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SAUER LAB
BIOLOGY DEPARTMENT
Current Members
Bob Sauer
Salvador E. Luria Professor of Biology
Principal Investigator (1978 - Present)
Email (bobsauer [at] mit.edu)Current C.V.
Kresge, N., Simoni, R., and Hill, R. (2009)
A Model for Protein Turnover: the Work of
Robert T. Sauer J Biol Chem 284(49): e22-e23, PMC2797215.
Professor Sauer teaches:
Graduate Biochemistry (7.51)
Robert A.Grant
esearch Scientist (2000 - Present)
Email (ragrant [at] mit.edu)Stein, B.J., Grant, R.A., Sauer, R.T., & Baker, T.A. (2016) Structural basis of an N-degron adaptor with more stringent specificity. Structure 2, 232-242.
Román-Hernández G, Hou JY, Grant RA, Sauer RT, Baker TA.(2011) The ClpS adaptor mediates staged delivery of N-end rule substrates to the AAA+ ClpAP protease. Mol Cell. Jul 22;43(2):217-28. PubMed PMID: 21777811; PubMed Central PMCID: PMC3168947.
Kim S, Grant RA, Sauer RT. Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell. 2011 Apr 1;145(1):67-78. PubMed PMID: 21458668; PubMed Central PMCID: PMC3075617.
Wang, K.H., Román-Hernández, G, Grant, R.A., Sauer, R.T. & Baker, T.A. (2008) The molecular basis of N-end rule recognition. Mol. Cell 32(3):406-14. PubMed PMID: 18995838; PubMed Central PMCID: PMC3114436 [Indexed for MEDLINE]
Chein, P., Grant, R.A., Sauer, R.T. & Baker, T.A. (2007) Structure and substrate specificity of an SspB ortholog: design implications for AAA+ adaptors. Structure 15, 139-145.
Sohn, J., Grant, R.A. & Sauer, R.T. (2007) Allosteric activation of DegS, a stress sensor PDZ-protease. Cell 131, 572-583.
Bolon, D.N., Grant, R.A., Baker, T.A. & Sauer, R.T. (2005) Specificity versus stability in computational protein design. Proc. Natl. Acad. Sci. USA 102, 12724-12729. pubmed. citation
Alireza Ghanbarpour
Postdoctoral Associate (2021 - Present)
Email (alirezag [at] mit.edu)
Grad student work at MSU: Ghanbarpour, A., Santos, E. M., Pinger, C., Assar, Z., Hossaini Nasr, S., Vasileiou, C., Spence, D., Borhan, B., & Geiger, J. H. (2020). Human Cellular Retinol Binding Protein II Forms a Domain-Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering. . Chembiochem : a European journal of chemical biology, 21(22), 3192–3196.
