Neuropathology and Applied Neurobiology最新文献

{"title":"Application of Oral Mucosal Epithelial Cells in Noninvasive Pathological Diagnosis of Neuronal Intranuclear Inclusion Disease.","authors":"Xiaowen Li, Yu Kong, Ying Ji, Xinyi Yuan, Jingwen Yang, Xiaosa Sun, Jin Tian, Maofeng Shi, Yuwen Li, Qingqing Ji, Zichang Yin, Xianhong Jia, Wenjing Song, Hao Chen, Lei Bao","doi":"10.1111/nan.70023","DOIUrl":"10.1111/nan.70023","url":null,"abstract":"<p><p>We employed a novel method for collecting oral mucosal epithelial cells, an anagar-paraffin double-embedding technique for cell fixation in cytopathological processing. OMEC biopsy demonstrated a high diagnostic efficacy for NIID: H&E staining revealed inclusions in 60% (12/20) of patients, TEM confirmed them in 40% (8/20) of cases and immunofluorescence detected p62-positive aggregates in 9/20 (45%) and uN2CpolyG in 8/20 (40%) of cases, respectively. OMEC biopsy is a simple, noninvasive technique for detecting intranuclear inclusions in NIID, avoiding the need for invasive surgical procedures such as skin or labial gland biopsies.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 4","pages":"e70023"},"PeriodicalIF":3.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144529025","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Collablots: Quantification of Collagen VI Levels and Its Structural Disorganisation in Cell Cultures From Patients With Collagen VI-Related Dystrophies.","authors":"Nadia Osegui-Barcenilla, Maria Sendino, Sergio Martín-González, Itziar González-Moro, Ainhoa Benito-Agustino, Noemi Torres-Conde, Andrea López-Martínez, Cecilia Jiménez-Mallebrera, Arístides López-Márquez, Virginia Arechavala-Gomeza","doi":"10.1111/nan.70020","DOIUrl":"10.1111/nan.70020","url":null,"abstract":"<p><strong>Aims: </strong>This study aims to develop a quantitative method for assessing collagen VI expression in cell cultures, which is crucial for the diagnosis and treatment of collagen VI-related dystrophies.</p><p><strong>Methods: </strong>We developed a combined in-cell western (ICW) and on-cell western (OCW) assay, which we have called 'collablot', to quantify collagen VI and its organisation in the extracellular matrix of cell cultures from patients and healthy controls. To optimise it, we optimised cell density and the protocols to induce collagen expression in cultures, as well as the cell fixation and permeabilisation methods. This was completed with a thorough selection of collagen antibodies and a collagen-hybridising peptide (CHP). We then used collablots to compare cultures from patients and controls and evaluate therapeutic interventions in the cultures.</p><p><strong>Results: </strong>Collablots enabled the quantification of collagen VI expression in both control and patient cells, aligning with immunocytochemistry findings and detecting variations in collagen VI expression following treatment of the cultures. Additionally, CHP analysis revealed a marked increase in collagen network disruption in patients compared to the controls.</p><p><strong>Conclusions: </strong>The collablot assay represents a suitable method for quantifying collagen VI expression and its organisation in culture and assessing the effect of therapies.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 3","pages":"e70020"},"PeriodicalIF":3.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12096143/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144120362","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alpha-Synuclein as a Potential Biomarker for Inclusion Body Myositis in Blood and Muscle.","authors":"Tobias Mayer, Leila Scholle, Laura Foerster, Ilka Schneider, Gisela Stoltenburg-Didinger, Karl-Stefan Delank, Thomas Kendzierski, Anna Koelsch, Kathleen Kleeberg, Torsten Kraya, Lorenzo Barba, Steffen Naegel, Anne Schänzer, Markus Otto, Alexander Mensch","doi":"10.1111/nan.70019","DOIUrl":"10.1111/nan.70019","url":null,"abstract":"<p><strong>Aims: </strong>Diagnosis of inclusion body myositis (IBM) is difficult and currently based on a combination of clinical and (immuno)histological findings. Biomarkers facilitating the diagnostic process are needed. Alpha-synuclein (αSN) aggregates are a known histological feature of IBM, but there is a lack of information on their diagnostic relevance. Furthermore, serum αSN concentrations in IBM have not been investigated.</p><p><strong>Methods: </strong>Immunohistochemical staining for αSN was performed on 63 biopsies (19 IBM, 21 other inflammatory myopathies, 20 other myopathies and 3 healthy controls), and αSN reactive fibres were quantified. The serum concentration of αSN was determined by ELISA in 156 serum samples (11 IBM, 25 other inflammatory myopathies, 53 hereditary myopathies, 30 mitochondriopathies and 37 healthy controls).</p><p><strong>Results: </strong>The proportion of fibres with αSN immunoreactivity was significantly higher in IBM compared to all groups (p < 0.001) and discriminated IBM against all other neuromuscular disorders with a sensitivity of 79% and a specificity of 85%, which further improved when only non-regenerating fibres were examined. In serum, αSN concentrations in IBM were generally not different from healthy controls. However, serum concentrations were inversely correlated with disease duration (r = -0.62, p = 0.04) and positively correlated with the IBM functional rating scale (r = 0.74, p = 0.01). Consequently, stratification according to these clinical parameters showed significantly lower serum αSN concentrations in late-stage, more severely affected patients.</p><p><strong>Conclusions: </strong>αSN reactivity may serve as an additional immunohistochemical marker for IBM diagnosis. Furthermore, this study indicates that αSN serum concentrations decrease with disease duration and clinical deterioration. Therefore, serum αSN may be provisionally considered a monitoring biomarker in IBM, pending further studies.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 3","pages":"e70019"},"PeriodicalIF":3.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12086613/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144094427","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multiplex Immunofluorescent Analysis of Alpha-Synuclein in Nigral Lewy Bodies With Heat-Induced Antibody Stripping Reveals an Intricate Multilayered Structure.","authors":"Dominik Hrabos, Satomi Hasegawa, Dorota Konickova","doi":"10.1111/nan.70024","DOIUrl":"10.1111/nan.70024","url":null,"abstract":"<p><p>In the study, we employ an affordable, tissue-saving, and precise simultaneous multiplex immunofluorescence method with heat-induced antibody stripping to identify and structurally analyse nigral Lewy bodies in dopaminergic neurones. Analysis of different alpha-synuclein epitopes and proteoforms reveals an almost uniform, onion-like morphology of the Lewy bodies. The N-terminal and C-terminal domains are predominantly accessible to antibody binding in the peripheral shell of the bodies.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 3","pages":"e70024"},"PeriodicalIF":3.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12122903/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144180901","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"MYL1-Related Congenital Myopathy: Clinical, Genetic and Pathological Insights.","authors":"Irene Madrigal, Cristina Villar-Vera, Gemma Arca, Jesica Expósito-Escudero, Laia Rodríguez-Revenga, Andres Piolatti-Luna, Nuria Muelas, Roger Vilchez, Maria Ciutad Celdran, Anna Codina, Berta Estévez-Arias, Laura Carrera-Garcia, Carlos Ortez, Leonardo Rodriguez-Carunchio, Giorgia Sebastiani, Inmaculada Azorin, Andrés Nascimento, Cristina Jou, Juan Jesus Vilchez, Daniel Natera-de Benito","doi":"10.1111/nan.70025","DOIUrl":"10.1111/nan.70025","url":null,"abstract":"<p><p>Congenital myopathies and congenital muscular dystrophies encompass heterogeneous clinical and genetic groups of disorders characterised by muscle weakness with antenatal or early postnatal onset. These conditions are categorised according to distinctive myopathological features and causative genes. Despite advances in diagnosis through massive parallel sequencing and progress in understanding the underlying pathogenesis, many aspects of these disorders remain poorly understood. MYL1-related congenital myopathy is an ultra-rare and severe condition, associated with a deficiency of essential/alkali light myosin and impaired development of fast-twitch type II muscle fibres. This study aims to advance the understanding of the phenotype and pathogenesis of MYL1-congenital myopathy. We analysed the clinical characteristics of two individuals harbouring three novel variants in the MYL1 gene. We conducted detailed genomic analysis and extensive studies on their muscles using histological, immunohistochemical, immunofluorescence, Western Blot and electron microscopy. Both individuals showed a very severe congenital myopathy, characterised by congenital hypotonia and weakness, requiring ventilatory and nutritional assistance. Muscle biopsy revealed dystrophic-like or myopathic changes, with notable smallness of fast-twitch type II fibres, often arranged around larger type I fibres, drawing a floret pattern. These fibres expressed developmental myosin and exhibited features of aberrant myofibrillogenesis. Type I myofibres exhibited correct sarcomere alignment, but like the small fast-twitch fibres, both showed distorted cell organelles, vacuolar aggregates and membranous debris, indicating autophagic impairment. Our findings confirm that bi-allelic MYL1 variants are associated with a severe congenital myopathy, characterised by a distinctive clinical and histopathological phenotype involving impaired type II fibre development. Additionally, our study reveals a role for MYL1 in the organisation and trophism of all muscle fibre types. SUMMARY: MYL1 biallelic variants cause severe congenital myopathy with early hypotonia and type II fibre hypotrophy. Muscle biopsy shows a distinct pattern, including floret-like fibre arrangement. Findings suggest a broader role for MYL1 in fibre organisation and autophagy across muscle fibre types.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 3","pages":"e70025"},"PeriodicalIF":3.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12147433/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144248829","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lecanemab Binds to Transgenic Mouse Model-Derived Amyloid-β Fibril Structures Resembling Alzheimer's Disease Type I, Type II and Arctic Folds.","authors":"Fernanda S Peralta Reyes, Simon Sommerhage, Dieter Willbold, Gunnar F Schröder, Lothar Gremer","doi":"10.1111/nan.70022","DOIUrl":"10.1111/nan.70022","url":null,"abstract":"<p><strong>Aims: </strong>Lecanemab, an Alzheimer's disease US Food and Drug Administration-approved monoclonal antibody, was previously reported to have a high affinity against intermediately sized amyloid-β aggregates. Subsequently, it was observed by immunogold labelling that lecanemab can also bind to human type I amyloid-β fibrils. To determine whether lecanemab binds to amyloid-β fibril structures other than type I, we analysed its binding capacity to various structurally defined and pathologically relevant amyloid-β fibrils.</p><p><strong>Methods: </strong>We performed immunogold labelling with lecanemab on extracted amyloid-β fibril preparations from six different Alzheimer´s disease mouse models whose structures were previously solved by cryo-EM and quantified the relative binding affinities of lecanemab to the different fibril polymorphs.</p><p><strong>Results: </strong>Our results show that lecanemab exhibits high binding affinity to amyloid-β fibril structures that have a flexible N-terminus in common, as is the case for type I, type II and murine type III amyloid-β fibril polymorphs, which resemble or are identical to human structures observed in sporadic and familial cases of Alzheimer's disease, including a case with the Arctic (E22G) mutation. In contrast, only weak lecanemab binding was observed for murine amyloid-β fibrils with a fixed and ordered N-terminus.</p><p><strong>Conclusions: </strong>These findings may also explain the low incidence of ARIA-E with lecanemab in clinical trials. This is because human meningeal amyloid-β fibrils derived from cerebral amyloid angiopathy affected brain tissue also contain a fixed and ordered N-terminus, most likely preventing lecanemab binding.</p><p><strong>Summary: </strong>Lecanemab binds to Aβ fibrils from several Alzheimer's disease tg-mice whose structures resemble the type I, type II and Arctic folds found in Alzheimer's patients, all of which share a flexible, unstructured N-terminus. Lecanemab is therefore expected to be active against all common familial and sporadic Alzheimer's cases containing these folds. Lecanemab binding ability is unaffected by and tolerates the Arctic E22G mutation, at least in type I or Arctic folds. Only weak, if any, lecanemab binding was observed to Aβ fibrils derived from tg-SwDI mice, whose structures DI1, DI2 and DI3 all share structured and fixed N-termini. Since the fixed N-termini of tg-SwDI DI1 fibrils and human meningeal Aβ40 fibrils derived from CAA-affected brain are identical, most likely preventing lecanemab binding, treatment with lecanemab may be less effective or ineffective against CAA, but may explain the reported beneficial low ARIA-E frequency with this antibody.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 3","pages":"e70022"},"PeriodicalIF":3.4,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12152531/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144266878","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Computational Analysis of SOD1-G93A Mouse Muscle Biomarkers for Comprehensive Assessment of ALS Progression.","authors":"Pedro Gómez-Gálvez, Victoria Navarro, Ana M Castro, Carmen Paradas, Luis M Escudero","doi":"10.1111/nan.70014","DOIUrl":"10.1111/nan.70014","url":null,"abstract":"<p><strong>Aims: </strong>To identify potential image biomarkers of neuromuscular disease by analysing morphological and network-derived features in skeletal muscle biopsies from a murine model of amyotrophic lateral sclerosis (ALS), the SOD1^G93A mouse and wild-type (WT) controls at distinct stages of disease progression.</p><p><strong>Methods: </strong>Using the NDICIA computational framework, we quantitatively evaluated histological differences between skeletal muscle biopsies from SOD1^G93A and WT mice. The process involved the selection of a subset of features revealing these differences. A subset of discriminative features was selected to characterise these differences, and their temporal dynamics were assessed across disease stages.</p><p><strong>Results: </strong>Our findings demonstrate that muscle pathology in the mutant model evolves from early alterations in muscle fibre arrangement, detectable at the presymptomatic stage through graph theory features, to the subsequent development of the typical morphological pattern of neurogenic atrophy at more advanced disease stages.</p><p><strong>Conclusions: </strong>Our assay identifies a neurogenic signature in mutant muscle biopsies, even when the disease is phenotypically imperceptible.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 2","pages":"e70014"},"PeriodicalIF":3.4,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143753640","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identical Seeding Characteristics and Cryo-EM Filament Structures in FTLD-Synuclein and Typical Multiple System Atrophy.","authors":"Patrick W Cullinane, Yang Yang, Viorica Chelban, Yee Yen Goh, Kirsten Ebanks, Toby Curless, Sarah Wrigley, Eduardo de Pablo-Fernández, Janice Holton, Sew Peak-Chew, Catarina Franco, Amanda L Woerman, Henry Houlden, Thomas T Warner, Sjors H W Scheres, Michel Goedert, Zane Jaunmuktane","doi":"10.1111/nan.70013","DOIUrl":"10.1111/nan.70013","url":null,"abstract":"<p><strong>Aims: </strong>The aim of this study is to identify the prevalence of frontotemporal dementia (FTD)/corticobasal syndrome (CBS) in a large cohort of pathologically confirmed cases of multiple system atrophy (MSA) and to determine the α-synuclein seeding characteristics and electron cryo-microscopy (cryo-EM) filament structure in frontotemporal lobar degeneration with MSA-type α-synuclein pathology (FTLD-synuclein).</p><p><strong>Methods: </strong>The archives of the Queen Square Brain Bank (1989-2023) were searched for histologically confirmed MSA cases, and those with a clinical diagnosis of FTD/CBS were reviewed for pathological features of FTLD-synuclein. Phosphotungstic acid (PTA)-precipitated brain homogenates from FTLD-synuclein, dementia with Lewy bodies (DLB) and G51D SNCA synucleinopathy cases were used to seed aggregation in α-syn140*A53T-YFP HEK293T cells. The structure of α-synuclein filaments from an FTLD-synuclein case was determined by cryo-EM.</p><p><strong>Results: </strong>We identified 283 cases of MSA. Four cases had a clinical diagnosis of CBS, one of which met pathological criteria for FTLD-synuclein. Genetic studies in this case were negative for SNCA variants, and PTA-precipitated brain homogenates seeded abundant cytoplasmic α-synuclein inclusions that were morphologically indistinguishable from those of typical MSA but distinct from those of G51D SNCA and DLB. MSA Type II α-synuclein filaments were identified by cryo-EM.</p><p><strong>Conclusions: </strong>FTD/CBS is rarely associated with MSA pathology. The cell seeding characteristics and cryo-EM findings support the classification of FTLD-synuclein as a subtype of MSA, differentiating it from genetic synucleinopathies, such as those with SNCA variants G51D and A53E, which have neuropathological features overlapping with MSA and Lewy body diseases. These cases expand the clinicopathological spectrum of MSA and FTLD and have implications for our understanding of selective neuronal vulnerability in MSA and the interpretation of α-synuclein biomarker studies.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 2","pages":"e70013"},"PeriodicalIF":3.4,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11937994/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143710730","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enhancing Lateral Resolution Using Two-Colour Direct Stochastic Optical Reconstruction Microscopy to Unravel Synaptic Tau Pathology in Alzheimer's Disease.","authors":"Érika Sánchez-Aced, Borja Moya-Llamas, Joaquim Aumatell Escabias, Soraya Torres, Martí Colom-Cadena, Jordi Pegueroles, Cristian de Quintana-Schmidt, Àlex Bayés, Laura Molina-Porcel, Iban Aldecoa, Olivia Belbin, Juan Fortea, Tara Spires-Jones, Sílvia Pujals, Sònia Sirisi, Alberto Lleó","doi":"10.1111/nan.70010","DOIUrl":"10.1111/nan.70010","url":null,"abstract":"<p><strong>Aims: </strong>In Alzheimer's disease (AD), the pathological accumulation of tau in synapses contributes to synapse dysfunction and loss. However, the small and complex structure of synapses limits the investigation when using conventional techniques. In this work, we describe the combination of array tomography (AT) with two-colour direct stochastic optical reconstruction microscopy (dSTORM) to enhance lateral resolution for resolving synaptic terminals in human postmortem brain.</p><p><strong>Methods: </strong>We applied this combination to study synapses in brain samples (from biopsy and postmortem) from healthy subjects and pathological synaptic tau (aggregates and oligomers) in samples from AD patients.</p><p><strong>Results: </strong>AT combined with dSTORM allowed the characterisation of the orientation and shape of the synaptic terminals and the synaptic cleft. In addition, this combination confirmed the presence of oligomeric tau in synaptic terminals in AD.</p><p><strong>Conclusions: </strong>Overall, we found that the combination of AT and two-colour dSTORM provides optimal resolution to detect pathological synaptic tau and its spatial relationship with presynaptic and postsynaptic terminals.</p>","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 2","pages":"e70010"},"PeriodicalIF":3.4,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143537473","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PLAG-Family Amplified CNS Embryonal Tumour With PLAG1 Immunohistochemical Expression: Expanding the Spectrum of Diagnostic Tools.","authors":"Antonio d'Amati, Flavia Adotti, Francesca Gianno, Domenico Cicala, Eugenio Covelli, Giuseppe Cinalli, Vittoria D'Onofrio, Maria Elena Errico, Lucia Quaglietta, Sabina Barresi, Sabrina Rossi, Evelina Miele, Manila Antonelli","doi":"10.1111/nan.70017","DOIUrl":"https://doi.org/10.1111/nan.70017","url":null,"abstract":"","PeriodicalId":19151,"journal":{"name":"Neuropathology and Applied Neurobiology","volume":"51 2","pages":"e70017"},"PeriodicalIF":4.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11984066/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144014052","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}