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Clostridium difficile ClpP Homologues are Capable of Uncoupled Activity and Exhibit Different Levels of Susceptibility to Acyldepsipeptide Modulation
Nathan P. Lavey
, Tyler Shadid
, Jimmy D. Ballard
,
Adam S. Duerfeldt
Research output
:
Contribution to journal
›
Article
›
peer-review
23
Scopus citations
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Dive into the research topics of 'Clostridium difficile ClpP Homologues are Capable of Uncoupled Activity and Exhibit Different Levels of Susceptibility to Acyldepsipeptide Modulation'. Together they form a unique fingerprint.
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Keyphrases
Clostridioides Difficile
100%
Acyldepsipeptide
100%
Caseinolytic Protease P
100%
Difficile
42%
P Systems
42%
ClpP2
42%
Protease
28%
Co-chaperone
28%
Small Molecules
14%
Genomic Data
14%
Genetic Characterization
14%
Virulence
14%
Spore-forming
14%
New Targets
14%
Operative
14%
Proteomics Data
14%
Pathogenic Bacteria
14%
Structural Characterization
14%
Normal Growth
14%
Homology Modeling
14%
Biological Characterization
14%
Characteristic Response
14%
SsrA
14%
Biochemistry, Genetics and Molecular Biology
Peptoclostridium difficile
100%
Protease
100%
Isoform
57%
Proteases
28%
Genetics
14%
Small Molecule
14%
Infectious Agent
14%
Genomics
14%
Proteomics
14%