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  1. Article ; Online: The Intractable Puzzle of Sporadic Creutzfeldt-Jakob Disease in Very Young People.

    Mead, Simon

    Neurology

    2021  Volume 97, Issue 17, Page(s) 801–802

    MeSH term(s) Adolescent ; Creutzfeldt-Jakob Syndrome/diagnostic imaging ; Creutzfeldt-Jakob Syndrome/epidemiology ; Humans
    Language English
    Publishing date 2021-09-08
    Publishing country United States
    Document type Editorial ; Comment
    ZDB-ID 207147-2
    ISSN 1526-632X ; 0028-3878
    ISSN (online) 1526-632X
    ISSN 0028-3878
    DOI 10.1212/WNL.0000000000012739
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  2. Article ; Online: Marked abnormalities of plasma protein biomarkers in Creutzfeldt-Jakob disease (CJD).

    Mead, Simon

    Journal of neurology, neurosurgery, and psychiatry

    2020  Volume 91, Issue 11, Page(s) 1137

    MeSH term(s) Biomarkers ; Blood Proteins ; Creutzfeldt-Jakob Syndrome/diagnosis ; Early Diagnosis ; Humans ; Plasma ; Prion Diseases
    Chemical Substances Biomarkers ; Blood Proteins
    Language English
    Publishing date 2020-09-14
    Publishing country England
    Document type Editorial ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 3087-9
    ISSN 1468-330X ; 0022-3050
    ISSN (online) 1468-330X
    ISSN 0022-3050
    DOI 10.1136/jnnp-2020-324307
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  3. Article ; Online: Lecanemab slows Alzheimer's disease: hope and challenges.

    Mead, Simon / Fox, Nick C

    The Lancet. Neurology

    2023  Volume 22, Issue 2, Page(s) 106–108

    MeSH term(s) Humans ; Alzheimer Disease/drug therapy ; Neurons
    Chemical Substances lecanemab (12PYH0FTU9)
    Language English
    Publishing date 2023-01-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 2081241-3
    ISSN 1474-4465 ; 1474-4422
    ISSN (online) 1474-4465
    ISSN 1474-4422
    DOI 10.1016/S1474-4422(22)00529-4
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  4. Article: The Future of Seed Amplification Assays and Clinical Trials.

    Coysh, Thomas / Mead, Simon

    Frontiers in aging neuroscience

    2022  Volume 14, Page(s) 872629

    Abstract: Prion-like seeded misfolding of host proteins is the leading hypothesised cause of neurodegenerative diseases. The exploitation of the mechanism in the protein misfolding cyclic amplification (PMCA) and real-time quaking-induced conversion (RT-QuIC) ... ...

    Abstract Prion-like seeded misfolding of host proteins is the leading hypothesised cause of neurodegenerative diseases. The exploitation of the mechanism in the protein misfolding cyclic amplification (PMCA) and real-time quaking-induced conversion (RT-QuIC) assays have transformed prion disease research and diagnosis and have steadily become more widely used for research into other neurodegenerative disorders. Clinical trials in adult neurodegenerative diseases have been expensive, slow, and disappointing in terms of clinical benefits. There are various possible factors contributing to the failure to identify disease-modifying treatments for adult neurodegenerative diseases, some of which include: limited accuracy of antemortem clinical diagnosis resulting in the inclusion of patients with the "incorrect" pathology for the therapeutic; the role of co-pathologies in neurodegeneration rendering treatments targeting one pathology alone ineffective; treatment of the primary neurodegenerative process too late, after irreversible secondary processes of neurodegeneration have become established or neuronal loss is already extensive; and preclinical models used to develop treatments not accurately representing human disease. The use of seed amplification assays in clinical trials offers an opportunity to tackle these problems by sensitively detecting
    Language English
    Publishing date 2022-06-22
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2558898-9
    ISSN 1663-4365
    ISSN 1663-4365
    DOI 10.3389/fnagi.2022.872629
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  5. Article ; Online: Gene expression and epigenetic markers of prion diseases.

    Viré, Emmanuelle A / Mead, Simon

    Cell and tissue research

    2022  Volume 392, Issue 1, Page(s) 285–294

    Abstract: Epigenetics, meaning the variety of mechanisms underpinning gene regulation and chromatin states, plays a key role in normal development as well as in disease initiation and progression. Epigenetic mechanisms like alteration of DNA methylation, histone ... ...

    Abstract Epigenetics, meaning the variety of mechanisms underpinning gene regulation and chromatin states, plays a key role in normal development as well as in disease initiation and progression. Epigenetic mechanisms like alteration of DNA methylation, histone modifications, and non-coding RNAs, have been proposed as biomarkers for diagnosis, classification, or monitoring of responsiveness to treatment in many diseases. In prion diseases, the profound associations with human aging, the effects of cell type and differentiation on in vitro susceptibility, and recently identified human risk factors, all implicate causal epigenetic mechanisms. Here, we review the current state of the art of epigenetics in prion diseases and its interaction with genetic determinants. In particular, we will review recent advances made by several groups in the field profiling DNA methylation and microRNA expression in mammalian prion diseases and the potential for these discoveries to be exploited as biomarkers.
    MeSH term(s) Animals ; Humans ; Epigenesis, Genetic ; DNA Methylation/genetics ; Biomarkers ; Prion Diseases/genetics ; Gene Expression ; Mammals/genetics
    Chemical Substances Biomarkers
    Language English
    Publishing date 2022-03-21
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 125067-x
    ISSN 1432-0878 ; 0302-766X
    ISSN (online) 1432-0878
    ISSN 0302-766X
    DOI 10.1007/s00441-022-03603-2
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  6. Article ; Online: Safe laboratory management of prions and proteopathic seeds.

    Mead, Simon / Evans, Thomas

    The Lancet. Neurology

    2021  Volume 20, Issue 12, Page(s) 981

    MeSH term(s) Alzheimer Disease ; Humans ; Prions ; tau Proteins
    Chemical Substances Prions ; tau Proteins
    Language English
    Publishing date 2021-11-19
    Publishing country England
    Document type Letter
    ZDB-ID 2081241-3
    ISSN 1474-4465 ; 1474-4422
    ISSN (online) 1474-4465
    ISSN 1474-4422
    DOI 10.1016/S1474-4422(21)00379-3
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  7. Article ; Online: Creutzfeldt-Jakob disease and other prion diseases.

    Zerr, Inga / Ladogana, Anna / Mead, Simon / Hermann, Peter / Forloni, Gianluigi / Appleby, Brian S

    Nature reviews. Disease primers

    2024  Volume 10, Issue 1, Page(s) 14

    Abstract: Prion diseases share common clinical and pathological characteristics such as spongiform neuronal degeneration and deposition of an abnormal form of a host-derived protein, termed prion protein. The characteristic features of prion diseases are long ... ...

    Abstract Prion diseases share common clinical and pathological characteristics such as spongiform neuronal degeneration and deposition of an abnormal form of a host-derived protein, termed prion protein. The characteristic features of prion diseases are long incubation times, short clinical courses, extreme resistance of the transmissible agent to degradation and lack of nucleic acid involvement. Sporadic and genetic forms of prion diseases occur worldwide, of which genetic forms are associated with mutations in PRNP. Human to human transmission of these diseases has occurred due to iatrogenic exposure, and zoonotic forms of prion diseases are linked to bovine disease. Significant progress has been made in the diagnosis of these disorders. Clinical tools for diagnosis comprise brain imaging and cerebrospinal fluid tests. Aggregation assays for detection of the abnormally folded prion protein have a clear potential to diagnose the disease in peripherally accessible biofluids. After decades of therapeutic nihilism, new treatment strategies and clinical trials are on the horizon. Although prion diseases are relatively rare disorders, understanding their pathogenesis and mechanisms of prion protein misfolding has significantly enhanced the field in research of neurodegenerative diseases.
    MeSH term(s) Animals ; Cattle ; Humans ; Creutzfeldt-Jakob Syndrome/diagnosis ; Creutzfeldt-Jakob Syndrome/genetics ; Creutzfeldt-Jakob Syndrome/pathology ; Prion Proteins/metabolism ; Prion Diseases/diagnosis ; Prion Diseases/genetics ; Prion Diseases/metabolism ; Brain/pathology
    Chemical Substances Prion Proteins
    Language English
    Publishing date 2024-02-29
    Publishing country England
    Document type Journal Article ; Review
    ISSN 2056-676X
    ISSN (online) 2056-676X
    DOI 10.1038/s41572-024-00497-y
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  8. Article ; Online: Preclinical biomarkers of prion infection and neurodegeneration.

    Mok, Tze How / Mead, Simon

    Current opinion in neurobiology

    2020  Volume 61, Page(s) 82–88

    Abstract: Therapeutic strategies and study designs for neurodegenerative diseases have started to explore the potential of preventive treatment in healthy people, emphasising characterisation of biomarkers capable of indicating proximity to clinical onset. This ... ...

    Abstract Therapeutic strategies and study designs for neurodegenerative diseases have started to explore the potential of preventive treatment in healthy people, emphasising characterisation of biomarkers capable of indicating proximity to clinical onset. This need is even more pressing for individuals at risk of prion disease given its rarity which virtually precludes the probability of recruiting enough numbers for well powered preventive trials based on clinical endpoints. Experimental mouse inoculation studies have revealed a rapid exponential rise in infectious titres followed by a relative plateau of considerable duration before clinical onset. This clinically silent incubation period represents a potential window of opportunity for the adaptation of ultrasensitive prion seeding assays to define the onset of prion infection, and for neurodegenerative biomarker discovery through similarly sensitive digital immunoassay platforms.
    MeSH term(s) Animals ; Biomarkers ; Prion Diseases ; Prions/analysis
    Chemical Substances Biomarkers ; Prions
    Language English
    Publishing date 2020-02-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1078046-4
    ISSN 1873-6882 ; 0959-4388
    ISSN (online) 1873-6882
    ISSN 0959-4388
    DOI 10.1016/j.conb.2020.01.009
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  9. Article ; Online: Genetic risk factors for Creutzfeldt-Jakob disease.

    Jones, Emma / Mead, Simon

    Neurobiology of disease

    2020  Volume 142, Page(s) 104973

    Abstract: Prion diseases are a group of fatal neurodegenerative disorders of mammals that share a central role for prion protein (PrP, gene PRNP) in their pathogenesis. Prions are infectious agents that account for the observed transmission of prion diseases ... ...

    Abstract Prion diseases are a group of fatal neurodegenerative disorders of mammals that share a central role for prion protein (PrP, gene PRNP) in their pathogenesis. Prions are infectious agents that account for the observed transmission of prion diseases between humans and animals in certain circumstances. The prion mechanism invokes a misfolded and multimeric assembly of PrP (a prion) that grows by templating of the normal protein and propagates by fission. Aside from the medical and public health notoriety of acquired prion diseases, the conditions have attracted interest as it has been realized that common neurodegenerative disorders share so-called prion-like mechanisms. In this article we will expand on recent evidence for new genetic loci that alter the risk of human prion disease. The most common human prion disease, sporadic Creutzfeldt-Jakob disease (sCJD), is characterized by the seemingly spontaneous appearance of prions in the brain. Genetic variation within PRNP is associated with all types of prion diseases, in particular, heterozygous genotypes at codons 129 and 219 have long been known to be strong protective factors against sCJD. A large number of rare mutations have been described in PRNP that cause autosomal dominant inherited prion diseases. Two loci recently identified by genome-wide association study increase sCJD risk, including variants in or near to STX6 and GAL3ST1. STX6 encodes syntaxin-6, a component of SNARE complexes with cellular roles that include the fusion of intracellular vesicles with target membranes. GAL3ST1 encodes cerebroside sulfotransferase, the only enzyme that sulfates sphingolipids to make sulfatides, a major lipid component of myelin. We discuss how these roles may modify the pathogenesis of prion diseases and their relevance for other neurodegenerative disorders.
    Language English
    Publishing date 2020-06-18
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1211786-9
    ISSN 1095-953X ; 0969-9961
    ISSN (online) 1095-953X
    ISSN 0969-9961
    DOI 10.1016/j.nbd.2020.104973
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  10. Article ; Online: Detection of Creutzfeldt-Jakob disease prions in skin: implications for healthcare.

    Nihat, Akin / Mead, Simon

    Genome medicine

    2018  Volume 10, Issue 1, Page(s) 22

    Abstract: Evidence has recently been reported of prion seeding activity in skin tissue from patients with sporadic Creutzfeldt-Jakob disease (sCJD). This is relevant information for infection control measures during surgery. The work uses very sensitive prion ... ...

    Abstract Evidence has recently been reported of prion seeding activity in skin tissue from patients with sporadic Creutzfeldt-Jakob disease (sCJD). This is relevant information for infection control measures during surgery. The work uses very sensitive prion assays now available for medical research, and may soon be adapted to related neurodegenerative disorders.
    MeSH term(s) Creutzfeldt-Jakob Syndrome/diagnosis ; Creutzfeldt-Jakob Syndrome/prevention & control ; Delivery of Health Care ; Humans ; Prions/metabolism ; Skin/metabolism ; Skin/pathology
    Chemical Substances Prions
    Language English
    Publishing date 2018-03-26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2484394-5
    ISSN 1756-994X ; 1756-994X
    ISSN (online) 1756-994X
    ISSN 1756-994X
    DOI 10.1186/s13073-018-0536-3
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