Results 51 to 60 of about 4,619 (182)

Host and bacterial proteases influence biofilm formation and virulence in a murine model of enterococcal catheter-associated urinary tract infection [PDF]

open access: yes, 2017
Urinary tract infections: targeting enzymes might help Identifying bacterial and host enzymes that support biofilm formation may help prevent urinary tract infections caused by catheters.
Caparon, Michael G   +5 more
core   +3 more sources

Species and genotype diversity of Plasmodium in malaria patients from Gabon analysed by next generation sequencing [PDF]

open access: yes, 2017
Background Six Plasmodium species are known to naturally infect humans. Mixed species infections occur regularly but morphological discrimination by microscopy is difficult and multiplicity of infection (MOI) can only be evaluated by molecular methods ...
Lalremruata, Albert   +10 more
core   +1 more source

ClpB is an essential stress regulator of Mycobacterium tuberculosis and endows survival advantage to dormant bacilli

open access: yesInternational Journal of Medical Microbiology, 2020
The ability to tolerate multiple host derived stresses, resist eradication and persist within the infected individuals is central to the pathogenicity of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB).
Prajna Tripathi   +4 more
doaj   +1 more source

Open and compressed conformations of Francisella tularensis ClpP [PDF]

open access: yes, 2017
Caseinolytic proteases are large oligomeric assemblies responsible for maintaining protein homeostasis in bacteria and in so doing influence a wide range of biological processes.
Alexopoulos   +28 more
core   +2 more sources

Bacterial caseinolytic proteases as novel targets for antibacterial treatment

open access: yesInternational Journal of Medical Microbiology, 2014
Bacterial Clp proteases are important for protein turnover and homeostasis in order to maintain vital cellular functions particularly under stress conditions. Apart from their crucial role in general protein quality control by degrading abnormally folded or otherwise aberrant or malfunctioning proteins, their temporally and spatially precise ...
Heike, Brötz-Oesterhelt, Peter, Sass
openaire   +2 more sources

Crystal Structure of the Caseinolytic Protease Gene Regulator, a Transcriptional Activator in Actinomycetes [PDF]

open access: yesJournal of Biological Chemistry, 2009
Human pathogens of the genera Corynebacterium and Mycobacterium possess the transcriptional activator ClgR (clp gene regulator) which in Corynebacterium glutamicum has been shown to regulate the expression of the ClpCP protease genes. ClgR specifically binds to pseudo-palindromic operator regions upstream of clpC and clpP1P2. Here, we present the first
Santina, Russo   +4 more
openaire   +2 more sources

Purification and proteolytic activity of Caseinolytic protease (Clp) from Lactobacillus plantarum IIA-1AS [PDF]

open access: yesAIP Conference Proceedings, 2020
A gene encoding caseinolytic protease (Clp) was isolated from Lactobacillus plantarum IIA-1A5 and overexpressed in Escherichia coli. This enzyme belongs to the serine protease and plays essential role in cellular protein homeostasis. This study investigated the purification and proteolytic activity of the protease produced by Lactobacillus plantarum ...
Olfa Mega   +3 more
openaire   +1 more source

Protease activity of extracellular enzyme produced by B. subtilis isolated from soil [PDF]

open access: yes, 2017
Background: Proteases produced by enzymatic method are more environments friendly than chemical process, and they have tremendous potential in the leather industry and in other several industries.
Ahamad, T. (Tasnim)   +10 more
core   +1 more source

Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery [PDF]

open access: yes, 2014
Caseinolytic peptidase P (ClpP), a double-ring peptidase with 14 subunits, collaborates with ATPases associated with diverse activities (AAA+) partners to execute ATP-dependent protein degradation.
Carney, Daniel W.   +3 more
core   +1 more source

Home - About - Disclaimer - Privacy