Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
about
Fundamental molecular mechanism for the cellular uptake of guanidinium-rich molecules.Surface presentation of functional peptides in solution determines cell internalization efficiency of TAT conjugated nanoparticlesLabel-free probe of HIV-1 TAT peptide binding to mimetic membranes.Translocation thermodynamics of linear and cyclic nonaarginine into model DPPC bilayer via coarse-grained molecular dynamics simulation: implications of pore formation and nonadditivity.Investigating Hydrophilic Pores in Model Lipid Bilayers Using Molecular Simulations: Correlating Bilayer Properties with Pore-Formation Thermodynamics.Protein transport across membranes: Comparison between lysine and guanidinium-rich carriers.Tempo-spatially resolved cellular dynamics of human immunodeficiency virus transacting activator of transcription (Tat) peptide-modified nanocargos in living cells.Sensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics.Penetration of HIV-1 Tat47-57 into PC/PE Bilayers Assessed by MD Simulation and X-ray Scattering.HIV-1 Tat membrane interactions probed using X-ray and neutron scattering, CD spectroscopy and MD simulationsCargo self-assembly rescues affinity of cell-penetrating peptides to lipid membranesFree energy of translocating an arginine-rich cell-penetrating peptide across a lipid bilayer suggests pore formation.Improving the endosomal escape of cell-penetrating peptides and their cargos: strategies and challenges.Targeting antibodies to the cytoplasm.Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides.Advances in studies of nanoparticle-biomembrane interactions.Thermodynamics of cell-penetrating HIV1 TAT peptide insertion into PC/PS/CHOL model bilayers through transmembrane pores: the roles of cholesterol and anionic lipids.Diatrack particle tracking software: review of applications and performance evaluation.Diffusion as a probe of peptide-induced membrane domain formation.Transfer of arginine into lipid bilayers is nonadditive.The thin line between cell-penetrating and antimicrobial peptides: the case of Pep-1 and Pep-1-K.NKCS, a Mutant of the NK-2 Peptide, Causes Severe Distortions and Perforations in Bacterial, But Not Human Model Lipid Membranes.Effect of arginine-rich cell penetrating peptides on membrane pore formation and life-times: a molecular simulation study.
P2860
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P2860
Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
@en
Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
@nl
type
label
Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
@en
Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
@nl
prefLabel
Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
@en
Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
@nl
P2860
P1433
P1476
Cell-penetrating HIV1 TAT peptides can generate pores in model membranes.
@en
P2093
Jan Peter Siebrasse
P2860
P304
P356
10.1016/J.BPJ.2010.03.065
P407
P577
2010-07-01T00:00:00Z