Karl R. Schmitz, Ph.D.
Affiliations: | 2003-2010 | University of Pennsylvania, Philadelphia, PA, United States | |
| 2010-2017 | Biology | Massachusetts Institute of Technology, Cambridge, MA, United States | |
| 2017- | Biological Sciences | University of Delaware, Newark, DE, United States |
Area:
Biochemistry, Biophysics, Structural Biology, ProteolysisGoogle:
"Karl Schmitz"Mean distance: (not calculated yet)
Cross-listing: Physiology Academic Tree
Parents
Sign in to add mentor| Kathryn M. Ferguson | grad student | 2010 | Penn | |
| (Antibodies directed against the extracellular region of the epidermal growth factor receptor adopt distinct modes of binding and inhibition.) | ||||
| Robert T. Sauer | post-doc | 2010-2017 | MIT | |
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Publications
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| Schmitz KR, Handy EL, Compton CL, et al. (2020) Acyldepsipeptide Antibiotics and a Bioactive Fragment Thereof Differentially Perturb Mycobacterium tuberculosis ClpXP1P2 Activity in vitro. Acs Chemical Biology |
| Amor AJ, Schmitz KR, Baker TA, et al. (2019) Roles of the ClpX IGF loops in ClpP association, dissociation, and protein degradation. Protein Science : a Publication of the Protein Society |
| Amor AJ, Schmitz KR, Sello JK, et al. (2016) Highly dynamic interactions maintain kinetic stability of the ClpXP protease during the ATP-fueled mechanical cycle. Acs Chemical Biology |
| Grant RA, Sauer RT, Schmitz KR, et al. (2016) Structure of HslU L199Q in HslUV complex Structure |
| Carney DW, Schmitz KR, Scruse AC, et al. (2015) Examination of a Structural Model of Peptidomimicry by Cyclic Acyldepsipeptide Antibiotics in Their Interaction with the ClpP Peptidase. Chembiochem : a European Journal of Chemical Biology |
| Stinson BM, Baytshtok V, Schmitz KR, et al. (2015) Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nature Structural & Molecular Biology. 22: 411-6 |
| Moravcevic K, Alvarado D, Schmitz KR, et al. (2015) Comparison of Saccharomyces cerevisiae F-BAR domain structures reveals a conserved inositol phosphate binding site. Structure (London, England : 1993). 23: 352-63 |
| Schmitz KR, Carney DW, Sello JK, et al. (2014) Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery. Proceedings of the National Academy of Sciences of the United States of America. 111: E4587-95 |
| Carney DW, Compton CL, Schmitz KR, et al. (2014) A simple fragment of cyclic acyldepsipeptides is necessary and sufficient for ClpP activation and antibacterial activity. Chembiochem : a European Journal of Chemical Biology. 15: 2216-20 |
| Cordova JC, Olivares AO, Shin Y, et al. (2014) Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine. Cell. 158: 647-58 |