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Edith H. Postel

Department of Molecular Biology

Princeton University

NJ 08540

USA

[email]@*.princeton.edu

Name/email consistency: high

 
 
 
 
 
 
 

Affiliation

  • Department of Molecular Biology, Princeton University, NJ 08540, USA. 1998 - 2003

References

  1. Multiple biochemical activities of NM23/NDP kinase in gene regulation. Postel, E.H. J. Bioenerg. Biomembr. (2003) [Pubmed]
  2. Escherichia coli nucleoside diphosphate kinase is a uracil-processing DNA repair nuclease. Postel, E.H., Abramczyk, B.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  3. Structure-based mutational and functional analysis identify human NM23-H2 as a multifunctional enzyme. Postel, E.H., Abramczyk, B.A., Gursky, S.K., Xu, Y. Biochemistry (2002) [Pubmed]
  4. Catalysis of DNA cleavage and nucleoside triphosphate synthesis by NM23-H2/NDP kinase share an active site that implies a DNA repair function. Postel, E.H., Abramczyk, B.M., Levit, M.N., Kyin, S. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  5. Human NM23/nucleoside diphosphate kinase regulates gene expression through DNA binding to nuclease-hypersensitive transcriptional elements. Postel, E.H., Berberich, S.J., Rooney, J.W., Kaetzel, D.M. J. Bioenerg. Biomembr. (2000) [Pubmed]
  6. Cleavage of DNA by human NM23-H2/nucleoside diphosphate kinase involves formation of a covalent protein-DNA complex. Postel, E.H. J. Biol. Chem. (1999) [Pubmed]
  7. NM23-NDP kinase. Postel, E.H. Int. J. Biochem. Cell Biol. (1998) [Pubmed]
 
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