Bob Sauer's Lab

ANDREW R. "DREW" NAGER

Andrew R. Nager
Graduate Student (2009-2012)
and Visiting Scientist through February 2013
Email (andrewrn [at] stanford.edu)
Damon Runyon Fellow
Stanford University School of Medicine
Nachury Lab (http://openwetware.org/wiki/Nachury )

Stinson, B.M., Nager, A.R., Glynn, S.E., Schmitz, K.R., 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.

Wohlever ML, Nager AR, Baker TA . & Sauer, RT (2013) Engineering fluorescent protein substrates for the AAA+ Lon Protease . Protein Eng Des Sei - Epub 2013. January 28. PMID 23359718.

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. Nat. Struct. Mol. Biol. 19, 616-622.

Nager, A.R., Baker, T.A. & Sauer, R.T. (2011) Stepwise unfolding of a β-barrel protein by the AAA+ ClpXP protease. J. Mol. Biol. 413, 4-16 .

Glynn, S.E., Martin, A., Nager, A.R., Baker, T.A. and Sauer R.T. (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell, 139, 744-756.

RANDALL MAULDIN

Randall Mauldin
Posdoctoral Associate (March 2010-June 2011)
and NIH Postdoctoral Fellow (July 2011- March 2012)
Email (rmauldin [at] alumni.unc.edu)

Scientist
Momenta Pharmaceuticals, Inc.

Mauldin, R.V., and Sauer R.T. (2013) Allosteric regulation of DegS protease subunits through a shared energy landscape. Nature Chemical Biology , 9, 90-96.

STEVEN GLYNN

Steven Glynn
Postdoc Associate (2005-January 2012)
Email (steven.glynn [at] stonybrook.edu)

Faculty
Stony Brook University

Stinson, B.M., Nager, A.R., Glynn, S.E., Schmitz, K.R., 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.

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. Nat. Struct. Mol. Biol. 19, 616-622.

Glynn, S.E., Martin, A., Nager, A.R., Baker, T.A. and Sauer R.T. (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell, 139, 744-756.

SANTIAGO LIMA

Santiago Lima
Postdoc Associate (2008-2010)
NIH Postdoc Fellow (July 2010-December 2011)
Email (slima [at] vcu.edu)
Postdoctoral Fellow
Virginia Commonwealth University

Lima, S., Guo, M.S., Chaba, R., Gross, C.A. & Sauer, R.T. (2013) Dual Molecular Signals Mediate the Bacterial Response to Outer-Membrane Stress. Science 340(6134):837-41.

JIEJIN CHEN

Jiejin Chen
Postdoc Associate (2009-November 2011)
Email (jiejinc [at] gmail.com)

Scientist I
Millennium Pharmaceuticals, Inc.

SHANKAR SUNDAR

Shankar Sundar
Graduate Student (2006-2011)
Email (ssundar06 [at] gmail.com)

Associate Consultant
Campbell Alliance

Sundar, S., Baker, T.A. & Sauer, R.T. (2012) The I domain of the AAA+ Hs1UV protease coordinates substrate binding, ATP hydrolysis, and protein degradation. Protein Science 21, 188-198.

Sundar, S., McGinness, K.E., Baker, T.A. & Sauer, R.T. (2010) Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease Hs1UV. J. Mol. Biol. 403, 420-429.

JUNGSAN SOHN

Jungsan "J" Sohn
NIH Postdoc Fellow (2008-2011)
Email (jsohn at jhmi.edu)

Faculty
Johns Hopkins University School of Medicine

Sohn J., Grant, R.A., Sauer, R.T. (2010) Allostery is an intrinsic property of the protease domain of DegS: Implications for enzyme function and evolution J. Biol. Chem. 285: 34039-47

Sohn J., Grant, R.A., Sauer, R.T. (2009) OMP peptides activate the DegS protease by a relief of inhibition mechanism. Structure 17, 1411-21

Sohn, J. & Sauer, R.T. (2009) OMP peptides modulate the activity of Degs protease by differential binding to active and inactive conformations. Mol. Cell 33, 64-74.

Sohn, J., Grant, R.A., Sauer, R.T. (2007) Allosteric activation of DegS, a stress sensor PDZ-protease. Cell. 131 572-583.