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  1. Article ; Online: Fluent molecular mixing of Tau isoforms in Alzheimer’s disease neurofibrillary tangles

    Aurelio J. Dregni / Pu Duan / Hong Xu / Lakshmi Changolkar / Nadia El Mammeri / Virginia M.-Y. Lee / Mei Hong

    Nature Communications, Vol 13, Iss 1, Pp 1-

    2022  Volume 11

    Abstract: The tau protein in Alzheimer’s disease contains two isoforms. Using solid-state NMR and seeded growth of isotopically labeled tau, here the authors determined that the two isoforms mix fluently on the molecular level to propagate the AD tau structure. ...

    Abstract The tau protein in Alzheimer’s disease contains two isoforms. Using solid-state NMR and seeded growth of isotopically labeled tau, here the authors determined that the two isoforms mix fluently on the molecular level to propagate the AD tau structure.
    Keywords Science ; Q
    Language English
    Publishing date 2022-05-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: α-Synuclein aggregates amplified from patient-derived Lewy bodies recapitulate Lewy body diseases in mice

    Norihito Uemura / Nicholas P. Marotta / Jahan Ara / Emily S. Meymand / Bin Zhang / Hiroshi Kameda / Masato Koike / Kelvin C. Luk / John Q. Trojanowski / Virginia M.-Y. Lee

    Nature Communications, Vol 14, Iss 1, Pp 1-

    2023  Volume 17

    Abstract: Abstract Extraction of α-Synuclein (αSyn) aggregates from Lewy body disease (LBD) brains has been widely described yet templated fibrillization of LB-αSyn often fails to propagate its structural and functional properties. We recently demonstrated that ... ...

    Abstract Abstract Extraction of α-Synuclein (αSyn) aggregates from Lewy body disease (LBD) brains has been widely described yet templated fibrillization of LB-αSyn often fails to propagate its structural and functional properties. We recently demonstrated that aggregates amplified from LB-αSyn (ampLB) show distinct biological activities in vitro compared to human αSyn preformed fibrils (hPFF) formed de novo. Here we compare the in vivo biological activities of hPFF and ampLB regarding seeding activity, latency in inducing pathology, distribution of pathology, inclusion morphology, and cell-type preference. Injection of ampLB into mice expressing only human αSyn (male Thy1:SNCA/Snca –/– mice) induced pathologies similar to those of LBD subjects that were distinct from those induced by hPFF-injection or developing spontaneously with aging. Importantly, αSyn aggregates in ampLB-injected Thy1:SNCA/Snca –/– mice maintained the unique biological and conformational features of original LB-αSyn. These results indicate that ampLB-injection, rather than conventional PFF-injection or αSyn overexpression, faithfully models key aspects of LBD.
    Keywords Science ; Q
    Language English
    Publishing date 2023-10-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Neurofibrillary tangle-like tau pathology induced by synthetic tau fibrils in primary neurons over-expressing mutant tau

    Guo, Jing L / Virginia M.Y. Lee

    Federation of European Biochemical Societies FEBS letters. 2013 Mar. 18, v. 587, no. 6

    2013  

    Abstract: Increasing evidence demonstrates the transmissibility of fibrillar species of tau protein, but this has never been directly tested in neurons, the cell type most affected by formation of tau inclusions in neurodegenerative tauopathies. Here we show that ... ...

    Abstract Increasing evidence demonstrates the transmissibility of fibrillar species of tau protein, but this has never been directly tested in neurons, the cell type most affected by formation of tau inclusions in neurodegenerative tauopathies. Here we show that synthetic tau fibrils made from recombinant protein not only time-dependently recruit normal tau into neurofibrillary tangle-like insoluble aggregates in primary hippocampal neurons over-expressing human tau, but also induce neuritic tau pathology in non-transgenic neurons. This study provides highly compelling support for the protein-only hypothesis of pathological tau transmission in primary neurons and describes a useful neuronal model for studying the pathogenesis of tauopathies.
    Keywords humans ; models ; mutants ; neurons ; pathogenesis ; primary transmission ; recombinant proteins
    Language English
    Dates of publication 2013-0318
    Size p. 717-723.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2013.01.051
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: An HDAC6-dependent surveillance mechanism suppresses tau-mediated neurodegeneration and cognitive decline

    Hanna Trzeciakiewicz / Deepa Ajit / Jui-Heng Tseng / Youjun Chen / Aditi Ajit / Zarin Tabassum / Rebecca Lobrovich / Claire Peterson / Natallia V. Riddick / Michelle S. Itano / Ashutosh Tripathy / Sheryl S. Moy / Virginia M. Y. Lee / John Q. Trojanowski / David J. Irwin / Todd J. Cohen

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 18

    Abstract: HDAC6 is a tau deacetylase and acetylation of tau inhibits its function and promotes aggregation. Here the authors show that HDAC6 protects against tau accumulation in a mouse model of tauopathy. ...

    Abstract HDAC6 is a tau deacetylase and acetylation of tau inhibits its function and promotes aggregation. Here the authors show that HDAC6 protects against tau accumulation in a mouse model of tauopathy.
    Keywords Science ; Q
    Language English
    Publishing date 2020-11-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Transmission of tauopathy strains is independent of their isoform composition

    Zhuohao He / Jennifer D. McBride / Hong Xu / Lakshmi Changolkar / Soo-jung Kim / Bin Zhang / Sneha Narasimhan / Garrett S. Gibbons / Jing L. Guo / Michael Kozak / Gerard D. Schellenberg / John Q. Trojanowski / Virginia M. -Y. Lee

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 18

    Abstract: Although normal human brains express 6 tau isoforms in equal ratio with 3 or 4 microtubule-binding repeat domains (3R and 4R), tau inclusions from different human tauopathy brains, now considered as different strains, have distinct isoform compositions ... ...

    Abstract Although normal human brains express 6 tau isoforms in equal ratio with 3 or 4 microtubule-binding repeat domains (3R and 4R), tau inclusions from different human tauopathy brains, now considered as different strains, have distinct isoform compositions and strain properties and the relationship between these two parts is unclear. Here the authors generate a new transgenic mouse line expressing 6 human tau isoforms with equal 3R and 4R ratios, recapitulate distinct human tau strains in mouse brains with similar isoform compositions and cell type specificities, and further show the strain transmission pattern is independent of its isoform composition.
    Keywords Science ; Q
    Language English
    Publishing date 2020-01-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: An HDAC6-dependent surveillance mechanism suppresses tau-mediated neurodegeneration and cognitive decline

    Hanna Trzeciakiewicz / Deepa Ajit / Jui-Heng Tseng / Youjun Chen / Aditi Ajit / Zarin Tabassum / Rebecca Lobrovich / Claire Peterson / Natallia V. Riddick / Michelle S. Itano / Ashutosh Tripathy / Sheryl S. Moy / Virginia M. Y. Lee / John Q. Trojanowski / David J. Irwin / Todd J. Cohen

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 18

    Abstract: HDAC6 is a tau deacetylase and acetylation of tau inhibits its function and promotes aggregation. Here the authors show that HDAC6 protects against tau accumulation in a mouse model of tauopathy. ...

    Abstract HDAC6 is a tau deacetylase and acetylation of tau inhibits its function and promotes aggregation. Here the authors show that HDAC6 protects against tau accumulation in a mouse model of tauopathy.
    Keywords Science ; Q
    Language English
    Publishing date 2020-11-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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  7. Article ; Online: Transmission of tauopathy strains is independent of their isoform composition

    Zhuohao He / Jennifer D. McBride / Hong Xu / Lakshmi Changolkar / Soo-jung Kim / Bin Zhang / Sneha Narasimhan / Garrett S. Gibbons / Jing L. Guo / Michael Kozak / Gerard D. Schellenberg / John Q. Trojanowski / Virginia M. -Y. Lee

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 18

    Abstract: Although normal human brains express 6 tau isoforms in equal ratio with 3 or 4 microtubule-binding repeat domains (3R and 4R), tau inclusions from different human tauopathy brains, now considered as different strains, have distinct isoform compositions ... ...

    Abstract Although normal human brains express 6 tau isoforms in equal ratio with 3 or 4 microtubule-binding repeat domains (3R and 4R), tau inclusions from different human tauopathy brains, now considered as different strains, have distinct isoform compositions and strain properties and the relationship between these two parts is unclear. Here the authors generate a new transgenic mouse line expressing 6 human tau isoforms with equal 3R and 4R ratios, recapitulate distinct human tau strains in mouse brains with similar isoform compositions and cell type specificities, and further show the strain transmission pattern is independent of its isoform composition.
    Keywords Science ; Q
    Language English
    Publishing date 2020-01-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Conserved Lysine Acetylation within the Microtubule-Binding Domain Regulates MAP2/Tau Family Members.

    Andrew W Hwang / Hanna Trzeciakiewicz / Dave Friedmann / Chao-Xing Yuan / Ronen Marmorstein / Virginia M Y Lee / Todd J Cohen

    PLoS ONE, Vol 11, Iss 12, p e

    2016  Volume 0168913

    Abstract: Lysine acetylation has emerged as a dominant post-translational modification (PTM) regulating tau proteins in Alzheimer's disease (AD) and related tauopathies. Mass spectrometry studies indicate that tau acetylation sites cluster within the microtubule- ... ...

    Abstract Lysine acetylation has emerged as a dominant post-translational modification (PTM) regulating tau proteins in Alzheimer's disease (AD) and related tauopathies. Mass spectrometry studies indicate that tau acetylation sites cluster within the microtubule-binding region (MTBR), a region that is highly conserved among tau, MAP2, and MAP4 family members, implying that acetylation could represent a conserved regulatory mechanism for MAPs beyond tau. Here, we combined mass spectrometry, biochemical assays, and cell-based approaches to demonstrate that the tau family members MAP2 and MAP4 are also subject to reversible acetylation. We identify a cluster of lysines in the MAP2 and MAP4 MTBR that undergo CBP-catalyzed acetylation, many of which are conserved in tau. Similar to tau, MAP2 acetylation can occur in a cysteine-dependent auto-regulatory manner in the presence of acetyl-CoA. Furthermore, tubulin reduced MAP2 acetylation, suggesting tubulin binding dictates MAP acetylation status. Taken together, these results uncover a striking conservation of MAP2/Tau family post-translational modifications that could expand our understanding of the dynamic mechanisms regulating microtubules.
    Keywords Medicine ; R ; Science ; Q
    Subject code 571
    Language English
    Publishing date 2016-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo

    Sílvia Porta / Yan Xu / Clark R. Restrepo / Linda K. Kwong / Bin Zhang / Hannah J. Brown / Edward B. Lee / John Q. Trojanowski / Virginia M.-Y. Lee

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 15

    Abstract: Cell-to-cell transmission of TDP43 occurs in cell cultures and may contribute to pathological TDP43 propagation in FTLD-TDP. In this study, the authors demonstrate using mouse models that a single intracerebral injection of human brain-derived ... ...

    Abstract Cell-to-cell transmission of TDP43 occurs in cell cultures and may contribute to pathological TDP43 propagation in FTLD-TDP. In this study, the authors demonstrate using mouse models that a single intracerebral injection of human brain-derived pathological TDP43 from FTLD-TDP cases initiates the process of seeding and spreading of TDP43 pathology in a spatio-temporal dependent manner in the brain.
    Keywords Science ; Q
    Language English
    Publishing date 2018-10-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo

    Sílvia Porta / Yan Xu / Clark R. Restrepo / Linda K. Kwong / Bin Zhang / Hannah J. Brown / Edward B. Lee / John Q. Trojanowski / Virginia M.-Y. Lee

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 15

    Abstract: Cell-to-cell transmission of TDP43 occurs in cell cultures and may contribute to pathological TDP43 propagation in FTLD-TDP. In this study, the authors demonstrate using mouse models that a single intracerebral injection of human brain-derived ... ...

    Abstract Cell-to-cell transmission of TDP43 occurs in cell cultures and may contribute to pathological TDP43 propagation in FTLD-TDP. In this study, the authors demonstrate using mouse models that a single intracerebral injection of human brain-derived pathological TDP43 from FTLD-TDP cases initiates the process of seeding and spreading of TDP43 pathology in a spatio-temporal dependent manner in the brain.
    Keywords Science ; Q
    Language English
    Publishing date 2018-10-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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