{"doi":"10.1007/s00401-013-1080-2","title":"Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation","abstract":null,"journal":"Acta Neuropathologica","year":2013,"id":611798,"datarank":0.7037021823343717,"base_score":4.6913478822291435,"endowment":4.6913478822291435,"self_citation_contribution":0.7037021823343717,"citation_network_contribution":0.0,"self_endowment_contribution":0.7037021823343717,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":108,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":2,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":672778,"name":"Xuehua Wang","orcid":"0000-0002-5317-6822","position":1,"is_corresponding":false},{"id":364191,"name":"Chao Wang","orcid":"0000-0002-8054-3472","position":2,"is_corresponding":false},{"id":1574851,"name":"Peter Dongmin Sohn","orcid":null,"position":3,"is_corresponding":false},{"id":813572,"name":"Panos Theofilas","orcid":"0000-0001-9701-1352","position":4,"is_corresponding":false},{"id":1574852,"name":"Manu Sidhu","orcid":null,"position":5,"is_corresponding":false},{"id":1574853,"name":"John Benjamin Arevalo","orcid":null,"position":6,"is_corresponding":false},{"id":572161,"name":"Helmut Heinsen","orcid":"0000-0002-4688-4441","position":7,"is_corresponding":false},{"id":226820,"name":"Eric J. 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Because hyperphosphorylation alone does not necessarily cause tau aggregation, other post-translational modifications have been recently explored. Tau acetylation promotes aggregation and inhibits tau's ability to stabilize microtubules. Recent studies have shown co-localization of acetylated and phosphorylated tau in AD and some 4R tauopathies. We developed a novel monoclonal antibody against acetylated tau at lysine residue 274, which recognizes both 3R and 4R tau, and used immunohistochemistry and immunofluorescence to probe 22 cases, including AD and another eight familial or sporadic tauopathies. Acetylated tau was identified in all tauopathies except argyrophilic grain disease (AGD). AGD is an age-associated, common but atypical 4R tauopathy, not always associated with clinical progression. Pathologically, AGD is characterized by neuropil grains, pre-neurofibrillary tangles, and oligodendroglial coiled bodies, all recognized by phospho-tau antibodies. The lack of acetylated tau in these inclusions suggests that AGD represents a distinctive tauopathy. Our data converge with previous findings to raise the hypothesis that AGD could play a protective role against the spread of AD-related tau pathology. Tau acetylation as a key modification for the propagation tau toxicity deserves further investigation.","is_dataset_classified":null,"base_score":4.6913478822291435,"endowment":4.6913478822291435,"datacite_reuse_total":2,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23371364","pmcid":"PMC3692283","openalex_id":"https://openalex.org/W2164226163","authors":[],"funders":[{"funder_name":"NIA NIH HHS","grant_id":"R01AG040311","title":null},{"funder_name":"NIA NIH HHS","grant_id":"R01 AG030207","title":null},{"funder_name":"NIA NIH HHS","grant_id":"R01 AG033017","title":null},{"funder_name":"NIA NIH HHS","grant_id":"R01 AG036884","title":null},{"funder_name":"NIA NIH HHS","grant_id":"P01 AG019724","title":null},{"funder_name":"NIA NIH HHS","grant_id":"P50 AG023501","title":null},{"funder_name":"National Institutes of Health","grant_id":"5R01AG030207-05","title":"The Role of Cathepsin B and Cystatin C in Alzheimer's Disease"},{"funder_name":"National Institutes of Health","grant_id":"5P50AG023501-03","title":"DATA MANAGEMENT AND BIOSTATISTICS"},{"funder_name":"National Institutes of Health","grant_id":"1R01AG040311-01A1","title":"Brainstem as an early site in AD and FTLD: closing the etiopathogenic gap"}],"total_grants":9,"fwci":5.6495,"citation_percentile":0.96880719,"influential_citations":0,"citation_trend":[{"year":2013,"count":7},{"year":2014,"count":8},{"year":2015,"count":6},{"year":2016,"count":13},{"year":2017,"count":13},{"year":2018,"count":8},{"year":2019,"count":11},{"year":2020,"count":7},{"year":2021,"count":6},{"year":2022,"count":10},{"year":2023,"count":4},{"year":2024,"count":6},{"year":2025,"count":7},{"year":2026,"count":2}],"oa_status":"green","license":"Springer TDM","oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3692283","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3692283","host_type":"repository"},{"url":"http://link.springer.com/content/pdf/10.1007/s00401-013-1080-2.pdf","host_type":"publisher"},{"url":"http://link.springer.com/article/10.1007/s00401-013-1080-2/fulltext.html","host_type":"publisher"},{"url":"http://link.springer.com/content/pdf/10.1007/s00401-013-1080-2","host_type":"publisher"},{"url":"https://doi.org/10.1007/s00401-013-1080-2","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23371364","host_type":"repository"},{"url":"https://escholarship.org/uc/item/7570q4r5","host_type":"repository"},{"url":"http://europepmc.org/articles/PMC3692283","host_type":"repository"},{"url":"https://europepmc.org/articles/pmc3692283?pdf=render","host_type":""},{"url":"https://dx.doi.org/10.1007/s00401-013-1080-2","host_type":""},{"url":"https://escholarship.org/content/qt7570q4r5/qt7570q4r5.pdf","host_type":""},{"url":"https://doi.org/https://doi.org/10.1007/s00401-013-1080-2","host_type":""}],"fields_of_study":["Alzheimer's disease research and treatments","Parkinson's Disease Mechanisms and Treatments","Cellular transport and secretion","0301 basic medicine","03 medical and health sciences","0302 clinical medicine"],"mesh_terms":["Acetylation","Aged","Aged, 80 and over","Brain","Diagnosis, Differential","Female","Humans","Immunohistochemistry","Male","Middle Aged","Phosphorylation","Protein Processing, Post-Translational","Neurofibrillary Tangles","tau Proteins","Tauopathies","Plaque, Amyloid"],"keywords":["Tauopathy","Tau protein","Acetylation","Neurodegeneration","Hyperphosphorylation","Pathology","Biology","Neuroscience","Alzheimer's disease","Disease","Cell biology","Biochemistry","Medicine","Phosphorylation","Male","Aging","Amyloid","Clinical Sciences","610","Plaque, Amyloid","tau Proteins","Neurodegenerative","630","Diagnosis, Differential","Diagnosis","Acquired Cognitive Impairment","80 and over","2.1 Biological and endogenous factors","Humans","Alzheimer's Disease Related Dementias (ADRD)","Protein Processing","Plaque","Aged","Aged, 80 and over","Neurology & Neurosurgery","Biomedical and Clinical Sciences","Neurosciences","Post-Translational","Alzheimer's Disease including Alzheimer's Disease Related Dementias (AD/ADRD)","Brain","Neurofibrillary Tangles","Middle Aged","Immunohistochemistry","Brain Disorders","Frontotemporal Dementia (FTD)","Tauopathies","Neurological","Differential","Dementia","Female","Autopsy","Tau","Protein Processing, Post-Translational","Human"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. 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