J T Stivers

Summary

Affiliation: National Institute of Standards and Technology
Country: USA

Publications

  1. pmc 2-Aminopurine fluorescence studies of base stacking interactions at abasic sites in DNA: metal-ion and base sequence effects
    J T Stivers
    Center for Advanced Research in Biotechnology, University of Maryland, Biotechnology Institute and theNational Institute for Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, USA
    Nucleic Acids Res 26:3837-44. 1998
  2. ncbi request reprint Stereochemical outcome and kinetic effects of Rp- and Sp-phosphorothioate substitutions at the cleavage site of vaccinia type I DNA topoisomerase
    J T Stivers
    Center for Advanced Research in Biotechnology of the University of Maryland and the National Institute for Standards and Technology, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA
    Biochemistry 39:5561-72. 2000
  3. ncbi request reprint Heteronuclear NMR and crystallographic studies of wild-type and H187Q Escherichia coli uracil DNA glycosylase: electrophilic catalysis of uracil expulsion by a neutral histidine 187
    A C Drohat
    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, National Institute for Standards and Technology, Rockville, Maryland 20850, USA
    Biochemistry 38:11876-86. 1999
  4. ncbi request reprint Stressing-out DNA? The contribution of serine-phosphodiester interactions in catalysis by uracil DNA glycosylase
    R M Werner
    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and National Institute for Standards and Technology, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA
    Biochemistry 39:12585-94. 2000
  5. ncbi request reprint Escherichia coli uracil DNA glycosylase: NMR characterization of the short hydrogen bond from His187 to uracil O2
    A C Drohat
    Center for Advanced Research in Biotechnology of the National Institute of Standards and Technology and the University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA
    Biochemistry 39:11865-75. 2000
  6. ncbi request reprint Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase
    A C Drohat
    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, National Institute for Standards and Technology, Rockville, Maryland 20850, USA
    Biochemistry 38:11866-75. 1999
  7. ncbi request reprint Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase
    J T Stivers
    Center for Advanced Research in Biotechnology, University of Maryland, National Institute for Standards and Technology, Rockville 20850, USA
    Biochemistry 38:952-63. 1999
  8. ncbi request reprint Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited
    G Xiao
    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute for Standards and Technology, Rockville, 20850, USA
    Proteins 35:13-24. 1999

Collaborators

  • K W Pankiewicz
  • B Nawrot
  • A C Drohat
  • G Xiao
  • G L Gilliland
  • M Tordova
  • J Jagadeesh
  • R M Werner
  • J E Ladner
  • R G Gordley
  • Y L Jiang
  • G J Jagadeesh
  • E Ferguson
  • K A Watanabe

Detail Information

Publications8

  1. pmc 2-Aminopurine fluorescence studies of base stacking interactions at abasic sites in DNA: metal-ion and base sequence effects
    J T Stivers
    Center for Advanced Research in Biotechnology, University of Maryland, Biotechnology Institute and theNational Institute for Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, USA
    Nucleic Acids Res 26:3837-44. 1998
    ..On the basis of these fluorescence studies a model for the local base stacking interactions at these AB sites is proposed...
  2. ncbi request reprint Stereochemical outcome and kinetic effects of Rp- and Sp-phosphorothioate substitutions at the cleavage site of vaccinia type I DNA topoisomerase
    J T Stivers
    Center for Advanced Research in Biotechnology of the University of Maryland and the National Institute for Standards and Technology, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA
    Biochemistry 39:5561-72. 2000
    ..The interaction of His-265 with the pro-Rp nonbridging oxygen is inconsistent with the proposal that this conserved residue acts as a general acid in the strand cleavage reaction...
  3. ncbi request reprint Heteronuclear NMR and crystallographic studies of wild-type and H187Q Escherichia coli uracil DNA glycosylase: electrophilic catalysis of uracil expulsion by a neutral histidine 187
    A C Drohat
    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, National Institute for Standards and Technology, Rockville, Maryland 20850, USA
    Biochemistry 38:11876-86. 1999
    ..Rather, we propose a concerted mechanism involving general base catalysis by Asp64 and electrophilic stabilization of the developing enolate on uracil O2 by a neutral His187...
  4. ncbi request reprint Stressing-out DNA? The contribution of serine-phosphodiester interactions in catalysis by uracil DNA glycosylase
    R M Werner
    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and National Institute for Standards and Technology, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA
    Biochemistry 39:12585-94. 2000
    ..S., et al. (2000) Proc Natl. Acad. Sci. 94, 5083], there is no evidence that conformational strain of the glycosidic bond induced by serine pinching plays a major role in the 10(12)-fold rate enhancement brought about by UDG...
  5. ncbi request reprint Escherichia coli uracil DNA glycosylase: NMR characterization of the short hydrogen bond from His187 to uracil O2
    A C Drohat
    Center for Advanced Research in Biotechnology of the National Institute of Standards and Technology and the University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA
    Biochemistry 39:11865-75. 2000
    ..The role of this H bond in catalysis by UDG and several approaches to quantify the H bond energy are discussed...
  6. ncbi request reprint Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase
    A C Drohat
    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, National Institute for Standards and Technology, Rockville, Maryland 20850, USA
    Biochemistry 38:11866-75. 1999
    ..In the following paper of this issue we establish by crystallography and heteronuclear NMR spectroscopy that the imidazole of His187 is neutral during the catalytic cycle of UDG...
  7. ncbi request reprint Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase
    J T Stivers
    Center for Advanced Research in Biotechnology, University of Maryland, National Institute for Standards and Technology, Rockville 20850, USA
    Biochemistry 38:952-63. 1999
    ..Thus, base flipping contributes little to the free energy of DNA binding but contributes greatly to specificity through an induced-fit mechanism...
  8. ncbi request reprint Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited
    G Xiao
    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute for Standards and Technology, Rockville, 20850, USA
    Proteins 35:13-24. 1999
    ..The catalytic mechanism of UDG is critically discussed with respect to these results...