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TranscriptomicsThe antimicrobial peptide-sensing system aps of Staphylococcus aureus
Staphylococcus aureus is a leading cause of hospital-associated infections. In addition, highly virulent strains of methicillin-resistant S. aureus (MRSA) are currently spreading outside health care settings. Survival in the human host is largely defined by the ability of S. aureus to resist mechani...
ORGANISM(S): Staphylococcus aureus 
2008-04-06 | E-GEOD-8400 | biostudies-arrayexpress
TranscriptomicsA Gram-positive three-component antimicrobial peptide-sensing system
To survive during colonization or infection of the human body, microorganisms must defeat antimicrobial peptides, which represent a key component of innate host defense in phagocytes and on epithelia. However, is not known how the clinically important group of Gram-positive bacteria sense antimicrob...
ORGANISM(S): Staphylococcus epidermidis 
2010-05-26 | E-GEOD-7163 | biostudies-arrayexpress
TranscriptomicsQuantitative Different Analysis of antimicrobial peptide LL37 expressed in E.coli Top 10 under aerobic and anaerobic condition.
We reported the transcriptional profiles of E.coli expressing antimicrobial peptide LL37 under stress response condition. 4 samples, two groups, one group is under aerobic condition, the other group is under anaerobic condition. One of samples is E.coli which expressed LL37 as induction in each gro...
ORGANISM(S): Escherichia coli 
2013-08-21 | E-GEOD-43408 | biostudies-arrayexpress
ProteomicsShort cationic antimicrobial peptide RWRWRW-NH2 inhibits cell wall biosynthesis and bacterial respiration by delocalizing essential membrane proteins
Antimicrobial peptides are potent antibacterial agents. The subclass of short cationic RW-rich peptides is known to target the bacterial membrane. We employed the synthetic hexapeptide RWRWRW-NH2 to characterize in-depth the impact of short cationic RW-rich peptides on bacterial physiology and the b...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 
2014-03-06 | PXD000181 | Pride
Short cationic antimicrobial peptide Bacillus subtilis Antibiotics 
TranscriptomicsThe antimicrobial peptide-sensing system aps of Staphylococcus aureus
Staphylococcus aureus is a leading cause of hospital-associated infections. In addition, highly virulent strains of methicillin-resistant S. aureus (MRSA) are currently spreading outside health care settings. Survival in the human host is largely defined by the ability of S. aureus to resist mechani...
ORGANISM(S): Chlamydia pneumoniae AR39 Borreliella burgdorferi B31 Coxiella burnetii RSA 493 Rickettsia rickettsii Staphylococcus aureus Chlamydia muridarum Staphylococcus epidermidis RP62A Chlamydia caviae GPIC Staphylococcus haemolyticus JCSC1435 Staphylococcus epidermidis ATCC 12228 Staphylococcus aureus subsp. aureus MW2 Granulibacter bethesdensis Coxiella burnetii Chlamydia trachomatis D/UW-3/CX 
2008-04-07 | GSE8400 | GEO
UnknownIn Silico Structural Evaluation of Short Cationic Antimicrobial Peptides.
Not available
S-EPMC6160961 | biostudies-literature
UnknownBare Iron Oxide Nanoparticles as Drug Delivery Carrier for the Short Cationic Peptide Lasioglossin.
Not available
S-EPMC8146918 | biostudies-literature
GenomicsStaphylococcus aureus
The antimicrobial peptide-sensing system aps of Staphylococcus aureus
PRJNA101451 | ENA
TranscriptomicsTranscription profiling of human monocytic cells THP-1 stimulated with LPS (10ng/ml) in presence or absence of LL-37 (5 ug/ml), as well as with the peptide alone, for 4 hours
The objective of the study was to evaluate transcriptional response of endotoxin-stimulated human monocytic cells in presence or absence of host defense peptide LL-37 at low physiologically relevant concentrations. Human monocytic cells THP-1 were stimulated with LPS (10ng/ml) in presence or absenc...
ORGANISM(S): Homo sapiens 
2006-12-07 | E-FPMI-6 | biostudies-arrayexpress
UnknownInteraction of a short antimicrobial peptide on charged lipid bilayer: A case study on aurein 1.2 peptide.
Not available
S-EPMC10074906 | biostudies-literature
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