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  1. Book: Prion proteins

    Caughey, Byron

    (Advances in protein chemistry ; 57)

    2001  

    Author's details ed. by Byron Caughey
    Series title Advances in protein chemistry ; 57
    Collection
    Keywords Prionprotein
    Subject Prion-Protein
    Language English
    Size XIII, 405 S. : Ill., graph. Darst.
    Publisher Academic Press
    Publishing place San Diego u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT013105011
    ISBN 0-12-034257-X ; 978-0-12-034257-0
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Uc I Zs 241 -57- verfügbar in Königswinter Königswinter

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  2. Article ; Online: RT-QuIC and Related Assays for Detecting and Quantifying Prion-like Pathological Seeds of α-Synuclein.

    Srivastava, Ankit / Alam, Parvez / Caughey, Byron

    Biomolecules

    2022  Volume 12, Issue 4

    Abstract: Various disease-associated forms or strains of α-synuclein ( ... ...

    Abstract Various disease-associated forms or strains of α-synuclein (αSyn
    MeSH term(s) Humans ; Lewy Body Disease/diagnosis ; Lewy Body Disease/metabolism ; Multiple System Atrophy ; Parkinson Disease/diagnosis ; Parkinson Disease/metabolism ; Prions ; Synucleinopathies/diagnosis ; alpha-Synuclein/metabolism
    Chemical Substances Prions ; alpha-Synuclein
    Language English
    Publishing date 2022-04-14
    Publishing country Switzerland
    Document type Journal Article ; Review ; Research Support, N.I.H., Intramural
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom12040576
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Real-Time Quaking- Induced Conversion Assays for Prion Diseases, Synucleinopathies, and Tauopathies.

    Vascellari, Sarah / Orrù, Christina D / Caughey, Byron

    Frontiers in aging neuroscience

    2022  Volume 14, Page(s) 853050

    Abstract: Prion diseases, synucleinopathies and tauopathies are neurodegenerative disorders characterized by deposition of abnormal protein aggregates in brain and other tissues. These aggregates consist ... ...

    Abstract Prion diseases, synucleinopathies and tauopathies are neurodegenerative disorders characterized by deposition of abnormal protein aggregates in brain and other tissues. These aggregates consist of
    Language English
    Publishing date 2022-03-10
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2558898-9
    ISSN 1663-4365
    ISSN 1663-4365
    DOI 10.3389/fnagi.2022.853050
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  4. Article ; Online: Structural biology of ex vivo mammalian prions.

    Artikis, Efrosini / Kraus, Allison / Caughey, Byron

    The Journal of biological chemistry

    2022  Volume 298, Issue 8, Page(s) 102181

    Abstract: The structures of prion protein (PrP)-based mammalian prions have long been elusive. However, cryo-EM has begun to reveal the near-atomic resolution structures of fully infectious ex vivo mammalian prion fibrils as well as relatively innocuous synthetic ... ...

    Abstract The structures of prion protein (PrP)-based mammalian prions have long been elusive. However, cryo-EM has begun to reveal the near-atomic resolution structures of fully infectious ex vivo mammalian prion fibrils as well as relatively innocuous synthetic PrP amyloids. Comparisons of these various types of PrP fibrils are now providing initial clues to structural features that correlate with pathogenicity. As first indicated by electron paramagnetic resonance and solid-state NMR studies of synthetic amyloids, all sufficiently resolved PrP fibrils of any sort (n > 10) have parallel in-register intermolecular β-stack architectures. Cryo-EM has shown that infectious brain-derived prion fibrils of the rodent-adapted 263K and RML scrapie strains have much larger ordered cores than the synthetic fibrils. These bona fide prion strains share major structural motifs, but the conformational details and the overall shape of the fibril cross sections differ markedly. Such motif variations, as well as differences in sequence within the ordered polypeptide cores, likely contribute to strain-dependent templating. When present, N-linked glycans and glycophosphatidylinositol (GPI) anchors project outward from the fibril surface. For the mouse RML strain, these posttranslational modifications have little effect on the core structure. In the GPI-anchored prion structures, a linear array of GPI anchors along the twisting fibril axis appears likely to bind membranes in vivo, and as such, may account for pathognomonic membrane distortions seen in prion diseases. In this review, we focus on these infectious prion structures and their implications regarding prion replication mechanisms, strains, transmission barriers, and molecular pathogenesis.
    MeSH term(s) Amyloid/chemistry ; Animals ; Biology ; Mammals/metabolism ; Mice ; Prion Diseases/metabolism ; Prion Proteins ; Prions/metabolism ; Scrapie/metabolism ; Sheep
    Chemical Substances Amyloid ; Prion Proteins ; Prions
    Language English
    Publishing date 2022-06-23
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2022.102181
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Proteopathic Seed Amplification Assays for Neurodegenerative Disorders.

    Ferreira, Natália do Carmo / Caughey, Byron

    Clinics in laboratory medicine

    2020  Volume 40, Issue 3, Page(s) 257–270

    Abstract: The need for etiological biomarkers for neurodegenerative diseases involving protein aggregation has prompted development of ultrasensitive cellular and cell-free assays based on the prion-like seeding capacity of such aggregates. Among them, prion RT- ... ...

    Abstract The need for etiological biomarkers for neurodegenerative diseases involving protein aggregation has prompted development of ultrasensitive cellular and cell-free assays based on the prion-like seeding capacity of such aggregates. Among them, prion RT-QuIC assays allow accurate antemortem Creutzfeldt-Jakob disease diagnosis using cerebrospinal fluid and nasal brushings. Analogous assays for synucleinopathies (e.g., Parkinson disease and dementia with Lewy bodies) provide unprecedented diagnostic sensitivity using cerebrospinal fluid. Biosensor cell and tau RT-QuIC assays can detect and discriminate tau aggregates associated with multiple tauopathies (e.g., Alzheimer disease and frontotemporal degeneration). An expanding panel of seed amplification assays should improve diagnostics and therapeutics development.
    MeSH term(s) Amyloid/analysis ; Amyloid/metabolism ; Animals ; Cell Line ; Cells, Cultured ; Cytological Techniques ; Humans ; Mice ; Molecular Diagnostic Techniques ; Neurodegenerative Diseases/diagnosis ; Neurodegenerative Diseases/physiopathology ; Protein Aggregation, Pathological ; Sensitivity and Specificity ; tau Proteins/analysis ; tau Proteins/metabolism
    Chemical Substances Amyloid ; tau Proteins
    Language English
    Publishing date 2020-06-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 604580-7
    ISSN 1557-9832 ; 0272-2712
    ISSN (online) 1557-9832
    ISSN 0272-2712
    DOI 10.1016/j.cll.2020.04.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1695: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates.

    Caughey, Byron / Kraus, Allison

    Viruses

    2019  Volume 11, Issue 11

    Abstract: The prion-like spreading and accumulation of specific protein aggregates appear to be central to the pathogenesis of many human diseases, including Alzheimer's and Parkinson's. Accumulating evidence indicates that inoculation of tissue extracts from ... ...

    Abstract The prion-like spreading and accumulation of specific protein aggregates appear to be central to the pathogenesis of many human diseases, including Alzheimer's and Parkinson's. Accumulating evidence indicates that inoculation of tissue extracts from diseased individuals into suitable experimental animals can in many cases induce the aggregation of the disease-associated protein, as well as related pathological lesions. These findings, together with the history of the prion field, have raised the questions about whether such disease-associated protein aggregates are transmissible between humans by casual or iatrogenic routes, and, if so, do they propagate enough in the new host to cause disease? These practical considerations are important because real, and perhaps even only imagined, risks of human-to-human transmission of diseases such as Alzheimer's and Parkinson's may force costly changes in clinical practice that, in turn, are likely to have unintended consequences. The prion field has taught us that a single protein, PrP, can aggregate into forms that can propagate exponentially in vitro, but range from being innocuous to deadly when injected into experimental animals in ways that depend strongly on factors such as conformational subtleties, routes of inoculation, and host responses. In assessing the hazards posed by various disease-associated, self-propagating protein aggregates, it is imperative to consider both their actual transmissibilities and the pathological consequences of their propagation, if any, in recipient hosts.
    MeSH term(s) Alzheimer Disease/etiology ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid/chemistry ; Amyloid/metabolism ; Animals ; Humans ; Membrane Proteins/metabolism ; Parkinson Disease/etiology ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Prion Diseases/transmission ; Prions/metabolism ; Prions/pathogenicity ; Protein Aggregates ; Protein Folding ; Scrapie/etiology ; Scrapie/metabolism ; Synucleins/metabolism ; Virulence
    Chemical Substances Amyloid ; Membrane Proteins ; Prions ; Protein Aggregates ; Synucleins ; tau 40 protein, human
    Language English
    Publishing date 2019-11-09
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v11111044
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates

    Caughey, Byron / Kraus, Allison

    Viruses. 2019 Nov. 09, v. 11, no. 11

    2019  

    Abstract: The prion-like spreading and accumulation of specific protein aggregates appear to be central to the pathogenesis of many human diseases, including Alzheimer’s and Parkinson’s. Accumulating evidence indicates that inoculation of tissue extracts from ... ...

    Abstract The prion-like spreading and accumulation of specific protein aggregates appear to be central to the pathogenesis of many human diseases, including Alzheimer’s and Parkinson’s. Accumulating evidence indicates that inoculation of tissue extracts from diseased individuals into suitable experimental animals can in many cases induce the aggregation of the disease-associated protein, as well as related pathological lesions. These findings, together with the history of the prion field, have raised the questions about whether such disease-associated protein aggregates are transmissible between humans by casual or iatrogenic routes, and, if so, do they propagate enough in the new host to cause disease? These practical considerations are important because real, and perhaps even only imagined, risks of human-to-human transmission of diseases such as Alzheimer’s and Parkinson’s may force costly changes in clinical practice that, in turn, are likely to have unintended consequences. The prion field has taught us that a single protein, PrP, can aggregate into forms that can propagate exponentially in vitro, but range from being innocuous to deadly when injected into experimental animals in ways that depend strongly on factors such as conformational subtleties, routes of inoculation, and host responses. In assessing the hazards posed by various disease-associated, self-propagating protein aggregates, it is imperative to consider both their actual transmissibilities and the pathological consequences of their propagation, if any, in recipient hosts.
    Keywords disease transmission ; hosts ; human diseases ; humans ; laboratory animals ; pathogenesis ; pathogenicity ; prions ; protein aggregates
    Language English
    Dates of publication 2019-1109
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v11111044
    Database NAL-Catalogue (AGRICOLA)

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  8. Article ; Online: Pathogenic prion structures at high resolution.

    Caughey, Byron / Standke, Heidi G / Artikis, Efrosini / Hoyt, Forrest / Kraus, Allison

    PLoS pathogens

    2022  Volume 18, Issue 6, Page(s) e1010594

    MeSH term(s) Humans ; PrPSc Proteins/chemistry ; Prion Diseases ; Prions/chemistry
    Chemical Substances PrPSc Proteins ; Prions
    Language English
    Publishing date 2022-06-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1010594
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Sensitive detection of pathological seeds of α-synuclein, tau and prion protein on solid surfaces.

    Orrú, Christina D / Groveman, Bradley R / Hughson, Andrew G / Barrio, Tomás / Isiofia, Kachi / Race, Brent / Ferreira, Natalia C / Gambetti, Pierluigi / Schneider, David A / Masujin, Kentaro / Miyazawa, Kohtaro / Ghetti, Bernardino / Zanusso, Gianluigi / Caughey, Byron

    PLoS pathogens

    2024  Volume 20, Issue 4, Page(s) e1012175

    Abstract: Prions or prion-like aggregates such as those composed of PrP, α-synuclein, and tau are key features of proteinopathies such as prion, Parkinson's and Alzheimer's diseases, respectively. Their presence on solid surfaces may be biohazardous under some ... ...

    Abstract Prions or prion-like aggregates such as those composed of PrP, α-synuclein, and tau are key features of proteinopathies such as prion, Parkinson's and Alzheimer's diseases, respectively. Their presence on solid surfaces may be biohazardous under some circumstances. PrP prions bound to solids are detectable by ultrasensitive real-time quaking-induced conversion (RT-QuIC) assays if the solids can be immersed in assay wells or the prions transferred to pads. Here we show that prion-like seeds can remain detectable on steel wires for at least a year, or even after enzymatic cleaning and sterilization. We also show that contamination of larger objects with pathological seeds of α-synuclein, tau, and PrP can be detected by simply assaying a sampling medium that has been transiently applied to the surface. Human α-synuclein seeds in dementia with Lewy bodies brain tissue were detected by α-synuclein RT-QuIC after drying of tissue dilutions with concentrations as low as 10-6 onto stainless steel. Tau RT-QuIC detected tau seeding activity on steel exposed to Alzheimer's disease brain tissue diluted as much as a billion fold. Prion RT-QuIC assays detected seeding activity on plates exposed to brain dilutions as extreme as 10-5-10-8 from prion-affected humans, sheep, cattle and cervids. Sampling medium collected from surgical instruments used in necropsies of sporadic Creutzfeldt-Jakob disease-infected transgenic mice was positive down to 10-6 dilution. Sensitivity for prion detection was not sacrificed by omitting the recombinant PrP substrate from the sampling medium during its application to a surface and subsequent storage as long as the substrate was added prior to performing the assay reaction. Our findings demonstrate practical prototypic surface RT-QuIC protocols for the highly sensitive detection of pathologic seeds of α-synuclein, tau, and PrP on solid objects.
    MeSH term(s) tau Proteins/metabolism ; alpha-Synuclein/metabolism ; alpha-Synuclein/analysis ; Humans ; Prion Proteins/metabolism ; Animals ; Mice ; Brain/metabolism ; Brain/pathology ; Prions/metabolism ; Lewy Body Disease/metabolism
    Chemical Substances tau Proteins ; alpha-Synuclein ; Prion Proteins ; Prions
    Language English
    Publishing date 2024-04-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1012175
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Accommodation of In-Register N-Linked Glycans on Prion Protein Amyloid Cores.

    Artikis, Efrosini / Roy, Amitava / Verli, Hugo / Cordeiro, Yraima / Caughey, Byron

    ACS chemical neuroscience

    2020  Volume 11, Issue 24, Page(s) 4092–4097

    Abstract: Although prion protein fibrils can have either parallel-in-register intermolecular β-sheet (PIRIBS) or, probably, β-solenoid architectures, the plausibility of PIRIBS architectures for the usually glycosylated natural prion strains has been questioned ... ...

    Abstract Although prion protein fibrils can have either parallel-in-register intermolecular β-sheet (PIRIBS) or, probably, β-solenoid architectures, the plausibility of PIRIBS architectures for the usually glycosylated natural prion strains has been questioned based the expectation that such glycans would not fit if stacked in-register on each monomer within a fibril. To directly assess this issue, we have added N-linked glycans to a recently reported cryo-electron microscopy-based human prion protein amyloid model with a PIRIBS architecture and performed
    MeSH term(s) Amyloid ; Cryoelectron Microscopy ; Humans ; Polysaccharides ; Prion Proteins/genetics ; Prions
    Chemical Substances Amyloid ; Polysaccharides ; Prion Proteins ; Prions
    Language English
    Publishing date 2020-11-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ISSN 1948-7193
    ISSN (online) 1948-7193
    DOI 10.1021/acschemneuro.0c00635
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