Membrane-active peptides and the clustering of anionic lipids.
about
Controls and constrains of the membrane disrupting action of Aurein 1.2.Dual action of BPC194: a membrane active peptide killing bacterial cellsHigh-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments.Antimicrobial peptide cWFW kills by combining lipid phase separation with autolysis.N-acylated peptides derived from human lactoferricin perturb organization of cardiolipin and phosphatidylethanolamine in cell membranes and induce defects in Escherichia coli cell division.Enhanced amphiphilic profile of a short β-stranded peptide improves its antimicrobial activity.Collagen-like antimicrobial peptides.Correlating antimicrobial activity and model membrane leakage induced by nylon-3 polymers and detergentsCationic cell-penetrating peptide binds to planar lipid bilayers containing negatively charged lipids but does not induce conductive poresNegatively Charged Lipids as a Potential Target for New Amphiphilic Aminoglycoside Antibiotics: A BIOPHYSICAL STUDY.Interactions between fengycin and model bilayers quantified by coarse-grained molecular dynamics.Transient potential gradients and impedance measures of tethered bilayer lipid membranes: pore-forming peptide insertion and the effect of electroporation.Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Strategies to stabilize cell penetrating peptides for in vivo applications.The phospholipid code: a key component of dying cell recognition, tumor progression and host-microbe interactionsProbing the disparate effects of arginine and lysine residues on antimicrobial peptide/bilayer association.Antimicrobial activity of GN peptides and their mode of action.Killing of melanoma cells and their metastases by human lactoferricin derivatives requires interaction with the cancer marker phosphatidylserineThermodynamics of cell-penetrating HIV1 TAT peptide insertion into PC/PS/CHOL model bilayers through transmembrane pores: the roles of cholesterol and anionic lipids.Hydrophobic mismatch demonstrated for membranolytic peptides, and their use as molecular rulers to measure bilayer thickness in native cells.Antimicrobial Peptides Derived from Fusion Peptides of Influenza A Viruses, a Promising Approach to Designing Potent Antimicrobial Agents.Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation.Structural location determines functional roles of the basic amino acids of KR-12, the smallest antimicrobial peptide from human cathelicidin LL-37.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.Arginine-lysine positional swap of the LL-37 peptides reveals evolutional advantages of the native sequence and leads to bacterial probes.Antibiotic gold: tethering of antimicrobial peptides to gold nanoparticles maintains conformational flexibility of peptides and improves trypsin susceptibility.Selectivity and Mechanism of Fengycin, an Antimicrobial Lipopeptide from Molecular Dynamics.Action of the multifunctional peptide BP100 on native biomembranes examined by solid-state NMRMembrane Active Peptides and Their Biophysical Characterization
P2860
Q27306846-40047E35-C185-4DD2-BC99-8D7F90B5C8AAQ27324554-46DD42B1-093E-4B90-90A1-3C954B762D52Q27692605-0987F4F7-D7F7-4983-B81B-402C22B8BE2EQ30841307-9F8084D7-3444-4FD4-94C7-D3DE148B8F55Q35111141-25A1CA4A-C1B4-439E-B816-EC8047B96FC7Q35548618-5C687D3B-2CDD-455A-A3DE-C87896A7CA8AQ36043457-FCDCBF20-4119-4A14-9BDE-FA47E3CF7596Q36338409-B7DA3B77-85C9-4DC2-B936-40317E2AA03CQ36824514-F66AF958-5685-4E38-9C85-A58EEAD0C944Q37034460-2FF8D832-3DE4-4134-BC67-55F5846DC42AQ37294089-0EFE23DC-D89A-4A65-89BD-812F4CD089BDQ37533527-019A4DD6-AC93-4782-92F2-63BDC76AEAE0Q37639825-6D4D7C89-A249-435F-9211-3329396FF2CBQ38602460-DAF0D489-DEBF-4C03-B0B0-61A08512D55AQ38602808-E205D66B-D7F7-459A-9C50-1B656780FCFEQ38674487-EFD2D83E-BCE8-4E67-AFD8-CC1D39DBB0BCQ38932433-BD124816-6A34-4495-8FDE-A8F1A002395FQ38994009-08761C6D-EC59-4977-8EF9-53F560586500Q40643109-8F035FE8-43AE-434F-8F74-F4D61976F98BQ41147373-D2C61A82-04DB-46A8-8200-A6E920C35F02Q41592128-B2F4B1C2-4404-4B33-A7DE-95881D109514Q41852119-DB4EEC15-10D8-4AF5-9C8B-25DFC24A9BB9Q42053270-6D35BBEA-2224-470B-97B6-98DC161C2793Q42917720-D4B91167-B19E-429D-A2B9-C0696571960DQ46375567-B939AF10-47EC-4BB3-858D-134B9A7FDA04Q48147426-CDE4323D-D82F-4191-B4D6-90D418D58A21Q49617979-EA3D9D09-65B2-4D6F-B259-2D580F29F117Q57528301-1928E0A9-7852-4782-B5F5-8DECE7D55DEBQ58717273-EBA57D6C-1528-4196-A860-D876749B050A
P2860
Membrane-active peptides and the clustering of anionic lipids.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Membrane-active peptides and the clustering of anionic lipids.
@en
type
label
Membrane-active peptides and the clustering of anionic lipids.
@en
prefLabel
Membrane-active peptides and the clustering of anionic lipids.
@en
P2093
P2860
P1433
P1476
Membrane-active peptides and the clustering of anionic lipids
@en
P2093
P2860
P304
P356
10.1016/J.BPJ.2012.06.004
P407
P577
2012-07-17T00:00:00Z