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  1. Article: New RAD51 Inhibitors to Target Homologous Recombination in Human Cells

    Shkundina, Irina S. / Gall, Alexander A. / Dick, Alexej / Cocklin, Simon / Mazin, Alexander V.

    Genes. 2021 June 16, v. 12, no. 6

    2021  

    Abstract: Targeting DNA repair proteins with small-molecule inhibitors became a proven anti-cancer strategy. Previously, we identified an inhibitor of a major protein of homologous recombination (HR) RAD51, named B02. B02 inhibited HR in human cells and sensitized ...

    Abstract Targeting DNA repair proteins with small-molecule inhibitors became a proven anti-cancer strategy. Previously, we identified an inhibitor of a major protein of homologous recombination (HR) RAD51, named B02. B02 inhibited HR in human cells and sensitized them to chemotherapeutic drugs in vitro and in vivo. Here, using a medicinal chemistry approach, we aimed to improve the potency of B02. We identified the B02 analog, B02-isomer, which inhibits HR in human cells with significantly higher efficiency. We also show that B02-iso sensitizes triple-negative breast cancer MDA-MB-231 cells to the PARP inhibitor (PARPi) olaparib.
    Keywords DNA repair ; breast neoplasms ; chemistry ; drug therapy ; homologous recombination ; humans
    Language English
    Dates of publication 2021-0616
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2527218-4
    ISSN 2073-4425
    ISSN 2073-4425
    DOI 10.3390/genes12060920
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: New RAD51 Inhibitors to Target Homologous Recombination in Human Cells.

    Shkundina, Irina S / Gall, Alexander A / Dick, Alexej / Cocklin, Simon / Mazin, Alexander V

    Genes

    2021  Volume 12, Issue 6

    Abstract: Targeting DNA repair proteins with small-molecule inhibitors became a proven anti-cancer strategy. Previously, we identified an inhibitor of a major protein of homologous recombination (HR) RAD51, named B02. B02 inhibited HR in human cells and sensitized ...

    Abstract Targeting DNA repair proteins with small-molecule inhibitors became a proven anti-cancer strategy. Previously, we identified an inhibitor of a major protein of homologous recombination (HR) RAD51, named B02. B02 inhibited HR in human cells and sensitized them to chemotherapeutic drugs
    Language English
    Publishing date 2021-06-16
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2527218-4
    ISSN 2073-4425 ; 2073-4425
    ISSN (online) 2073-4425
    ISSN 2073-4425
    DOI 10.3390/genes12060920
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants.

    Shkundina, Irina S / Kushnirov, Vitaly V / Tuite, Mick F / Ter-Avanesyan, Michael D

    Genetics

    2006  Volume 172, Issue 2, Page(s) 827–835

    Abstract: The cytoplasmic [PSI+] determinant of Saccharomyces cerevisiae is the prion form of the Sup35 protein. Oligopeptide repeats within the Sup35 N-terminal domain (PrD) presumably are required for the stable [PSI+] inheritance that in turn involves ... ...

    Abstract The cytoplasmic [PSI+] determinant of Saccharomyces cerevisiae is the prion form of the Sup35 protein. Oligopeptide repeats within the Sup35 N-terminal domain (PrD) presumably are required for the stable [PSI+] inheritance that in turn involves fragmentation of Sup35 polymers by the chaperone Hsp104. The nonsense suppressor [PSI+] phenotype can vary in efficiency probably due to different inheritable Sup35 polymer structures. Here we study the ability of Sup35 mutants with various deletions of the oligopeptide repeats to support [PSI+] propagation. We define the minimal region of the Sup35-PrD necessary to support [PSI+] as amino acids 1-64, which include the first two repeats, although a longer fragment, 1-83, is required to maintain weak [PSI+] variants. Replacement of wild-type Sup35 with deletion mutants decreases the strength of the [PSI+] phenotype. However, with one exception, reintroducing the wild-type Sup35 restores the original phenotype. Thus, the specific prion fold defining the [PSI+] variant can be preserved by the mutant Sup35 protein despite the change of phenotype. Coexpression of wild-type and mutant Sup35 containing three, two, one, or no oligopeptide repeats causes variant-specific [PSI+] elimination. These data suggest that [PSI+] variability is primarily defined by differential folding of the Sup35-PrD oligopeptide-repeat region.
    MeSH term(s) Base Sequence ; Genetic Variation ; Oligopeptides/chemistry ; Oligopeptides/genetics ; Oligopeptides/physiology ; Peptide Termination Factors ; Phenotype ; Plasmids ; Prions/chemistry ; Prions/genetics ; Prions/physiology ; Protein Folding ; Protein Structure, Tertiary/genetics ; Repetitive Sequences, Amino Acid/genetics ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/physiology ; Sequence Deletion
    Chemical Substances Oligopeptides ; Peptide Termination Factors ; Prions ; SUP35 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2006-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2167-2
    ISSN 1943-2631 ; 0016-6731
    ISSN (online) 1943-2631
    ISSN 0016-6731
    DOI 10.1534/genetics.105.048660
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Purification and analysis of prion and amyloid aggregates.

    Kushnirov, Vitaly V / Alexandrov, Ilya M / Mitkevich, Olga V / Shkundina, Irina S / Ter-Avanesyan, Michael D

    Methods (San Diego, Calif.)

    2006  Volume 39, Issue 1, Page(s) 50–55

    Abstract: Amyloids and prions represent aggregates of misfolded proteins, which consist of protein polymer fibrils with cross-beta sheet structure. Understanding of their occurrence and role is developing rapidly. Initially, they were found associated with ... ...

    Abstract Amyloids and prions represent aggregates of misfolded proteins, which consist of protein polymer fibrils with cross-beta sheet structure. Understanding of their occurrence and role is developing rapidly. Initially, they were found associated with mammalian diseases, mainly of neurodegenerative nature. Now they are known to relate to a range of non-disease phenomena in different species from mammals to lower eukaryotes. Uncovering new prion- and amyloid-related processes may be helped greatly by a procedure for purification of amyloid polymers. Studies of growth and propagation of these polymers require methods for determination of their size. Here, we describe such methods. They rely on the treatment with cold SDS or Sarcosyl detergents, which do not dissolve amyloids, but solubilize almost all non-amyloid complexes and associations between amyloid fibers. This allows purifying amyloids by centrifugation in the presence of these detergents. The size of amyloid polymers may be analyzed by electrophoresis in agarose gels containing SDS. Two procedures are described for determining the proportion between polymers and monomers of a particular protein using polyacrylamide gels.
    MeSH term(s) Amyloid/analysis ; Amyloid/isolation & purification ; Centrifugation ; Detergents/chemistry ; Electrophoresis, Agar Gel ; Electrophoresis, Polyacrylamide Gel ; Peptide Termination Factors ; Prions/analysis ; Prions/isolation & purification ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae Proteins/analysis ; Saccharomyces cerevisiae Proteins/isolation & purification
    Chemical Substances Amyloid ; Detergents ; Peptide Termination Factors ; Prions ; SUP35 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2006-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1066584-5
    ISSN 1095-9130 ; 1046-2023
    ISSN (online) 1095-9130
    ISSN 1046-2023
    DOI 10.1016/j.ymeth.2006.04.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3239: Show issues Location:
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  5. Article: Novel non-Mendelian determinant involved in the control of translation accuracy in Saccharomyces cerevisiae.

    Volkov, Kirill V / Aksenova, Anna Yu / Soom, Malle J / Osipov, Kirill V / Svitin, Anton V / Kurischko, Cornelia / Shkundina, Irina S / Ter-Avanesyan, Michael D / Inge-Vechtomov, Sergey G / Mironova, Ludmila N

    Genetics

    2001  Volume 160, Issue 1, Page(s) 25–36

    Abstract: Two cytoplasmically inherited determinants related by their manifestation to the control of translation accuracy were previously described in yeast. Cells carrying one of them, [PSI(+)], display a nonsense suppressor phenotype and contain a prion form of ...

    Abstract Two cytoplasmically inherited determinants related by their manifestation to the control of translation accuracy were previously described in yeast. Cells carrying one of them, [PSI(+)], display a nonsense suppressor phenotype and contain a prion form of the Sup35 protein. Another element, [PIN(+)], determines the probability of de novo generation of [PSI(+)] and results from a prion form of several proteins, which can be functionally unrelated to Sup35p. Here we describe a novel nonchromosomal determinant related to the SUP35 gene. This determinant, designated [ISP(+)], was identified as an antisuppressor of certain sup35 mutations. We observed its loss upon growth on guanidine hydrochloride and subsequent spontaneous reappearance with high frequency. The reversible curability of [ISP(+)] resembles the behavior of yeast prions. However, in contrast to known prions, [ISP(+)] does not depend on the chaperone protein Hsp104. Though manifestation of both [ISP(+)] and [PSI(+)] is related to the SUP35 gene, the maintenance of [ISP(+)] does not depend on the prionogenic N-terminal domain of Sup35p and Sup35p is not aggregated in [ISP(+)] cells, thus ruling out the possibility that [ISP(+)] is a specific form of [PSI(+)]. We hypothesize that [ISP(+)] is a novel prion involved in the control of translation accuracy in yeast.
    MeSH term(s) Alleles ; Chromosomes, Fungal ; Culture Media/metabolism ; Extrachromosomal Inheritance ; Fungal Proteins/genetics ; Gene Expression Regulation, Fungal ; Genes, Dominant ; Guanidine/metabolism ; Heat-Shock Proteins/physiology ; Nuclear Proteins ; Peptide Termination Factors ; Prions/genetics ; Protein Biosynthesis/physiology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces pombe Proteins ; Suppression, Genetic
    Chemical Substances Culture Media ; Fungal Proteins ; Heat-Shock Proteins ; Nuclear Proteins ; Peptide Termination Factors ; Prions ; Psi protein, S pombe ; SUP35 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces pombe Proteins ; HsP104 protein, S cerevisiae (143012-44-6) ; Guanidine (JU58VJ6Y3B)
    Language English
    Publishing date 2001-02-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2167-2
    ISSN 1943-2631 ; 0016-6731
    ISSN (online) 1943-2631
    ISSN 0016-6731
    DOI 10.1093/genetics/160.1.25
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.B 767: Show issues Location:
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