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  1. Article ; Online: Reconstitution of the Alzheimer's Disease Tau Core Structure from Recombinant Tau

    Glynn, Calina / Chun, Joshua E / Donahue, Cameron C / Nadler, Monica J S / Fan, Zhanyun / Hyman, Bradley T

    Biochemistry

    2023  Volume 63, Issue 2, Page(s) 194–201

    Abstract: The protein tau misfolds into disease-specific fibrillar structures in more than 20 neurodegenerative diseases collectively referred to as tauopathies. To understand and prevent disease-specific mechanisms of filament formation, ...

    Abstract The protein tau misfolds into disease-specific fibrillar structures in more than 20 neurodegenerative diseases collectively referred to as tauopathies. To understand and prevent disease-specific mechanisms of filament formation,
    MeSH term(s) Humans ; Alzheimer Disease/metabolism ; Cryoelectron Microscopy ; Neurofibrillary Tangles/chemistry ; tau Proteins/chemistry ; tau Proteins/genetics ; Protein Structure, Quaternary
    Chemical Substances tau Proteins
    Language English
    Publishing date 2023-12-28
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.3c00425
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Specific detection of tau seeding activity in Alzheimer's disease using rationally designed biosensor cells.

    Lathuiliere, Aurelien / Jo, Youhwa / Perbet, Romain / Donahue, Cameron / Commins, Caitlin / Quittot, Noé / Fan, Zhanyun / Bennett, Rachel E / Hyman, Bradley T

    Molecular neurodegeneration

    2023  Volume 18, Issue 1, Page(s) 53

    Abstract: Background: The prion-like propagation of tau in neurodegenerative disorders implies that misfolded pathological tau can recruit the normal protein and template its aggregation. Here, we report the methods for the development of sensitive biosensor cell ...

    Abstract Background: The prion-like propagation of tau in neurodegenerative disorders implies that misfolded pathological tau can recruit the normal protein and template its aggregation. Here, we report the methods for the development of sensitive biosensor cell lines for the detection of tau seeding activity.
    Results: We performed the rational design of novel tau probes based on the current structural knowledge of pathological tau aggregates in Alzheimer's disease. We generated Förster resonance energy transfer (FRET)-based biosensor stable cell lines and characterized their sensitivity, specificity, and overall ability to detect bioactive tau in human samples. As compared to the reference biosensor line, the optimized probe design resulted in an increased efficiency in the detection of tau seeding. The increased sensitivity allowed for the detection of lower amount of tau seeding competency in human brain samples, while preserving specificity for tau seeds found in Alzheimer's disease.
    Conclusions: This next generation of FRET-based biosensor cells is a novel tool to study tau seeding activity in Alzheimer's disease human samples, especially in samples with low levels of seeding activity, which may help studying early tau-related pathological events.
    MeSH term(s) Humans ; Alzheimer Disease/metabolism ; Tauopathies/metabolism ; tau Proteins/metabolism ; Brain/metabolism ; Biosensing Techniques
    Chemical Substances tau Proteins
    Language English
    Publishing date 2023-08-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2244557-2
    ISSN 1750-1326 ; 1750-1326
    ISSN (online) 1750-1326
    ISSN 1750-1326
    DOI 10.1186/s13024-023-00643-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Alzheimer proteopathic tau seeds are biochemically a forme fruste of mature paired helical filaments.

    Kumar, Mukesh / Quittot, Noé / Dujardin, Simon / Schlaffner, Christoph N / Viode, Arthur / Wiedmer, Anne / Beerepoot, Pieter / Chun, Joshua E / Glynn, Calina / Fernandes, Analiese R / Donahue, Cameron / Steen, Judith A / Hyman, Bradley T

    Brain : a journal of neurology

    2024  Volume 147, Issue 2, Page(s) 637–648

    Abstract: Aggregation prone molecules, such as tau, form both historically well characterized fibrillar deposits (neurofibrillary tangles) and recently identified phosphate-buffered saline (PBS) extract species called proteopathic seeds. Both can cause normal ... ...

    Abstract Aggregation prone molecules, such as tau, form both historically well characterized fibrillar deposits (neurofibrillary tangles) and recently identified phosphate-buffered saline (PBS) extract species called proteopathic seeds. Both can cause normal endogenous tau to undergo templated misfolding. The relationship of these seeds to the fibrils that define tau-related diseases is unknown. We characterized the aqueous extractable and sarkosyl insoluble fibrillar tau species derived from human Alzheimer brain using mass spectrometry and in vitro bioassays. Post-translational modifications (PTMs) including phosphorylation, acetylation and ubiquitination are identified in both preparations. PBS extract seed competent tau can be distinguished from sarkosyl insoluble tau by the presence of overlapping, but less abundant, PTMs and an absence of some PTMs unique to the latter. The presence of ubiquitin and other PTMs on the PBS-extracted tau species correlates with the amount of tau in the seed competent size exclusion fractions, with the bioactivity and with the aggressiveness of clinical disease. These results demonstrate that the PTMs present on bioactive, seed competent PBS extract tau species are closely related to, but distinct from, the PTMs of mature paired helical filaments, consistent with the idea that they are a forme fruste of tau species that ultimately form fibrils.
    MeSH term(s) Humans ; Neurofibrillary Tangles/metabolism ; Alzheimer Disease/metabolism ; tau Proteins/metabolism ; Protein Processing, Post-Translational ; Phosphorylation
    Chemical Substances tau Proteins
    Language English
    Publishing date 2024-01-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 80072-7
    ISSN 1460-2156 ; 0006-8950
    ISSN (online) 1460-2156
    ISSN 0006-8950
    DOI 10.1093/brain/awad378
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ui II Zs.26: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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