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However, most of the specific phosphorylation sites remain to be determined, and their relevance regarding pathogenicity and clinical and pathological phenotypic diversity in FTLD\u2013TDP and ALS\u2013TDP remains to be identified. Here, we generated a novel antibody raised against TDP-43 phosphorylated at serine 375 (pTDP-43\n                    <jats:sup>S375<\/jats:sup>\n                    ) located in the low-complexity domain, and used it to investigate the presence of S375 phosphorylation in a series (\n                    <jats:italic>n<\/jats:italic>\n                    \u2009=\u200944) of FTLD\u2013TDP and ALS\u2013TDP cases. Immunoblot analysis demonstrated phosphorylation of S375 to be a consistent feature of pathological TDP-43 species, including full-length and C-terminal fragments, in all FTLD\u2013TDP subtypes examined (A\u2013C) and in ALS\u2013TDP. Of particular interest, however, detailed immunohistochemical analysis showed striking differences in the immunoreactivity profile of inclusions with the pTDP-43\n                    <jats:sup>S375<\/jats:sup>\n                    antiserum among pathological subtypes. TDP-43 pathology of ALS\u2013TDP, FTLD\u2013TDP type B (including cases with the\n                    <jats:italic>C9orf72<\/jats:italic>\n                    mutation), and FTLD\u2013TDP type C all showed strong pTDP-43\n                    <jats:sup>S375<\/jats:sup>\n                    immunoreactivity that was similar in amount and morphology to that seen with an antibody against TDP-43 phosphorylated at S409\/410 used as the gold standard. In stark contrast, TDP-43 pathology in sporadic and genetic forms of FTLD\u2013TDP type A (including cases with\n                    <jats:italic>GRN<\/jats:italic>\n                    and\n                    <jats:italic>C9orf72<\/jats:italic>\n                    mutations) was found to be almost completely negative by pTDP-43\n                    <jats:sup>S375<\/jats:sup>\n                    immunohistochemistry. These data suggest a subtype-specific, conformation-dependent binding of pTDP-43\n                    <jats:sup>S375<\/jats:sup>\n                    antiserum to TDP-43 aggregates, consistent with the idea of distinct structural TDP-43 conformers (i.e., TDP-43 strains) as the molecular basis for the phenotypic diversity in TDP-43 proteinopathies.\n                  <\/jats:p>","DOI":"10.1007\/s00401-020-02207-w","type":"journal-article","created":{"date-parts":[[2020,8,10]],"date-time":"2020-08-10T17:02:54Z","timestamp":1597078974000},"page":"645-658","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":38,"title":["Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD\u2013TDP subtypes"],"prefix":"10.1007","volume":"140","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6232-4057","authenticated-orcid":false,"given":"Manuela","family":"Neumann","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Petra","family":"Frick","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesca","family":"Paron","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonas","family":"Kosten","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emanuele","family":"Buratti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian R.","family":"Mackenzie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2020,8,10]]},"reference":[{"key":"2207_CR1","doi-asserted-by":"publisher","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","volume":"351","author":"T Arai","year":"2006","unstructured":"Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H et al. 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