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  1. Article ; Online: Plasma hemopexin as a potential regulator of vascular responsiveness to angiotensin II.

    Bakker, Winston W / Spaans, Floor / el Bakkali, Loubna / Borghuis, Theo / van Goor, Harry / van Dijk, Evert / Buijnink, Joshua / Faas, Marijke M

    Reproductive sciences (Thousand Oaks, Calif.)

    2013  Volume 20, Issue 3, Page(s) 234–237

    Abstract: This brief review focuses on the functional activities of plasma hemopexin recently recognized by several authors. In particular, the protease-like activity of hemopexin in vitro is linked with downregulation of the vascular angiotensin II receptor in ... ...

    Abstract This brief review focuses on the functional activities of plasma hemopexin recently recognized by several authors. In particular, the protease-like activity of hemopexin in vitro is linked with downregulation of the vascular angiotensin II receptor in vivo, leading to vascular expansion. Also a potential mechanism of inhibition of hemopexin activity by extracellular adenosine triphosphate is considered.
    MeSH term(s) Angiotensin II/blood ; Animals ; Female ; Hemopexin/physiology ; Humans ; Male ; Pregnancy ; Protein Binding/physiology ; Vasoconstriction/physiology ; Vasodilation/physiology
    Chemical Substances Angiotensin II (11128-99-7) ; Hemopexin (9013-71-2)
    Language English
    Publishing date 2013-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2276411-2
    ISSN 1933-7205 ; 1933-7191
    ISSN (online) 1933-7205
    ISSN 1933-7191
    DOI 10.1177/1933719112446081
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4113: 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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  2. Article ; Online: A viral kinase mimics S6 kinase to enhance cell proliferation.

    Bhatt, Aadra Prashant / Wong, Jason P / Weinberg, Marc S / Host, Kurtis M / Giffin, Louise C / Buijnink, Joshua / van Dijk, Evert / Izumiya, Yoshihiro / Kung, Hsing-Jien / Temple, Brenda R S / Damania, Blossom

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

    2016  Volume 113, Issue 28, Page(s) 7876–7881

    Abstract: Viruses depend upon the host cell for manufacturing components of progeny virions. To mitigate the inextricable dependence on host cell protein synthesis, viruses can modulate protein synthesis through a variety of mechanisms. We report that the viral ... ...

    Abstract Viruses depend upon the host cell for manufacturing components of progeny virions. To mitigate the inextricable dependence on host cell protein synthesis, viruses can modulate protein synthesis through a variety of mechanisms. We report that the viral protein kinase (vPK) encoded by open reading frame 36 (ORF36) of Kaposi's sarcoma-associated herpesvirus (KSHV) enhances protein synthesis by mimicking the function of the cellular protein S6 kinase (S6KB1). Similar to S6KB1, vPK phosphorylates the ribosomal S6 protein and up-regulates global protein synthesis. vPK also augments cellular proliferation and anchorage-independent growth. Furthermore, we report that both vPK and S6KB1 phosphorylate the enzyme 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 2 (PFKFB2) and that both kinases promote endothelial capillary tubule formation.
    MeSH term(s) Computer Simulation ; HEK293 Cells ; Herpesvirus 8, Human/enzymology ; Human Umbilical Vein Endothelial Cells ; Humans ; Models, Molecular ; Ribosomal Protein S6 Kinases, 70-kDa/chemistry ; Ribosomal Protein S6 Kinases, 70-kDa/metabolism ; Substrate Specificity ; Viral Proteins/chemistry ; Viral Proteins/metabolism
    Chemical Substances Viral Proteins ; Ribosomal Protein S6 Kinases, 70-kDa (EC 2.7.11.1) ; ribosomal protein S6 kinase, 70kD, polypeptide 1 (EC 2.7.11.1)
    Language English
    Publishing date 2016-06-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1600587113
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1148: Show issues Location:
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  3. Article: Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis.

    de la Fuente van Bentem, Sergio / Anrather, Dorothea / Dohnal, Ilse / Roitinger, Elisabeth / Csaszar, Edina / Joore, Jos / Buijnink, Joshua / Carreri, Alessandro / Forzani, Celine / Lorkovic, Zdravko J / Barta, Andrea / Lecourieux, David / Verhounig, Andreas / Jonak, Claudia / Hirt, Heribert

    Journal of proteome research

    2008  Volume 7, Issue 6, Page(s) 2458–2470

    Abstract: An estimated one-third of all proteins in higher eukaryotes are regulated by phosphorylation by protein kinases (PKs). Although plant genomes encode more than 1000 PKs, the substrates of only a small fraction of these kinases are known. By mass ... ...

    Abstract An estimated one-third of all proteins in higher eukaryotes are regulated by phosphorylation by protein kinases (PKs). Although plant genomes encode more than 1000 PKs, the substrates of only a small fraction of these kinases are known. By mass spectrometry of peptides from cytoplasmic- and nuclear-enriched fractions, we determined 303 in vivo phosphorylation sites in Arabidopsis proteins. Among 21 different PKs, 12 were phosphorylated in their activation loops, suggesting that they were in their active state. Immunoblotting and mutational analysis confirmed a tyrosine phosphorylation site in the activation loop of a GSK3/shaggy-like kinase. Analysis of phosphorylation motifs in the substrates suggested links between several of these PKs and many target sites. To perform quantitative phosphorylation analysis, peptide arrays were generated with peptides corresponding to in vivo phosphorylation sites. These peptide chips were used for kinome profiling of subcellular fractions as well as H 2O 2-treated Arabidopsis cells. Different peptide phosphorylation profiles indicated the presence of overlapping but distinct PK activities in cytosolic and nuclear compartments. Among different H 2O 2-induced PK targets, a peptide of the serine/arginine-rich (SR) splicing factor SCL30 was most strongly affected. SRPK4 (SR protein-specific kinase 4) and MAPKs (mitogen-activated PKs) were found to phosphorylate this peptide, as well as full-length SCL30. However, whereas SRPK4 was constitutively active, MAPKs were activated by H 2O 2. These results suggest that SCL30 is targeted by different PKs. Together, our data demonstrate that a combination of mass spectrometry with peptide chip phosphorylation profiling has a great potential to unravel phosphoproteome dynamics and to identify PK substrates.
    MeSH term(s) Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/cytology ; Arabidopsis/metabolism ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/metabolism ; Argonaute Proteins ; Cells, Cultured ; Cyclin-Dependent Kinases/chemistry ; Cyclin-Dependent Kinases/metabolism ; GTPase-Activating Proteins/chemistry ; GTPase-Activating Proteins/metabolism ; Glycogen Synthase Kinase 3/chemistry ; Glycogen Synthase Kinase 3/metabolism ; Hydrogen Peroxide/pharmacology ; Mass Spectrometry/methods ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; Myelin Basic Protein/chemistry ; Myelin Basic Protein/metabolism ; Peptides/chemistry ; Peptides/metabolism ; Phosphoproteins/metabolism ; Phosphorylases/chemistry ; Phosphorylases/metabolism ; Phosphorylation/drug effects ; Protein Array Analysis/methods ; Protein Kinases/chemistry ; Protein Kinases/metabolism ; Proteomics/methods
    Chemical Substances AGO1 protein, Arabidopsis ; Arabidopsis Proteins ; Argonaute Proteins ; GTPase-Activating Proteins ; Myelin Basic Protein ; Peptides ; Phosphoproteins ; topless protein, Arabidopsis ; Hydrogen Peroxide (BBX060AN9V) ; Phosphorylases (EC 2.4.1.-) ; Protein Kinases (EC 2.7.-) ; Cyclin-Dependent Kinases (EC 2.7.11.22) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; ATSK11 protein, Arabidopsis (EC 2.7.11.26) ; Glycogen Synthase Kinase 3 (EC 2.7.11.26)
    Language English
    Publishing date 2008-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078618-9
    ISSN 1535-3893
    ISSN 1535-3893
    DOI 10.1021/pr8000173
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 6189: Show issues Location:
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