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  1. Article ; Online: The advent of Alzheimer treatments will change the trajectory of human aging.

    Selkoe, Dennis J

    Nature aging

    2024  Volume 4, Issue 4, Page(s) 453–463

    Abstract: Slowing neurodegenerative disorders of late life has lagged behind progress on other chronic diseases. But advances in two areas, biochemical pathology and human genetics, have now identified early pathogenic events, enabling molecular hypotheses and ... ...

    Abstract Slowing neurodegenerative disorders of late life has lagged behind progress on other chronic diseases. But advances in two areas, biochemical pathology and human genetics, have now identified early pathogenic events, enabling molecular hypotheses and disease-modifying treatments. A salient example is the discovery that antibodies to amyloid ß-protein, long debated as a causative factor in Alzheimer's disease (AD), clear amyloid plaques, decrease levels of abnormal tau proteins and slow cognitive decline. Approval of amyloid antibodies as the first disease-modifying treatments means a gradually rising fraction of the world's estimated 60 million people with symptomatic disease may decline less or even stabilize. Society is entering an era in which the unchecked devastation of AD is no longer inevitable. This Perspective considers the impact of slowing AD and other neurodegenerative disorders on the trajectory of aging, allowing people to survive into late life with less functional decline. The implications of this moment for medicine and society are profound.
    MeSH term(s) Humans ; Alzheimer Disease/drug therapy ; tau Proteins/metabolism ; Aging/metabolism ; Cognitive Dysfunction
    Chemical Substances tau Proteins
    Language English
    Publishing date 2024-04-19
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2662-8465
    ISSN (online) 2662-8465
    DOI 10.1038/s43587-024-00611-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Alzheimer's drugs: Does reducing amyloid work?-Response.

    Selkoe, Dennis J

    Science (New York, N.Y.)

    2021  Volume 374, Issue 6567, Page(s) 545–546

    MeSH term(s) Alzheimer Disease/drug therapy ; Amyloid ; Amyloid beta-Peptides ; Amyloidogenic Proteins ; Humans ; Pharmaceutical Preparations
    Chemical Substances Amyloid ; Amyloid beta-Peptides ; Amyloidogenic Proteins ; Pharmaceutical Preparations
    Language English
    Publishing date 2021-10-28
    Publishing country United States
    Document type Letter ; Comment
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.abm3288
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  3. Article ; Online: Soluble oligomers or insoluble fibrils? Scientific commentary on "Tau seeding and spreading in vivo is supported by both AD-derived fibrillar and oligomeric tau".

    Stern, Andrew M / Selkoe, Dennis J

    Acta neuropathologica

    2023  Volume 146, Issue 6, Page(s) 861–862

    Language English
    Publishing date 2023-09-21
    Publishing country Germany
    Document type Letter ; Comment
    ZDB-ID 1079-0
    ISSN 1432-0533 ; 0001-6322
    ISSN (online) 1432-0533
    ISSN 0001-6322
    DOI 10.1007/s00401-023-02633-6
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  4. Article ; Online: Treatments for Alzheimer's disease emerge.

    Selkoe, Dennis J

    Science (New York, N.Y.)

    2021  Volume 373, Issue 6555, Page(s) 624–626

    MeSH term(s) Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Alzheimer Disease/prevention & control ; Amyloid Precursor Protein Secretases/antagonists & inhibitors ; Amyloid beta-Peptides/immunology ; Amyloid beta-Peptides/metabolism ; Animals ; Antibodies, Monoclonal, Humanized/therapeutic use ; Biomarkers/analysis ; Brain/metabolism ; Brain/pathology ; Clinical Trials as Topic ; Enzyme Inhibitors/therapeutic use ; Humans ; Immunotherapy ; Mice ; Neurofibrillary Tangles/drug effects ; Neurofibrillary Tangles/pathology ; Plaque, Amyloid/drug therapy ; tau Proteins/metabolism
    Chemical Substances Amyloid beta-Peptides ; Antibodies, Monoclonal, Humanized ; Biomarkers ; Enzyme Inhibitors ; MAPT protein, human ; tau Proteins ; aducanumab (105J35OE21) ; gantenerumab (4DF060P933) ; Amyloid Precursor Protein Secretases (EC 3.4.-)
    Language English
    Publishing date 2021-08-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.abi6401
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  5. Article ; Online: The Parkinson-Associated Toxin Paraquat Shifts Physiological α-Synuclein Tetramers toward Monomers That Can Be Calpain-Truncated and Form Oligomers.

    Nuber, Silke / Selkoe, Dennis J

    The American journal of pathology

    2023  Volume 193, Issue 5, Page(s) 520–531

    Abstract: Abnormal aggregation of α-synuclein (αS) is thought to initiate neuronal dysfunction and death in Parkinson disease (PD). In addition to higher-molecular-weight, oligomeric, and polymeric forms of αS associated with neurotoxicity and disease, recent ... ...

    Abstract Abnormal aggregation of α-synuclein (αS) is thought to initiate neuronal dysfunction and death in Parkinson disease (PD). In addition to higher-molecular-weight, oligomeric, and polymeric forms of αS associated with neurotoxicity and disease, recent findings indicate the occurrence of physiological tetrameric assemblies in healthy neurons in culture and in brain. Herein, the PD-associated neurotoxin paraquat reduced physiological tetramers and led to calpain-truncated monomers and an approximately 70-kDa apparent oligomer different in size from physiological αS multimers. These truncated and oligomeric forms could also be generated by calpain cleavage of pure, recombinant human αS in vitro. Moreover, they were detected in the brains of tetramer-abrogating, E46K-amplified (3K) mice that model PD. These results indicate that paraquat triggers membrane damage and aberrant calpain activity that can induce a pathologic shift of tetramers toward an excess of full-length and truncated monomers, the accumulation of αS oligomers, and insoluble cytoplasmic αS puncta. The findings suggest that an environmental precipitant of PD can alter αS tetramer/monomer equilibrium, as already shown for several genetically caused forms of PD.
    MeSH term(s) Mice ; Humans ; Animals ; alpha-Synuclein/toxicity ; Parkinson Disease ; Calpain ; Paraquat/toxicity
    Chemical Substances alpha-Synuclein ; Calpain (EC 3.4.22.-) ; Paraquat (PLG39H7695)
    Language English
    Publishing date 2023-02-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2943-9
    ISSN 1525-2191 ; 0002-9440
    ISSN (online) 1525-2191
    ISSN 0002-9440
    DOI 10.1016/j.ajpath.2023.01.010
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  6. Book ; Conference proceedings: Synaptic plasticity and the mechanism of Alzheimer's disease

    Selkoe, Dennis J.

    (Research and perspectives in Alzheimer's disease)

    2008  

    Event/congress Colloque Médecine et Recherche (2007, Paris)
    Author's details [Colloque Médecine et Recherche ... Paris on April 16, 2007]. Dennis J. Selkoe ... (ed.)
    Series title Research and perspectives in Alzheimer's disease
    Keywords Alzheimerkrankheit ; Synapse ; Plastizität
    Subject Verformbarkeit ; Alzheimer-Krankheit ; Alzheimersche Krankheit ; Alzheimer-Demenz ; Morbus Alzheimer ; Greisenblödsinn ; Alzheimer's Disease
    Language English
    Size XII, 183 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place Berlin u.a.
    Publishing country Germany
    Document type Book ; Conference proceedings
    HBZ-ID HT015441692
    ISBN 978-3-540-76329-1 ; 3-540-76329-5 ; 9783540763307 ; 3540763309
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2008 A 1577 order for loan Magazin

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  7. Article ; Online: Unfairness to Patients With Alzheimer Disease in Medicare's Coverage of Antiamyloid Immunotherapy.

    Stern, Andrew M / Selkoe, Dennis J

    JAMA neurology

    2022  Volume 79, Issue 10, Page(s) 962–963

    MeSH term(s) Aged ; Alzheimer Disease/therapy ; Humans ; Immunotherapy ; Insurance Coverage ; Medicare ; United States
    Language English
    Publishing date 2022-08-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2702023-X
    ISSN 2168-6157 ; 2168-6149
    ISSN (online) 2168-6157
    ISSN 2168-6149
    DOI 10.1001/jamaneurol.2022.2131
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  8. Article ; Online: Early network dysfunction in Alzheimer's disease.

    Selkoe, Dennis J

    Science (New York, N.Y.)

    2019  Volume 365, Issue 6453, Page(s) 540–541

    MeSH term(s) Alzheimer Disease ; Brain ; Humans ; Neurons
    Language English
    Publishing date 2019-08-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.aay5188
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  9. Article ; Online: Alzheimer disease and aducanumab: adjusting our approach.

    Selkoe, Dennis J

    Nature reviews. Neurology

    2019  Volume 15, Issue 7, Page(s) 365–366

    MeSH term(s) Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Antibodies, Monoclonal, Humanized/therapeutic use ; Clinical Trials as Topic ; Humans ; Treatment Failure
    Chemical Substances Amyloid beta-Peptides ; Antibodies, Monoclonal, Humanized ; aducanumab (105J35OE21)
    Language English
    Publishing date 2019-06-17
    Publishing country England
    Document type Journal Article
    ZDB-ID 2491514-2
    ISSN 1759-4766 ; 1759-4758
    ISSN (online) 1759-4766
    ISSN 1759-4758
    DOI 10.1038/s41582-019-0205-1
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  10. Article ; Online: Light at the End of the Amyloid Tunnel

    Selkoe, Dennis J

    Biochemistry

    2018  Volume 57, Issue 41, Page(s) 5921–5922

    MeSH term(s) Amyloid ; Amyloidosis ; Biochemistry ; Humans ; Periodicals as Topic
    Chemical Substances Amyloid
    Language English
    Publishing date 2018-10-01
    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.8b00985
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