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Lysines and cysteines: partners in stress?
Rabe von Pappenheim, Fabian; Tittmann, Kai.
  • Rabe von Pappenheim F; Department of Molecular Enzymology, Göttingen Center of Molecular Biosciences, Georg August University Göttingen, Julia-Lermontowa-Weg 3, D-37077 Göttingen, Germany; Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany. Electronic address: fpappen@gwdg.de.
  • Tittmann K; Department of Molecular Enzymology, Göttingen Center of Molecular Biosciences, Georg August University Göttingen, Julia-Lermontowa-Weg 3, D-37077 Göttingen, Germany; Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany. Electronic address: ktittma@gwdg.de.
Trends Biochem Sci ; 47(5): 372-374, 2022 05.
Article in English | MEDLINE | ID: covidwho-1821500
ABSTRACT
Modifications of cysteine residues in redox-sensitive proteins are key to redox signaling and stress response in all organisms. A novel type of redox switch was recently discovered that comprises lysine and cysteine residues covalently linked by an nitrogen-oxygen-sulfur (NOS) bridge. Here, we discuss chemical and biological implications of this discovery.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Cysteine / Lysine Language: English Journal: Trends Biochem Sci Year: 2022 Document Type: Article

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Cysteine / Lysine Language: English Journal: Trends Biochem Sci Year: 2022 Document Type: Article