Results 111 to 120 of about 171,782 (185)

Structural Switching of Staphylococcus aureus Clp Protease [PDF]

open access: yesJournal of Biological Chemistry, 2011
Jie Zhang   +5 more
openaire   +1 more source

Identification of new protein substrates for the chloroplast ATP-dependent Clp protease supports its constitutive role in Arabidopsis

open access: yes, 2008
International audienceThe ATP-dependent Clp protease in plant chloroplasts consists of a heterogeneous proteolytic core containing multiple ClpP and ClpR paralogs.
Stanne, Tara M,   +6 more
core   +1 more source

Structural switching of Staphylococcus aureus Clp protease: a key to understanding protease dynamics.

open access: yesThe Journal of biological chemistry, 2011
ATP-dependent Clp protease (ClpP) is an attractive new target for the development of anti-infective agents. The ClpP protease consists of two heptameric rings that enclose a large chamber containing 14 proteolytic active sites. Recent studies indicate that ClpP likely undergoes conformational switching between an extended and degraded active state ...
Jie, Zhang   +5 more
openaire   +1 more source

Differential contributions of ClpX and ClpP to pulmonary virulence in classical and hypervirulent Klebsiella pneumoniae

open access: yesInfection and Immunity
Klebsiella pneumoniae is an opportunistic Gram-negative pathogen and a common cause of antibiotic-resistant infections including neonatal sepsis and hospital-acquired pneumonia. K.
Nathan M. Lin   +3 more
doaj   +1 more source

Purification of the Caseinolytic protease ClpP.

open access: yes, 2022
The caseinolytic protease P (ClpP) is an essential protein for bacteria and bacterial derived organelles. It belongs to the AAA+ family of proteases and has proteolytic activity, thereby, it plays an important role in protein digestion.
Pedrós Manzanares, Laura   +1 more
core  

Identification and analysis of Clp protease substrates in "C. crescentus"

open access: yes, 2004
Proteolysis is an irreversible regulatory mechanism by which cells can remove a protein whose function is no longer required or if its presence in a particular cellular compartment and/or at a certain time is harmful to the cell. Degradation of cytoplasmic proteins is energy dependent, and in prokaryotic cells is carried out by five ATP-dependent ...
openaire   +2 more sources

Virulence in bacteriophage Mu: A case of transdominant proteolysis by the Escherichia coli Clp serine protease

open access: yes, 1992
The importance of proteases in gene regulation is well documented in both prokaryotic and eukaryotic systems. Here we describe the first example of genetic regulation controlled by the Escherichia coli Clp ATP-dependent serine protease.
Toussaint, Ariane   +3 more
core   +1 more source

Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis

open access: yesMicrobial Cell Factories
Background Bacillus subtilis is widely used for industrial enzyme production due to its capacity to efficiently secrete proteins. However, secretion efficiency of enzymes varies widely, and optimizing secretion is crucial to make production commercially ...
Biwen Wang   +5 more
doaj   +1 more source

Interference with Clp protease impairs carotenoid accumulation during tomato fruit ripening

open access: yes
Profound metabolic and structural changes are required for fleshy green fruits to ripen and become colorful and tasty. In tomato (Solanum lycopersicum), fruit ripening involves the differentiation of chromoplasts, specialized plastids that accumulate ...
Li, Li   +6 more
core  

Structure and function of ATP-dependent protease Clp(Chaperonin-linked-protease)

open access: yesSeibutsu Butsuri, 2000
T. Ishikawa   +6 more
openaire   +2 more sources

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