Translational Neurodegeneration最新文献

{"title":"The emerging role and therapeutic targeting of autophagy-lysosome pathway in the pathogenesis of Parkinson's disease.","authors":"Takahiro Shimizu, Sanem Isik, Nitika Kamath, Zhenyu Yue","doi":"10.1186/s40035-026-00555-3","DOIUrl":"10.1186/s40035-026-00555-3","url":null,"abstract":"<p><p>Parkinson's disease (PD) is a progressive neurodegenerative disorder characterized by dopaminergic neuron loss and the accumulation of misfolded α-synuclein, yet the underlying mechanisms remain incompletely understood. Over the past two decades, genetic discoveries have highlighted the convergence of multiple familial PD genes on the autophagy-lysosome pathway (ALP), a key cellular system responsible for the degradation and recycling of intracellular components. Recent studies have further revealed that components of the ALP not only mediate the clearance of α-synuclein aggregates but also, under certain pathological conditions, contribute to their propagation via lysosomal exocytosis or secretory autophagy. The precise functions of autophagy are highly context-dependent, with neuronal and glial cells exhibiting distinct ALP dynamics that shift with development, stress, and aging. In this review, we summarize current knowledge on the physiological regulation of autophagy in the brain and critically examine its involvement in PD pathogenesis, incorporating mechanistic insights from familial models and emerging evidence from sporadic PD. We also explore translational implications, focusing on efforts to identify ALP-related biomarkers in cerebrospinal fluid and urine, and on the therapeutic potential of modulating ALP activity. Although the causality between ALP dysfunction and PD remains elusive, mounting evidence supports its contribution to disease progression, particularly through impaired lysosomal homeostasis and disrupted intracellular trafficking. Future research should aim to define cell type-specific ALP alterations, clarify the bidirectional interactions between α-synuclein and autophagic machinery, and develop in vivo tools to monitor autophagy activity and secretory signatures. A deeper understanding of these processes will be crucial for refining PD models, discovering robust fluid biomarkers, and designing targeted therapies capable of modifying disease trajectory.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13151188/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147843204","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A new dawn for Parkinson's disease: commentary on the emergence of stem cell-based therapies.","authors":"Rosalie Elvira, Wai Hon Chooi, Hongyan Wang, Eng King Tan, Zhi Dong Zhou","doi":"10.1186/s40035-026-00556-2","DOIUrl":"10.1186/s40035-026-00556-2","url":null,"abstract":"<p><p>The field of regenerative medicine for Parkinson's disease (PD) has reached a pivotal moment. After decades of preclinical research, recent first-in-human clinical trials demonstrated that cell replacement therapy using stem cell-derived dopaminergic neurons is not only feasible and safe but also shows promising signs of efficacy. Here we analyze three landmark 2025 studies, including the phase I/II trial of allogeneic induced pluripotent stem cell-derived dopaminergic progenitors, that mark a significant leap forward for PD therapy. We discuss principles underpinning the therapy, the historical context of fetal tissue transplants, findings from recent trials, and critical challenges. The convergence of robust cell manufacturing, precise stereotactic surgery, and advanced neuroimaging provides compelling evidence that stem cell-based therapies are potentially a viable treatment paradigm for PD.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13126771/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147782065","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"N-terminally acetylated Met11-Tau: a new pathological truncated Tau species with functional relevance in Alzheimer's disease.","authors":"Sarah Guedjdal, Coline Leghay, Maxime Derisbourg, Sabiha Eddarkaoui, Simon Lecerf, Florian Vermon, Raphaelle Caillierez, Séverine Begard, Claire Regost, Charlotte Laloux, Paulo J da Costa, Kevin Carvalho, Giovanni Chiappetta, Yann Verdier, Valérie Buée-Scherrer, Vincent Deramecourt, Susanna Schraen, David Blum, Franck Martin, Luc Buée, Malika Hamdane","doi":"10.1186/s40035-026-00550-8","DOIUrl":"https://doi.org/10.1186/s40035-026-00550-8","url":null,"abstract":"<p><strong>Background: </strong>Tauopathies are a group of neurodegenerative diseases, including Alzheimer's disease (AD), characterized by progressive accumulation of pathological Tau proteins. Among the diverse Tau species, truncated variants are emerging as key contributors, yet their identity remains elusive, particularly for the N-terminal truncated ones. The present study identifies and characterizes a novel N-terminally truncated and N-alpha-acetylated form of the Tau protein, named AcMet11-Tau.</p><p><strong>Methods: </strong>We identified AcMet11-Tau by further analyses of previous proteomic data (capillary liquid chromatography-tandem mass spectrometry). We developed a monoclonal antibody, termed 2H2D11, by hybridoma method. The specificity of 2H2D11 was validated by ELISA, Western blot and immunohistochemistry. Expression of AcMet11-Tau in transgenic mouse model of Tau pathology and postmortem brain tissues was analyzed by ELISA and/or immunohistochemistry. Overexpression of AcMet11-Tau in the mouse brain was achieved by stereotaxic injections of lentiviral vectors carrying the coding sequence in the hippocampus. To neutralize AcMet11-Tau, transgenic mice received repeated intraperitoneal immunizations with either 2H2D11 or control antibody. The effects on Tau pathology were assessed by immunohistochemistry, qPCR, and behavioral assays.</p><p><strong>Results: </strong>Using 2H2D11, the newly developed antibody specifically targeting the AcMet11-Tau variant, we demonstrated that this species accumulated early in degenerating neurons in both transgenic mouse models of AD-related Tau pathology and post-mortem brain tissues from AD patients. Importantly, in vivo functional experiments revealed that expression of this truncated Tau species exacerbated Tau pathology in the transgenic mice, whereas targeted immunotherapeutic with the specific 2H2D11 antibody significantly reduced pathological Tau accumulation and prevented associated memory impairments.</p><p><strong>Conclusion: </strong>These findings position this newly identified Tau variant as a marker of neurofibrillary degeneration and a Tau species that contributes to disease-associated pathological processes, supporting its potential as a therapeutic target in Tau-related disorders, notably AD.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13123110/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147782108","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Drp1-CoQ10-Coa6-ETC axis represents a therapeutic potential for working memory impairment caused by neuronal mitochondrial dysfunction.","authors":"Jingjing Tie, Shujiao Li, Xin Huang, Keke Ren, Ziwei Ni, Xiaodong Li, Changlei Zhu, Hui Liu, Feifei Wu, Yanling Yang, Yayun Wang","doi":"10.1186/s40035-026-00552-6","DOIUrl":"https://doi.org/10.1186/s40035-026-00552-6","url":null,"abstract":"<p><strong>Background: </strong>Coenzyme Q10 (CoQ10) is a key mitochondrial electron carrier and a widely used dietary supplement with potential neurological benefits. However, the mechanisms underlying its effect in ameliorating memory deficits caused by cerebellar injury are not fully understood. In this study, we investigated the effects of long-term CoQ10 supplementation on working memory and the underlying mechanisms.</p><p><strong>Methods: </strong>Network pharmacology analysis was used to identify genetic targets of CoQ10 in cerebellar injury-related cognitive impairment. Purkinje cell (PC)-specific Drp1-deficient mice (PC-Drp1^-/-) were generated to model mitochondrial dysfunction. Behavioral performance was evaluated using the eight-arm radial maze. Mitochondrial structure and respiratory chain complex levels were evaluated by morphological and biochemical assays. Molecular targets of CoQ10 were identified using integrated drug-target engagement approaches, and their functional relevance was tested by viral vector-mediated overexpression.</p><p><strong>Results: </strong>The PC-Drp1^-/- mice displayed progressive working memory impairment and decreased PC density, accompanied by disrupted mitochondrial morphology and reduced activities of electron transport chain complexes III-V. Long-term CoQ10 treatment significantly reduced working memory errors and preserved PC numbers in PC-Drp1^-/- mice. Target engagement analyses identified cytochrome c oxidase assembly factor 6 (Coa6) as a direct binding target of CoQ10. Viral vector-mediated overexpression of Coa6 in PCs partially recapitulated the CoQ10-associated improvements in respiratory chain complex levels and working memory, whereas Coa6 knockdown attenuated these benefits.</p><p><strong>Conclusions: </strong>CoQ10 directly interacts with Coa6 to enhance mitochondrial respiratory chain function and preserve PC integrity in the context of Drp1 deficiency. Our findings suggest a promising mechanistic pathway for CoQ10-based intervention in memory deficits associated with mitochondrial dysfunction.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13112672/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147782137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dysfunction of the neurovascular unit as a temporal driver in Alzheimer's pathogenesis.","authors":"Lifang Wang, Lei Han, Shiping Liu","doi":"10.1186/s40035-026-00548-2","DOIUrl":"https://doi.org/10.1186/s40035-026-00548-2","url":null,"abstract":"<p><p>Extensive studies have shown that cerebrovascular dysfunction is a critical factor in the onset and progression of Alzheimer's disease (AD). Neurovascular unit (NVU) is impaired in AD brains, including damage of tight junction between endothelial cells, degeneration of pericytes, activation of astrocytes and microglia, and apoptosis of neurons. As decreased cerebral blood flow is observed before amyloid-beta (Aβ) generation, it is supposed that NVU dysfunction may precede and exacerbate the pathological state of AD neural system, and that the events of NVU dysfunction and Aβ deposition synergistically promote AD progression. Technological breakthroughs of three-dimensional NVU organoids, spatial transcriptomics with single-cell resolution, and development of artificial intelligence technology, such as machine learning and deep learning, offer the possibility of constructing accurate functional structural models. Here we systematically review the NVU dysfunction during AD progression as well as the applications of spatial transcriptomics and organoid technology in NVU studies.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13101311/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147782056","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Drug repurposing for disease-modifying effects in multiple system atrophy.","authors":"Seong Ho Jeong, Jin Young Shin, Phil Hyu Lee","doi":"10.1186/s40035-026-00551-7","DOIUrl":"10.1186/s40035-026-00551-7","url":null,"abstract":"<p><p>Multiple system atrophy (MSA) is a rapidly progressive neurodegenerative disorder lacking any proven disease-modifying therapy. Drug repurposing offers a strategy to accelerate the development of treatments by utilizing agents originally approved for other indications. This review summarizes repurposed drugs investigated as disease-modifying therapies for MSA, spanning preclinical in vitro and animal studies and clinical trials. We focus on agents targeting key pathogenic mechanisms in MSA-including α-synuclein aggregation (e.g., sirolimus/rapamycin, rifampicin, lithium, nilotinib, epigallocatechin gallate), neuroinflammation (e.g., minocycline, intravenous immunoglobulin), mitochondrial dysfunction and excitotoxicity (e.g., ubiquinol, rasagiline, safinamide, riluzole), and impaired neurotrophic support (e.g., fluoxetine/selective serotonin reuptake inhibitors, insulin, exendin-4). For each, we discuss mechanisms of action, experimental model outcomes, and clinical trial results. While numerous repurposed agents showed promise in MSA models, most failed to demonstrate significant disease-slowing effects in clinical trials. However, ubiquinol has recently emerged as a notable exception, with a Phase 2 randomized controlled trial showing a significant reduction in motor progression compared to placebo-marking the first placebo-controlled evidence of disease modification in MSA. Limitations such as small sample sizes, late-stage patient enrollment, and tolerability issues (e.g., with lithium) have hampered past trials. Nonetheless, ongoing studies and emerging approaches such as combination therapies hold promise. Continued exploration of repurposed therapies, along with improved trial design and biomarker development, is warranted to finally achieve a disease-modifying treatment for MSA.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13097543/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147730094","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"NDST3 suppression restores lysosomal acidification and ameliorates amyloid-β and MAPT/tau pathology in Alzheimer's disease.","authors":"Chuanhua Ge, Kun Wang, Huiyuan Tang, Yiling Ke, Huai Wang, Qiang Fu, Yun Xiu, Yongzheng Guo, Yun-Fang Jia, Zhimin Long, Guiqiong He, Qing Tang","doi":"10.1186/s40035-026-00549-1","DOIUrl":"https://doi.org/10.1186/s40035-026-00549-1","url":null,"abstract":"<p><strong>Background: </strong>Impairment of lysosomal acidification has recently been identified as a critical driver of amyloid-β and MAPT/tau pathology in Alzheimer's disease (AD). Restoring lysosomal acidification is a promising strategy for AD treatment. N-deacetylase and N-sulfotransferase 3 (NDST3) is a newly discovered tubulin deacetylase that regulates lysosomal acidification by influencing the recruitment of V-ATPase V1 subunits to lysosomes. Nevertheless, the role of NDST3 in AD remains entirely unexplored.</p><p><strong>Methods: </strong>We began by comparing the effects of NDST3 and histone deacetylase 6 (HDAC6), a well-known tubulin deacetylase with established roles in AD, on lysosomal acidification. Using HT22 cell-based models of AD, we knocked down NDST3 to examine its role in lysosomal acidification and degradative function in the context of this disease. We also evaluated the expression profile of NDST3 in both in vitro and in vivo models of AD. Finally, we investigated the consequences of NDST3 suppression on lysosomal acidity and related AD pathological features in the hippocampi of 3 × Tg-AD mice.</p><p><strong>Results: </strong>NDST3 differs from HDAC6 in the subcellular spatial patterns of catalyzing microtubule deacetylation but parallels HDAC6 in regulating lysosomal pH. In HT22 cells with APP695^Swe overexpression, knockdown of NDST3 lowered lysosomal pH by promoting the assembly of the V-ATPase holoenzyme on the lysosomal membrane and enhanced the autophagic degradation of aberrant Aβ and MAPT/tau. Notably, NDST3 levels were found to be elevated in the brains of AD models and patients. Reducing NDST3 expression in the hippocampi of 3 × Tg-AD mice facilitated lysosomal reacidification, which decreased the abnormal accumulation of amyloid plaques and MAPT/tau tangles, mitigated neuronal damage, and ameliorated cognitive deficits.</p><p><strong>Conclusions: </strong>Our study identified NDST3 as a key factor regulating lysosomal acidity in AD. Suppressing NDST3 restores lysosomal function in AD and protects against AD pathology, highlighting NDST3 as a promising therapeutic target for AD.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13097816/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147782087","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tau conformation, distribution and PET imaging correlations in progressive supranuclear palsy.","authors":"Chong Dong, Jing-Hong Ma, Hong-Wen Qiao, Gilles D Tamagnan, Piu Chan, Shu-Ying Liu","doi":"10.1186/s40035-026-00545-5","DOIUrl":"10.1186/s40035-026-00545-5","url":null,"abstract":"<p><p>Progressive supranuclear palsy (PSP) is a primary tauopathy characterized by aggregation of pathological tau. Recent advances in cryo-electron microscopy have enabled the classification of tauopathies at near-atomic resolution, revealing disease-specific tau filament conformations. These microstructural differences may influence the intracellular localization, intercellular propagation, and spatial distribution of tau pathology, as well as the microscopic binding profiles and macroscopic imaging signatures of tau positron emission tomography (PET) tracers. This review focuses on PSP by delineating its specific tau architecture and cellular and spatial distributions and how they differ in comparison with other major tauopathies and by critically discussing the clinical utility and limitations of tau PET. Through this integrative perspective, we aim to bridge neuropathological insights with in vivo PET findings.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13015156/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147515072","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Deciphering the microenvironment of adult neurogenesis: a perspective from neurodegenerative diseases.","authors":"Zheng-Kai Lao, Nan-Jie Xu","doi":"10.1186/s40035-026-00546-4","DOIUrl":"10.1186/s40035-026-00546-4","url":null,"abstract":"<p><p>Neurodegenerative diseases are characterized by progressive neuron loss and brain atrophy. While conventional studies focused on neuronal death as the primary cause of these diseases, accumulating evidence suggests that impaired neurogenesis, particularly the dysfunction of adult neural stem cells (NSCs), may also contribute significantly to disease pathogenesis. Adult neurogenesis occurs primarily in two adult NSC niches. These specialized niches are enriched with complex cytokine networks, neuronal activity, and non-cellular components such as the extracellular matrix. Understanding the regulation of NSCs in the adult brain and how their dysregulation exacerbates neurodegeneration provides novel insights into therapeutic strategies. This review proposes that dysfunction of the NSC microenvironment, rather than neuronal death alone, may drive neurodegeneration, and that restoring this microenvironment offers a novel research direction of stem cell-based therapies.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13011702/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147515108","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Axonopathy: mechanisms and potential therapeutic targets for neurodegenerative diseases.","authors":"Ruinan Shen, Kijung Sung, Jianqing Ding, Chengbiao Wu","doi":"10.1186/s40035-026-00543-7","DOIUrl":"10.1186/s40035-026-00543-7","url":null,"abstract":"<p><p>Axons are unique structural and functional features of nerve cells, which play a critical role in regulating neuronal homeostasis. Dysfunction and degeneration of axons (axonopathy) has been established as an early and prominent contributing mechanism to the pathogenesis of neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, Huntington's disease, and amyotrophic lateral sclerosis. In this review, we briefly summarize the structure and function of axons, and highlight recent advances in the understanding of the role of axons in health and disease. We argue that axons are a potential target for developing novel therapies for neurodegenerative diseases.</p>","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"15 1","pages":""},"PeriodicalIF":15.2,"publicationDate":"2026-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13011709/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147515105","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}