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CLPP gene

Known as: ClpP, E. COLI, HOMOLOG OF, ATP-dependent protease ClpAP (E. coli), proteolytic subunit, human, CASEINOLYTIC MITOCHONDRIAL MATRIX PEPTIDASE PROTEOLYTIC SUBUNIT 
National Institutes of Health

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ClpP protease, E coli

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2012
2012
Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX.
Highly Cited
2008
Highly Cited
2008
Decreased expression of the mitochondrial matrix proteases Lon and ClpP in cells from a patient with hereditary spastic paraplegia (SPG13)
2008
2008
ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: mechanistic studies of ATP-independent proteolysis.
ATP-dependent proteases are processive, meaning that they degrade full-length proteins into small peptide products without… 
Highly Cited
2007
Highly Cited
2007
Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1.
Mycobacterium tuberculosis caseinolytic protease ClpP1 (Mt ClpP1) is a self-compartmentalized protease consisting of two… 
Highly Cited
1999
Highly Cited
1999
Potential and limitations of BIOLOG for microbial community analysis
Characterization of community-level substrate utilization via incubation of environmental samples in BIOLOG microplates has been… 
Highly Cited
1998
Highly Cited
1998
Degradation of active-oxygen-modified ribulose-1,5-bisphosphate carboxylase/oxygenase by chloroplastic proteases requires ATP-hydrolysis
Abstract. Active oxygen (AO) species generated in plants under stress conditions trigger degradation of Rubisco (EC 4.1.1.39). To… 
Highly Cited
1998
Highly Cited
1998
Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP.
The ClpAP protease from Escherichia coli consists of the ATP-binding regulatory component, ClpA (subunit Mr 84 165), and the… 
Highly Cited
1998
Highly Cited
1998
Versatile Action of Escherichia coli ClpXP as Protease or Molecular Chaperone for Bacteriophage Mu Transposition*
The molecular chaperone ClpX of Escherichia coli plays two distinct functions for bacteriophage Mu DNA replication by… 
Highly Cited
1995
Highly Cited
1995
Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore.
The Escherichia coli ATP-dependent caseinolytic protease (Clp) is composed of two distinct subunits; protease, ClpP, and ATPase… 
Highly Cited
1994
Highly Cited
1994
Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli.
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