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  1. Article: Thickness Effects on the Martensite Transformations and Mechanical Properties of Nanocrystalline NiTi Wires.

    Baigonakova, Gulsharat A / Marchenko, Ekaterina S / Kovaleva, Marina A / Chudinova, Ekaterina A / Volinsky, Alex A / Zhang, Yi

    Nanomaterials (Basel, Switzerland)

    2022  Volume 12, Issue 24

    Abstract: This paper studied the features of the martensitic transformations and mechanical properties of 40, 60, and 90 µm thick NiTi wires with nanocrystalline B2 structures. It was established that the wires were composites and consisted of a TiNi matrix and a ... ...

    Abstract This paper studied the features of the martensitic transformations and mechanical properties of 40, 60, and 90 µm thick NiTi wires with nanocrystalline B2 structures. It was established that the wires were composites and consisted of a TiNi matrix and a TiO
    Language English
    Publishing date 2022-12-14
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2662255-5
    ISSN 2079-4991
    ISSN 2079-4991
    DOI 10.3390/nano12244442
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Heterogeneous Nuclear Ribonucleoproteins Involved in the Functioning of Telomeres in Malignant Cells.

    Shishkin, Sergey S / Kovalev, Leonid I / Pashintseva, Natalya V / Kovaleva, Marina A / Lisitskaya, Ksenia

    International journal of molecular sciences

    2019  Volume 20, Issue 3

    Abstract: Heterogeneous nuclear ribonucleoproteins (hnRNPs) are structurally and functionally distinct proteins containing specific domains and motifs that enable the proteins to bind certain nucleotide sequences, particularly those found in human telomeres. In ... ...

    Abstract Heterogeneous nuclear ribonucleoproteins (hnRNPs) are structurally and functionally distinct proteins containing specific domains and motifs that enable the proteins to bind certain nucleotide sequences, particularly those found in human telomeres. In human malignant cells (HMCs), hnRNP-A1-the most studied hnRNP-is an abundant multifunctional protein that interacts with telomeric DNA and affects telomerase function. In addition, it is believed that other hnRNPs in HMCs may also be involved in the maintenance of telomere length. Accordingly, these proteins are considered possible participants in the processes associated with HMC immortalization. In our review, we discuss the results of studies on different hnRNPs that may be crucial to solving molecular oncological problems and relevant to further investigations of these proteins in HMCs.
    MeSH term(s) Carrier Proteins/metabolism ; Cell Line, Tumor ; Heterogeneous-Nuclear Ribonucleoproteins/genetics ; Heterogeneous-Nuclear Ribonucleoproteins/metabolism ; Humans ; Multigene Family ; Multiprotein Complexes/metabolism ; Neoplasms/genetics ; Neoplasms/metabolism ; Protein Binding ; Telomerase/metabolism ; Telomere/genetics ; Telomere/metabolism
    Chemical Substances Carrier Proteins ; Heterogeneous-Nuclear Ribonucleoproteins ; Multiprotein Complexes ; Telomerase (EC 2.7.7.49)
    Language English
    Publishing date 2019-02-10
    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/ijms20030745
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Mitochondrial ATP Synthase and Mild Uncoupling by Butyl Ester of Rhodamine 19, C4R1.

    Zorova, Ljubava D / Pevzner, Irina B / Khailova, Ljudmila S / Korshunova, Galina A / Kovaleva, Marina A / Kovalev, Leonid I / Serebryakova, Marina V / Silachev, Denis N / Sudakov, Roman V / Zorov, Savva D / Rokitskaya, Tatyana I / Popkov, Vasily A / Plotnikov, Egor Y / Antonenko, Yuri N / Zorov, Dmitry B

    Antioxidants (Basel, Switzerland)

    2023  Volume 12, Issue 3

    Abstract: The homeostasis of the transmembrane potential of hydrogen ions in mitochondria is a prerequisite for the normal mitochondrial functioning. However, in different pathological conditions it is advisable to slightly reduce the membrane potential, while ... ...

    Abstract The homeostasis of the transmembrane potential of hydrogen ions in mitochondria is a prerequisite for the normal mitochondrial functioning. However, in different pathological conditions it is advisable to slightly reduce the membrane potential, while maintaining it at levels sufficient to produce ATP that will ensure the normal functioning of the cell. A number of chemical agents have been found to provide mild uncoupling; however, natural proteins residing in mitochondrial membrane can carry this mission, such as proteins from the UCP family, an adenine nucleotide translocator and a dicarboxylate carrier. In this study, we demonstrated that the butyl ester of rhodamine 19, C4R1, binds to the components of the mitochondrial ATP synthase complex due to electrostatic interaction and has a good uncoupling effect. The more hydrophobic derivative C12R1 binds poorly to mitochondria with less uncoupling activity. Mass spectrometry confirmed that C4R1 binds to the β-subunit of mitochondrial ATP synthase and based on molecular docking, a C4R1 binding model was constructed suggesting the binding site on the interface between the α- and β-subunits, close to the anionic amino acid residues of the β-subunit. The association of the uncoupling effect with binding suggests that the ATP synthase complex can provide induced uncoupling.
    Language English
    Publishing date 2023-03-04
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2704216-9
    ISSN 2076-3921
    ISSN 2076-3921
    DOI 10.3390/antiox12030646
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Mitochondrial ATP Synthase and Mild Uncoupling by Butyl Ester of Rhodamine 19, C4R1

    Zorova, Ljubava D. / Pevzner, Irina B. / Khailova, Ljudmila S. / Korshunova, Galina A. / Kovaleva, Marina A. / Kovalev, Leonid I. / Serebryakova, Marina V. / Silachev, Denis N. / Sudakov, Roman V. / Zorov, Savva D. / Rokitskaya, Tatyana I. / Popkov, Vasily A. / Plotnikov, Egor Y. / Antonenko, Yuri N. / Zorov, Dmitry B.

    Antioxidants. 2023 Mar. 04, v. 12, no. 3

    2023  

    Abstract: The homeostasis of the transmembrane potential of hydrogen ions in mitochondria is a prerequisite for the normal mitochondrial functioning. However, in different pathological conditions it is advisable to slightly reduce the membrane potential, while ... ...

    Abstract The homeostasis of the transmembrane potential of hydrogen ions in mitochondria is a prerequisite for the normal mitochondrial functioning. However, in different pathological conditions it is advisable to slightly reduce the membrane potential, while maintaining it at levels sufficient to produce ATP that will ensure the normal functioning of the cell. A number of chemical agents have been found to provide mild uncoupling; however, natural proteins residing in mitochondrial membrane can carry this mission, such as proteins from the UCP family, an adenine nucleotide translocator and a dicarboxylate carrier. In this study, we demonstrated that the butyl ester of rhodamine 19, C4R1, binds to the components of the mitochondrial ATP synthase complex due to electrostatic interaction and has a good uncoupling effect. The more hydrophobic derivative C12R1 binds poorly to mitochondria with less uncoupling activity. Mass spectrometry confirmed that C4R1 binds to the β-subunit of mitochondrial ATP synthase and based on molecular docking, a C4R1 binding model was constructed suggesting the binding site on the interface between the α- and β-subunits, close to the anionic amino acid residues of the β-subunit. The association of the uncoupling effect with binding suggests that the ATP synthase complex can provide induced uncoupling.
    Keywords H-transporting ATP synthase ; adenine nucleotides ; amino acids ; dicarboxylic acids ; electrostatic interactions ; homeostasis ; hydrogen ; hydrophobicity ; mass spectrometry ; membrane potential ; mitochondria ; mitochondrial membrane ; models ; rhodamines
    Language English
    Dates of publication 2023-0304
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article ; Online
    ZDB-ID 2704216-9
    ISSN 2076-3921
    ISSN 2076-3921
    DOI 10.3390/antiox12030646
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: Study of Splicing Factor, Proline- and Glutamine-rich by Proteomic Techniques in Human Malignant and Nonmalignant Cell Lines.

    Pashintseva, Natalya V / Shishkin, Sergey S / Lisitskaya, Kseniya V / Kovalev, Leonid I / Kovaleva, Marina A / Eryomina, Lidia S / Kamenikhina, Inna A / Novikova, Lyudmila A / Sadykhov, Elchin G

    Protein and peptide letters

    2016  Volume 23, Issue 11, Page(s) 958–966

    Abstract: Splicing factor, proline- and glutamine-rich protein (SFPQ), was identified in eight human cultivated cell lines by proteomic approaches. The cell proteins have been separated by means of two-dimensional gel electrophoresis in two modifications and ... ...

    Abstract Splicing factor, proline- and glutamine-rich protein (SFPQ), was identified in eight human cultivated cell lines by proteomic approaches. The cell proteins have been separated by means of two-dimensional gel electrophoresis in two modifications and identified by matrix-assisted laser desorption ionization mass spectrometry with further tandem mass spectrometry. The analysis of proteins from three human sarcomas cell lines (RD, U-2 OS and SK-UT-1B), three human renal adenocarcinomas cell lines (A-498, 769-P and OKP-GS), and two prostate adenocarcinomas cell lines (DU-145 and PC-3) revealed several electrophoretic isoforms of SFPQ protein. Differences between theoretical and experimental molecular masses and isoelectric points of SFPQ protein have been observed. Detailed investigation of SFPQ peptides by tandem mass spectrometry has detected new phosphorylation state of threonine residue in 168 position of SFPQ isoform in rhabdomyosarcoma cell line. Furthermore, SFPQ has not been identified during proteomic study of several nonmalignant cell lines, including cultured human mesenchymal stromal cells and myoblasts. However, SFPQ has been found in all malignant cell lines in high quantity. In particular, its fractions are abundant in sarcomas cell lines as opposed to nonmalignant mesenchymal cells. It is assumed that high quantity of SFPQ in sarcomas cell lines may affect tumorigenesis.
    MeSH term(s) Adenocarcinoma/pathology ; Carcinogenesis/pathology ; Carcinoma, Renal Cell/pathology ; Cell Line, Tumor ; Electrophoresis, Gel, Two-Dimensional ; Humans ; Kidney Neoplasms/pathology ; Male ; PTB-Associated Splicing Factor/analysis ; PTB-Associated Splicing Factor/metabolism ; Prostatic Neoplasms/pathology ; Protein Isoforms/analysis ; Protein Isoforms/metabolism ; Proteomics ; Rhabdomyosarcoma/pathology ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Tandem Mass Spectrometry
    Chemical Substances PTB-Associated Splicing Factor ; Protein Isoforms
    Language English
    Publishing date 2016-09-13
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1280776-x
    ISSN 1875-5305 ; 0929-8665
    ISSN (online) 1875-5305
    ISSN 0929-8665
    DOI 10.2174/0929866523666160914174007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4452: 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)
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  6. Article ; Online: Enzyme immunoassay and proteomic characterization of troponin I as a marker of mammalian muscle compounds in raw meat and some meat products.

    Zvereva, Elena A / Kovalev, Leonid I / Ivanov, Alexei V / Kovaleva, Marina A / Zherdev, Anatoly V / Shishkin, Sergey S / Lisitsyn, Andrey B / Chernukha, Irina M / Dzantiev, Boris B

    Meat science

    2015  Volume 105, Page(s) 46–52

    Abstract: The skeletal muscle protein troponin I (TnI) has been characterized as a potential thermally stable and species-specific biomarker of mammalian muscle tissues in raw meat and meat products. This study proposed a technique for the quantification of TnI ... ...

    Abstract The skeletal muscle protein troponin I (TnI) has been characterized as a potential thermally stable and species-specific biomarker of mammalian muscle tissues in raw meat and meat products. This study proposed a technique for the quantification of TnI comprising protein extraction and sandwich enzyme-linked immunosorbent assay (ELISA). The technique is characterized by a TnI detection limit of 4.8 ng/ml with quantifiable concentrations ranging from 8.7 to 52 ng/ml. The method was shown to be suitable for detection of TnI in mammalian (beef, pork, lamb, and horse) meat but not in poultry (chicken, turkey, and duck) meat. In particular, the TnI content in beef was 0.40 3 ± 0.058 mg/g of wet tissue. The TnI estimations obtained for the pork and beef samples using ELISA were comparable to the proteomic analysis results. Thus, the quantitative study of TnI can be a convenient way to assess the mammalian muscle tissue content of various meat products.
    MeSH term(s) Animals ; Antibodies, Monoclonal/analysis ; Antibodies, Monoclonal/metabolism ; Antibody Specificity ; Biomarkers/analysis ; Cattle ; Enzyme-Linked Immunosorbent Assay ; Food Inspection/methods ; Horses ; Limit of Detection ; Meat/analysis ; Meat Products/analysis ; Muscle, Skeletal/chemistry ; Muscle, Skeletal/metabolism ; Peptide Fragments/analysis ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Protein Stability ; Proteomics/methods ; Reproducibility of Results ; Russia ; Sheep, Domestic ; Sus scrofa ; Troponin I/analysis ; Troponin I/chemistry ; Troponin I/metabolism
    Chemical Substances Antibodies, Monoclonal ; Biomarkers ; Peptide Fragments ; Troponin I
    Language English
    Publishing date 2015-07
    Publishing country England
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 753319-6
    ISSN 1873-4138 ; 0309-1740
    ISSN (online) 1873-4138
    ISSN 0309-1740
    DOI 10.1016/j.meatsci.2015.03.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

    Z 4037: Show issues

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