The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
about
The surfactant peptide KL4 in lipid monolayers: phase behavior, topography, and chemical distributionPulmonary surfactant pathophysiology: current models and open questionsAtomic force microscope image contrast mechanisms on supported lipid bilayersEffects of lung surfactant proteins, SP-B and SP-C, and palmitic acid on monolayer stability.The Pulmonary Surfactant: Impact of Tobacco Smoke and Related Compounds on Surfactant and Lung DevelopmentThe pulmonary surfactant: impact of tobacco smoke and related compounds on surfactant and lung developmentSize influences the effect of hydrophobic nanoparticles on lung surfactant model systemsEnhanced efficacy of porcine lung surfactant extract by utilization of its aqueous swelling dynamics.Environmental tobacco smoke effects on lung surfactant film organization.Overcoming rapid inactivation of lung surfactant: analogies between competitive adsorption and colloid stability.Effect of hydrophobic surfactant peptides SP-B and SP-C on binary phospholipid monolayers. I. Fluorescence and dark-field microscopy.The role of surfactant proteins in DPPC enrichment of surface filmsInteraction of lung surfactant proteins with anionic phospholipids.Effect of hydrophobic surfactant proteins SP-B and SP-C on binary phospholipid monolayers: II. Infrared external reflectance-absorption spectroscopy.Deacylated pulmonary surfactant protein SP-C transforms from alpha-helical to amyloid fibril structure via a pH-dependent mechanism: an infrared structural investigation.Electrostatic barrier to recovery of dipalmitoylphosphatidylglycerol monolayers after collapseMore than a monolayer: relating lung surfactant structure and mechanics to compositionKeeping lung surfactant where it belongs: protein regulation of two-dimensional viscosityBiomimetic N-terminal alkylation of peptoid analogues of surfactant protein CLipid-protein interactions alter line tensions and domain size distributions in lung surfactant monolayersAn elevated level of cholesterol impairs self-assembly of pulmonary surfactant into a functional film.Atomic force microscopy studies of functional and dysfunctional pulmonary surfactant films. I. Micro- and nanostructures of functional pulmonary surfactant films and the effect of SP-A.Competitive adsorption: a physical model for lung surfactant inactivation.Lung surfactants and different contributions to thin film stability.Influence of lipid saturation grade and headgroup charge: a refined lung surfactant adsorption model.Nanoparticle interaction with model lung surfactant monolayers.Blistering of langmuir-blodgett bilayers containing anionic phospholipids as observed by atomic force microscopy.Distribution of the surfactant-associated protein C within a lung surfactant model film investigated by near-field optical microscopy.Detection of peptide-lipid interactions in mixed monolayers, using isotherms, atomic force microscopy, and fourier transform infrared analyses.Analysis of lung surfactant model systems with time-of-flight secondary ion mass spectrometry.Formation of three-dimensional protein-lipid aggregates in monolayer films induced by surfactant protein B.Fluorescence light microscopy of pulmonary surfactant at the air-water interface of an air bubble of adjustable size.The molecular mechanism of monolayer-bilayer transformations of lung surfactant from molecular dynamics simulations.A modified squeeze-out mechanism for generating high surface pressures with pulmonary surfactantPulmonary surfactant protein SP-C counteracts the deleterious effects of cholesterol on the activity of surfactant films under physiologically relevant compression-expansion dynamics.The N-terminal segment of pulmonary surfactant lipopeptide SP-C has intrinsic propensity to interact with and perturb phospholipid bilayers.Pulmonary surfactant model systems catch the specific interaction of an amphiphilic peptide with anionic phospholipid.Palmitoylation of pulmonary surfactant protein SP-C is critical for its functional cooperation with SP-B to sustain compression/expansion dynamics in cholesterol-containing surfactant films.Solubility versus electrostatics: what determines lipid/protein interaction in lung surfactant.Surfactant protein C peptides with salt-bridges ("ion-locks") promote high surfactant activities by mimicking the α-helix and membrane topography of the native protein
P2860
Q28261677-D1E8FBC1-F8DD-4E00-8CC6-D65B2B20AB26Q28285439-E7398F45-6447-40A1-AC96-49C9781D9D24Q28344531-E288932C-9D65-43BD-A1BB-06A58E699767Q28363708-E5573BFC-3883-41B7-9456-A7E6CEEC5D49Q28388253-942B8A94-4557-4FD3-A548-4D2AD84A350BQ28388325-F55677C8-491D-4720-BCCC-567DDEC615B7Q28395134-ED495061-CD41-4265-A0E9-3A69554BBFE7Q31052512-7C0AEE58-4C3D-4ABC-B8EC-EC9D03DB52ECQ33396842-77A368AC-37CF-412B-ABD8-4FA5991CBF70Q33712598-32F03BF6-A877-4782-9A46-2A616D7821CCQ34171049-E28A754B-DE7D-4894-8FEC-AE05A91968FBQ34174566-BE4580E5-0F0A-42F3-96CE-EF42AF8FEF43Q34175840-2B77AAF6-4253-4209-A925-F10726916AE5Q34180142-0D2E3B2C-4B90-4F3D-92EE-F82E5A9FD550Q34183112-2A450714-517F-4533-86FD-E8DE8E1B0084Q34184833-790B4CF0-2C91-486E-BD90-500E4D9098DCQ34188206-EE893AA8-142F-47BE-BAC0-B1BA917DA2A1Q34350413-FCCF0D0F-FA4C-4F0F-B0C1-367DE20D9A90Q35187671-158C6627-D749-4C51-A33D-D17C267E1FD8Q35649508-953E80FF-DBCC-4238-8116-C7CAFF237A7FQ35850999-AD08F4DD-8543-4AD1-AAD4-7EE5FF0F7424Q36538215-887EE023-5815-478C-8024-D3FDBD1E04C3Q37320766-27217879-C49E-447C-B65F-1B7662C587DDQ38840748-471B31BF-6516-4AD2-B935-D59A4CC5E7C9Q39594125-55388C22-AE2F-4E02-9AFF-836D1836C9CAQ39758077-668AE088-AF64-4291-BC56-93FF44FC43C8Q40150094-2D16BCAE-79CF-41F1-9EFC-475AE598DB77Q40157051-7DA525E1-F31F-494F-88DA-B6CFA8CBFD02Q40158289-4EE77217-4CCF-45C1-A1F7-DADEEF385B94Q40166969-99A6CB1C-0F67-4696-B23E-78DB1049C392Q40168585-F8DD1912-FEE9-41C0-83B0-AEAE6AAC5AA1Q40210778-0FBB94C1-6866-4BD2-8171-08A04AD7589BQ40320317-0023A2D0-8746-4CAF-ADD7-DADB98FC0E1DQ41097884-AAE26C7E-AB23-4265-98B2-8D0E084FF776Q41850314-11409AB4-9373-4623-97B4-11DA56F6BD01Q42023831-293D70FF-FA7E-460D-98A4-E30DCF15D501Q42183433-6F70356D-97C1-4EE0-BF1B-5A9FB6E857F7Q42364805-B56FB46A-063D-44F1-9B24-2ACC30628F6DQ42468968-732FFFAF-3EAE-43D7-9E8D-E75CCE3F8760Q42742507-83CA3DD8-0F80-4E5C-A245-D3CEBDAD9B89
P2860
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
@en
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
@nl
type
label
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
@en
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
@nl
prefLabel
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
@en
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
@nl
P2093
P2860
P1433
P1476
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(97)78687-9
P407
P577
1997-01-01T00:00:00Z