FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation
Chen, Dailu, Wosztyl, Aleksandra, Mullapudi, Vishruth, Bali, Sofia, Vacquer-Alicea, Jaime, Melhem, Shamiram, Seelaar, Harro, John Van Swieten, Diamond, Marc I, Joachimiak, Lukasz A
Published in bioRxiv (13.08.2022)
Published in bioRxiv (13.08.2022)
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Tau seeding without tauopathy
Lacroix, Michael S, Hitt, Brian D, Beaver, Joshua D, Terpack, Sandi Jo, Gleason, Kelly, Tamminga, Carol A, Evers, Bret M, White, Charles L, Diamond, Marc I
Published in bioRxiv (06.02.2022)
Published in bioRxiv (06.02.2022)
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Site-specific hyperphosphorylation of tau inhibits its fibrillization in vitro, blocks its seeding capacity in cells, and disrupts its microtubule binding; Implications for the native state stabilization of tau
Lashuel, Hilal A, Haj-Yahya, Mahmood, Gopinath Pushparathinam, Kolla Rajasekhar, Mirbaha, Hilda, Diamond, Marc I
Published in bioRxiv (18.09.2019)
Published in bioRxiv (18.09.2019)
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The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds
Saha, Itika, Yuste-Checa, Patricia, Miguel Da Silva Padilha, Guo, Qiang, Körner, Roman, Holthusen, Hauke, Trinkaus, Victoria A, Dudanova, Irina, Fernández-Busnadiego, Rubén, Baumeister, Wolfgang, Sanders, David W, Gautam, Saurabh, Diamond, Marc I, Franz-Ulrich Hartl, Hipp, Mark S
Published in bioRxiv (19.02.2022)
Published in bioRxiv (19.02.2022)
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Tau monomer encodes strains
Sharma, Apurwa M, Thomas, Talitha L, Woodard, Danae R, Kashmer, Omar M, Diamond, Marc I
Published in bioRxiv (17.05.2018)
Published in bioRxiv (17.05.2018)
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Inert and seed-competent tau monomers suggest structural origins of aggregation
Mirbaha, Hilda, Chen, Dailu, Morozova, Olga A, Ruff, Kiersten M, Sharma, Apurwa, Liu, Xiaohua, Pappu, Rohit V, Colby, David W, Mirzaei, Hamid, Joachimiak, Lukasz A, Diamond, Marc I
Published in bioRxiv (15.03.2018)
Published in bioRxiv (15.03.2018)
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