [20]. Owing to its localisation and abundance, presynaptic terminals are widely considered the initial sites where α-synuclein pathology may arise in Parkinson’s disease. This concept is supported by findings from animal models, where expression of aggregation-prone forms of α-synuclein—such as C-terminally truncated variants or virally introduced full-length protein—leads to aggregate formation and defects in dopamine storage and release, without necessarily causing immediate neuronal death [21, 22]. One mechanism that may underlie these effects involves disruption of synaptic SNARE protein distribution, which is critical for vesicle fusion processes [23]. Furthermore, in vitro studies have demonstrated that soluble oligomeric α-synuclein can inhibit SNARE-dependent lipid mixing, suggesting that early aggregation may directly interfere with synaptic vesicle fusion at the plasma membrane [24, 25]. Notably, these early synaptic disturbances may not be permanent. Experimental studies in animal systems have shown that reducing α-synuclein expression can lead to partial removal of aggregates and improvement in both synaptic activity and behavioural outcomes, indicating that early pathological changes may be reversible [26]. In vitro experiments reveal that α-synuclein aggregation into amyloid fibrils follows a nucleation-dependent process. This begins with an initial lag phase, after which fibril growth accelerates rapidly in a manner dependent on protein concentration [27]. Such kinetics suggest that once a sufficient number of aggregation-prone intermediates form, they can act as nucleation centres or “seeds,” facilitating the addition of soluble α-synuclein monomers to growing fibrils. A key determinant of this aggregation behaviour is the central hydrophobic region of α-synuclein, referred to as the non-amyloid-β component (NAC) domain, which drives the formation of high molecular weight aggregates [28]. These inherent structural features support a model in which α-synuclein promotes disease through self-templating and propagation of misfolded conformations. In line with this, several mutations linked to familial Parkinson’s disease—including A53T, H50Q, and E46K—have been consistently shown to enhance aggregation rates [27–31]. Similarly, gene duplication or triplication of SNCA can increase the likelihood of aggregation by elevating the concentration of aggregation-prone protein species. However, not all mutations enhance aggregation in the same way. For instance, the A30P and G51D variants reduce the affinity of α-synuclein for lipid membranes and synaptic vesicles, and also impair the formation of α-helical structure in the N-terminal region [32, 33]. These findings suggest that, within the complex intracellular environment, α-synuclein aggregation is governed not only by its intrinsic structural properties but also by its interactions with cellular membranes and lipid components. In aqueous solution, α-synuclein exists largely as an intrinsically disordered protein lacking a fixed three-dimensional structure. However, its conformation changes upon association with lipid membranes, especially those containing negatively charged phospholipids or exhibiting high curvature, where the N-terminal region adopts an α-helical structure [34–36]. This membrane-bound state is considered to stabilise the protein and may limit its conversion into β-sheet-rich aggregated forms [37]. Moreover, interaction with membranes is thought to promote the formation of functional multimeric assemblies of α-synuclein [38, 39], which contribute to physiological processes such as SNARE complex formation and synaptic vesicle turnover [40]. Interestingly, membrane components can also have the opposite effect under certain conditions. Studies have shown that lipids and detergent-like molecules may enhance the rate of α-synuclein fibril formation [41, 42]. The impact of these interactions depends largely on the lipid environment [43, 44] as well as the relative proportion of protein to lipid or detergent. When lipid levels are low, aggregation is generally promoted, whereas higher lipid concentrations tend to suppress this process [45]. One possible explanation is that membrane surfaces confine α-synuclein molecules within limited areas, thereby increasing their local concentration and favouring the initiation of aggregation once a critical threshold is reached. The aggregation process may also involve transient structural intermediates, including partially helical forms of α-synuclein, as indicated by nuclear magnetic resonance (NMR) studies [46].
In addition to membrane composition, local physicochemical conditions around membrane compartments can further influence aggregation behaviour. Variations in pH or intracellular calcium (Ca²?) levels are likely to modulate the structural dynamics of α-synuclein (Fig. 1). For example, binding of Ca²? to the C-terminal region has been reported to trigger conformational changes that destabilise the N-terminal domain, thereby promoting aggregation-prone states [47]. Under acidic conditions, the net negative charge of α-synuclein—especially at its C-terminal region—is diminished. This reduction in electrostatic repulsion enables closer intramolecular interactions, favouring hydrophobic collapse and the generation of a partially folded intermediate structure [48]. In addition to these factors, truncation of the C-terminal region of α-synuclein—such as that occurring through stress-induced activation of proteolytic enzymes—has also been reported to enhance its aggregation propensity [21]. Notably, aggregation of α-synuclein at membrane surfaces can itself compromise membrane integrity through multiple mechanisms [49, 50]. This disruption may lead to leakage of protons (H?), resulting in local alterations in pH within intracellular compartments such as endosomes, lysosomes, or synaptic vesicles. Such changes in the microenvironment can further promote α-synuclein aggregation, thereby amplifying the process. Once aggregates are formed, α-synuclein can interact with key transmembrane proteins associated with various organelles. For example, it has been shown to bind to SERCA in the endoplasmic reticulum [51], TOM20 in mitochondria [52], and LAMP2A in lysosomes [53], leading to functional impairment of these organelles. These interactions contribute to a self-perpetuating cycle of cellular dysfunction, progressively affecting synaptic integrity and neuronal viability (Fig. 1B). The idea that α-synuclein aggregation begins at or near membrane structures and subsequently disrupts organelle function is supported by observations of Lewy body ultrastructure. Early electron microscopy studies revealed that Lewy bodies contain a dense, osmiophilic core composed of components such as neuromelanin, lipofuscin, mitochondria, dense-core vesicles, and endosomal elements, surrounded by radially arranged or irregular fibrillar structures [54]. More recent investigations using advanced imaging techniques, including correlative light and electron microscopy as well as tomography, have confirmed that Lewy bodies represent highly complex and crowded assemblies. These structures contain a mixture of membrane fragments, vesicular compartments, and structurally altered organelles interspersed with α-synuclein fibrils [55]. Importantly, similar patterns of organelle sequestration and dysfunction have been reproduced in experimental neuronal models of α-synuclein aggregation, further supporting the relevance of these mechanisms to disease pathology [56].
Spread of α-synuclein pathology via cell non-autonomous processes
The detection of α-synuclein inclusions in transplanted embryonic neurons many years after implantation into patients provided early evidence that pathogenic α-synuclein species can move from host tissue into grafted cells. Within these recipient cells, they may act as templates, promoting the misfolding and aggregation of endogenous α-synuclein in a manner reminiscent of prion-like mechanisms [57, 58]. These findings aligned with earlier neuropathological observations by Braak and colleagues, who proposed that Lewy pathology progresses along anatomically connected neural circuits. In this framework, the disease is thought to begin in regions such as the dorsal motor nucleus of the vagus or the olfactory system and then extend progressively to more rostral brain areas [59].
Evidence from experimental models supports the concept of trans-neuronal spread. In transgenic mice, human α-synuclein has been shown to transfer into neurons grafted into the striatum [60]. Moreover, introduction of recombinant or patient-derived α-synuclein assemblies into the brains of wild-type mice induces the formation of inclusions accompanied by progressive neuronal degeneration [61–63]. Comparable outcomes have been observed in primate studies following the administration of fibrillar α-synuclein or Lewy body extracts [64, 65]. Several mechanisms have been proposed to explain how α-synuclein aggregates enter cells. Endocytosis appears to be a major route [66], although alternative pathways such as transfer via tunnelling nanotubes [67] and uptake mediated by heparan sulfate proteoglycans through macropinocytosis have also been described [68]. The relative contribution of these pathways may depend on the specific cell type or subcellular environment [68, 69], and whether a dedicated receptor for α-synuclein fibrils exists remains uncertain [70]. While neuronal connectivity plays an important role in shaping the spread of pathology—stronger synaptic connections facilitating transmission between regions [71–73]—it is not the sole determinant. Experimental studies have shown that the distribution of pathology does not always strictly follow anatomical connections [74]. Additional factors, including cell-specific levels of α-synuclein expression [71, 73, 75], the complexity of axonal projections, and metabolic stress—particularly in highly vulnerable neuronal populations such as dopaminergic and cholinergic neurons [76]—also influence disease progression. Furthermore, the activation state of glial cells, especially microglia, may modulate the extent and pattern of pathology [77, 78]. The presence of Lewy pathology within the enteric nervous system has led to the hypothesis that α-synuclein aggregates may spread between the gut and the brain. Epidemiological studies indicate that vagotomy is associated with a reduced risk of PD, supporting a gut-to-brain transmission pathway [79]. Experimental work in animals shows that different forms of α-synuclein—including monomers, oligomers, and fibrils—can be transported from the intestine to the brain via axonal transport mechanisms [80]. Injection of fibrillar α-synuclein into the intestinal wall initiates pathological changes in the dorsal motor nucleus of the vagus, which subsequently extend to other brain regions. This process can be prevented by vagotomy or in the absence of endogenous α-synuclein [81]. However, studies in primates suggest that the spread of α-synuclein pathology may also occur independently of the vagus nerve and in both directions, implying the involvement of systemic pathways [82]. One possible mechanism is the release of α-synuclein within extracellular vesicles, levels of which are elevated in PD patients even during early disease stages [83, 84]. Supporting this, systemic administration of α-synuclein fibrils can induce brain pathology in rodents [85], and circulating α-synuclein aggregates have been detected in the blood of PD patients, although their functional role remains unclear [86].
Structural heterogeneity and toxic species of α-synuclein
The precise forms of α-synuclein responsible for neurotoxicity in PD are not yet fully defined. A β-sheet-rich conformation is widely regarded as a key structural feature required for both aggregation seeding and toxicity. Advanced single-molecule studies indicate that multiple oligomeric species can arise during fibril formation; however, only those resistant to proteinase K digestion—indicative of stable β-sheet structure—exhibit cytotoxic properties [87, 88]. These oligomeric assemblies are estimated to consist of approximately 30 monomers [89], whereas stable fibrils require larger assemblies, typically involving around 70 monomers and reaching lengths of approximately 40 nm [90]. A dynamic balance exists between oligomeric intermediates and mature fibrils [87, 91], suggesting that both forms may contribute to disease processes. While aggregation kinetics vary among different α-synuclein mutants, the formation of oligomeric intermediates appears to be a common feature, pointing to their potential importance in toxicity [91]. Consistent with this, experimental studies in animals show that α-synuclein variants favouring oligomer formation cause greater dopaminergic neuron loss compared to those promoting fibril formation [92]. In contrast, fibrillar species are more efficient at initiating aggregation when introduced into living systems [85]. One possible explanation for these observations is that oligomers arise during the assembly or breakdown of fibrils within neurons and represent the primary toxic species. Their formation and stability may be influenced by factors such as post-translational modifications or incomplete protein degradation. For example, oxidative stress in dopaminergic neurons can generate reactive intermediates that stabilise toxic oligomeric forms of α-synuclein [93, 94]. Phosphorylation at serine 129 is a prominent modification observed in aggregated α-synuclein [95], although its role in promoting or inhibiting aggregation remains unclear [95–97]. Another important feature of α-synuclein is its ability to form structurally distinct fibrillar polymorphs, often referred to as strains. These can be generated under different experimental conditions [98, 99] and have also been identified in patient-derived samples using advanced structural techniques [100–102]. The precise structural forms of α-synuclein that act as seeding-competent species within intact human neurons have yet to be clearly defined. In addition, it remains uncertain how experimental factors—such as the use of detergents or amplification protocols—may alter or bias the structural features of these assemblies. Despite these limitations, the identification and characterisation of distinct fibrillar strains of α-synuclein have led to the idea that structural heterogeneity may underlie the diverse clinical presentations observed across α-synucleinopathies. Supporting this concept, studies using human iPSC-derived dopaminergic neurons [75] and experimental animal models [103] have demonstrated that strains derived from Multiple System Atrophy (MSA) brain homogenates exhibit greater toxicity than those obtained from Lewy body-related disorders. Consistent with this, intracerebral injection of MSA-derived material into transgenic mice induces widespread α-synuclein aggregation and marked neurodegeneration, whereas extracts from Parkinson’s disease (PD) brains produce comparatively milder effects [104, 105]. These experimental findings reflect the more aggressive disease course observed in MSA, which typically results in mortality within 7–10 years of onset. The mechanisms responsible for differences in toxicity between α-synuclein strains remain incompletely understood. Although neuronal loss requires a critical level of protein aggregation—dependent in part on the availability of monomeric α-synuclein [75]—other contributing factors are likely involved. Structural variations between strains may influence how they interact with the cellular proteome. In particular, differences in amino acid residues exposed on the surface of each conformer (Fig. 1A) could affect protein binding, susceptibility to post-translational modifications, and the ability to evade cellular defence mechanisms. Proteomic analyses using proximity-dependent biotinylation have revealed that α-synuclein aggregates interact with a large network of cellular proteins within an approximate radius of 10 nm during their assembly. While close to 1000 interacting proteins were identified, only 56 displayed strain-specific differences, including the Parkinson’s disease-associated protein DJ-1 [75]. Mutations leading to loss of DJ-1 function are known to cause autosomal recessive PD with Lewy body pathology [106]. Furthermore, experimental deletion of DJ-1 in human iPSC-derived neuronal models enhances seeded aggregation and increases neuronal susceptibility to toxicity [75], possibly due to the absence of its deglycase activity [107]. Post-translational modifications such as glycation may further promote the accumulation of misfolded α-synuclein by impairing normal degradation pathways. For instance, modification of lysine residues—including N-terminal lysine 12—can hinder ubiquitination, thereby reducing the efficiency of proteasomal clearance [75, 108–110]. At the same time, cellular chaperone systems, including HSC70 and members of the HSP90 family, are capable of mediating fibril disassembly through recognition of motifs within the N-terminal region of α-synuclein [111]. However, the effectiveness of these mechanisms may vary depending on the structural properties of individual strains. It is therefore conceivable that certain α-synuclein conformations gain a selective advantage by escaping cellular quality control systems, allowing them to persist and exert toxic effects. In contrast, interactions with protective proteins such as DJ-1 may help limit damage in more resilient neuronal populations. Supporting this idea, experimental studies have shown that α-synuclein pathology induced by fibrillar species can be transient in specific brain regions, suggesting that some cell types possess more efficient clearance mechanisms [73, 74]. The characteristics of α-synuclein strains may also be shaped by the cellular environment in which aggregation occurs. For example, oligodendrocytes have been shown to convert misfolded α-synuclein into conformations resembling those found in MSA, a process not observed in neurons [105]. Beyond disrupting protein homeostasis, these aggregates may also sequester essential cellular proteins, rendering them functionally inactive. In addition, different fibrillar polymorphs have been shown to interact distinctly with the plasma membrane in neuronal systems, resulting in altered distribution of key proteins such as α3-Na?/K?-ATPase and various synaptic receptors [112].
Translation of α-synuclein aggregation research into clinical applications
Progress in understanding the mechanisms of α-synuclein aggregation and its propagation across neuronal networks has opened new avenues for therapeutic intervention. Both active and passive immunotherapeutic strategies have demonstrated the ability to reduce α-synuclein pathology in preclinical models [113]. In parallel, small-molecule inhibitors targeting aggregation processes have shown promising efficacy in experimental studies [114, 115]. Targeting broader mechanisms involved in the uptake or clearance of pathogenic aggregates may also represent a viable therapeutic strategy. Clinical trials have evaluated monoclonal antibodies directed against α-synuclein, including prasinezumab (PRX002), which binds to the C-terminal region [116], and cinpanemab (BIIB054), which targets the N-terminal region [117]. Although both antibodies recognise aggregated forms of α-synuclein, it remains uncertain whether they effectively target the specific species responsible for disease progression. While these trials did not achieve their primary endpoints, prasinezumab was associated with a modest slowing of motor decline, particularly in patients with more advanced disease, prompting further investigation in ongoing studies. One of the major challenges in this field is the absence of reliable biomarkers to assess target engagement within the central nervous system. Currently, no positron emission tomography (PET) tracer is available for visualising α-synuclein aggregates, although advances in structural biology, particularly cryo-electron microscopy, may facilitate future development. Techniques adapted from prion research, such as RT-QuIC and PMCA, have been successfully applied to detect α-synuclein seeding activity in cerebrospinal fluid [118, 119] and peripheral tissues [120]. These assays demonstrate high diagnostic performance, with reported sensitivities and specificities of 80–90% [121], and may also identify individuals at risk during the prodromal phase [122]. Furthermore, analysis of aggregation kinetics using PMCA can distinguish between PD and MSA with high accuracy [100]. With further refinement, these approaches may prove valuable for patient stratification and monitoring of therapeutic response.
CONCLUSIONS
Since the identification of α-synuclein as a key component of Lewy bodies and the discovery of mutations in the SNCA gene, significant advances have been made in understanding its role in neurodegenerative disease. Evidence from experimental models indicates that disease pathology arises from a toxic gain of function associated with misfolded α-synuclein, likely initiated at synaptic sites. These aggregates interfere with essential cellular processes, including synaptic vesicle recycling and organelle function, ultimately leading to neuronal dysfunction. The capacity of α-synuclein to undergo self-templated aggregation provides a plausible explanation for the progressive nature of disease, although the extent to which this mechanism operates in the human brain remains to be fully clarified. Variability in strain structure, cellular context, and protein interactions likely contributes to the clinical heterogeneity observed across α-synucleinopathies. Future work aimed at resolving the structural diversity of α-synuclein assemblies, developing robust biomarkers, and refining experimental models will be essential for advancing therapeutic strategies. A more personalised approach to treatment, potentially initiated during the prodromal stage of disease, may offer improved clinical outcomes, particularly if therapies are tailored to specific molecular subtypes.
CONCLUSION
By increasing productivity, accuracy, and patient-centered care, artificial intelligence (AI) is revolutionizing the pharmacy industry. Personalized medicine, quicker medication discovery, and improved patient safety through improved monitoring and decision-making are all made possible by it. Despite its advantages, its adoption requires addressing issues including data security, ethical problems, and workforce adaption. To overcome these obstacles, cooperation among healthcare providers, appropriate training, and robust regulatory frameworks are crucial. AI has the potential to greatly enhance pharmacy practice and healthcare outcomes with continuing research and responsible application. AI is anticipated to further simplify pharmaceutical operations and lower total healthcare expenses in the future. In the end, its integration will help create a healthcare system that is more patient-centered, proactive, and predictive
REFERENCES
Sachin Tanwar*, Ashutosh Upadhayay, S. Gopika, Sanjeev Kumar, Amit, Aniket, Yogendra Singh, Pathogenic Initiation and Propagation of ?-Synuclein Aggregation in Parkinson’s Disease: A COMPREHENSIVE REVIEW, Int. J. of Pharm. Sci., 2026, Vol 4, Issue 5, 2202-2220. https://doi.org/10.5281/zenodo.20113504
10.5281/zenodo.20113504
