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, Proteolysis
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"Karl Schmitz"
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Cross-listing: Physiology Academic Tree

Parents

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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
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