GPI-anchored proteins are organized in submicron domains at the cell surface.
about
The specificity for the differentiation blocking activity of carcinoembryonic antigen resides in its glycophosphatidyl-inositol anchorMembrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMPProteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranesGPIHBP1 is responsible for the entry of lipoprotein lipase into capillariesDual role of lipopolysaccharide (LPS)-binding protein in neutralization of LPS and enhancement of LPS-induced activation of mononuclear cellsHomo-FRET microscopy in living cells to measure monomer-dimer transition of GFP-tagged proteins.Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and -2Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers.Lipid rafts, cholesterol, and the brainFluorescence probe partitioning between Lo/Ld phases in lipid membranesVirus entry, assembly, budding, and membrane raftsGlycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicronsCritical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcepsilonRI and their association with detergent-resistant membranesSpecific association of glycoprotein B with lipid rafts during herpes simplex virus entryDetergent-resistant membranes and the protein composition of lipid raftsCurrent approaches to studying membrane organizationMembrane microdomains: from seeing to understandingCell-surface translational dynamics of nicotinic acetylcholine receptorsA critical survey of methods to detect plasma membrane raftsEmerging research and clinical development trends of liposome and lipid nanoparticle drug delivery systemsSalt-induced remodeling of spatially restricted clathrin-independent endocytic pathways in Arabidopsis rootProbing membrane protein interactions with their lipid raft environment using single-molecule tracking and Bayesian inference analysisPrecise positioning of myosin VI on endocytic vesicles in vivoLipids and membrane microdomains in HIV-1 replicationInfluenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.LAT, the linker for activation of T cells: a bridge between T cell-specific and general signaling pathwaysAtomic force microscopy studies of ganglioside GM1 domains in phosphatidylcholine and phosphatidylcholine/cholesterol bilayers.Caveolae/lipid rafts in fibroblast-like synoviocytes: ectopeptidase-rich membrane microdomainsBinding of cross-linked glycosylphosphatidylinositol-anchored proteins to discrete actin-associated sites and cholesterol-dependent domainsGPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment.Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: nanoscopic domain formation driven by cholesterolRelationship of lipid rafts to transient confinement zones detected by single particle trackingCholesterol depletion reduces apical transport capacity in epithelial Madin-Darby canine kidney cellsNeuronal conduction of excitation without action potentials based on ceramide productionMannose receptor (MR) engagement by mesothelin GPI anchor polarizes tumor-associated macrophages and is blocked by anti-MR human recombinant antibodyA role for lipid rafts in B cell antigen receptor signaling and antigen targetingIntegrin leukocyte function-associated antigen-1-mediated cell binding can be activated by clustering of membrane raftsBayesian decision tree for the classification of the mode of motion in single-molecule trajectoriesPartitioning of the plasma membrane Ca2+-ATPase into lipid rafts in primary neurons: effects of cholesterol depletionThe membrane environment of endogenous cellular prion protein in primary rat cerebellar neurons
P2860
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P2860
GPI-anchored proteins are organized in submicron domains at the cell surface.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
GPI-anchored proteins are organized in submicron domains at the cell surface.
@en
GPI-anchored proteins are organized in submicron domains at the cell surface.
@nl
type
label
GPI-anchored proteins are organized in submicron domains at the cell surface.
@en
GPI-anchored proteins are organized in submicron domains at the cell surface.
@nl
prefLabel
GPI-anchored proteins are organized in submicron domains at the cell surface.
@en
GPI-anchored proteins are organized in submicron domains at the cell surface.
@nl
P356
P1433
P1476
GPI-anchored proteins are organized in submicron domains at the cell surface.
@en
P2888
P304
P356
10.1038/29563
P407
P577
1998-08-01T00:00:00Z
P5875
P6179
1025389798