User:Andrew R. Nager: Difference between revisions
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==Contact Info== | ==Contact Info== | ||
[[Image: | [[Image:Drew.png#file|thumb|right|]] | ||
*Andrew R. Nager | *Andrew R. Nager | ||
*Stanford University | *Stanford University | ||
*Beckman Center, Rm | *Beckman Center, Rm B107 | ||
*279 Campus Drive | *279 Campus Drive | ||
*Stanford, CA 94205-5345 | *Stanford, CA 94205-5345 | ||
*[ | *[mailto:andrew.r.nager@gmail.com email] | ||
I work in [ | I work in [http://openwetware.org/wiki/Nachury Max Nachury] 's lab at Stanford University. | ||
==Education== | ==Education== | ||
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* 2012, PhD, Massachusetts Institute of Technology | * 2012, PhD, Massachusetts Institute of Technology | ||
* 2008, BS, Vanderbilt University | * 2008, BS, Vanderbilt University | ||
==Awards== | |||
* 2013, Damon Runyon Fellowship Award [http://www.damonrunyon.org link] | |||
* 2013, Martin and Beate Block early-career physicist [http://www.aspenphys.org/physicists/winter/block.html link] | |||
==Research interests== | ==Research interests== | ||
<!-- Feel free to add brief descriptions to your research interests as well --> | <!-- Feel free to add brief descriptions to your research interests as well --> | ||
Biophysics of primary cilia. | |||
==Publications== | ==Publications== | ||
• | • <ins>Nager, A.R.</ins>, Baker, T.A., & Sauer, R.T. (2013) The kinetics of refolding of partially denatured substrates dictates susceptibility to ClpXP degradation. In submission. | ||
• *Stinson, B., <ins>*Nager, A.R.</ins>, *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. [http://www.sciencedirect.com/science/article/pii/S0092867413003516 link] | |||
• Wohlever, M.L., <ins>Nager, A.R.</ins>, Baker, T.A., & Sauer, R.T. (2013) Engineering fluorescent protein substrates for the AAA+ Lon protease. '''Protein Engineering and Design''', in press. [http://peds.oxfordjournals.org/content/early/2013/01/28/protein.gzs105.long link] | |||
• Glynn, S.E., <ins>Nager, A.R.</ins>, 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. [http://www.nature.com/nsmb/journal/v19/n6/full/nsmb.2288.html link] | • Glynn, S.E., <ins>Nager, A.R.</ins>, 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. [http://www.nature.com/nsmb/journal/v19/n6/full/nsmb.2288.html link] | ||
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• Glynn, S.E., Martin, A., <ins>Nager, A.R.</ins>, 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. [http://www.sciencedirect.com/science/article/pii/S0092867409013075 link] | • Glynn, S.E., Martin, A., <ins>Nager, A.R.</ins>, 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. [http://www.sciencedirect.com/science/article/pii/S0092867409013075 link] | ||
• Fanning, E., Klimovich, V., & <ins>Nager, A.R.</ins> (2006) A dynamic model for replication protein A (RPA) function in DNA processing pathways. '''Nucleic Acids Research''', 34(15): 4126-37. [http://nar.oxfordjournals.org/content/34/15/4126.long link] | • Fanning, E., Klimovich, V., & <ins>Nager, A.R.</ins> (2006) A dynamic model for replication protein A (RPA) function in DNA processing pathways. '''Nucleic Acids Research''', 34(15): 4126-37. [review article] [http://nar.oxfordjournals.org/content/34/15/4126.long link] | ||
- * denotes equal contribution | |||
==Useful links== | ==Useful links== | ||
*[[OpenWetWare:Welcome|Introductory tutorial]] | *[[OpenWetWare:Welcome|Introductory tutorial]] | ||
*[[Help|OpenWetWare help pages]] | *[[Help|OpenWetWare help pages]] | ||
Latest revision as of 12:21, 13 May 2013
I am a new member of OpenWetWare!
Contact Info
- Andrew R. Nager
- Stanford University
- Beckman Center, Rm B107
- 279 Campus Drive
- Stanford, CA 94205-5345
I work in Max Nachury 's lab at Stanford University.
Education
- 2012, PhD, Massachusetts Institute of Technology
- 2008, BS, Vanderbilt University
Awards
Research interests
Biophysics of primary cilia.
Publications
• 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
