R
Robert T. Sauer
Researcher at Massachusetts Institute of Technology
Publications - 408
Citations - 42127
Robert T. Sauer is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Repressor & Protein degradation. The author has an hindex of 106, co-authored 402 publications receiving 40181 citations. Previous affiliations of Robert T. Sauer include University of California, San Francisco & Harvard University.
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Journal ArticleDOI
Deletion of the prc (tsp) gene provides evidence for additional tail-specific proteolytic activity in Escherichia coli K-12.
Karen R. Silber,Robert T. Sauer +1 more
TL;DR: It is indicated that at least one additional carboxy-terminal-specific proteolytic system must exist in E. coli for the selective degradation in vivo of proteins with nonpolar carboxyl termini.
Antibacterial Activity of and Resistance to Small Molecule Inhibitors of the ClpP Peptidase
TL;DR: Chemical syntheses and evaluations of structurally diverse β-lactones are reported, which have a privileged structure for selective, suicide inhibition of the self-compartmentalized ClpP peptidase, and this work defines a mechanism by which bacteria could resist the toxic effects of ClPP inhibitors.
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Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens.
Katherine Amberg-Johnson,Sanjay B. Hari,Suresh M. Ganesan,Hernan Lorenzi,Robert T. Sauer,Jacquin C. Niles,Ellen Yeh +6 more
TL;DR: FtsH1 is the first novel factor required for apicoplast biogenesis identified in a phenotypic screen and will have significant advantages with improved drug kinetics and multistage efficacy against multiple human parasites.
Journal ArticleDOI
Tolerance of a protein helix to multiple alanine and valine substitutions
TL;DR: At the majority of positions in alpha-helix lambda repressor, tertiary interactions with other parts of the protein can be viewed as an environmental "buffer" that help to diminish the helix destabilizing effects of valine mutations and allow these mutations to be tolerated at frequencies similar to alanine mutations.
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Unique Contacts Direct High-Priority Recognition of the Tetrameric Mu Transposase-DNA Complex by the AAA+ Unfoldase ClpX
TL;DR: It is concluded that an extended set of potential enzyme contacts are exposed upon assembly of the tetramer and function as internal guides to recruit ClpX, thereby ensuring that the tet Krameric complex is a high-priority substrate.