Danna B Zimmer

Summary

Affiliation: University of Maryland
Country: USA

Publications

  1. doi request reprint Evolution of the S100 family of calcium sensor proteins
    Danna B Zimmer
    Center for Biomolecular Therapeutics and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, MD 20102, USA
    Cell Calcium 53:170-9. 2013
  2. pmc In vivo screening of S100B inhibitors for melanoma therapy
    Danna B Zimmer
    Department of Biochemistry and Molecular Biology, Center for BioMolecular Therapeutics, The University of Maryland School of Medicine, Baltimore, MD, USA
    Methods Mol Biol 963:303-17. 2013
  3. pmc S100A1 and calmodulin compete for the same binding site on ryanodine receptor
    Nathan T Wright
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA
    J Biol Chem 283:26676-83. 2008
  4. pmc The Qgamma component of intra-membrane charge movement is present in mammalian muscle fibres, but suppressed in the absence of S100A1
    Benjamin L Prosser
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N Greene Street, Baltimore, MD 21201, USA
    J Physiol 587:4523-41. 2009
  5. pmc Simultaneous recording of intramembrane charge movement components and calcium release in wild-type and S100A1-/- muscle fibres
    Benjamin L Prosser
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N Greene Street, Baltimore, MD 21201, USA
    J Physiol 587:4543-59. 2009
  6. pmc Solution structure of S100A1 bound to the CapZ peptide (TRTK12)
    Nathan T Wright
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, MD 21201, USA
    J Mol Biol 386:1265-77. 2009
  7. pmc S100A1 promotes action potential-initiated calcium release flux and force production in skeletal muscle
    Benjamin L Prosser
    Center for Biomedical Engineering and Technology, University of Maryland, Baltimore, Maryland, USA
    Am J Physiol Cell Physiol 299:C891-902. 2010
  8. ncbi request reprint S100A1 binds to the calmodulin-binding site of ryanodine receptor and modulates skeletal muscle excitation-contraction coupling
    Benjamin L Prosser
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA
    J Biol Chem 283:5046-57. 2008
  9. ncbi request reprint The three-dimensional solution structure of Ca(2+)-bound S100A1 as determined by NMR spectroscopy
    Nathan T Wright
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N Greene St, Baltimore, MD 21201, USA
    J Mol Biol 353:410-26. 2005
  10. ncbi request reprint Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR
    Richard R Rustandi
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, Maryland 21201, USA
    Biochemistry 41:788-96. 2002

Collaborators

  • Martin F Schneider
  • Richard M Lovering
  • Werner Melzer
  • Donna M Baldisseri
  • Benjamin L Prosser
  • Nathan T Wright
  • David J Weber
  • Erick O Hern├índez-Ochoa
  • Kristen M Varney
  • Richard R Rustandi
  • Zoita Andronache
  • Paul T Wilder
  • Michael T Morgan
  • Brian R Cannon
  • Rotimi O Olojo
  • Yewei Liu
  • Rossitza K Gitti
  • Joseph Markowitz
  • Karen C Ellis
  • Alexander Landar
  • Shannon M Hamilton
  • Keith G Inman
  • Peter Nizner
  • Aimee Landar

Detail Information

Publications10

  1. doi request reprint Evolution of the S100 family of calcium sensor proteins
    Danna B Zimmer
    Center for Biomolecular Therapeutics and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, MD 20102, USA
    Cell Calcium 53:170-9. 2013
    ..Examination of annotated S100s in lower vertebrates suggests that the ancestral S100 was a member of the A1/A10/A11/B/P/Z subgroup and arose near the emergence of vertebrates approximately 500 million years ago...
  2. pmc In vivo screening of S100B inhibitors for melanoma therapy
    Danna B Zimmer
    Department of Biochemistry and Molecular Biology, Center for BioMolecular Therapeutics, The University of Maryland School of Medicine, Baltimore, MD, USA
    Methods Mol Biol 963:303-17. 2013
    ..This chapter briefly describes the development of S100B inhibitors, termed SBiXs, for melanoma therapy with a focus on the inclusion of in vivo screening at an early stage in the drug discovery process...
  3. pmc S100A1 and calmodulin compete for the same binding site on ryanodine receptor
    Nathan T Wright
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA
    J Biol Chem 283:26676-83. 2008
    ..A model for regulating muscle contraction is presented in which Ca(2+)-S100A1 and Ca(2+)-CaM compete directly for the same binding site on the ryanodine receptor...
  4. pmc The Qgamma component of intra-membrane charge movement is present in mammalian muscle fibres, but suppressed in the absence of S100A1
    Benjamin L Prosser
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N Greene Street, Baltimore, MD 21201, USA
    J Physiol 587:4523-41. 2009
    ..These results shed light on voltage sensor activation in mammalian muscle, and support S100A1 as a positive regulator of the voltage sensor and Ca(2+) release channel in skeletal muscle EC coupling...
  5. pmc Simultaneous recording of intramembrane charge movement components and calcium release in wild-type and S100A1-/- muscle fibres
    Benjamin L Prosser
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N Greene Street, Baltimore, MD 21201, USA
    J Physiol 587:4543-59. 2009
    ..The decreased Ca(2+) release at each voltage is insufficient to activate Q(gamma) in fibres lacking S100A1...
  6. pmc Solution structure of S100A1 bound to the CapZ peptide (TRTK12)
    Nathan T Wright
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, MD 21201, USA
    J Mol Biol 386:1265-77. 2009
    ..Such comparisons, including those with other S100-target and S100-drug complexes, provide the basis for designing novel small-molecule inhibitors that could be specific for blocking one or more S100-target protein interactions...
  7. pmc S100A1 promotes action potential-initiated calcium release flux and force production in skeletal muscle
    Benjamin L Prosser
    Center for Biomedical Engineering and Technology, University of Maryland, Baltimore, Maryland, USA
    Am J Physiol Cell Physiol 299:C891-902. 2010
    ..We conclude that the absence of S100A1 suppresses physiological AP-induced Ca(2+) release flux, resulting in impaired contractile activation and force production in skeletal muscle...
  8. ncbi request reprint S100A1 binds to the calmodulin-binding site of ryanodine receptor and modulates skeletal muscle excitation-contraction coupling
    Benjamin L Prosser
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA
    J Biol Chem 283:5046-57. 2008
    ..This warrants further investigation into the use of S100A1 as a therapeutic target for the treatment of both cardiac and skeletal myopathies...
  9. ncbi request reprint The three-dimensional solution structure of Ca(2+)-bound S100A1 as determined by NMR spectroscopy
    Nathan T Wright
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N Greene St, Baltimore, MD 21201, USA
    J Mol Biol 353:410-26. 2005
    ....
  10. ncbi request reprint Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR
    Richard R Rustandi
    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, Maryland 21201, USA
    Biochemistry 41:788-96. 2002
    ..As with S100B, it is likely that the second EF-hand of apo-S100A1 reorients dramatically upon the addition of Ca(2+), which can explain the Ca(2+) dependence that S100A1 has for binding several of its biological targets...