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  1. Article ; Online: Mapping of Prion Structures in the Yeast Rnq1.

    Galliamov, Arthur A / Malukhina, Alena D / Kushnirov, Vitaly V

    International journal of molecular sciences

    2024  Volume 25, Issue 6

    Abstract: The Rnq1 protein is one of the best-studied yeast prions. It has a large potentially prionogenic C-terminal region of about 250 residues. However, a previous study indicated that only 40 C-terminal residues form a prion structure. Here, we mapped the ... ...

    Abstract The Rnq1 protein is one of the best-studied yeast prions. It has a large potentially prionogenic C-terminal region of about 250 residues. However, a previous study indicated that only 40 C-terminal residues form a prion structure. Here, we mapped the actual and potential prion structures formed by Rnq1 and its variants truncated from the C-terminus in two [
    MeSH term(s) Prions/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Prions ; Saccharomyces cerevisiae Proteins ; RNQ1 protein, S cerevisiae
    Language English
    Publishing date 2024-03-17
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms25063397
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  2. Article ; Online: Michael Ter-Avanesyan (1949-2018) - life in science.

    Kushnirov, Vitaly V

    Prion

    2019  Volume 13, Issue 1, Page(s) 37–40

    Abstract: This commentary describes scientific path and accomplishments of our late colleague, Prof. Michael D. Ter-Avanesyan, who made several seminal contributions into prion research. ...

    Abstract This commentary describes scientific path and accomplishments of our late colleague, Prof. Michael D. Ter-Avanesyan, who made several seminal contributions into prion research.
    MeSH term(s) History, 20th Century ; History, 21st Century ; Prions/metabolism ; Saccharomyces cerevisiae/genetics
    Chemical Substances Prions
    Language English
    Publishing date 2019-01-28
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article ; Portrait
    ISSN 1933-690X
    ISSN (online) 1933-690X
    DOI 10.1080/19336896.2019.1567201
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Structural Bases of Prion Variation in Yeast.

    Kushnirov, Vitaly V / Dergalev, Alexander A / Alieva, Maya K / Alexandrov, Alexander I

    International journal of molecular sciences

    2022  Volume 23, Issue 10

    Abstract: Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as ... ...

    Abstract Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast prions are of interest both on their own and as a model for amyloids and prions in general. In this review, we consider the structure of yeast prions and its variation, how such structures determine the balance of aggregated and soluble prion protein through interaction with chaperones and how the aggregated state affects the non-prion functions of these proteins.
    MeSH term(s) Amyloid/metabolism ; Molecular Chaperones/metabolism ; Prions/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Amyloid ; Molecular Chaperones ; Prions ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2022-05-20
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms23105738
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  4. Article ; Online: Amyloid Fragmentation and Disaggregation in Yeast and Animals.

    Kushnirov, Vitaly V / Dergalev, Alexander A / Alexandrov, Alexander I

    Biomolecules

    2021  Volume 11, Issue 12

    Abstract: Amyloids are filamentous protein aggregates that are associated with a number of incurable diseases, termed amyloidoses. Amyloids can also manifest as infectious or heritable particles, known as prions. While just one prion is known in humans and animals, ...

    Abstract Amyloids are filamentous protein aggregates that are associated with a number of incurable diseases, termed amyloidoses. Amyloids can also manifest as infectious or heritable particles, known as prions. While just one prion is known in humans and animals, more than ten prion amyloids have been discovered in fungi. The propagation of fungal prion amyloids requires the chaperone Hsp104, though in excess it can eliminate some prions. Even though Hsp104 acts to disassemble prion fibrils, at normal levels it fragments them into multiple smaller pieces, which ensures prion propagation and accelerates prion conversion. Animals lack Hsp104, but disaggregation is performed by the same complement of chaperones that assist Hsp104 in yeast-Hsp40, Hsp70, and Hsp110. Exogenous Hsp104 can efficiently cooperate with these chaperones in animals and promotes disaggregation, especially of large amyloid aggregates, which indicates its potential as a treatment for amyloid diseases. However, despite the significant effects, Hsp104 and its potentiated variants may be insufficient to fully dissolve amyloid. In this review, we consider chaperone mechanisms acting to disassemble heritable protein aggregates in yeast and animals, and their potential use in the therapy of human amyloid diseases.
    MeSH term(s) Amyloid/chemistry ; Amyloid/metabolism ; Animals ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Fungi/metabolism ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/metabolism ; Humans ; Models, Molecular ; Prions/chemistry ; Prions/metabolism ; Protein Aggregates ; Protein Conformation
    Chemical Substances Amyloid ; Fungal Proteins ; Heat-Shock Proteins ; Prions ; Protein Aggregates
    Language English
    Publishing date 2021-12-15
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom11121884
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Perturbations in the Heme and Siroheme Biosynthesis Pathways Causing Accumulation of Fluorescent Free Base Porphyrins and Auxotrophy in

    Karginov, Azamat V / Alexandrov, Alexander I / Kushnirov, Vitaly V / Agaphonov, Michael O

    Journal of fungi (Basel, Switzerland)

    2021  Volume 7, Issue 10

    Abstract: The biosynthesis of cyclic tetrapyrrol chromophores such as heme, siroheme, and chlorophyll involves the formation of fluorescent porphyrin precursors or compounds, which become fluorescent after oxidation. To ... ...

    Abstract The biosynthesis of cyclic tetrapyrrol chromophores such as heme, siroheme, and chlorophyll involves the formation of fluorescent porphyrin precursors or compounds, which become fluorescent after oxidation. To identify
    Language English
    Publishing date 2021-10-19
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2784229-0
    ISSN 2309-608X ; 2309-608X
    ISSN (online) 2309-608X
    ISSN 2309-608X
    DOI 10.3390/jof7100884
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Mutable yeast prion variants are stabilized by a defective Hsp104 chaperone.

    Huang, Yu-Wen / Kushnirov, Vitaly V / King, Chih-Yen

    Molecular microbiology

    2020  Volume 115, Issue 4, Page(s) 774–788

    Abstract: Gorkovskiy et al. observed that many [ ... ...

    Abstract Gorkovskiy et al. observed that many [PSI
    MeSH term(s) Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Peptide Termination Factors/metabolism ; Prions/genetics ; Prions/metabolism ; Protein Folding ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Deletion
    Chemical Substances Heat-Shock Proteins ; Molecular Chaperones ; Peptide Termination Factors ; Prions ; SUP35 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; HsP104 protein, S cerevisiae (143012-44-6)
    Language English
    Publishing date 2020-12-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/mmi.14643
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2502: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Proteinase K resistant cores of prions and amyloids.

    Kushnirov, Vitaly V / Dergalev, Alexander A / Alexandrov, Alexander I

    Prion

    2020  Volume 14, Issue 1, Page(s) 11–19

    Abstract: Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resistant ...

    Abstract Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resistant to treatment with proteinase K (PK). Amyloids can have structural variants, which can be distinguished by the patterns of their digestion by PK. In this review, we describe and compare studies of the resistant cores of various amyloids from different organisms. These data provide insight into the fine structure of amyloids and their variants as well as raise interesting questions, such as those concerning the differences between amyloids obtained
    MeSH term(s) Amyloid/chemistry ; Amyloid/metabolism ; Animals ; Endopeptidase K/metabolism ; Humans ; Prions/chemistry ; Prions/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; alpha-Synuclein/metabolism
    Chemical Substances Amyloid ; Prions ; Saccharomyces cerevisiae Proteins ; alpha-Synuclein ; Endopeptidase K (EC 3.4.21.64)
    Language English
    Publishing date 2020-01-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2267671-5
    ISSN 1933-690X ; 1933-690X
    ISSN (online) 1933-690X
    ISSN 1933-690X
    DOI 10.1080/19336896.2019.1704612
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: CAR1 as a new selective marker for genetic engineering of wine yeasts.

    Urakov, Valery N / Mardanov, Andrey V / Alexandrov, Alexander I / Ruzhitskiy, Aleksandr O / Ravin, Nikolai V / Kushnirov, Vitaly V

    Journal of microbiological methods

    2023  Volume 214, Page(s) 106840

    Abstract: A common problem in engineering industrial yeasts, and wine yeasts in particular, is the lack or scarcity of selective markers for introducing desired genetic changes. Almost all such markers, which are usually auxotrophic mutations, would reduce the ... ...

    Abstract A common problem in engineering industrial yeasts, and wine yeasts in particular, is the lack or scarcity of selective markers for introducing desired genetic changes. Almost all such markers, which are usually auxotrophic mutations, would reduce the growth characteristics of yeast strains. However, a potentially useful marker could be the CAR1 gene encoding arginase, the deletion of which reduces the accumulation of the carcinogen ethyl carbamate in wine, making such a deletion beneficial for wine production and maintainable in wine yeast strains. Here we demonstrate the use of the CAR1 gene as a selective marker. First, we observe that complete deletion of CAR1 in a triploid wine strain of Saccharomyces cerevisiae causes strong growth inhibition on a medium containing arginine as the only nitrogen source. Then, we show that strains with CAR1 deletion can be reliably transformed using CAR1 as a plasmid marker. Thus, the CAR1 gene can be used as a convenient selective marker in genetic engineering of wine yeasts, in particular using CRISPR/Cas9 technology.
    MeSH term(s) Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Wine/analysis ; Genetic Engineering ; Urethane ; Fermentation ; Yeasts/genetics
    Chemical Substances Saccharomyces cerevisiae Proteins ; Urethane (3IN71E75Z5)
    Language English
    Publishing date 2023-10-10
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 604916-3
    ISSN 1872-8359 ; 0167-7012
    ISSN (online) 1872-8359
    ISSN 0167-7012
    DOI 10.1016/j.mimet.2023.106840
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1849: 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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  9. Article ; Online: Structural Bases of Prion Variation in Yeast

    Vitaly V. Kushnirov / Alexander A. Dergalev / Maya K. Alieva / Alexander I. Alexandrov

    International Journal of Molecular Sciences, Vol 23, Iss 5738, p

    2022  Volume 5738

    Abstract: Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as ... ...

    Abstract Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast prions are of interest both on their own and as a model for amyloids and prions in general. In this review, we consider the structure of yeast prions and its variation, how such structures determine the balance of aggregated and soluble prion protein through interaction with chaperones and how the aggregated state affects the non-prion functions of these proteins.
    Keywords amyloid ; prion ; prion structure ; yeast ; Sup35 ; chaperones ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Language English
    Publishing date 2022-05-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Dangerous Stops: Nonsense Mutations Can Dramatically Increase Frequency of Prion Conversion.

    Dergalev, Alexander A / Urakov, Valery N / Agaphonov, Michael O / Alexandrov, Alexander I / Kushnirov, Vitaly V

    International journal of molecular sciences

    2021  Volume 22, Issue 4

    Abstract: Amyloid formation is associated with many incurable diseases. For some of these, sporadic cases are much more common than familial ones. Some reports point to the role of somatic cell mosaicism in these cases via origination of amyloids in a limited ... ...

    Abstract Amyloid formation is associated with many incurable diseases. For some of these, sporadic cases are much more common than familial ones. Some reports point to the role of somatic cell mosaicism in these cases via origination of amyloids in a limited number of cells, which can then spread through tissues. However, specific types of sporadic mutations responsible for such effects are unknown. In order to identify mutations capable of increasing the de novo appearance of amyloids, we searched for such mutants in the yeast prionogenic protein Sup35. We introduced to yeast cells an additional copy of the
    MeSH term(s) Amyloid/metabolism ; Amyloidosis/genetics ; Amyloidosis/metabolism ; Amyloidosis/pathology ; Codon, Nonsense ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Mass Spectrometry ; Prions/chemistry ; Prions/genetics ; Prions/metabolism ; Protein Aggregates ; RNA Splicing
    Chemical Substances Amyloid ; Codon, Nonsense ; Fungal Proteins ; Prions ; Protein Aggregates
    Language English
    Publishing date 2021-02-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22041542
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