User:Andrew R. Nager

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Contact Info

  • Andrew R. Nager
  • Stanford University
  • Beckman Center, Rm B107
  • 279 Campus Drive
  • Stanford, CA 94205-5345
  • email

I work in Max Nachury 's lab at Stanford University.


  • 2012, PhD, Massachusetts Institute of Technology
  • 2008, BS, Vanderbilt University


  • 2013, Damon Runyon Fellowship Award link
  • 2013, Martin and Beate Block early-career physicist link

Research interests

Biophysics of primary cilia.


Nager, A.R., Baker, T.A., & Sauer, R.T. (2013) The kinetics of refolding of partially denatured substrates dictates susceptibility to ClpXP degradation. In submission.

• *Stinson, B., *Nager, A.R., *Glynn, S.E., Schmitz, K., Baker, T.A., & Sauer, R.T. (2013) Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell, 153(3): 628-39. link

• Wohlever, M.L., Nager, A.R., Baker, T.A., & Sauer, R.T. (2013) Engineering fluorescent protein substrates for the AAA+ Lon protease. Protein Engineering and Design, in press. link

• Glynn, S.E., Nager, A.R., Baker, T.A., & Sauer, R.T. (2012) Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine. Nature Structure and Molecular Biology, 19(6): 616-22. link

Nager, A.R., Baker, T.A., & Sauer, R.T. (2011) Stepwise unfolding of a beta barrel protein by the AAA+ ClpXP protease. Journal of Molecular Biology, 413(1):4-16. link

• Gaidukov, L., Nager, A.R., Xu, S., Penman, M., & Krieger, M. (2011) Glycine dimerization motif in the N-terminal transmembrane domain of the high density lipoprotein receptor SR-BI required for normal receptor oligomerization and lipid transport. Journal of Biological Chemistry, 286(21): 18452-64. link

• Glynn, S.E., Martin, A., Nager, A.R., Baker, T.A., & Sauer, R.T. (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell, 139(4): 744-56. link

• Fanning, E., Klimovich, V., & Nager, A.R. (2006) A dynamic model for replication protein A (RPA) function in DNA processing pathways. Nucleic Acids Research, 34(15): 4126-37. [review article] link

- * denotes equal contribution

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