The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR.
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NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A (1-8) - melittin (1-12) hybrid peptidesSolution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx moriThe solution structure of the active domain of CAP18--a lipopolysaccharide binding protein from rabbit leukocytesReciprocal Interactions between Nematodes and Their Microbial EnvironmentsAnimal antimicrobial peptides: an overview.Immobilization of Escherichia coli cells by use of the antimicrobial peptide cecropin P1.Antibacterial Activity of Recombinant Pig Intestinal Parasite Cecropin P4 Peptide Secreted from Pichia pastoris.Crystallization and preliminary X-ray analysis of cecropin B from Bombyx mori.Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy.Functional Roles of Aromatic Residues and Helices of Papiliocin in its Antimicrobial and Anti-inflammatory Activities.Structure and function of papiliocin with antimicrobial and anti-inflammatory activities isolated from the swallowtail butterfly, Papilio xuthus.Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy.Lysine-enriched cecropin-mellitin antimicrobial peptides with enhanced selectivityAnti-inflammatory activities of cecropin A and its mechanism of action.Pegylation of antimicrobial peptides maintains the active peptide conformation, model membrane interactions, and antimicrobial activity while improving lung tissue biocompatibility following airway delivery.The outer membranes of Brucella spp. are resistant to bactericidal cationic peptides.Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine.The use of antimicrobial peptides in ophthalmology: an experimental study in corneal preservation and the management of bacterial keratitisAntibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure.Crumpled structure of the custom hydrophobic lytic peptide cecropin B3.Helix induction in antimicrobial peptides by alginate in biofilms.Effect of interaction with coesite silica on the conformation of Cecropin P1 using explicit solvent molecular dynamics simulation.Hydrocarbon-stapled lipopeptides exhibit selective antimicrobial activity.The dependence of membrane permeability by the antibacterial peptide cecropin B and its analogs, CB-1 and CB-3, on liposomes of different composition.Anionic C-terminal proregion of nematode antimicrobial peptide cecropin P4 precursor inhibits antimicrobial activity of the mature peptide.Solution structure of a cathelicidin-derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy.Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit leukocytes.A novel cecropin B-derived peptide with antibacterial and potential anti-inflammatory properties
P2860
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P2860
The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
The structure of the mammalian ...... ion, determined by proton-NMR.
@en
The structure of the mammalian ...... ion, determined by proton-NMR.
@nl
type
label
The structure of the mammalian ...... ion, determined by proton-NMR.
@en
The structure of the mammalian ...... ion, determined by proton-NMR.
@nl
prefLabel
The structure of the mammalian ...... ion, determined by proton-NMR.
@en
The structure of the mammalian ...... ion, determined by proton-NMR.
@nl
P2860
P1433
P1476
The structure of the mammalian ...... ion, determined by proton-NMR.
@en
P2093
P2860
P304
P356
10.1111/J.1432-1033.1992.TB17273.X
P407
P577
1992-10-01T00:00:00Z