Acta Neuropathologica最新文献

{"title":"From a prion seed to a tree of discoveries: Byron Caughey’s RT-QuIC legacy in protein misfolding research","authors":"Bradley R. Groveman,&nbsp;Sarah Vascellari,&nbsp;Matilde Bongianni,&nbsp;Andrew G. Hughson,&nbsp;Gianluigi Zanusso,&nbsp;Christina D. Orrú","doi":"10.1007/s00401-026-03094-3","DOIUrl":"10.1007/s00401-026-03094-3","url":null,"abstract":"<div><p>Early and accurate detection of prions is essential for effective disease management and potential therapeutic intervention. Similar challenges extend across other protein misfolding diseases, which require ultrasensitive methods for detection, discrimination, and quantification of “prion-like” pathological proteins. Over a scientific career spanning multiple decades, Dr. Byron Caughey investigated mechanisms of prion conversion and replication, pioneered cell-free prion conversion assays, and steadfastly pursued increasingly sensitive, specific, robust, and high-throughput methods for prion amplification. His breakthrough development and continued refinement of the Real-Time Quaking-Induced Conversion (RT-QuIC) assay revolutionized prion research and helped extend seed amplification technology across the broader field of protein misfolding diseases. These assays have been developed through seminal contributions by many eminent scientists, and the breadth of this rapidly expanding field extends well beyond the scope of this review. Accordingly, we focus here on honoring Dr. Byron Caughey’s legacy by highlighting his foundational contributions to in vitro amplification and ultrasensitive detection of disease-associated protein aggregates. We further highlight the visionary, multidisciplinary, and collaborative nature of his work including the expansion of the platform to strain discrimination, surveillance, misfolded protein quantification, therapeutic research, higher throughput assay formats and the detection of other disease-associated misfolded proteins, including α-synuclein, tau, SOD1, and more.</p></div>","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149092435","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Amyloid-β plaque diversity across brain regions in Alzheimer’s disease and its relation to major clinicopathological traits","authors":"Antonia Neubauer,&nbsp;Paul Feyen,&nbsp;Susanna Pekrun,&nbsp;Sigrun Roeber,&nbsp;Viktoria Ruf,&nbsp;Felix L. Strübing,&nbsp;Jochen Herms","doi":"10.1007/s00401-026-03096-1","DOIUrl":"10.1007/s00401-026-03096-1","url":null,"abstract":"<div><p>Amyloid beta (Aβ) deposition and tau accumulation are neuropathological hallmarks of Alzheimer’s disease (AD). While Aβ deposits present with a wide morphological variety, a comprehensive, cross-regional overview of Aβ plaque composition in AD and associations with clinicopathological traits are missing. In this study, we systematically documented the abundance and morphological diversity of Aβ plaques in up to 23 brain regions of 84 advanced AD cases. Deposits were segmented with a random forest pixel classifier in 4G8 diaminobenzidine stains and classified into six classes using a convolutional neural network (cored, diffuse light, diffuse dense, compact, small dense plaques, cerebral amyloid angiopathy (CAA)). Deposit counts were correlated between classes, regions, and tau load using Pearson correlation. Associations between plaque densities and co-pathologies, sex, ApoE, familial vs. sporadic cases, age at clinical onset, disease duration, and age at death were examined. Our classification model achieved a recall of 81.5% and a precision of 82.4% in the test set. Cortical brain regions showed the highest Aβ plaque loads, predominantly consisting of diffuse light and small dense plaques. Plaque densities correlated within and across the hippocampal and cortical regions. Abundances of diffuse dense, small dense, and compact plaques were positively correlated with one another, while densities of cored plaques and CAA did not correlate with other plaque classes. Only cored plaques were positively correlated with the entorhinal tau load, while other plaque classes, except CAA, showed negative correlations. Notably, female sex was associated with more diffuse plaques, and ApoE4 was associated with diffuse dense and small dense plaques. Earlier age at onset and death were associated with higher densities of diffuse light plaques. Overall, associations varied across brain regions and plaque classes. Cored plaques and CAA stand out statistically from other Aβ deposits, suggesting distinct association patterns in the course of the disease.</p></div>","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00401-026-03096-1.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149089003","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":"Neurogenic muscular atrophy in NHP2-related dyskeratosis congenita in a family: pathological and molecular insights","authors":"Doriana Misceo,&nbsp;Lisa Lirussi,&nbsp;Ellen-Ann Antal,&nbsp;Alma Sikiric,&nbsp;Kristin Ørstavik,&nbsp;Pål Marius Bjørnstad,&nbsp;Arvind Y. M. Sundaram,&nbsp;Areej Ibrahim Elkamil,&nbsp;Q. Ying Esbensen,&nbsp;Tordis Bøker,&nbsp;Sverre Henning Brorson,&nbsp;Eystein Hellstrøm Hoddevik,&nbsp;Hilde Loge Nilsen,&nbsp;Eirik Frengen,&nbsp;Petter Strømme","doi":"10.1007/s00401-026-03088-1","DOIUrl":"10.1007/s00401-026-03088-1","url":null,"abstract":"","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149089076","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"SOD1 co-pathologies in the brain: insights from neuropathological evidence and implications","authors":"Evellyn Mayla de Azevedo,&nbsp;Victoria Simões Bernardo,&nbsp;Marcelo M. S. Lima,&nbsp;Elis Cristina Araujo Eleutherio,&nbsp;Tiago Fleming Outeiro","doi":"10.1007/s00401-026-03090-7","DOIUrl":"10.1007/s00401-026-03090-7","url":null,"abstract":"<div><p>Superoxide dismutase 1 (SOD1), originally regarded as an antioxidant enzyme, is now recognized as a multifunctional protein whose conformational instability and aggregation contribute to neurodegeneration. The emerging evidence suggests that SOD1 pathology extends beyond amyotrophic lateral sclerosis, supporting a role in multiple neurodegenerative diseases. This review summarizes current neuropathological evidence of SOD1 co-pathologies in the human brain, with particular emphasis on its associations with TAR DNA-binding protein 43 (TDP-43), tau, alpha-synuclein, amyloid-β, and other aggregation-prone proteins. We examine the distribution of pathological SOD1 species across neurodegenerative diseases, their coexistence in affected brain regions, and potential mechanisms underlying these interactions, including oxidative stress, impaired proteostasis, aberrant phase separation, and cross-seeding. We also discuss emerging observations of SOD1 pathology in neurological conditions beyond classical neurodegenerative diseases, raising the possibility that SOD1 misfolding represents a broader cellular response to neuronal injury. Collectively, the available evidence supports a shift from viewing SOD1 as a disease-specific protein to considering it a potential participant in interconnected proteopathic networks. Although the functional significance of SOD1 co-pathologies remains incompletely understood, elucidating the molecular basis of aggregation may provide new insights into disease onset and progression, improving our understanding of neurodegenerative mechanisms, and facilitating the development of biomarkers and the identification of therapeutic targets across diverse proteinopathies.</p></div>","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00401-026-03090-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149089004","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":"Functional proteomic and phosphoproteomic profiling of routine FFPE CNS tumor tissue complements genomic and epigenomic characterization","authors":"Dennis Friedel,&nbsp;Rhaissa Ribeiro da Silva,&nbsp;Ivan Abdulrazak Ahmed,&nbsp;Beatriz Martins Wolff,&nbsp;Anna Neuerburg,&nbsp;Ramona Irsevic,&nbsp;Shiva Ahmadi,&nbsp;Ashok Kumar Jayavelu,&nbsp;Andreas E. Kulozik,&nbsp;Olaf Witt,&nbsp;Stefan M. Pfister,&nbsp;Sandro M. Krieg,&nbsp;Wolfgang Wick,&nbsp;Andreas von Deimling,&nbsp;David E. Reuss,&nbsp;Felix Sahm,&nbsp;Philipp Sievers","doi":"10.1007/s00401-026-03091-6","DOIUrl":"10.1007/s00401-026-03091-6","url":null,"abstract":"<div><p>Genomic and DNA methylation-based analyses have transformed the classification of central nervous system (CNS) tumors by enabling robust molecular diagnosis and subclassification. However, these approaches primarily define tumor identity and do not directly capture the functional state of intracellular signaling networks. Proteomic and phosphoproteomic profiling provide complementary molecular layers by measuring protein abundance and site-specific phosphorylation. Recent methodological advances have made a comprehensive analysis of formalin-fixed, paraffin-embedded (FFPE) tissue increasingly feasible, raising the question of how functional proteomic information can complement established molecular diagnostics. Here, we applied an FFPE-compatible workflow for proteomic and phosphoproteomic profiling of ten comprehensively characterized glioblastomas, including five <i>EGFR</i>-amplified and five non-amplified tumors. Mass spectrometry generated robust proteomic and phosphoproteomic coverage across all cases. Global proteomic profiling revealed group-associated protein abundance and pathway differences, including increased EGFR abundance in <i>EGFR</i>-amplified tumors, while showing substantial intertumoral overlap. Protein-abundance-adjusted phosphoproteomic profiles similarly showed partial group-level separation with substantial intertumoral overlap. Differential analysis of protein-abundance-adjusted phosphoproteomic data identified 443 phosphosites based on predefined exploratory statistical criteria. Kinase-substrate enrichment further revealed coordinated EGFR- and SRC-family-associated signaling with marked variability across individual tumors. These findings demonstrate that routine FFPE tissue retains biologically coherent functional information at both the protein abundance and phosphosignaling levels that can be interpreted alongside genomic and epigenomic data. Phosphoproteomics therefore represents an orthogonal functional layer that may complement established molecular characterization of CNS tumors.</p></div>","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00401-026-03091-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149035417","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":"Deletion or immunotherapeutic blockade of FcγRIIb (CD32b) impairs α-Syn propagation in vivo","authors":"James M. Hennegan,&nbsp;Michael J. Hurley,&nbsp;Matthew Colley,&nbsp;Kerry L. Cox,&nbsp;Leon R. Douglas,&nbsp;Patrick J. Duriez,&nbsp;Robert J. Oldham,&nbsp;Mark S. Cragg,&nbsp;Björn Frendéus,&nbsp;Ali Roghanian,&nbsp;Jessica L. Teeling","doi":"10.1007/s00401-026-03082-7","DOIUrl":"10.1007/s00401-026-03082-7","url":null,"abstract":"<div><p>Parkinson’s disease (PD), the most prevalent neurodegenerative movement disorder, is characterised by widespread alpha-synuclein (α-Syn) pathology in the brain and the progressive degeneration of nigrostriatal dopaminergic neurons. Experimental and clinicopathological data support a templated, prion-like component to α-Syn spread; however, the cellular mechanisms governing fibril uptake and intercellular transmission remain incompletely defined. Fc gamma receptor IIb (FcγRIIb or CD32b), the sole cross-species inhibitory Fcγ receptor, has been implicated in α-Syn internalisation in vitro, though its contribution to α-Syn propagation in vivo is not well established. Here, we examine the role of FcγRIIb in α-Syn seeding, propagation, and neurotoxicity in vivo using the preformed fibril (PFF) α-Syn intracranial injection model in mice. Genetic ablation of murine FcγRII reduced phosphorylated α-Syn (pα-Syn) burden and anatomical distribution across multiple brain regions at 90 days post-PFF injection, consistent with impaired development of Lewy-like pathology. Attenuated pα-Syn pathology was accompanied by reduced microglial reactivity, preservation of nigrostriatal dopaminergic integrity, and protection from PFF-associated motor and exploratory deficits. In parallel, pharmacological blockade of human (h) FcγRIIb using monoclonal antibodies reduced acute-phase pα-Syn accumulation in hFcγRIIb-transgenic mice following PFF challenge. Collectively, these findings identify FcγRIIb as a critical regulator of α-Syn propagation in vivo and support receptor-targeted blockade as a mechanistically distinct and therapeutically tractable strategy for modifying disease progression in PD and related α-synucleinopathies.</p></div>","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00401-026-03082-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149035416","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":"Integrative synaptosome multi-omics reveals disrupted synapse organization and localized cryptic transcripts in C9ORF72-frontotemporal dementia","authors":"Ashton M. Spillman,&nbsp;Eric B. Alsop,&nbsp;Lauren M. Gittings,&nbsp;Krystine Garcia-Mansfield,&nbsp;Ignazio Piras,&nbsp;Anna Bonfitto,&nbsp;Melissa N. Martinez,&nbsp;Ritin Sharma,&nbsp;Kim R. Preller,&nbsp;Matthew Huentelman,&nbsp;Patrick Pirrotte,&nbsp;Kendall Van Keuren-Jensen,&nbsp;Rita Sattler","doi":"10.1007/s00401-026-03084-5","DOIUrl":"10.1007/s00401-026-03084-5","url":null,"abstract":"<div><p>Frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) are linked neurodegenerative diseases characterized by both synaptic dysfunction and TDP-43 pathology. A hexanucleotide repeat expansion (HRE) in the <i>C9ORF72</i> (C9) gene represents the most common genetic cause of FTD and ALS, yet the synapse-specific mechanisms underlying disease pathogenesis remain poorly understood. Here, we performed integrated multi-omic profiling of synaptosomes enriched from postmortem frontal cortex and patient-derived induced pluripotent stem cell (iPSC)-cortical neurons to define molecular alterations associated with C9-FTD-mediated synaptic dysfunction. Proteomic profiling of frontal cortex-derived synaptosomes identified 1,324 differentially abundant proteins (p&lt;0.05) enriched in pathways regulating synaptic vesicle transport and synapse organization, while synaptosomal RNA sequencing revealed 2,835 differentially expressed protein-coding genes. C9-FTD iPSC-cortical neurons exhibited reductions in excitatory and inhibitory postsynaptic markers, accompanied by progressive impairment of neuronal network activity, supporting both structural and functional deficits. iPSC-derived synaptosomes recapitulated key molecular pathways observed in patient brain, revealing convergent dysregulation of synaptic signaling pathways. Comparative analyses revealed divergence between protein and RNA alterations, consistent with the disruption of regulatory processes that link RNA and protein abundance in diseased synapses. Consistent with TDP-43 loss-of-function pathology we identified cryptic exon (CE)-containing transcripts within C9-FTD frontal cortex-derived synaptosomes, including <i>KALRN</i> and <i>STMN2,</i> providing evidence that aberrantly spliced RNAs localize to synaptic compartments. Together, these findings define convergent molecular pathways underlying synapse vulnerability in both C9-FTD model systems and identify synaptic localization of CE-containing transcripts as a previously unrecognized feature of TDP-43 proteinopathy.</p></div>","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00401-026-03084-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149035414","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":"Integrated multi-omics identifies lineage-dependent myeloid cells recruitment and the APP-CD74 axis as an immunoregulatory target in pediatric high-grade glioma","authors":"Zhuang Wang,&nbsp;Ambuj Kumar,&nbsp;Banlanjo Umaru,&nbsp;Archana Mahadevan Iyer,&nbsp;Komal Khan,&nbsp;Hao-Han Pang,&nbsp;Maryam Fouladi,&nbsp;Rachid Drissi","doi":"10.1007/s00401-026-03089-0","DOIUrl":"10.1007/s00401-026-03089-0","url":null,"abstract":"<div><p>Diffuse intrinsic pontine glioma (DIPG) is a devastating pediatric brain tumor with limited treatment options. Emerging evidence indicates infiltration of tumor-associated macrophages (TAMs) within tumor sites, accompanied by an immunosuppressive tumor microenvironment (TME). However, the mechanisms underlying macrophage recruitment and communication between TAMs and other cellular compartments within brain tumors remain poorly understood. Bulk RNA sequencing of 26 DIPG autopsy specimens with matched normal brain tissue, single-cell RNA sequencing data from eight DIPG patients integrated with public pediatric high-grade glioma (pHGG) datasets, and in vitro transwell and flow cytometry assays collectively indicated that DIPG tumors actively recruit monocytes through chemokine-mediated mechanisms. The chemokine expression of tumor cells is driven by a mesenchymal-like (MES-like) lineage state rather than histone mutations, as evidenced by significant correlation between MES-like lineage scores and chemokine expression scores across 46 pHGG cell lines. CellChat analysis predicted APP-CD74 signaling as a prominent tumor cell-TAM interaction pathway, supported by immunofluorescence validation. Notably, <i>APP</i> expression was significantly reduced in DIPG tumor tissues compared with normal brain tissue at both the RNA and protein levels. Recombinant APP stimulation of THP-1-derived macrophages induced a robust proinflammatory response, including upregulation of M1-like markers, enrichment of interferon-related pathways, and elevated secretion of inflammatory cytokines. Collectively, these findings suggest that reduced <i>APP</i> expression in tumor may contribute to a non-inflammatory TAM phenotype and an immunosuppressive microenvironment. Furthermore, protein modeling and docking analyses identified the APP-CD74 binding interface, providing a structural basis for therapeutic targeting.</p></div>","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00401-026-03089-0.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149020369","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":"Life at the interface: Byron Caughey’s search for prion disease inhibitors through chemistry, structure, and cell physiology","authors":"James A. Carroll,&nbsp;Jakub Soukup,&nbsp;Bradley R. Groveman,&nbsp;Christina D. Orrú,&nbsp;Brent Race,&nbsp;Cathryn L. Haigh","doi":"10.1007/s00401-026-03080-9","DOIUrl":"10.1007/s00401-026-03080-9","url":null,"abstract":"<div><p>The search for effective therapeutics that can bring hope to patients and families affected by rare prion diseases is ongoing. Self-propagating, misfolded proteins underlie a broad range of neurodegenerative disorders that include prion diseases as well as more common conditions such as Parkinson’s and Alzheimer’s disease. Byron Caughey was a pioneer in the field of prion therapeutic discovery. His seminal contributions in drug development included elucidating disease biochemistry, understanding the need to target conformational changes, and developing cell-free conversion assays to monitor protein misfolding in real time. These advances laid the foundation for therapeutic strategies aimed at preventing, slowing or reversing the conversion of native protein into a pathogenic, seed-competent conformer and/or its assembly into amyloid fibrils. Within the Caughey laboratory, small molecule inhibitors targeting the misfolded prion, the process of conversion and aggregation, or stimulating disassembly were studied intensively. More recent approaches targeted the relocation, removal or downregulation of the normal protein substrate. These efforts in combination with high-resolution structural characterization of the infectious prions now offer new opportunities for intelligent drug design. Equally important to drug discovery have been advances in the development of sensitive and reliable methods to detect the agent and its clearance, which is necessary to validate that putative treatments are efficacious. Herein, we highlight 4 decades of Byron Caughey’s contributions and dedication to the search for anti-prion therapeutics.</p></div>","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148987091","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Colonic LRRK2 expression is increased in Crohn’s disease but not in Parkinson’s disease and idiopathic RBD","authors":"Johannes van der Haas,&nbsp;Marine Mantel,&nbsp;Loïc Sellier-Montaigne,&nbsp;Adrien de Guilhem de Lataillade,&nbsp;Tony Durand,&nbsp;Thibauld Oullier,&nbsp;Catherine Le Berre,&nbsp;Franck Letournel,&nbsp;Malvyne Rolli-Derkinderen,&nbsp;Laurène Leclair-Visonneau,&nbsp;Pascal Derkinderen","doi":"10.1007/s00401-026-03087-2","DOIUrl":"10.1007/s00401-026-03087-2","url":null,"abstract":"","PeriodicalId":7012,"journal":{"name":"Acta Neuropathologica","volume":"152 1","pages":""},"PeriodicalIF":10.3,"publicationDate":"2026-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148987092","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}