Tom Ellenberger, D.V.M., Ph.D.


Biochemistry and Molecular Biophysics





Research in the Ellenberger laboratory focuses on the molecular structures and cellular functions of proteins that replicate DNA, repair chemical damage, and regulate chromatin structure. These enzymes and regulatory proteins ensure the faithful transmission of our genetic blueprint to future generations.



  • Chris A. Brosey, Chris Ho, Winnie Z. Long, Sukrit Singh, Kathryn Burnett, Greg L. Hura, Jay C. Nix, Gregory R. Bowman, Tom Ellenberger, and John A. Tainer
    Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor
    Structure. 24(12):2067-2079. (2016) (Abstract)

  • Kukshal, V., Kim, I.K., Hura, G.L., Tomkinson, A.E., Tainer, J.A. and Ellenberger, T.
    Human DNA ligase III bridges two DNA ends to promote specific intermolecular DNA end joining.
    Nucleic Acids Res. 43:7021-7031 (2015). (Abstract)

  • Chen, X., Kim, IK., Honaker, Y., Paudval, S.C., Koh, W.K., Sparks, M., Lis, S., Piwnica-Worms, H., Ellenberger, T. and You, Z.
    14-3-3 proteins restrain the Exo1 nuclease to prevent overresection.
    J Biol Chem 290 12300-12312 (2015). (Abstract)

  • Pascal, J.M. and Ellenberger, T.
    The rise and fall of poly(ADP-ribose): An enzymatic perspective.
    DNA Repair 43:7021-7031 (2015). (Abstract)

  • Ghisays, F., Brace, C.S., Yackly, S.M., Kwon, H.J., Mills, K.F., Kashentseva, E., Dmitriev, I.P., Curiel, D.T., Imai, S.I. and Ellenberger, T.
    The N-Terminal Domain of SIRT1 Is a Positive Regulator of Endogenous SIRT1-Dependent Deacetylation and Transcriptional Outputs.
    Cell Rep. S2211-1247:00182-00185 (2015). (Abstract)

  • Kim, IK., Stegeman, R.A., Brosey, C.A. and Ellenberger, T.
    A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase.
    J Biol Chem 290:3775-3783 (2015.) (Abstract)

  • Wallen, J.R., Majka, J. and Ellenberger, T.
    Discrete interactions between bacteriophage T7 primase-helicase and DNA polymerase drive the formation of a priming complex containing two copies of DNA polymerase.
    Biochemistry 52:4026-4036 (2013). (Abstract)

  • Della-Maria, J., Hegde, M.L., McNeill, D.R., Matsumoto, Y., Tsai, M.S., Ellenberger, T., Wilson, D.M., Mitra, S. and Tomkinson, A.E.
    The interaction between polynucleotide kinase phosphatase and the DNA repair protein XRCC1 is critical for repair of DNA alkylation damage and stable association at DNA damage sites.
    J Biol Chem 287:39233-39244 (2012). (Abstract)

  • Kim, I.K., Kiefer, J.R., Ho, C.M., Stegeman, R.A., Classen, S., Tainer, J.A. and Ellenberger, T.
    Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element.
    Nat Struct Mol Biol 19:653-656 (2012). (Abstract)

  • Ellenberger, T.
    An arresting development in transcription.
    Mol Cell. 46:3-4 (2012). (Abstract)