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  1. Article ; Online: The Functions of N

    Zhigalova, Nadezhda A / Oleynikova, Katerina Yu / Ruzov, Alexey S / Ermakov, Alexander S

    Biochemistry. Biokhimiia

    2023  Volume 89, Issue 1, Page(s) 159–172

    Abstract: ... ...

    Abstract N
    MeSH term(s) Methyltransferases/genetics ; RNA, Nuclear/metabolism ; Methylation ; Gene Expression Regulation ; RNA, Messenger/metabolism ; Adenosine/analogs & derivatives
    Chemical Substances Methyltransferases (EC 2.1.1.-) ; RNA, Nuclear ; N-methyladenosine (CLE6G00625) ; RNA, Messenger ; Adenosine (K72T3FS567)
    Language English
    Publishing date 2023-10-20
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1109-5
    ISSN 1608-3040 ; 0006-2979 ; 0320-9717
    ISSN (online) 1608-3040
    ISSN 0006-2979 ; 0320-9717
    DOI 10.1134/S0006297924010103
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 220: 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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  2. Article ; Online: Mechanical Tensions Regulate Gene Expression in the

    Eroshkin, Fedor M / Fefelova, Elena A / Bredov, Denis V / Orlov, Eugeny E / Kolyupanova, Nataliya M / Mazur, Alexander M / Sokolov, Alexey S / Zhigalova, Nadezhda A / Prokhortchouk, Egor B / Nesterenko, Alexey M / Zaraisky, Andrey G

    International journal of molecular sciences

    2024  Volume 25, Issue 2

    Abstract: During gastrulation and neurulation, the chordamesoderm and overlying neuroectoderm of vertebrate embryos converge under the control of a specific genetic programme to the dorsal midline, simultaneously extending along it. However, whether mechanical ... ...

    Abstract During gastrulation and neurulation, the chordamesoderm and overlying neuroectoderm of vertebrate embryos converge under the control of a specific genetic programme to the dorsal midline, simultaneously extending along it. However, whether mechanical tensions resulting from these morphogenetic movements play a role in long-range feedback signaling that in turn regulates gene expression in the chordamesoderm and neuroectoderm is unclear. In the present work, by using a model of artificially stretched explants of
    MeSH term(s) Animals ; Stress, Mechanical ; Xenopus laevis/genetics ; 4-Butyrolactone ; Gene Expression
    Chemical Substances A-factor (Streptomyces) (51311-41-2) ; 4-Butyrolactone (OL659KIY4X)
    Language English
    Publishing date 2024-01-10
    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/ijms25020870
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Cytoskeletal Protein Zyxin Inhibits the Activity of Genes Responsible for Embryonic Stem Cell Status.

    Parshina, Elena A / Eroshkin, Fedor M / Оrlov, Eugeny E / Gyoeva, Fatima K / Shokhina, Arina G / Staroverov, Dmitry B / Belousov, Vsevolod V / Zhigalova, Nadezhda A / Prokhortchouk, Egor B / Zaraisky, Andrey G / Martynova, Natalia Y

    Cell reports

    2020  Volume 33, Issue 7, Page(s) 108396

    Abstract: Zyxin is a cytoskeletal LIM-domain protein that regulates actin cytoskeleton assembly and gene expression. In the present work, we find that zyxin downregulation in Xenopus laevis embryos reduces the expression of numerous genes that regulate cell ... ...

    Abstract Zyxin is a cytoskeletal LIM-domain protein that regulates actin cytoskeleton assembly and gene expression. In the present work, we find that zyxin downregulation in Xenopus laevis embryos reduces the expression of numerous genes that regulate cell differentiation, but it enhances that of several genes responsible for embryonic stem cell status, specifically klf4, pou5f3.1, pou5f3.2, pou5f3.3, and vent2.1/2. For pou5f3 family genes (mammalian POU5F1/OCT4 homologs), we show that this effect is the result of mRNA stabilization due to complex formation with the Y-box protein Ybx1. When bound to Ybx1, zyxin interferes with the formation of these complexes, thereby stimulating pou5f3 mRNA degradation. In addition, in zebrafish embryos and human HEK293 cells, zyxin downregulation increases mRNA levels of the pluripotency genes KLF4, NANOG, and POU5F1/OCT4. Our findings indicate that zyxin may play a role as a switch among morphogenetic cell movement, differentiation, and embryonic stem cell status.
    MeSH term(s) Animals ; Body Patterning/genetics ; Cell Differentiation/genetics ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/metabolism ; Embryonic Stem Cells/metabolism ; Embryonic Stem Cells/physiology ; Gene Expression Regulation, Developmental/genetics ; HEK293 Cells ; Humans ; Morphogenesis ; Neural Plate/metabolism ; Octamer Transcription Factor-3/genetics ; Octamer Transcription Factor-3/metabolism ; Xenopus laevis/metabolism ; Zebrafish/metabolism ; Zyxin/metabolism ; Zyxin/physiology
    Chemical Substances Cytoskeletal Proteins ; Octamer Transcription Factor-3 ; Zyxin
    Language English
    Publishing date 2020-11-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2020.108396
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Optimized method for preparation of IgG-binding bacterial magnetic nanoparticles.

    Grouzdev, Denis S / Dziuba, Marina V / Kurek, Denis V / Ovchinnikov, Alexander I / Zhigalova, Nadezhda A / Kuznetsov, Boris B / Skryabin, Konstantin G

    PloS one

    2014  Volume 9, Issue 10, Page(s) e109914

    Abstract: In this study, the optimized method for designing IgG-binding magnetosomes based on integration of IgG-binding fusion proteins into magnetosome membrane in vitro is presented. Fusion proteins Mbb and Mistbb consisting of magnetosome membrane protein MamC ...

    Abstract In this study, the optimized method for designing IgG-binding magnetosomes based on integration of IgG-binding fusion proteins into magnetosome membrane in vitro is presented. Fusion proteins Mbb and Mistbb consisting of magnetosome membrane protein MamC and membrane associating protein Mistic from Bacillus subtilis as anchors and BB-domains of Staphylococcus aureus protein A as IgG-binding region were used. With Response Surface Methodology (RSM) the highest level of proteins integration into magnetosome membrane was achieved under the following parameters: pH 8.78, without adding NaCl and 55 s of vortexing for Mbb; pH 9.48, 323 mM NaCl and 55 s of vortexing for Mistbb. Modified magnetosomes with Mbb and Mistbb displayed on their surface demonstrated comparable levels of IgG-binding activity, suggesting that both proteins could be efficiently used as anchor molecules. We also demonstrated that such modified magnetosomes are stable in PBS buffer during at least two weeks. IgG-binding magnetosomes obtained by this approach could serve as a multifunctional platform for displaying various types of antibodies.
    MeSH term(s) Bacterial Proteins/metabolism ; Immunoglobulin G/metabolism ; Magnetite Nanoparticles/chemistry ; Magnetosomes/chemistry ; Membrane Proteins/metabolism ; Protein Binding ; Staphylococcal Protein A/metabolism ; Staphylococcus aureus/metabolism
    Chemical Substances Bacterial Proteins ; Immunoglobulin G ; Magnetite Nanoparticles ; Membrane Proteins ; Staphylococcal Protein A
    Language English
    Publishing date 2014-10-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0109914
    Database MEDical Literature Analysis and Retrieval System OnLINE

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