Host-defense antimicrobial peptides: importance of structure for activity.
about
Sap transporter mediated import and subsequent degradation of antimicrobial peptides in HaemophilusHigh-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micellesCAMP: Collection of sequences and structures of antimicrobial peptidesA theoretical approach to spot active regions in antimicrobial proteins.Molecular characterization of a novel big defensin from clam Venerupis philippinarum.Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studiesRational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic indexAntimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link.Infectious Disease: Connecting Innate Immunity to Biocidal Polymers.Synthetic, biologically active amphiphilic peptidesNylon-3 polymers with selective antifungal activityModels of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels.Design of an α-helical antimicrobial peptide with improved cell-selective and potent anti-biofilm activityDe novo designed synthetic mimics of antimicrobial peptides.Antimicrobial peptides: modes of mechanism, modulation of defense responses.Modes of action of Leishmanicidal antimicrobial peptides.Recent development of small antimicrobial peptidomimetics.AApeptides as a new class of antimicrobial agents.Antimicrobial γ-AApeptides (WO2013112548): a patent evaluation.Tuning the biological activity profile of antibacterial polymers via subunit substitution pattern.The development of antimicrobial γ-AApeptides.Antimicrobial peptides with selective antitumor mechanisms: prospect for anticancer applications.Comparison of biophysical and biologic properties of alpha-helical enantiomeric antimicrobial peptides.Design and expression of peptides with antimicrobial activity against Salmonella typhimurium.Penetration of milk-derived antimicrobial peptides into phospholipid monolayers as model biomembranes.SapF-mediated heme-iron utilization enhances persistence and coordinates biofilm architecture of Haemophilus.
P2860
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P2860
Host-defense antimicrobial peptides: importance of structure for activity.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Host-defense antimicrobial peptides: importance of structure for activity.
@ast
Host-defense antimicrobial peptides: importance of structure for activity.
@en
Host-defense antimicrobial peptides: importance of structure for activity.
@nl
type
label
Host-defense antimicrobial peptides: importance of structure for activity.
@ast
Host-defense antimicrobial peptides: importance of structure for activity.
@en
Host-defense antimicrobial peptides: importance of structure for activity.
@nl
prefLabel
Host-defense antimicrobial peptides: importance of structure for activity.
@ast
Host-defense antimicrobial peptides: importance of structure for activity.
@en
Host-defense antimicrobial peptides: importance of structure for activity.
@nl
P356
P1476
Host-defense antimicrobial peptides: importance of structure for activity.
@en
P2093
P304
P356
10.2174/1381612023395358
P577
2002-01-01T00:00:00Z