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  1. Article ; Online: Correction: Drug development targeting degeneration of the basal forebrain cholinergic system: its time has come.

    Alam, John J / Nixon, Ralph A

    Molecular neurodegeneration

    2023  Volume 18, Issue 1, Page(s) 81

    Language English
    Publishing date 2023-11-09
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2244557-2
    ISSN 1750-1326 ; 1750-1326
    ISSN (online) 1750-1326
    ISSN 1750-1326
    DOI 10.1186/s13024-023-00678-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Drug development targeting degeneration of the basal forebrain cholinergic system: its time has come.

    Alam, John J / Nixon, Ralph A

    Molecular neurodegeneration

    2023  Volume 18, Issue 1, Page(s) 74

    MeSH term(s) Humans ; Basal Forebrain/pathology ; Alzheimer Disease/pathology ; Nerve Degeneration/pathology ; Cholinergic Agents ; Cholinergic Neurons
    Chemical Substances Cholinergic Agents
    Language English
    Publishing date 2023-10-04
    Publishing country England
    Document type Journal Article
    ZDB-ID 2244557-2
    ISSN 1750-1326 ; 1750-1326
    ISSN (online) 1750-1326
    ISSN 1750-1326
    DOI 10.1186/s13024-023-00663-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Book: Cytoskeleton of the Nervous System

    Nixon, Ralph A. / Yuan, Aidong

    (Advances in neurobiology ; 3)

    2011  

    Author's details Ralph A. Nixon ; Aidong Yuan, ed
    Series title Advances in neurobiology ; 3
    Collection
    Language English
    Size XV, 774 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place New York, NY u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT016725759
    ISBN 978-1-4419-6786-2 ; 9781441967879 ; 1-4419-6786-9 ; 1441967877
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2011 A 1125 order for loan Magazin

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  4. Article ; Online: The aging lysosome: An essential catalyst for late-onset neurodegenerative diseases.

    Nixon, Ralph A

    Biochimica et biophysica acta. Proteins and proteomics

    2020  Volume 1868, Issue 9, Page(s) 140443

    Abstract: Lysosomes figure prominently in theories of aging as the proteolytic system most responsible for eliminating growing burdens of damaged proteins and organelles in aging neurons and other long lived cells. Newer evidence shows that diverse experimental ... ...

    Abstract Lysosomes figure prominently in theories of aging as the proteolytic system most responsible for eliminating growing burdens of damaged proteins and organelles in aging neurons and other long lived cells. Newer evidence shows that diverse experimental measures known to extend lifespan in invertebrate aging models share the property of boosting lysosomal clearance of substrates through the autophagy pathway. Maintaining an optimal level of lysosome acidification is particularly crucial for these anti-aging effects. The exceptional dependence of neurons on fully functional lysosomes is reflected by the neurological phenotypes that develop in congenital lysosomal storage disorders, which commonly present as severe neurodevelopmental or neurodegenerative conditions even though the lysosomal deficit maybe systemic. Similar connections are now being appreciated between primary lysosomal deficit and the risk for late age-onset neurodegenerative disorders. In diseases such as Alzheimer's and Parkinson's, as in aging alone, primary lysosome dysfunction due to acidification impairment is emerging as a frequent theme, supported by the growing list of familial neurodegenerative disorders that involve primary vATPase dysfunction. The additional cellular roles played by intraluminal pH in sensing nutrient and stress and modulating cellular signaling have further expanded the possible ways that lysosomal pH dysregulation in aging and disease can disrupt neuronal function. Here, we consider the impact of cellular aging on lysosomes and how the changes during aging may create the tipping point for disease emergence in major late-age onset neurodegenerative disorders.
    MeSH term(s) Aging/metabolism ; Alzheimer Disease/metabolism ; Animals ; Autophagy/physiology ; Humans ; Hydrogen-Ion Concentration ; Hydrolases ; Lysosomes/metabolism ; Neurodegenerative Diseases/metabolism ; Oxidative Stress ; Parkinson Disease/metabolism ; Proteolysis
    Chemical Substances Hydrolases (EC 3.-)
    Language English
    Publishing date 2020-05-13
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2918798-9
    ISSN 1878-1454 ; 1570-9639
    ISSN (online) 1878-1454
    ISSN 1570-9639
    DOI 10.1016/j.bbapap.2020.140443
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Autolysosomal acidification failure as a primary driver of Alzheimer disease pathogenesis.

    Lee, Ju-Hyun / Nixon, Ralph A

    Autophagy

    2022  Volume 18, Issue 11, Page(s) 2763–2764

    Abstract: Genetic evidence has increasingly linked lysosome dysfunction to an impaired autophagy-lysosomal pathway (ALP) flux in Alzheimer disease (AD) although the relationship of these abnormalities to other pathologies is unclear. In our recent investigation on ...

    Abstract Genetic evidence has increasingly linked lysosome dysfunction to an impaired autophagy-lysosomal pathway (ALP) flux in Alzheimer disease (AD) although the relationship of these abnormalities to other pathologies is unclear. In our recent investigation on the origin of impaired autophagic flux in AD, we established the critical early role of defective lysosomes in five mouse AD models. To assess
    MeSH term(s) Animals ; Mice ; Alzheimer Disease/pathology ; Amyloid beta-Protein Precursor/metabolism ; Autophagy/physiology ; Amyloid beta-Peptides/metabolism ; Lysosomes/metabolism ; Plaque, Amyloid/metabolism ; Disease Models, Animal ; Hydrogen-Ion Concentration ; Mice, Transgenic
    Chemical Substances Amyloid beta-Protein Precursor ; Amyloid beta-Peptides
    Language English
    Publishing date 2022-08-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2022.2110729
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Posttranscriptional regulation of neurofilament proteins and tau in health and disease.

    Yuan, Aidong / Nixon, Ralph A

    Brain research bulletin

    2022  Volume 192, Page(s) 115–127

    Abstract: Neurofilament and tau proteins are neuron-specific cytoskeletal proteins that are enriched in axons, regulated by many of the same protein kinases, interact physically, and are the principal constituents of neurofibrillary lesions in major adult-onset ... ...

    Abstract Neurofilament and tau proteins are neuron-specific cytoskeletal proteins that are enriched in axons, regulated by many of the same protein kinases, interact physically, and are the principal constituents of neurofibrillary lesions in major adult-onset dementias. Both proteins share functions related to the modulation of stability and functions of the microtubule network in axons, axonal transport and scaffolding of organelles, long-term synaptic potentiation, and learning and memory. Expression of these proteins is regulated not only at the transcriptional level but also through posttranscriptional control of pre-mRNA splicing, mRNA stability, transport, localization, local translation and degradation. Current evidence suggests that posttranscriptional determinants of their levels are usually regulated by RNA-binding proteins and microRNAs primarily through 3'-untranslated regions of neurofilament and tau mRNAs. Dysregulations of neurofilament and tau expression caused by mutations or pathologies of RNA-binding proteins such as TDP43, FUS and microRNAs are increasingly recognized in association with varied neurological disorders. In this review, we summarize the current understanding of posttranscriptional control of neurofilament and tau by examining the posttranscriptional regulation of neurofilament and tau by RNA-binding proteins and microRNAs implicated in health and diseases.
    MeSH term(s) Neurofilament Proteins/genetics ; Neurofilament Proteins/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism ; Axons/metabolism ; Axonal Transport ; MicroRNAs/genetics ; MicroRNAs/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
    Chemical Substances Neurofilament Proteins ; tau Proteins ; MicroRNAs ; RNA-Binding Proteins
    Language English
    Publishing date 2022-10-29
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 197620-5
    ISSN 1873-2747 ; 0361-9230
    ISSN (online) 1873-2747
    ISSN 0361-9230
    DOI 10.1016/j.brainresbull.2022.10.017
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  7. Article ; Online: Disease-modifying pharmacological approaches to correcting basal forebrain cholinergic neuronal (BFCN) dysfunction and degeneration.

    Alam, John J / Nixon, Ralph A

    Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology

    2021  Volume 47, Issue 1, Page(s) 405–406

    MeSH term(s) Alzheimer Disease ; Basal Forebrain ; Cholinergic Agents ; Cholinergic Neurons ; Humans
    Chemical Substances Cholinergic Agents
    Language English
    Publishing date 2021-08-13
    Publishing country England
    Document type News ; Research Support, N.I.H., Extramural
    ZDB-ID 639471-1
    ISSN 1740-634X ; 0893-133X
    ISSN (online) 1740-634X
    ISSN 0893-133X
    DOI 10.1038/s41386-021-01135-x
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    Zs.A 2379: Show issues Location:
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  8. Article: Neurofilament Proteins as Biomarkers to Monitor Neurological Diseases and the Efficacy of Therapies.

    Yuan, Aidong / Nixon, Ralph A

    Frontiers in neuroscience

    2021  Volume 15, Page(s) 689938

    Abstract: Biomarkers of neurodegeneration and neuronal injury have the potential to improve diagnostic accuracy, disease monitoring, prognosis, and measure treatment efficacy. Neurofilament proteins (NfPs) are well suited as biomarkers in these contexts because ... ...

    Abstract Biomarkers of neurodegeneration and neuronal injury have the potential to improve diagnostic accuracy, disease monitoring, prognosis, and measure treatment efficacy. Neurofilament proteins (NfPs) are well suited as biomarkers in these contexts because they are major neuron-specific components that maintain structural integrity and are sensitive to neurodegeneration and neuronal injury across a wide range of neurologic diseases. Low levels of NfPs are constantly released from neurons into the extracellular space and ultimately reach the cerebrospinal fluid (CSF) and blood under physiological conditions throughout normal brain development, maturation, and aging. NfP levels in CSF and blood rise above normal in response to neuronal injury and neurodegeneration independently of cause. NfPs in CSF measured by lumbar puncture are about 40-fold more concentrated than in blood in healthy individuals. New ultra-sensitive methods now allow minimally invasive measurement of these low levels of NfPs in serum or plasma to track disease onset and progression in neurological disorders or nervous system injury and assess responses to therapeutic interventions. Any of the five Nf subunits - neurofilament light chain (NfL), neurofilament medium chain (NfM), neurofilament heavy chain (NfH), alpha-internexin (INA) and peripherin (PRPH) may be altered in a given neuropathological condition. In familial and sporadic Alzheimer's disease (AD), plasma NfL levels may rise as early as 22 years before clinical onset in familial AD and 10 years before sporadic AD. The major determinants of elevated levels of NfPs and degradation fragments in CSF and blood are the magnitude of damaged or degenerating axons of fiber tracks, the affected axon caliber sizes and the rate of release of NfP and fragments at different stages of a given neurological disease or condition directly or indirectly affecting central nervous system (CNS) and/or peripheral nervous system (PNS). NfPs are rapidly emerging as transformative blood biomarkers in neurology providing novel insights into a wide range of neurological diseases and advancing clinical trials. Here we summarize the current understanding of intracellular NfP physiology, pathophysiology and extracellular kinetics of NfPs in biofluids and review the value and limitations of NfPs and degradation fragments as biomarkers of neurodegeneration and neuronal injury.
    Language English
    Publishing date 2021-09-27
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2411902-7
    ISSN 1662-453X ; 1662-4548
    ISSN (online) 1662-453X
    ISSN 1662-4548
    DOI 10.3389/fnins.2021.689938
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: New perspectives on lysosomes in ageing and neurodegenerative disease.

    Nixon, Ralph A

    Ageing research reviews

    2016  Volume 32, Page(s) 1

    Language English
    Publishing date 2016
    Publishing country England
    Document type Editorial
    ZDB-ID 2075672-0
    ISSN 1872-9649 ; 1568-1637
    ISSN (online) 1872-9649
    ISSN 1568-1637
    DOI 10.1016/j.arr.2016.11.001
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    Zs.A 5579: Show issues Location:
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  10. Article ; Online: Amyloid precursor protein and endosomal-lysosomal dysfunction in Alzheimer's disease: inseparable partners in a multifactorial disease.

    Nixon, Ralph A

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2017  Volume 31, Issue 7, Page(s) 2729–2743

    Abstract: ... AD arises, progresses, and may be effectively therapeutically targeted.-Nixon, R. A. Amyloid ...

    Abstract Abnormalities of the endosomal-lysosomal network (ELN) are a signature feature of Alzheimer's disease (AD). These include the earliest known cytopathology that is specific to AD and that affects endosomes and induces the progressive failure of lysosomes, each of which are directly linked by distinct mechanisms to neurodegeneration. The origins of ELN dysfunction and β-amyloidogenesis closely overlap, which reflects their common genetic basis, the established early involvement of endosomes and lysosomes in amyloid precursor protein (APP) processing and clearance, and the pathologic effect of certain APP metabolites on ELN functions. Genes that promote β-amyloidogenesis in AD (APP, PSEN1/2, and APOE4) have primary effects on ELN function. The importance of primary ELN dysfunction to pathogenesis is underscored by the mutations in more than 35 ELN-related genes that, thus far, are known to cause familial neurodegenerative diseases even though different pathogenic proteins may be involved. In this article, I discuss growing evidence that implicates AD gene-driven ELN disruptions as not only the antecedent pathobiology that underlies β-amyloidogenesis but also as the essential partner with APP and its metabolites that drive the development of AD, including tauopathy, synaptic dysfunction, and neurodegeneration. The striking amelioration of diverse deficits in animal AD models by remediating ELN dysfunction further supports a need to integrate APP and ELN relationships, including the role of amyloid-β, into a broader conceptual framework of how AD arises, progresses, and may be effectively therapeutically targeted.-Nixon, R. A. Amyloid precursor protein and endosomal-lysosomal dysfunction in Alzheimer's disease: inseparable partners in a multifactorial disease.
    MeSH term(s) Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Endosomes/metabolism ; Endosomes/pathology ; Gene Expression Regulation ; Humans ; Lysosomes/metabolism ; Lysosomes/pathology
    Chemical Substances Amyloid beta-Protein Precursor
    Language English
    Publishing date 2017-06-28
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.201700359
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