Rational combinatorial design of pore-forming beta-sheet peptides.
about
Type AII lantibiotic bovicin HJ50 with a rare disulfide bond: structure, structure-activity relationships and mode of actionImplicit Membrane Investigation of the Stability of Antimicrobial Peptide β-Barrels and Arcs.Conversion of a porin-like peptide channel into a gramicidin-like channel by glycine to D-alanine substitutions.pH-Dependent lytic peptides discovered by phage display.Beta-sheet pore-forming peptides selected from a rational combinatorial library: mechanism of pore formation in lipid vesicles and activity in biological membranes.Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes.Zinc(II) coordination complexes as membrane-active fluorescent probes and antibiotics.High-throughput selection of transmembrane sequences that enhance receptor tyrosine kinase activationHigh-throughput discovery of broad-spectrum peptide antibiotics.Broad-spectrum antimicrobial peptides by rational combinatorial design and high-throughput screening: the importance of interfacial activity.A novel dendrimeric peptide with antimicrobial properties: structure-function analysis of SB056.Describing the mechanism of antimicrobial peptide action with the interfacial activity modelGain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening.Synthetic molecular evolution of pore-forming peptides by iterative combinatorial library screening.Generation of novel cationic antimicrobial peptides from natural non-antimicrobial sequences by acid-amide substitutionToward the de novo design of antimicrobial peptides: Lack of correlation between peptide permeabilization of lipid vesicles and antimicrobial, cytolytic, or cytotoxic activity in living cells.Conformational Fine-Tuning of Pore-Forming Peptide Potency and Selectivity.Determining the mechanism of membrane permeabilizing peptides: identification of potent, equilibrium pore-formersDesigned supramolecular filamentous peptides: balance of nanostructure, cytotoxicity and antimicrobial activity.Antimicrobial activity, improved cell selectivity and mode of action of short PMAP-36-derived peptides against bacteria and CandidaMembrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Computational studies of peptide-induced membrane pore formation.An unprecedented alteration in mode of action of IsCT resulting its translocation into bacterial cytoplasm and inhibition of macromolecular syntheses.Polar residues in transmembrane helices can decrease electrophoretic mobility in polyacrylamide gels without causing helix dimerization.Spontaneous membrane-translocating peptides by orthogonal high-throughput screening.Characterization of antimicrobial peptide activity by electrochemical impedance spectroscopy.
P2860
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P2860
Rational combinatorial design of pore-forming beta-sheet peptides.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Rational combinatorial design of pore-forming beta-sheet peptides.
@ast
Rational combinatorial design of pore-forming beta-sheet peptides.
@en
type
label
Rational combinatorial design of pore-forming beta-sheet peptides.
@ast
Rational combinatorial design of pore-forming beta-sheet peptides.
@en
prefLabel
Rational combinatorial design of pore-forming beta-sheet peptides.
@ast
Rational combinatorial design of pore-forming beta-sheet peptides.
@en
P2093
P2860
P356
P1476
Rational combinatorial design of pore-forming beta-sheet peptides.
@en
P2093
Jessica R Marks
Joshua M Rausch
William C Wimley
P2860
P304
10511-10515
P356
10.1073/PNAS.0502013102
P407
P577
2005-07-14T00:00:00Z