LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 91

Search options

  1. Article ; Online: Cofactor molecules: Essential partners for infectious prions.

    Supattapone, Surachai

    Progress in molecular biology and translational science

    2020  Volume 175, Page(s) 53–75

    Abstract: The protein-only hypothesis predicts that infectious mammalian prions are composed solely of ... ...

    Abstract The protein-only hypothesis predicts that infectious mammalian prions are composed solely of PrP
    MeSH term(s) Animals ; Catalysis ; Humans ; Models, Biological ; PrPSc Proteins/metabolism ; Prions/chemistry ; Prions/isolation & purification ; Prions/metabolism ; Prions/pathogenicity
    Chemical Substances PrPSc Proteins ; Prions
    Language English
    Publishing date 2020-08-24
    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.2020.07.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs 357: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Correction: Emergence of Prions Selectively Resistant to Combination Drug Therapy.

    Burke, Cassandra M / Mark, Kenneth M K / Kun, Judit / Beauchemin, Kathryn S / Supattapone, Surachai

    PLoS pathogens

    2024  Volume 20, Issue 1, Page(s) e1011919

    Abstract: This corrects the article DOI: 10.1371/journal.ppat.1008581.]. ...

    Abstract [This corrects the article DOI: 10.1371/journal.ppat.1008581.].
    Language English
    Publishing date 2024-01-08
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011919
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Hydrogen Peroxide-induced Cell Death in Mammalian Cells.

    Chidawanyika, Tamutenda / Supattapone, Surachai

    Journal of cellular signaling

    2020  Volume 2, Issue 3, Page(s) 206–211

    Abstract: Hydrogen peroxide ( ... ...

    Abstract Hydrogen peroxide (H
    Language English
    Publishing date 2020-05-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3040876-3
    ISSN 2692-0638 ; 2692-0638
    ISSN (online) 2692-0638
    ISSN 2692-0638
    DOI 10.33696/signaling.2.052
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Correction

    Cassandra M Burke / Kenneth M K Mark / Judit Kun / Kathryn S Beauchemin / Surachai Supattapone

    PLoS Pathogens, Vol 20, Iss 1, p e

    Emergence of Prions Selectively Resistant to Combination Drug Therapy.

    2024  Volume 1011919

    Abstract: This corrects the article DOI:10.1371/journal.ppat.1008581.]. ...

    Abstract [This corrects the article DOI:10.1371/journal.ppat.1008581.].
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2024-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  5. Article ; Online: Phospholipid cofactor solubilization inhibits formation of native prions.

    Schwind, Abigail M / Walsh, Daniel J / Burke, Cassandra M / Supattapone, Surachai

    Journal of neurochemistry

    2023  Volume 166, Issue 5, Page(s) 875–884

    Abstract: Cofactor molecules are required to generate infectious mammalian prions in vitro. Mouse and hamster prions appear to have different cofactor preferences: Whereas both mouse and hamster prions can use phosphatidylethanolamine (PE) as a prion cofactor, ... ...

    Abstract Cofactor molecules are required to generate infectious mammalian prions in vitro. Mouse and hamster prions appear to have different cofactor preferences: Whereas both mouse and hamster prions can use phosphatidylethanolamine (PE) as a prion cofactor, only hamster prions can also use single-stranded RNA as an alternative cofactor. Here, we investigated the effect of detergent solubilization on rodent prion formation in vitro. We discovered that detergents that can solubilize PE (n-octylglucoside, n-octylgalactoside, and CHAPS) inhibit mouse prion formation in serial protein misfolding cyclic amplification (sPMCA) reactions using bank vole brain homogenate substrate, whereas detergents that are unable to solubilize PE (Triton X-100 and IPEGAL) have no effect. For all three PE-solubilizing detergents, inhibition of RML mouse prion formation was only observed above the critical micellar concentration (CMC). Two other mouse prion strains, Me7 and 301C, were also inhibited by the three PE-solubilizing detergents but not by Triton X-100 or IPEGAL. In contrast, none of the detergents inhibited hamster prion formation in parallel sPMCA reactions using the same bank vole brain homogenate substrate. In reconstituted sPMCA reactions using purified substrates, n-octylglucoside inhibited hamster prion formation when immunopurified bank vole PrP
    MeSH term(s) Cricetinae ; Mice ; Animals ; Prions/metabolism ; Phospholipids ; Octoxynol/pharmacology ; Detergents/pharmacology ; Prion Proteins ; Arvicolinae/genetics ; Arvicolinae/metabolism ; RNA
    Chemical Substances Prions ; Phospholipids ; Octoxynol (9002-93-1) ; Detergents ; Prion Proteins ; RNA (63231-63-0)
    Language English
    Publishing date 2023-08-07
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/jnc.15930
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ui II Zs.170: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Conformational diversity in purified prions produced in vitro.

    Walsh, Daniel J / Schwind, Abigail M / Noble, Geoffrey P / Supattapone, Surachai

    PLoS pathogens

    2023  Volume 19, Issue 1, Page(s) e1011083

    Abstract: Prion diseases are caused by misfolding of either wild-type or mutant forms of the prion protein (PrP) into self-propagating, pathogenic conformers, collectively termed PrPSc. Both wild-type and mutant PrPSc molecules exhibit conformational diversity in ... ...

    Abstract Prion diseases are caused by misfolding of either wild-type or mutant forms of the prion protein (PrP) into self-propagating, pathogenic conformers, collectively termed PrPSc. Both wild-type and mutant PrPSc molecules exhibit conformational diversity in vivo, but purified prions generated by the serial protein misfolding cyclic amplification (sPMCA) technique do not display this same diversity in vitro. This discrepancy has left a gap in our understanding of how conformational diversity arises at the molecular level in both types of prions. Here, we use continuous shaking instead of sPMCA to generate conformationally diverse purified prions in vitro. Using this approach, we show for the first time that wild type prions initially seeded by different native strains can propagate as metastable PrPSc conformers with distinguishable strain properties in purified reactions containing a single active cofactor. Propagation of these metastable PrPSc conformers requires appropriate shaking conditions, and changes in these conditions cause all the different PrPSc conformers to converge irreversibly into the same single conformer as that produced in sPMCA reactions. We also use continuous shaking to show that two mutant PrP molecules with different pathogenic point mutations (D177N and E199K) adopt distinguishable PrPSc conformations in reactions containing pure protein substrate without cofactors. Unlike wild-type prions, the conformations of mutant prions appear to be dictated by substrate sequence rather than seed conformation. Overall, our studies using purified substrates in shaking reactions show that wild-type and mutant prions use fundamentally different mechanisms to generate conformational diversity at the molecular level.
    MeSH term(s) Humans ; Prions/metabolism ; Prion Diseases/metabolism ; Prion Proteins ; Molecular Conformation
    Chemical Substances Prions ; Prion Proteins
    Language English
    Publishing date 2023-01-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011083
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Expanding the prion disease repertoire.

    Supattapone, Surachai

    Proceedings of the National Academy of Sciences of the United States of America

    2015  Volume 112, Issue 38, Page(s) 11748–11749

    MeSH term(s) Animals ; Female ; Humans ; Male ; Multiple System Atrophy/metabolism ; Parkinsonian Disorders/metabolism ; Prions/metabolism ; alpha-Synuclein/metabolism
    Chemical Substances Prions ; alpha-Synuclein
    Language English
    Publishing date 2015-09-22
    Publishing country United States
    Document type Comment ; Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1515143112
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: Synthesis of high titer infectious prions with cofactor molecules.

    Supattapone, Surachai

    The Journal of biological chemistry

    2014  Volume 289, Issue 29, Page(s) 19850–19854

    Abstract: ... Deleault, N. R., Walsh, D. J., Piro, J. R., Wang, F., Wang, X., Ma, J., Rees, J. R., and Supattapone, S ...

    Abstract Recently, synthetic prions with a high level of specific infectivity have been produced from chemically defined components in vitro. A major insight arising from these studies is that various classes of host-encoded cofactor molecules such as phosphatidylethanolamine and RNA molecules are required to form and maintain the specific conformation of infectious prions. Synthetic mouse prions formed with phosphatidylethanolamine exhibit levels of specific infectivity ∼1 million-fold greater than "protein-only" prions (Deleault, N. R., Walsh, D. J., Piro, J. R., Wang, F., Wang, X., Ma, J., Rees, J. R., and Supattapone, S. (2012) Proc. Natl. Acad. Sci. U.S.A. 109, E1938-E1946). Moreover, cofactor molecules also appear to regulate prion strain properties by limiting the potential conformations of the prion protein (see Deleault et al. above). The production of fully infectious synthetic prions provides new opportunities to study the mechanism of prion infectivity directly by structural and biochemical methods.
    MeSH term(s) Animals ; Cricetinae ; Mice ; Phosphatidylethanolamines/chemistry ; PrPSc Proteins/biosynthesis ; PrPSc Proteins/chemistry ; Prion Diseases/etiology ; Prions/biosynthesis ; Prions/chemistry ; Protein Conformation
    Chemical Substances Phosphatidylethanolamines ; PrPSc Proteins ; Prions ; phosphatidylethanolamine (39382-08-6)
    Language English
    Publishing date 2014-05-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.R113.511329
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: Alternating anti-prion regimens reduce combination drug resistance but do not further extend survival in scrapie-infected mice.

    Beauchemin, Kathryn S / Rees, Judy R / Supattapone, Surachai

    The Journal of general virology

    2021  Volume 102, Issue 12

    Abstract: Prion diseases are fatal and infectious neurodegenerative diseases in humans and other mammals caused by templated misfolding of the endogenous prion protein (PrP). Although there is currently no vaccine or therapy against prion disease, several classes ... ...

    Abstract Prion diseases are fatal and infectious neurodegenerative diseases in humans and other mammals caused by templated misfolding of the endogenous prion protein (PrP). Although there is currently no vaccine or therapy against prion disease, several classes of small-molecule compounds have been shown to increase disease-free incubation time in prion-infected mice. An apparent obstacle to effective anti-prion therapy is the emergence of drug-resistant strains during static therapy with either single compounds or multi-drug combination regimens. Here, we treated scrapie-infected mice with dynamic regimens that alternate between different classes of anti-prion drugs. The results show that alternating regimens containing various combinations of Anle138b, IND24 and IND116135 reduce the incidence of combination drug resistance, but do not significantly increase long-term disease-free survival compared to monotherapy. Furthermore, the alternating regimens induced regional vacuolation profiles resembling those generated by a single component of the alternating regimen, suggesting the emergence of strain dominance.
    MeSH term(s) Animals ; Brain/pathology ; Disease Models, Animal ; Disease-Free Survival ; Drug Resistance/drug effects ; Drug Therapy, Combination ; Infectious Disease Incubation Period ; Mice ; Prions/antagonists & inhibitors ; Prions/drug effects ; Scrapie/drug therapy ; Scrapie/mortality ; Scrapie/pathology
    Chemical Substances Prions
    Language English
    Publishing date 2021-12-14
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 219316-4
    ISSN 1465-2099 ; 0022-1317
    ISSN (online) 1465-2099
    ISSN 0022-1317
    DOI 10.1099/jgv.0.001705
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 610: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article ; Online: Conformational diversity in purified prions produced in vitro.

    Daniel J Walsh / Abigail M Schwind / Geoffrey P Noble / Surachai Supattapone

    PLoS Pathogens, Vol 19, Iss 1, p e

    2023  Volume 1011083

    Abstract: Prion diseases are caused by misfolding of either wild-type or mutant forms of the prion protein (PrP) into self-propagating, pathogenic conformers, collectively termed PrPSc. Both wild-type and mutant PrPSc molecules exhibit conformational diversity in ... ...

    Abstract Prion diseases are caused by misfolding of either wild-type or mutant forms of the prion protein (PrP) into self-propagating, pathogenic conformers, collectively termed PrPSc. Both wild-type and mutant PrPSc molecules exhibit conformational diversity in vivo, but purified prions generated by the serial protein misfolding cyclic amplification (sPMCA) technique do not display this same diversity in vitro. This discrepancy has left a gap in our understanding of how conformational diversity arises at the molecular level in both types of prions. Here, we use continuous shaking instead of sPMCA to generate conformationally diverse purified prions in vitro. Using this approach, we show for the first time that wild type prions initially seeded by different native strains can propagate as metastable PrPSc conformers with distinguishable strain properties in purified reactions containing a single active cofactor. Propagation of these metastable PrPSc conformers requires appropriate shaking conditions, and changes in these conditions cause all the different PrPSc conformers to converge irreversibly into the same single conformer as that produced in sPMCA reactions. We also use continuous shaking to show that two mutant PrP molecules with different pathogenic point mutations (D177N and E199K) adopt distinguishable PrPSc conformations in reactions containing pure protein substrate without cofactors. Unlike wild-type prions, the conformations of mutant prions appear to be dictated by substrate sequence rather than seed conformation. Overall, our studies using purified substrates in shaking reactions show that wild-type and mutant prions use fundamentally different mechanisms to generate conformational diversity at the molecular level.
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2023-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top