Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study - Wikidata - wikimedia - TriplyDB

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

http://www.wikidata.org/entity/Q34180721

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Structure and Mechanism of the Saposin-like Domain of a Plant Aspartic Protease Toll-like receptor 4 can recognize SapC-DOPS to stimulate macrophages to express several cytokines Molecular imaging of membrane interfaces reveals mode of beta-glucosidase activation by saposin C.Targeting and cytotoxicity of SapC-DOPS nanovesicles in pancreatic cancer.Effects of lipid composition and phase on the membrane interaction of the prion peptide 106-126 amide.Cytotoxicity and Selectivity in Skin Cancer by SapC-DOPS Nanovesicles.Imaging the Selective Binding of Synapsin to Anionic Membrane Domains

P2860

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P2860

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

http://www.wikidata.org/entity/Q34180721

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2003 nî lūn-bûn

@nan

2003 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի մարտին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@ast

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@en

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@nl

type

label

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@ast

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@en

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@nl

prefLabel

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@ast

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@en

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@nl

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Biophysical Journal

P1476

Phospholipid membrane interactions of saposin C: in situ atomic force microscopic study

@en

P2093

Gregory A Grabowski

http://www.w3.org/2001/XMLSchema#string

Hong Xing You

http://www.w3.org/2001/XMLSchema#string

Lei Yu

http://www.w3.org/2001/XMLSchema#string

Xiaoyang Qi

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting

Saposin fold revealed by the NMR structure of NK-lysin

Saposins: structure, function, distribution, and molecular genetics

Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease

Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure

Phospholipid membrane restructuring induced by saposin C: a topographic study using atomic force microscopy.

Interdigitated bilayer membranes.

Alcohol induces interdigitated domains in unilamellar phosphatidylcholine bilayers.

Atomic force microscope imaging of phospholipid bilayer degradation by phospholipase A2

Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.

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2043-2057

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scholarly article

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10.1016/S0006-3495(03)75012-7

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3

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2003-03-01T00:00:00Z

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10879854

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12609906

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1302773

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