Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles.
about
A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase.Effects of bilayer surface charge density on molecular adsorption and transport across liposome bilayersPulmonary surfactant protein SP-B is significantly more immunoreactive in anionic than in zwitterionic bilayers.Effect of acidic pH on the structure and lipid binding properties of porcine surfactant protein A. Potential role of acidification along its exocytic pathway.Role of surfactant protein A (SP-A)/lipid interactions for SP-A functions in the lung.Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: identification of SER(602), THR(723), AND SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-deFluorescence spectroscopy measures yeast PAH1-encoded phosphatidate phosphatase interaction with liposome membranesNatural Anti-Infective Pulmonary Proteins: In Vivo Cooperative Action of Surfactant Protein SP-A and the Lung Antimicrobial Peptide SP-BNComparison of lipid aggregation and self-aggregation activities of pulmonary surfactant-associated protein ASurfactant protein A forms extensive lattice-like structures on 1,2-dipalmitoylphosphatidylcholine/rough-lipopolysaccharide-mixed monolayers.Differential partitioning of pulmonary surfactant protein SP-A into regions of monolayers of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylcholine/dipalmitoylphosphatidylglycerol.Phase transitions in films of lung surfactant at the air-water interface.Interactions of pulmonary surfactant protein A with phospholipid monolayers change with pH.Differential effects of surfactant protein A on regional organization of phospholipid monolayers containing surfactant protein B or C.Pulmonary surfactant protein A interacts with gel-like regions in monolayers of pulmonary surfactant lipid extract.Molecular structures and interactions of pulmonary surfactant components.Surfactant protein A (SP-A) binds to phosphatidylserine and competes with annexin V binding on late apoptotic cells.Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein.Effect of surfactant protein A on the physical properties and surface activity of KL4-surfactant.Different modes of interaction of pulmonary surfactant protein SP-B in phosphatidylcholine bilayers.Endothelins specifically recognize lysophosphatidylcholine micelles.Role of the degree of oligomerization in the structure and function of human surfactant protein A.Impact of maltose modified poly(propylene imine) dendrimers on liver alcohol dehydrogenase (LADH) internal dynamics and structureTannic Acid-Lung Fluid Assemblies Promote Interaction and Delivery of Drugs to Lung Cancer Cells
P2860
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P2860
Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Tryptophan fluorescence study ...... A with phospholipid vesicles.
@en
Tryptophan fluorescence study ...... A with phospholipid vesicles.
@nl
type
label
Tryptophan fluorescence study ...... A with phospholipid vesicles.
@en
Tryptophan fluorescence study ...... A with phospholipid vesicles.
@nl
prefLabel
Tryptophan fluorescence study ...... A with phospholipid vesicles.
@en
Tryptophan fluorescence study ...... A with phospholipid vesicles.
@nl
P2860
P356
P1433
P1476
Tryptophan fluorescence study ...... n A with phospholipid vesicles
@en
P2093
P2860
P304
P356
10.1042/BJ2960585
P407
P478
296 ( Pt 3)
P577
1993-12-01T00:00:00Z