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Browsing by Subject phosphoryl hóa

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Showing results 1 to 9 of 9
  • OER000002319.pdf.jpg
  • Journal Article

  • A global, integrated view of the ubiquitylation site occupancy and dynamics

    • Authors : Prus, Gabriela (2023)

  • Ubiquitylation regulates virtually all proteins and biological processes in a cell. However, the global site-specific occupancy (stoichiometry) and turnover rate of ubiquitylation have never been quantified. Here, we present the first integrated picture of ubiquitylation site occupancy and half-life. Ubiquitylation occupancy spans four orders of magnitude, but the median ubiquitylation site occupancy is three orders of magnitude lower than that of 20...
  • OER000002921.pdf.jpg
  • Journal article

  • Distinct phosphorylation signals drive acceptor versus self-ubiquitination selection by Parkin

    • Authors : Dunkerley, Karen M. (2021)

  • The RBR E3 ligase parkin is recruited to the outer mitochondrial membrane (OMM) during oxidative stress where it becomes activated and ubiquitinates numerous proteins. Parkin activation involves bind ing of a phosphorylated ubiquitin (pUb), followed by phosphorylation of parkin itself, both mediated by the OMM kinase, PINK1. However, targeted mitochon drial proteins have little structural or sequence sim ilarity, with the commonality between su...
  • OER000002739.pdf.jpg
  • Journal article

  • PKD autoinhibition in trans regulates activation loop autophosphorylation in cis

    • Authors : Reinhardt, Ronja (2023)

  • Phosphorylation is a ubiquitous mechanism by which signals are transduced in cells. Protein kinases, enzymes that catalyze the phospho-transfer reaction are, themselves, often regulated by phosphorylation. Paradoxically, however, a substantial fraction of the more than 500 human protein kinases are capable of catalyzing their own activation loop phosphorylation. Commonly, these kinases perform this autophosphorylation reaction in trans, whereby transient dimerizat...
  • OER000002765.pdf.jpg
  • Journal article

  • Protein-Peptide Turnover Profiling reveals wiring of phosphorylation during protein maturation

    • Authors : Hammarén, Henrik M. (2023)

  • Post-translational modifications (PTMs) regulate various aspects of protein function, including degradation. Mass spectrometric methods that rely on pulsed metabolic labeling are very popular to quantify turnover rates on a proteome-wide scale. Such data have often been interpreted in the context of protein proteolytic stability. Here, we combine theoretical kinetic modeling with experimental pulsed stable isotope labeling of amino acids in cell culture&...
  • OER000002604.pdf.jpg
  • Journal article

  • Specific targeting and clustering of Phosphatidylserine lipids by RSV M protein is critical for virus particle production

    • Authors : Swain, Jitendriya (2023)

  • Human Respiratory Syncytial virus (RSV) is the leading cause of infantile bronchiolitis in the developed world and of childhood deaths in resource-poor settings. The elderly and the immunosuppressed are also affected. It is a major unmet target for vaccines and anti-viral drugs. RSV assembles and buds from the host cell plasma membrane by forming infections viral particles which are mostly filamentous. A key interaction during RSV asse...
  • OER000002498.pdf.jpg
  • Journal article

  • Structural Insights into the Iron Nitrogenase Complex

    • Authors : Schmidt, Frederik V.  (2023)

  • Nitrogenases are best known for catalysing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO2) and carbon monoxide to hydrocarbons, offering a pathway to recycle carbon waste into hydrocarbon products. Among the nitrogenase family the iron nitrogenase is the isozyme with the highest wildtype activity for the reduction of CO2, but the molecular architecture facilitating these&#...
  • OER000002614.pdf.jpg
  • Journal article

  • The cardiac myosin binding protein-C phosphorylation state as a function of multiple protein kinase and phosphatase activities

    • Authors : Kampourakis, Thomas (2023)

  • Phosphorylation of cardiac myosin binding protein-C (cMyBP-C) is a crucial determinant of cardiac myofilament function. Although cMyBP-C phosphorylation by various protein kinases has been extensively studied, the influence of protein phosphatases on cMyBP-C’s multiple phosphorylation sites has remained largely obscure. Here we provide a detailed biochemical characterization of cMyBP-C dephosphorylation by protein phosphatases 1 and 2A (PP1 and PP2A) and deve...
  • OER000002359.pdf.jpg
  • Journal Article

  • Validity of the cell-extracted proteome as a substrate pool for exploring phosphorylation motifs of kinases

    • Authors : Ishihama, Yasushi (2023)

  • Three representative protein kinases with different substrate preferences, ERK1 (Prodirected), CK2 (acidophilic), and PKA (basophilic), were used to investigate phosphorylation sequence motifs in substrate pools consisting of the proteomes from three different cell lines, MCF7 (human mammary carcinoma), HeLa (human cervical carcinoma), and Jurkat (human acute T-cell leukemia). Specifically, recombinant kinases were added to the cell-extracted proteomes to phosphorylate...