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Transient GPI-anchored protein homodimers are units for raft organization and function

Transient GPI-anchored protein homodimers are units for raft organization and function

http://www.wikidata.org/entity/Q58498251

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Dynamics of the actin cytoskeleton mediates receptor cross talk: An emerging concept in tuning receptor signaling Lipid Raft-Mediated Regulation of Hyaluronan-CD44 Interactions in Inflammation and Cancer A critical survey of methods to detect plasma membrane rafts Consequences of membrane topography Confined diffusion of transmembrane proteins and lipids induced by the same actin meshwork lining the plasma membrane.Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling Nanoscopic substructures of raft-mimetic liquid-ordered membrane domains revealed by high-speed single-particle tracking.Nutritional lipidomics: molecular metabolism, analytics, and diagnostics Golgi sorting regulates organization and activity of GPI proteins at apical membranes Lipids in cell biology: how can we understand them better?Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling.Ultrafast diffusion of a fluorescent cholesterol analog in compartmentalized plasma membranes Effect of receptor dimerization on membrane lipid raft structure continuously quantified on single cells by camera based fluorescence correlation spectroscopy.Analysis of lipid-composition changes in plasma membrane microdomains Exploring in vivo cholesterol-mediated interactions between activated EGF receptors in plasma membrane with single-molecule optical tracking.Dynamic label-free imaging of lipid nanodomains ABCA1-dependent sterol release: sterol molecule specificity and potential membrane domain for HDL biogenesis.A GPI processing phospholipase A2, PGAP6, modulates Nodal signaling in embryos by shedding CRIPTO.Single molecule analysis reveals coexistence of stable serotonin transporter monomers and oligomers in the live cell plasma membrane.Tracking single molecules at work in living cells.Microscopy approaches to investigate protein dynamics and lipid organization.Regulation of PrP(C) signaling and processing by dimerization.Membrane-cytoskeleton interactions in cholesterol-dependent domain formation.With or without rafts? Alternative views on cell membranes.Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs.EGF domain of coagulation factor IX is conducive to exposure of phosphatidylserine.An outlook on protein S-acylation in plants: what are the next steps?GPI-anchored proteins do not reside in ordered domains in the live cell plasma membrane.MDX-1097 induces antibody-dependent cellular cytotoxicity against kappa multiple myeloma cells and its activity is augmented by lenalidomide.Cellular encoding of Cy dyes for single-molecule imaging.The role of complement inhibitors beyond controlling inflammation.Implications of lipid moiety in oligomerization and immunoreactivities of GPI-anchored proteins.Discreet and distinct clustering of five model membrane proteins revealed by single molecule localization microscopy.High-fidelity protein targeting into membrane lipid microdomains in living cells.Binding of a pleurotolysin ortholog from Pleurotus eryngii to sphingomyelin and cholesterol-rich membrane domains.[Clathrin-independent endocytosis: free the way!].GPI-anchored proteins are confined in subdiffraction clusters at the apical surface of polarized epithelial cells.Two-Color Single-Molecule Tracking in Live Cells.Cortical actin nodes: Their dynamics and recruitment of podosomal proteins as revealed by super-resolution and single-molecule microscopy.Emphatic visualization of sphingomyelin-rich domains by inter-lipid FRET imaging using fluorescent sphingomyelins.

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Transient GPI-anchored protein homodimers are units for raft organization and function

http://www.wikidata.org/entity/Q58498251

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im Juli 2012 veröffentlichter wissenschaftlicher Artikel

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scientific article published on 22 July 2012

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в липні 2012

@uk

name

Transient GPI-anchored protein homodimers are units for raft organization and function

@en

Transient GPI-anchored protein homodimers are units for raft organization and function

@nl

type

label

Transient GPI-anchored protein homodimers are units for raft organization and function

@en

Transient GPI-anchored protein homodimers are units for raft organization and function

@nl

prefLabel

Transient GPI-anchored protein homodimers are units for raft organization and function

@en

Transient GPI-anchored protein homodimers are units for raft organization and function

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Nature Chemical Biology

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Transient GPI-anchored protein homodimers are units for raft organization and function

@en

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Akihiro Kusumi

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

Kenichi G N Suzuki

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

Koichiro M Hirosawa

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

Munenori Ishibashi

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

Rinshi S Kasai

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

Yoshihiro Miwa

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

P2860

Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin

Dynamic recruitment of phospholipase C gamma at transiently immobilized GPI-anchored receptor clusters induces IP3-Ca2+ signaling: single-molecule tracking study 2

Crystal structure of CD59: implications for molecular recognition of the complement proteins C8 and C9 in the membrane-attack complex

The molecular structure of green fluorescent protein

Lipid rafts and signal transduction

Direct observation of the nanoscale dynamics of membrane lipids in a living cell

Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells

Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation

Lipid domain structure of the plasma membrane revealed by patching of membrane components

Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides.

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774-783

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scholarly article

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10.1038/NCHEMBIO.1028

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9

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8

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Takahiro Fujiwara

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2012-07-22T00:00:00Z

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22820419

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