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
Rational Design of Selective and Bioactive Inhibitors of the Mycobacterium tuberculosis Proteasome
Kyle A. Totaro,Dominik Barthelme,Peter T. Simpson,Xiuju Jiang,Gang Lin,Carl Nathan,Robert T. Sauer,Jason K. Sello +7 more
TL;DR: The 20S core particle of the proteasome in Mycobacterium tuberculosis (Mtb) is a promising, yet unconventional, drug target as discussed by the authors, but they would only be therapeutically viable if they do not inhibit the essential 20S counterpart in humans.
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Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding.
TL;DR: The results support a mechanism in which unfolding grip is primarily mediated by non-specific van der Waal’s interactions between core side chains of the substrate tail and a subset of YVG loops at the top of the ClpX axial pore.
Journal ArticleDOI
Solution NMR studies of intact lambda repressor.
TL;DR: Using a combination of two and one-dimensional NMR spectroscopy, it is shown that in the intact bacteriophage lambda repressor, the N-terminal domain assumes the same global structure as when it remains isolated.
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Steric clashes with bound OMP peptides activate the DegS stress-response protease.
TL;DR: It is shown that OMP peptides initiate a steric clash between the PDZ domain and the L3 loop that results in a structural rearrangement of the loop and breaking of autoinhibitory interactions, resulting in proteolytic activation of DegS by OMP-peptide binding.
Substrate delivery by the AAA+ ClpX and ClpC1 unfoldases activates the mycobacterial ClpP1P2 peptidase
Karl R. Schmitz,Robert T. Sauer +1 more
TL;DR: In this paper, the reconstitution of protein degradation by mycobacterial Clp proteases in vitro and describe novel features of these enzymes that distinguish them from orthologues in other bacteria.