ArticleThe Journal of biological chemistry2020
Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease.
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Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Tau Disaggregation by a CNS-Permeable Small Molecule Reduces Fibril and Oligomer Burden and Preserves Proteostasis and Behavior.bioRxiv : the preprint server for biology · 2026Article
- Article
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- Emerging Role of Bispecific Antibodies in Precision Medicine, Cancer and Modern Therapeutics.Current oncology reports · 2026Review
- Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer's Disease, Parkinson's Disease and Prionopathies.International journal of molecular sciences · 2024Review
- High-molecular-weight oligomer tau (HMWoTau) species are dramatically increased in Braak-stage dependent manner in the frontal lobe of human brains, demonstrated by a novel oligomer Tau ELISA with a mouse monoclonal antibody (APNmAb005).FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- Generation of nanobodies with conformational specificity for tau oligomers that recognize tau aggregates from human Alzheimer's disease samples.Biomaterials science · 2024Article
- Tau-targeting therapies for Alzheimer disease: current status and future directions.Nature reviews. Neurology · 2023Review
- Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Disrupting pathologic phase transitions in neurodegeneration.The Journal of clinical investigation · 2023Review
- Levosimendan inhibits disulfide tau oligomerization and ameliorates tau pathology in TauExperimental & molecular medicine · 2023Article
- String/Cdc25 phosphatase is a suppressor of Tau-associated neurodegeneration.Disease models & mechanisms · 2023Article
- Targeting tau only extracellularly is likely to be less efficacious than targeting it both intra- and extracellularly.Seminars in cell & developmental biology · 2022Review
- Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Biophysical properties of a tau seed.Scientific reports · 2021Article
- Severe oligomeric tau toxicity can be reversed without long-term sequelae.Brain : a journal of neurology · 2021Article
- Fatal Attraction: The Case of Toxic Soluble Dimers of Truncated PQBP-1 Mutants in X-Linked Intellectual Disability.International journal of molecular sciences · 2021Review
- Observational
- Development of a pan-tau multivalent nanobody that binds tau aggregation motifs and recognizes pathological tau aggregates.Biotechnology progressArticle
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Authors and funding
16 authors at 5 institutions in 1 country.
Romany AbskharonDepartments of Chemistry and Biochemistry and Biological Chemistry, UCLA-DOE Institute UCLA, Los Angeles, California, USA.ORCID 0000-0003-1350-0189
Paul M SeidlerDepartments of Chemistry and Biochemistry and Biological Chemistry, UCLA-DOE Institute UCLA, Los Angeles, California, USA.ORCID 0000-0001-8530-7244
Michael R SawayaDepartments of Chemistry and Biochemistry and Biological Chemistry, UCLA-DOE Institute UCLA, Los Angeles, California, USA.ORCID 0000-0003-0874-9043
Duilio CascioDepartments of Chemistry and Biochemistry and Biological Chemistry, UCLA-DOE Institute UCLA, Los Angeles, California, USA.
Tianxiao P YangDepartments of Chemistry and Biochemistry and Biological Chemistry, UCLA-DOE Institute UCLA, Los Angeles, California, USA.
Stephan PhilippDepartment of Molecular Biology and Biochemistry, University of California, Irvine, California, USA.
Christopher Kazu WilliamsDepartment of Pathology & Laboratory Medicine, David Geffen School of Medicine at UCLA, Los Angeles, California, USA.
Kathy L NewellDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, Indiana, USA.ORCID 0000-0002-1648-7357
Bernardino GhettiDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, Indiana, USA.ORCID 0000-0002-1842-8019
Michael A DeTureDepartment of Neuroscience, Mayo Clinic, Jacksonville, Florida, USA.ORCID 0000-0002-4363-1262
Dennis W DicksonDepartment of Neuroscience, Mayo Clinic, Jacksonville, Florida, USA.
Harry V VintersDepartment of Pathology & Laboratory Medicine, David Geffen School of Medicine at UCLA, Los Angeles, California, USA.
Philip L FelgnerVaccine Research and Development Center, Department of Physiology and Biophysics, University of California Irvine, Irvine, California, USA.ORCID 0000-0002-4117-8505
Rie NakajimaVaccine Research and Development Center, Department of Physiology and Biophysics, University of California Irvine, Irvine, California, USA.
Charles G GlabeDepartment of Molecular Biology and Biochemistry, University of California, Irvine, California, USA.
David S EisenbergDepartments of Chemistry and Biochemistry and Biological Chemistry, UCLA-DOE Institute UCLA, Los Angeles, California, USA david@mbi.ucla.edu.ORCID 0000-0003-2432-5419
Howard Hughes Medical Institute · USUniversity of California, Irvine · USIndiana University School of MedicineJacksonville College · USUniversity of California, Los Angeles · US
Funding
Research Education ComponentP30AG010133 · NIA · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI SAYKIN, ANDREW J · 1991 to 2020
$37.3MUser Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2MTowards Treatment of Alzheimer’s Disease by Targeting Pathogenic Tau and Beta-Amyloid StructuresR01AG070895 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI DAVID EISENBERG · 2022 to 2026
$5.8MStructure and Inhibition of Amyloid in Alzheimer's DiseaseRF1AG054022 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2016 to 2018
$4.2MStructural Biology of Amyloid DiseaseR01AG029430 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2007 to 2016
$3.9MConformational polymorphisms of amyloid in AD and immunological biomarkers and therapeuticsRF1AG056507 · NIA · UNIVERSITY OF CALIFORNIA-IRVINE · PI GLABE, CHARLES G. · 2018 to 2019
$3.6MPixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8MIdentifying distinct tau polymorphs in Alzheimer’s disease and development of early diagnostics for aggregation of tau polymorphsR56AG061847 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2018 to 2018
$797kTau Structures: From Proteopathic to ProtectiveF32NS095661 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SEIDLER, PAUL MATTHEW · 2016 to 2018
$173kHoward Hughes Medical InstituteNCRR NIH HHS S10 RR029205NIA NIH HHS P30 AG010133NIA NIH HHS R01 AG029430NIA NIH HHS R01 AG070895NIA NIH HHS R56 AG061847NIA NIH HHS RF1 AG054022NIA NIH HHS RF1 AG056507NIGMS NIH HHS P30 GM124165NINDS NIH HHS F32 NS095661
Abstract
Soluble oligomers of aggregated tau accompany the accumulation of insoluble amyloid fibrils, a histological hallmark of Alzheimer disease (AD) and two dozen related neurodegenerative diseases. Both oligomers and fibrils seed the spread of Tau pathology, and by virtue of their low molecular weight and relative solubility, oligomers may be particularly pernicious seeds. Here, we report the formation of
Indexed as
Alzheimer DiseaseProtein MultimerizationCrystallography, X-RayHumansSingle-Chain Antibodiestau ProteinsMAPT protein, humanSingle-Chain Antibodiestau ProteinsAlzheimer diseaseamyloidantibodyantibody engineeringfibrilinhibitorneurodegenerationneurodegenerative diseaseoligomerizationprionprotein aggregationprotein crystallizationprotein structuretautauopathy
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