Andrzej Krezel, Ph.D.

Associate Professor

Biochemistry and Molecular Biophysics

Publications (PubMed / NIH)

Office: 262 McDonnell Science
Phone: 314-362-8482
Email: krezela(at)


Structural biology of transcriptional regulation in gastric pathogen Helicobacter pylori.

Krezel research


  • Shu, Q., Krezel, A.M., Cusumano, Z.T., Pinkner, J.S., Klein, R., Hultgren, S.J. and Frieden, C. Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation. Proc Natl Acad Sci USA 113:7130-7135 (2016). [Abstract]
  • Krishna, U., Romero-Gallo, J., Suarez, G., Azah, A., Krezel, A.M., Varga, M.G., Forsyth, M.H. and Peek, R.M. Jr. Genetic evolution of a Helicobacter pylori acid-sensing histidine kinase and gastric disease. J Infect Dis. (E-pub ahead of print.) (2016). [Abstract]
  • Borin, B.N., Tang, W. and Krezel, A.M. Helicobacter pylori RNA polyerase α-subunit D-terminal domain shows features unique to ε-proteobacteria and binds NikR/DNA complexes. Protein Science 23:454-463 (2014). [Abstract]
  • Borin, B.N., Tang, W., Nice, T.J., McCune, B.T., Virgin, H.W. and Krezel, A.M. Murine Norovirus Protein NS1/2 Aspartate to Glutamate Mutation, Sufficient for Persistence, Reorients Side Chain of Surface Exposed Tryptophan within a Novel Structured Domain. Proteins (E-pub ahead of print. (2013). [Abstract]
  • Loh, J.T., Gupta, S.S., Friedman, D.B., Krezel, A.M. and Cover, T.L. Analysis of protein expression regulated by the Helicobacter pylori ArsRS two-component signal transduction system. J Bacteriol. 192:2034-2043. (2010). [Abstract]
  • Gupta, S.S., Borin, B.N., Cover, T.L. and Krezel, A.M. Structural analysis of the DNA-binding domain of the Helicobacter pylori response regulator ArsR. J Biol Chem. 284:6536-6545 (2009). [Abstract]
  • Borin, B.N. and Krezel, A.M. Structure of HP0564 from Helicobacter pylori identifies it as a new transcriptional regulator. Proteins 73:265-268. (2008). [Abstract]
  • Hu, T., Krezel, A.M., Li, C. and Coffey, R.J. Structural studies of human Naked2: a biologically active intrinsically unstructured protein. Biochem Biophys Res Commun. 350:911-915 (2006). [Abstract]