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  1. Book ; Online ; E-Book: The molecular and cellular basis of neurodegenerative diseases

    Wolfe, Michael S.

    underlying mechanisms

    2018  

    Author's details edited by Michael S. Wolfe
    Language English
    Size 1 Online-Ressource (xiv, 546 Seiten), Illustrationen
    Publisher Elsevier AP
    Publishing place London
    Publishing country Great Britain
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT019648524
    ISBN 978-0-12-811305-9 ; 9780128113042 ; 0-12-811305-7 ; 0128113049
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article ; Online: γ-Secretase: once and future drug target for Alzheimer's disease.

    Wolfe, Michael S

    Expert opinion on drug discovery

    2024  Volume 19, Issue 1, Page(s) 5–8

    MeSH term(s) Humans ; Alzheimer Disease/drug therapy ; Amyloid Precursor Protein Secretases ; Amyloid beta-Peptides
    Chemical Substances Amyloid Precursor Protein Secretases (EC 3.4.-) ; Amyloid beta-Peptides
    Language English
    Publishing date 2024-01-08
    Publishing country England
    Document type Editorial
    ZDB-ID 2259618-5
    ISSN 1746-045X ; 1746-0441
    ISSN (online) 1746-045X
    ISSN 1746-0441
    DOI 10.1080/17460441.2023.2277350
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 6388: Show issues Location:
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  3. Book ; Online ; E-Book: Alzheimer’s disease II

    Wolfe, Michael S.

    (Topics in medicinal chemistry ; 24)

    2017  

    Author's details edited by Michael S. Wolfe
    Series title Topics in medicinal chemistry ; 24
    Collection
    Keywords Chemistry ; Neurosciences ; Pharmaceutical technology ; Medicinal chemistry ; Proteins
    Language English
    Size 1 Online-Ressource (VII, 202 Seiten), Illustrationen
    Publisher Springer
    Publishing place Cham
    Publishing country Switzerland
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT019405193
    ISBN 978-3-319-59460-6 ; 9783319594590 ; 3-319-59460-5 ; 3319594591
    DOI 10.1007/978-3-319-59460-6
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  4. Article ; Online: γ-Secretase as a drug target for familial Alzheimer's disease: the road less traveled.

    Wolfe, Michael S

    Future medicinal chemistry

    2022  Volume 14, Issue 19, Page(s) 1341–1343

    MeSH term(s) Alzheimer Disease/drug therapy ; Amyloid Precursor Protein Secretases ; Amyloid beta-Peptides ; Humans ; Mutation
    Chemical Substances Amyloid beta-Peptides ; Amyloid Precursor Protein Secretases (EC 3.4.-)
    Language English
    Publishing date 2022-08-30
    Publishing country England
    Document type Editorial ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1756-8927
    ISSN (online) 1756-8927
    DOI 10.4155/fmc-2022-0178
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Targeting γ-Secretase for Familial Alzheimer's Disease.

    Wolfe, Michael S

    Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents

    2021  Volume 30, Issue 7, Page(s) 1321–1327

    Abstract: Familial Alzheimer's disease (FAD) is a rare early-onset genetic form of a common dementia of old age. Striking in middle age, FAD is caused by missense mutations in three genes: ...

    Abstract Familial Alzheimer's disease (FAD) is a rare early-onset genetic form of a common dementia of old age. Striking in middle age, FAD is caused by missense mutations in three genes:
    Language English
    Publishing date 2021-05-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1116702-6
    ISSN 1054-2523
    ISSN 1054-2523
    DOI 10.1007/s00044-021-02744-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3444: Show issues Location:
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  6. Article ; Online: Probing Mechanisms and Therapeutic Potential of γ-Secretase in Alzheimer's Disease.

    Wolfe, Michael S

    Molecules (Basel, Switzerland)

    2021  Volume 26, Issue 2

    Abstract: The membrane-embedded γ-secretase complex carries out hydrolysis within the lipid bilayer in proteolyzing nearly 150 different membrane protein substrates. Among these substrates, the amyloid precursor protein (APP) has been the most studied, as ... ...

    Abstract The membrane-embedded γ-secretase complex carries out hydrolysis within the lipid bilayer in proteolyzing nearly 150 different membrane protein substrates. Among these substrates, the amyloid precursor protein (APP) has been the most studied, as generation of aggregation-prone amyloid β-protein (Aβ) is a defining feature of Alzheimer's disease (AD). Mutations in APP and in presenilin, the catalytic component of γ-secretase, cause familial AD, strong evidence for a pathogenic role of Aβ. Substrate-based chemical probes-synthetic peptides and peptidomimetics-have been critical to unraveling the complexity of γ-secretase, and small drug-like inhibitors and modulators of γ-secretase activity have been essential for exploring the potential of the protease as a therapeutic target for Alzheimer's disease. Such chemical probes and therapeutic prototypes will be reviewed here, with concluding commentary on the future directions in the study of this biologically important protease complex and the translation of basic findings into therapeutics.
    MeSH term(s) Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Amyloid Precursor Protein Secretases/antagonists & inhibitors ; Amyloid Precursor Protein Secretases/genetics ; Amyloid Precursor Protein Secretases/metabolism ; Animals ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Humans ; Molecular Conformation ; Neuroprotective Agents/chemistry ; Neuroprotective Agents/pharmacology
    Chemical Substances Enzyme Inhibitors ; Neuroprotective Agents ; Amyloid Precursor Protein Secretases (EC 3.4.-)
    Language English
    Publishing date 2021-01-13
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules26020388
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 81: Show issues

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  7. Article ; Online: Unraveling the complexity of γ-secretase.

    Wolfe, Michael S

    Seminars in cell & developmental biology

    2020  Volume 105, Page(s) 3–11

    Abstract: γ-Secretase was initially defined as a proteolytic activity that cleaves within the transmembrane of the amyloid precursor protein (APP) to produce the amyloid β-peptide of Alzheimer's disease. The discovery of mutations in APP and the presenilins ... ...

    Abstract γ-Secretase was initially defined as a proteolytic activity that cleaves within the transmembrane of the amyloid precursor protein (APP) to produce the amyloid β-peptide of Alzheimer's disease. The discovery of mutations in APP and the presenilins associated with familial Alzheimer's disease and their effects on APP processing dovetailed with pharmacological studies on γ-secretase, leading to the revelation that presenilins are unprecedented membrane-embedded aspartyl proteases. Other members of what became known as the γ-secretase complex were subsequently identified. In parallel with these advances, connections between presenilins and Notch receptors essential to metazoan development became evident, resulting in the concurrent realization that γ-secretase also carries out intramembrane proteolysis of Notch as part of its signaling mechanism. Substantial progress has been made toward elucidating how γ-secretase carries out complex processing of transmembrane domains, how it goes awry in familial Alzheimer's disease, the scope of its substrates, and the atomic details of its structure. Critical questions remain for future study, toward further unraveling the complexity of this unique membrane-embedded proteolytic machine and its roles in biology and disease.
    MeSH term(s) Alzheimer Disease/genetics ; Amyloid Precursor Protein Secretases/metabolism ; Humans
    Chemical Substances Amyloid Precursor Protein Secretases (EC 3.4.-)
    Language English
    Publishing date 2020-01-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2020.01.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2918: Show issues Location:
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  8. Article ; Online: Membrane protein takes the brakes off.

    Wolfe, Michael S

    Science (New York, N.Y.)

    2019  Volume 363, Issue 6426, Page(s) 453–454

    MeSH term(s) Diffusion ; Lipids ; Membrane Proteins ; Viscosity
    Chemical Substances Lipids ; Membrane Proteins
    Language English
    Publishing date 2019-01-31
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.aaw2865
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 77: Show issues

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  9. Article ; Online: Structure and mechanism of the γ-secretase intramembrane protease complex.

    Wolfe, Michael S / Miao, Yinglong

    Current opinion in structural biology

    2022  Volume 74, Page(s) 102373

    Abstract: γ-Secretase is a membrane protein complex that proteolyzes within the transmembrane domain of >100 substrates, including those derived from the amyloid precursor protein and the Notch family of cell surface receptors. The nine-transmembrane presenilin is ...

    Abstract γ-Secretase is a membrane protein complex that proteolyzes within the transmembrane domain of >100 substrates, including those derived from the amyloid precursor protein and the Notch family of cell surface receptors. The nine-transmembrane presenilin is the catalytic component of this aspartyl protease complex that carries out hydrolysis in the lipid bilayer. Advances in cryoelectron microscopy have led to the elucidation of the structure of the γ-secretase complex at atomic resolution. Recently, structures of the enzyme have been determined with bound APP- or Notch-derived substrates, providing insight into the nature of substrate recognition and processing. Molecular dynamics simulations of substrate-bound enzymes suggest dynamic mechanisms of intramembrane proteolysis. Structures of the enzyme bound to small-molecule inhibitors and modulators have also been solved, setting the stage for rational structure-based drug discovery targeting γ-secretase.
    MeSH term(s) Amyloid Precursor Protein Secretases/metabolism ; Amyloid beta-Protein Precursor/chemistry ; Cell Membrane/metabolism ; Cryoelectron Microscopy ; Receptors, Notch/metabolism
    Chemical Substances Amyloid beta-Protein Precursor ; Receptors, Notch ; Amyloid Precursor Protein Secretases (EC 3.4.-)
    Language English
    Publishing date 2022-04-20
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2022.102373
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3206: Show issues Location:
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  10. Article ; Online: In search of pathogenic amyloid β-peptide in familial Alzheimer's disease.

    Wolfe, Michael S

    Progress in molecular biology and translational science

    2019  Volume 168, Page(s) 71–78

    Abstract: Early-onset familial Alzheimer's disease (FAD) is pathologically and clinically similar to the more common late-onset sporadic form of the disease. The study of rare genetic mutations that cause FAD should provide insight into the pathogenesis of ... ...

    Abstract Early-onset familial Alzheimer's disease (FAD) is pathologically and clinically similar to the more common late-onset sporadic form of the disease. The study of rare genetic mutations that cause FAD should provide insight into the pathogenesis of sporadic Alzheimer's disease. FAD mutations have only been found in the substrate (amyloid precursor protein, APP) and protease (γ-secretase) that produces the amyloid-β peptide (Aβ). The secreted, aggregation-prone 42-residue Aβ peptide (Aβ42) has long been considered the pathogenic entity in Alzheimer's disease. However, recent understanding of the complexity of the processing of APP by γ-secretase and the effects of FAD mutations on this processing suggest other forms of Aβ as potentially pathogenic.
    MeSH term(s) Alzheimer Disease/etiology ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid Precursor Protein Secretases/metabolism ; Amyloid beta-Peptides/adverse effects ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Humans ; Mutation
    Chemical Substances APP protein, human ; Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Amyloid Precursor Protein Secretases (EC 3.4.-)
    Language English
    Publishing date 2019-07-13
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 2471995-X
    ISSN 1878-0814 ; 0079-6603 ; 1877-1173
    ISSN (online) 1878-0814
    ISSN 0079-6603 ; 1877-1173
    DOI 10.1016/bs.pmbts.2019.07.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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