A hydrophobic patch in the competence-stimulating Peptide, a pneumococcal competence pheromone, is essential for specificity and biological activity.
about
Competence-independent activity of pneumococcal EndA [corrected] mediates degradation of extracellular dna and nets and is important for virulenceDownsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potencyProbing bacterial transmembrane histidine kinase receptor-ligand interactions with natural and synthetic moleculesComparison of transformation frequencies among selected Streptococcus pneumoniae serotypes.Inhibition of competence development, horizontal gene transfer and virulence in Streptococcus pneumoniae by a modified competence stimulating peptide.Peptide signaling in the staphylococci.Saturated alanine scanning mutagenesis of the pneumococcus competence stimulating peptide identifies analogs that inhibit genetic transformation.A method for structure-activity analysis of quorum-sensing signaling peptides from naturally transformable streptococci.An electrostatic interaction between BlpC and BlpH dictates pheromone specificity in the control of bacteriocin production and immunity in Streptococcus pneumoniaeCompetence in Streptococcus pneumoniae is regulated by the rate of ribosomal decoding errors.Prediction and analysis of quorum sensing peptides based on sequence features.Structure-activity analysis of quorum-sensing signaling peptides from Streptococcus mutans.Pneumococcal Competence Coordination Relies on a Cell-Contact Sensing Mechanism.The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide.Bacterial behaviors associated with the quorum-sensing peptide pheromone ('alarmone') in streptococci.Positive selection in the ComC-ComD system of Streptococcal Species.Structure-Activity Relationships of the Competence Stimulating Peptides (CSPs) in Streptococcus pneumoniae Reveal Motifs Critical for Intra-group and Cross-group ComD Receptor Activation.Fusion peptide P15-CSP shows antibiofilm activity and pro-osteogenic activity when deposited as a coating on hydrophilic but not hydrophobic surfaces.Membrane Topology and Structural Insights into the Peptide Pheromone Receptor ComD, A Quorum-Sensing Histidine Protein Kinase of Streptococcus mutans.Analysis of the amino acid sequence specificity determinants of the enterococcal cCF10 sex pheromone in interactions with the pheromone-sensing machinery.Structural Characterization of Competence-Stimulating Peptide Analogues Reveals Key Features for ComD1 and ComD2 Receptor Binding in Streptococcus pneumoniaeDefining the hydrophobic interactions that drive competence stimulating peptide (CSP)-ComD binding in Streptococcus pneumoniae.
P2860
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P2860
A hydrophobic patch in the competence-stimulating Peptide, a pneumococcal competence pheromone, is essential for specificity and biological activity.
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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name
A hydrophobic patch in the com ...... icity and biological activity.
@en
A hydrophobic patch in the com ...... icity and biological activity.
@nl
type
label
A hydrophobic patch in the com ...... icity and biological activity.
@en
A hydrophobic patch in the com ...... icity and biological activity.
@nl
prefLabel
A hydrophobic patch in the com ...... icity and biological activity.
@en
A hydrophobic patch in the com ...... icity and biological activity.
@nl
P2093
P2860
P1476
A hydrophobic patch in the com ...... icity and biological activity.
@en
P2093
Ola Johnsborg
Per Eugen Kristiansen
Trinelise Blomqvist
P2860
P304
P356
10.1128/JB.188.5.1744-1749.2006
P407
P577
2006-03-01T00:00:00Z