Sonja A Dames

Summary

Country: Germany

Publications

  1. pmc Structural basis for the association of the redox-sensitive target of rapamycin FATC domain with membrane-mimetic micelles
    Sonja A Dames
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland
    J Biol Chem 285:7766-75. 2010
  2. pmc Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C
    Sonja A Dames
    Department of Chemistry, Technische Universitat Munchen, Lichtenbergstrasse 4, 85747 Garching, Germany
    J Biol Chem 286:36907-20. 2011
  3. doi request reprint 1H, 15N, and 13C assignments of the N-terminal activation domain of Dictyostelium discoideum Formin C
    Sonja A Dames
    Department of Chemistry, Biomolecular NMR Spectroscopy, Technische Universitat Munchen, Garching, Germany
    Biomol NMR Assign 5:47-9. 2011
  4. pmc Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb
    Sonja A Dames
    Department of Structural Biology, Biozentrum Basel, University of Basel, 4003 Basel, Switzerland
    Proc Natl Acad Sci U S A 104:14312-7. 2007
  5. ncbi request reprint NMR assignment of the Cyclin T-binding domain of human Hexim1
    Sonja A Dames
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstr 70, Basel, 4056, Switzerland
    J Biomol NMR 36:39. 2006
  6. ncbi request reprint The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability
    Sonja A Dames
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland
    J Biol Chem 280:20558-64. 2005
  7. doi request reprint Insights into the low adhesive capacity of human T-cadherin from the NMR structure of Its N-terminal extracellular domain
    Sonja A Dames
    Department of Structural Biology, University of Basel, Klingelbergstr 70, 4056 Basel, Switzerland
    J Biol Chem 283:23485-95. 2008
  8. pmc NMR- and circular dichroism-monitored lipid binding studies suggest a general role for the FATC domain as membrane anchor of phosphatidylinositol 3-kinase-related kinases (PIKK)
    Lisa A M Sommer
    Department of Chemistry, Technische Universitat Munchen, Lichtenbergstrasse 4, 85747 Garching, Germany
    J Biol Chem 288:20046-63. 2013
  9. pmc A fast and simple method for probing the interaction of peptides and proteins with lipids and membrane-mimetics using GB1 fusion proteins and NMR spectroscopy
    Lisa A M Sommer
    Department of Chemistry, Biomolecular NMR Spectroscopy, Technische Universitat Munchen, Munich, Germany
    Protein Sci 21:1566-70. 2012
  10. doi request reprint The FKBP-rapamycin binding domain of human TOR undergoes strong conformational changes in the presence of membrane mimetics with and without the regulator phosphatidic acid
    Diana C Rodriguez Camargo
    Biomolecular NMR Spectroscopy, Department of Chemistry, Technische Universitat Munchen, Munich, Germany
    Biochemistry 51:4909-21. 2012

Collaborators

Detail Information

Publications11

  1. pmc Structural basis for the association of the redox-sensitive target of rapamycin FATC domain with membrane-mimetic micelles
    Sonja A Dames
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland
    J Biol Chem 285:7766-75. 2010
    ....
  2. pmc Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C
    Sonja A Dames
    Department of Chemistry, Technische Universitat Munchen, Lichtenbergstrasse 4, 85747 Garching, Germany
    J Biol Chem 286:36907-20. 2011
    ..Our cellular localization studies show that both the GBD and the FH3 domain are required for ForC targeting to cell-cell contacts and early phagocytic cups and macropinosomes...
  3. doi request reprint 1H, 15N, and 13C assignments of the N-terminal activation domain of Dictyostelium discoideum Formin C
    Sonja A Dames
    Department of Chemistry, Biomolecular NMR Spectroscopy, Technische Universitat Munchen, Garching, Germany
    Biomol NMR Assign 5:47-9. 2011
    ..Chemical shifts have been deposited at the BioMagResBank under the BMRB accession number 17,029. The N-terminal region of the 131 kDa ForC protein is supposed to form a GTPase-binding domain required for activation of the formin...
  4. pmc Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb
    Sonja A Dames
    Department of Structural Biology, Biozentrum Basel, University of Basel, 4003 Basel, Switzerland
    Proc Natl Acad Sci U S A 104:14312-7. 2007
    ..Thus, our studies provide structural insights how Hexim1 recognizes the Cyclin T1 subunit of P-TEFb, which is a key step toward the regulation of transcription elongation...
  5. ncbi request reprint NMR assignment of the Cyclin T-binding domain of human Hexim1
    Sonja A Dames
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstr 70, Basel, 4056, Switzerland
    J Biomol NMR 36:39. 2006
  6. ncbi request reprint The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability
    Sonja A Dames
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland
    J Biol Chem 280:20558-64. 2005
    ..Because the amount of TOR mRNA is not changed, the redox state of the FATC disulfide bond is probably influencing the degradation of TOR...
  7. doi request reprint Insights into the low adhesive capacity of human T-cadherin from the NMR structure of Its N-terminal extracellular domain
    Sonja A Dames
    Department of Structural Biology, University of Basel, Klingelbergstr 70, 4056 Basel, Switzerland
    J Biol Chem 283:23485-95. 2008
    ..The apparent low adhesiveness of T-cadherin suggests that it is likely to be involved in reversible and dynamic cellular adhesion-deadhesion processes, which are consistent with its role in cell growth and migration...
  8. pmc NMR- and circular dichroism-monitored lipid binding studies suggest a general role for the FATC domain as membrane anchor of phosphatidylinositol 3-kinase-related kinases (PIKK)
    Lisa A M Sommer
    Department of Chemistry, Technische Universitat Munchen, Lichtenbergstrasse 4, 85747 Garching, Germany
    J Biol Chem 288:20046-63. 2013
    ..In contrast, the FATC domains of the other PIKKs are rather unstructured in the isolated form and only significantly populate α-helical secondary structure upon interaction with membrane mimetics. ..
  9. pmc A fast and simple method for probing the interaction of peptides and proteins with lipids and membrane-mimetics using GB1 fusion proteins and NMR spectroscopy
    Lisa A M Sommer
    Department of Chemistry, Biomolecular NMR Spectroscopy, Technische Universitat Munchen, Munich, Germany
    Protein Sci 21:1566-70. 2012
    ..To demonstrate the usefulness of the approach, we show NMR binding data for the wild type protein and a leucine to alanine mutant...
  10. doi request reprint The FKBP-rapamycin binding domain of human TOR undergoes strong conformational changes in the presence of membrane mimetics with and without the regulator phosphatidic acid
    Diana C Rodriguez Camargo
    Biomolecular NMR Spectroscopy, Department of Chemistry, Technische Universitat Munchen, Munich, Germany
    Biochemistry 51:4909-21. 2012
    ..Consistent with overlapping binding surfaces for different lipids and the FKBP12-rapamycin complex, binding of the inhibitor complex protects the FRB domain from interactions with membrane mimetics at lower lipid concentrations...
  11. doi request reprint A fast and simple method to prepare the FKBP-rapamycin binding domain of human target of rapamycin for NMR binding assays
    Sonja A Dames
    Biozentrum Basel, Department of Structural Biology, University of Basel, Klingelbergstr 70, 4056 Basel, Switzerland
    Protein Expr Purif 59:31-7. 2008
    ..The procedure is very simple and can easily be scaled up to prepare large amounts of functional protein for high-throughput cancer drug screening assays by NMR and other techniques...