Anti-tuberculosis activity of α-helical antimicrobial peptides: de novo designed L- and D-enantiomers versus L- and D-LL-37.
about
Two human host defense ribonucleases against mycobacteria, the eosinophil cationic protein (RNase 3) and RNase 7"Specificity Determinants" Improve Therapeutic Indices of Two Antimicrobial Peptides Piscidin 1 and Dermaseptin S4 Against the Gram-negative Pathogens Acinetobacter baumannii and Pseudomonas aeruginosaTargeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides.Rational design of α-helical antimicrobial peptides to target Gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: utilization of charge, 'specificity determinants,' total hydrophobicity, hydrophobe type and location as desigUnnatural amino acid analogues of membrane-active helical peptides with anti-mycobacterial activity and improved stability.Short, Synthetic Cationic Peptides Have Antibacterial Activity against Mycobacterium smegmatis by Forming Pores in Membrane and Synergizing with Antibiotics.The Human Cathelicidin Antimicrobial Peptide LL-37 as a Potential Treatment for Polymicrobial Infected WoundsEmpirical comparison of web-based antimicrobial peptide prediction tools.The Synergistic Antimicrobial Effects of Novel Bombinin and Bombinin H Peptides from the Skin Secretion of Bombina orientalis.Combined Bioinformatic and Rational Design Approach To Develop Antimicrobial Peptides against Mycobacterium tuberculosis.Antimicrobial activity and interactions of cationic peptides derived from Galleria mellonella cecropin D-like peptide with model membranes.Improved protease stability of the antimicrobial peptide Pin2 substituted with D-amino acids.Reduction of helical content by insertion of a disulfide bond leads to an antimicrobial peptide with decreased hemolytic activity.Host Antimicrobial Peptides: The Promise of New Treatment Strategies against Tuberculosis.Polymorphism in cathelicidin gene (CAMP) that alters Hypoxia-inducible factor (HIF-1α::ARNT) binding is not associated with tuberculosis.Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides.IL-36/LXR axis modulates cholesterol metabolism and immune defense to Mycobacterium tuberculosis.Role of positively charged residues on the polar and non-polar faces of amphipathic α-helical antimicrobial peptides on specificity and selectivity for Gram-negative pathogens.
P2860
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P2860
Anti-tuberculosis activity of α-helical antimicrobial peptides: de novo designed L- and D-enantiomers versus L- and D-LL-37.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Anti-tuberculosis activity of ...... tiomers versus L- and D-LL-37.
@ast
Anti-tuberculosis activity of ...... tiomers versus L- and D-LL-37.
@en
type
label
Anti-tuberculosis activity of ...... tiomers versus L- and D-LL-37.
@ast
Anti-tuberculosis activity of ...... tiomers versus L- and D-LL-37.
@en
prefLabel
Anti-tuberculosis activity of ...... tiomers versus L- and D-LL-37.
@ast
Anti-tuberculosis activity of ...... tiomers versus L- and D-LL-37.
@en
P2093
P2860
P1476
Anti-tuberculosis activity of ...... tiomers versus L- and D-LL-37.
@en
P2093
James Whitehurst
Kevin O Kisich
Martin I Voskuil
Michael P Higgins
Robert S Hodges
Ziqing Jiang
P2860
P304
P356
10.2174/092986611794578288
P577
2011-03-01T00:00:00Z