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  1. Article ; Online: Antiprion systems in yeast cooperate to cure or prevent the generation of nearly all [

    Son, Moonil / Wickner, Reed B

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

    2022  Volume 119, Issue 28, Page(s) e2205500119

    Abstract: ...

    Abstract [
    MeSH term(s) Amyloidogenic Proteins ; Amyloidosis ; Heat-Shock Proteins/metabolism ; Prions/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Amyloidogenic Proteins ; Heat-Shock Proteins ; Prions ; Saccharomyces cerevisiae Proteins ; HsP104 protein, S cerevisiae (143012-44-6)
    Language English
    Publishing date 2022-07-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2205500119
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  2. Article ; Online: Genomic fold of a "naked" ssRNA virus is critical for stability and propagation.

    Fujimura, Tsutomu / Esteban, Rosa / Wickner, Reed B

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

    2023  Volume 120, Issue 30, Page(s) e2309329120

    MeSH term(s) RNA, Viral/genetics ; Genomics
    Chemical Substances RNA, Viral
    Language English
    Publishing date 2023-07-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2309329120
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  3. Article ; Online: Anti-prion systems in yeast.

    Wickner, Reed B

    The Journal of biological chemistry

    2019  Volume 294, Issue 5, Page(s) 1729–1738

    Abstract: Yeast prions have become important models for the study of the basic mechanisms underlying human amyloid diseases. Yeast prions are pathogenic (unlike the [Het-s] prion ... ...

    Abstract Yeast prions have become important models for the study of the basic mechanisms underlying human amyloid diseases. Yeast prions are pathogenic (unlike the [Het-s] prion of
    MeSH term(s) Humans ; Prions/antagonists & inhibitors ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Prions ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2019-02-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.TM118.004168
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  4. Article ; Online: Anti-Prion Systems in

    Son, Moonil / Wickner, Reed B

    Viruses

    2022  Volume 14, Issue 9

    Abstract: Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein. These prions arise spontaneously in the cell without known reason, and their ... ...

    Abstract Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein. These prions arise spontaneously in the cell without known reason, and their effects were generally considered to be fatal based on prion diseases in humans or mammals. However, the wide array of prion studies in yeast including filamentous fungi revealed that their effects can range widely, from lethal to very mild (even cryptic) or functional, depending on the nature of the prion protein and the specific prion variant (or strain) made by the same prion protein but with a different conformation. This prion biology is affected by an array of molecular chaperone systems, such as Hsp40, Hsp70, Hsp104, and combinations of them. In parallel with the systems required for prion propagation, yeast has multiple anti-prion systems, constantly working in the normal cell without overproduction of or a deficiency in any protein, which have negative effects on prions by blocking their formation, curing many prions after they arise, preventing prion infections, and reducing the cytotoxicity produced by prions. From the protectors of nascent polypeptides (Ssb1/2p, Zuo1p, and Ssz1p) to the protein sequesterase (Btn2p), the disaggregator (Hsp104), and the mysterious Cur1p, normal levels of each can cure the prion variants arising in its absence. The controllers of mRNA quality, nonsense-mediated mRNA decay proteins (Upf1, 2, 3), can cure newly formed prion variants by association with a prion-forming protein. The regulator of the inositol pyrophosphate metabolic pathway (Siw14p) cures certain prion variants by lowering the levels of certain organic compounds. Some of these proteins have other cellular functions (e.g., Btn2), while others produce an anti-prion effect through their primary role in the normal cell (e.g., ribosomal chaperones). Thus, these anti-prion actions are the innate defense strategy against prions. Here, we outline the anti-prion systems in yeast that produce innate immunity to prions by a multi-layered operation targeting each step of prion development.
    MeSH term(s) Diphosphates/metabolism ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Humans ; Inositol/metabolism ; Molecular Chaperones/metabolism ; Polymers/metabolism ; Prion Proteins/metabolism ; Prions/chemistry ; RNA Helicases/metabolism ; RNA, Messenger/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Trans-Activators/metabolism
    Chemical Substances Diphosphates ; Heat-Shock Proteins ; Molecular Chaperones ; Polymers ; Prion Proteins ; Prions ; RNA, Messenger ; Saccharomyces cerevisiae Proteins ; Trans-Activators ; HsP104 protein, S cerevisiae (143012-44-6) ; Inositol (4L6452S749) ; RNA Helicases (EC 3.6.4.13) ; UPF1 protein, human (EC 3.6.4.13)
    Language English
    Publishing date 2022-09-01
    Publishing country Switzerland
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14091945
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Human proteins curing yeast prions.

    Wu, Songsong / Edskes, Herman K / Wickner, Reed B

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

    2023  Volume 120, Issue 45, Page(s) e2314781120

    Abstract: Recognition that common human amyloidoses are prion diseases makes the use of ... ...

    Abstract Recognition that common human amyloidoses are prion diseases makes the use of the
    MeSH term(s) Animals ; Humans ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Prions/genetics ; Prions/metabolism ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Mutation ; Amyloid/genetics ; Amyloid/metabolism ; Glutathione Peroxidase/genetics ; Glutathione Peroxidase/metabolism ; Fungal Proteins/metabolism ; Mammals/metabolism ; RNA Splicing Factors/genetics ; Nuclear Proteins/metabolism ; DNA Repair Enzymes/genetics
    Chemical Substances Saccharomyces cerevisiae Proteins ; Prions ; HSP70 Heat-Shock Proteins ; Amyloid ; Glutathione Peroxidase (EC 1.11.1.9) ; Fungal Proteins ; PRPF19 protein, human (EC 6.5.1.-) ; RNA Splicing Factors ; Nuclear Proteins ; DNA Repair Enzymes (EC 6.5.1.-)
    Language English
    Publishing date 2023-10-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2314781120
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  6. Article ; Online: Prions are the greatest protein misfolding problem, and yeast has several solutions.

    Wickner, Reed B / Edskes, Herman K / Wu, Songsong / Gregg, Kristen

    PLoS pathogens

    2023  Volume 19, Issue 5, Page(s) e1011333

    MeSH term(s) Saccharomyces cerevisiae/metabolism ; Prions/metabolism ; Protein Folding ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Prions ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2023-05-04
    Publishing country United States
    Document type Journal Article ; 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.1011333
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  7. Article ; Online: Genetics is the logic of life (at least of mine).

    Wickner, Reed B

    FEMS yeast research

    2018  Volume 19, Issue 1

    Abstract: I retrace my path from math to medicine to biochemistry to yeast genetics, my focus on infectious diseases of yeast and finally prions. My discovery of yeast prions relied on my particular focus on the logical relations of non-chromosomal genetic ... ...

    Abstract I retrace my path from math to medicine to biochemistry to yeast genetics, my focus on infectious diseases of yeast and finally prions. My discovery of yeast prions relied on my particular focus on the logical relations of non-chromosomal genetic elements and the chromosomal genes involved in their propagation and expression. Pursuing an understanding of yeast prions involved structural biology based on genetics, solid-state NMR, population genetics and more genetics.
    MeSH term(s) Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Genetics, Microbial/trends ; History, 20th Century ; History, 21st Century ; Molecular Biology/trends ; Prions/chemistry ; Prions/metabolism ; Protein Folding ; Yeasts/genetics ; Yeasts/metabolism
    Chemical Substances Fungal Proteins ; Prions
    Language English
    Publishing date 2018-10-17
    Publishing country England
    Document type Autobiography ; Historical Article ; Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2036775-2
    ISSN 1567-1364 ; 1567-1356
    ISSN (online) 1567-1364
    ISSN 1567-1356
    DOI 10.1093/femsyr/foy115
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  8. Article ; Online: Prions are the greatest protein misfolding problem, and yeast has several solutions.

    Reed B Wickner / Herman K Edskes / Songsong Wu / Kristen Gregg

    PLoS Pathogens, Vol 19, Iss 5, p e

    2023  Volume 1011333

    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2023-05-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article: Anti-Prion Systems in Saccharomyces cerevisiae Turn an Avalanche of Prions into a Flurry

    Son, Moonil / Wickner, Reed B.

    Viruses. 2022 Sept. 01, v. 14, no. 9

    2022  

    Abstract: Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein. These prions arise spontaneously in the cell without known reason, and their ... ...

    Abstract Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein. These prions arise spontaneously in the cell without known reason, and their effects were generally considered to be fatal based on prion diseases in humans or mammals. However, the wide array of prion studies in yeast including filamentous fungi revealed that their effects can range widely, from lethal to very mild (even cryptic) or functional, depending on the nature of the prion protein and the specific prion variant (or strain) made by the same prion protein but with a different conformation. This prion biology is affected by an array of molecular chaperone systems, such as Hsp40, Hsp70, Hsp104, and combinations of them. In parallel with the systems required for prion propagation, yeast has multiple anti-prion systems, constantly working in the normal cell without overproduction of or a deficiency in any protein, which have negative effects on prions by blocking their formation, curing many prions after they arise, preventing prion infections, and reducing the cytotoxicity produced by prions. From the protectors of nascent polypeptides (Ssb1/2p, Zuo1p, and Ssz1p) to the protein sequesterase (Btn2p), the disaggregator (Hsp104), and the mysterious Cur1p, normal levels of each can cure the prion variants arising in its absence. The controllers of mRNA quality, nonsense-mediated mRNA decay proteins (Upf1, 2, 3), can cure newly formed prion variants by association with a prion-forming protein. The regulator of the inositol pyrophosphate metabolic pathway (Siw14p) cures certain prion variants by lowering the levels of certain organic compounds. Some of these proteins have other cellular functions (e.g., Btn2), while others produce an anti-prion effect through their primary role in the normal cell (e.g., ribosomal chaperones). Thus, these anti-prion actions are the innate defense strategy against prions. Here, we outline the anti-prion systems in yeast that produce innate immunity to prions by a multi-layered operation targeting each step of prion development.
    Keywords Saccharomyces cerevisiae ; amyloid ; biochemical pathways ; cytotoxicity ; heat-shock protein 40 ; innate immunity ; inositols ; polymers ; polypeptides ; prions ; yeasts
    Language English
    Dates of publication 2022-0901
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14091945
    Database NAL-Catalogue (AGRICOLA)

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  10. Article ; Online: Normal levels of ribosome-associated chaperones cure two groups of [PSI+] prion variants.

    Son, Moonil / Wickner, Reed B

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

    2020  Volume 117, Issue 42, Page(s) 26298–26306

    Abstract: The yeast prion [PSI+] is a self-propagating amyloid of the translation termination factor, Sup35p. For known pathogenic prions, such as [PSI+], a single protein can form an array of different amyloid structures (prion variants) each stably inherited and ...

    Abstract The yeast prion [PSI+] is a self-propagating amyloid of the translation termination factor, Sup35p. For known pathogenic prions, such as [PSI+], a single protein can form an array of different amyloid structures (prion variants) each stably inherited and with differing biological properties. The ribosome-associated chaperones, Ssb1/2p (Hsp70s), and RAC (Zuo1p (Hsp40) and Ssz1p (Hsp70)), enhance de novo protein folding by protecting nascent polypeptide chains from misfolding and maintain translational fidelity by involvement in translation termination. Ssb1/2p and RAC chaperones were previously found to inhibit [PSI+] prion generation. We find that most [PSI+] variants arising in the absence of each chaperone were cured by restoring normal levels of that protein. [PSI+] variants hypersensitive to Ssb1/2p have distinguishable biological properties from those hypersensitive to Zuo1p or Ssz1p. The elevated [PSI+] generation frequency in each deletion strain is not due to an altered [PIN+], another prion that primes [PSI+] generation. [PSI+] prion generation/propagation may be inhibited by Ssb1/2/RAC chaperones by ensuring proper folding of nascent Sup35p, thus preventing its joining amyloid fibers. Alternatively, the effect of RAC/Ssb mutations on translation termination and the absence of an effect on the [URE3] prion suggest an effect on the mature Sup35p such that it does not readily join amyloid filaments. Ssz1p is degraded in
    MeSH term(s) HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Peptide Termination Factors/genetics ; Peptide Termination Factors/metabolism ; Prions/genetics ; Protein Biosynthesis ; Ribosomes/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances HSP70 Heat-Shock Proteins ; Heat-Shock Proteins ; Molecular Chaperones ; Peptide Termination Factors ; Prions ; SSB1 protein, S cerevisiae ; SSZ1 protein, S cerevisiae ; SUP35 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; ZUO1 protein, S cerevisiae
    Language English
    Publishing date 2020-10-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2016954117
    Database MEDical Literature Analysis and Retrieval System OnLINE

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