Publications

Found 21 results
Filters: Author is Sauer, Robert T  [Clear All Filters]
Journal Article
Levchenko, I., Grant, R. A., Flynn, J. M., Sauer, R. T., and Baker, T. A. (2005) Versatile modes of peptide recognition by the AAA+ adaptor protein SspB. Nat Struct Mol Biol. 12, 520-5
Brown, B. L., Kardon, J. R., Sauer, R. T., and Baker, T. A. (2018) Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure. 10.1016/j.str.2018.02.012
Chien, P., Grant, R. A., Sauer, R. T., and Baker, T. A. (2007) Structure and substrate specificity of an SspB ortholog: design implications for AAA+ adaptors. Structure. 15, 1296-305
Baytshtok, V., Fei, X., Grant, R. A., Baker, T. A., and Sauer, R. T. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure. 24, 1766-1777
Stein, B. J., Grant, R. A., Sauer, R. T., and Baker, T. A. (2016) Structural Basis of an N-Degron Adaptor with More Stringent Specificity. Structure. 24, 232-42
Hari, S. B., Grant, R. A., and Sauer, R. T. (2018) Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase.. Structure. 10.1016/j.str.2018.06.008
Bolon, D. N., Grant, R. A., Baker, T. A., and Sauer, R. T. (2005) Specificity versus stability in computational protein design. Proc Natl Acad Sci U S A. 102, 12724-9
Sohn, J., Grant, R. A., and Sauer, R. T. (2009) OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure. 17, 1411-21
Bolon, D. N., Grant, R. A., Baker, T. A., and Sauer, R. T. (2004) Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease. Mol Cell. 16, 343-50
Stinson, B. M., Nager, A. R., Glynn, S. E., Schmitz, K. R., Baker, T. A., and Sauer, R. T. (2013) Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell. 153, 628-39
Román-Hernández, G., Grant, R. A., Sauer, R. T., and Baker, T. A. (2009) Molecular basis of substrate selection by the N-end rule adaptor protein ClpS. Proc Natl Acad Sci U S A. 106, 8888-93
Wang, K. H., Román-Hernández, G., Grant, R. A., Sauer, R. T., and Baker, T. A. (2008) The molecular basis of N-end rule recognition. Mol Cell. 32, 406-14
Baytshtok, V., Fei, X., Shih, T. - T., Grant, R. A., Santos, J. C., Baker, T. A., and Sauer, R. T. (2021) Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Rep. 34, 108639
Schreiter, E. R., Sintchak, M. D., Guo, Y., Chivers, P. T., Sauer, R. T., and Drennan, C. L. (2003) Crystal structure of the nickel-responsive transcription factor NikR. Nat Struct Biol. 10, 794-9
Schmitz, K. R., Carney, D. W., Sello, J. K., and Sauer, R. T. (2014) Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery. Proc Natl Acad Sci U S A. 111, E4587-95
Baytshtok, V., Chen, J., Glynn, S. E., Nager, A. R., Grant, R. A., Baker, T. A., and Sauer, R. T. (2017) Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. J Biol Chem. 292, 5695-5704
Kim, S., Grant, R. A., and Sauer, R. T. (2011) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell. 145, 67-78
Tabtiang, R. K., Cezairliyan, B. O., Grant, R. A., Cochrane, J. C., and Sauer, R. T. (2005) Consolidating critical binding determinants by noncyclic rearrangement of protein secondary structure. Proc Natl Acad Sci U S A. 102, 2305-9
Mawla, G. D., Hall, B. M., Cárcamo-Oyarce, G., Grant, R. A., Zhang, J. Jia, Kardon, J. R., Ribbeck, K., Sauer, R. T., and Baker, T. A. (2020) ClpP1P2 peptidase activity promotes biofilm formation in P. aeruginosa. Mol Microbiol. 10.1111/mmi.14649
Sohn, J., Grant, R. A., and 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., and Sauer, R. T. (2007) Allosteric activation of DegS, a stress sensor PDZ protease. Cell. 131, 572-83