Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect
about
Cathelicidins: family of antimicrobial peptides. A reviewAntimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR studyComputational prediction of the optimal oligomeric state for membrane-inserted β-barrels of protegrin-1 and related mutants.Implicit Membrane Investigation of the Stability of Antimicrobial Peptide β-Barrels and Arcs.Membrane interactions and pore formation by the antimicrobial peptide protegrin.Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process.How to lose a kink and gain a helix: pH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers.Comparative molecular dynamics simulation studies of protegrin-1 monomer and dimer in two different lipid bilayersAntimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studiesMechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.Computational studies of protegrin antimicrobial peptides: a review.Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link.Models of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels.Mechanism of membrane permeation induced by synthetic β-hairpin peptides.Computational studies of peptide-induced membrane pore formation.Mechanical properties that influence antimicrobial peptide activity in lipid membranes.Antimicrobial peptides and their analogs: searching for new potential therapeutics.Defining the genetic relationship of protegrin-related sequences and the in vivo expression of protegrins.Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs.Probing Oligomerized Conformations of Defensin in the Membrane.Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.Rational Design of Cyclic Antimicrobial Peptides Based on BPC194 and BPC198.Solid-state NMR structures of integral membrane proteins.
P2860
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P2860
Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect
description
2007 nî lūn-bûn
@nan
2007 թուականին հրատարակուած գիտական յօդուած
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2007 թվականին հրատարակված գիտական հոդված
@hy
2007年の論文
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2007年論文
@yue
2007年論文
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2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
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name
Conformational study of the pr ...... lipid bilayers and its effect
@ast
Conformational study of the pr ...... lipid bilayers and its effect
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Conformational study of the pr ...... lipid bilayers and its effect
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Conformational study of the pr ...... lipid bilayers and its effect
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type
label
Conformational study of the pr ...... lipid bilayers and its effect
@ast
Conformational study of the pr ...... lipid bilayers and its effect
@en
Conformational study of the pr ...... lipid bilayers and its effect
@en-gb
Conformational study of the pr ...... lipid bilayers and its effect
@nl
prefLabel
Conformational study of the pr ...... lipid bilayers and its effect
@ast
Conformational study of the pr ...... lipid bilayers and its effect
@en
Conformational study of the pr ...... lipid bilayers and its effect
@en-gb
Conformational study of the pr ...... lipid bilayers and its effect
@nl
P2860
P356
P1476
Conformational study of the pr ...... lipid bilayers and its effect
@en
P2093
Hyunbum Jang
P2860
P2888
P356
10.1186/1472-6807-7-21
P407
P577
2007-01-01T00:00:00Z
P5875
P6179
1050268550