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21 in total

1. Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad.

Authors: Andrew R Buller; Craig A Townsend
Journal: Proc Natl Acad Sci U S A Date: 2013-02-04 Impact factor: 11.205

2. Clostridium difficile ClpP Homologues are Capable of Uncoupled Activity and Exhibit Different Levels of Susceptibility to Acyldepsipeptide Modulation.

Authors: Nathan P Lavey; Tyler Shadid; Jimmy D Ballard; Adam S Duerfeldt
Journal: ACS Infect Dis Date: 2018-11-26 Impact factor: 5.084

3. Insights into structural network responsible for oligomerization and activity of bacterial virulence regulator caseinolytic protease P (ClpP) protein.

Authors: Malte Gersch; Anja List; Michael Groll; Stephan A Sieber
Journal: J Biol Chem Date: 2012-01-30 Impact factor: 5.157

4. Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad.

Authors: Evelyn Zeiler; Anja List; Ferdinand Alte; Malte Gersch; Rudolf Wachtel; Marcin Poreba; Marcin Drag; Michael Groll; Stephan A Sieber
Journal: Proc Natl Acad Sci U S A Date: 2013-06-24 Impact factor: 11.205

Vibralactone as a tool to study the activity and structure of the ClpP1P2 complex from Listeria monocytogenes.

1. Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad.

2. Clostridium difficile ClpP Homologues are Capable of Uncoupled Activity and Exhibit Different Levels of Susceptibility to Acyldepsipeptide Modulation.

3. Insights into structural network responsible for oligomerization and activity of bacterial virulence regulator caseinolytic protease P (ClpP) protein.

4. Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad.

5. A Concise Total Synthesis of (±)-Vibralactone.

6. Novel Electrophilic Scaffold for Imaging of Essential Penicillin-Binding Proteins in Streptococcus pneumoniae.

Review 7. Applications of small molecule probes in dissecting mechanisms of bacterial virulence and host responses.

8. Substrate delivery by the AAA+ ClpX and ClpC1 unfoldases activates the mycobacterial ClpP1P2 peptidase.

9. Chemical tools for selective activity profiling of bacterial penicillin-binding proteins.

Review 10. Structural determinants of regulated proteolysis in pathogenic bacteria by ClpP and the proteasome.