Membrane-bound basic peptides sequester multivalent (PIP2), but not monovalent (PS), acidic lipids.
about
The emerging role of phosphoinositide clustering in intracellular trafficking and signal transductionCounterion-mediated cluster formation by polyphosphoinositidesDual regulation of diacylglycerol kinase (DGK)-θ: polybasic proteins promote activation by phospholipids and increase substrate affinityBIN1/M-Amphiphysin2 induces clustering of phosphoinositides to recruit its downstream partner dynamin.Synaptotagmin 1 modulates lipid acyl chain order in lipid bilayers by demixing phosphatidylserineProtein diffusion on charged membranes: a dynamic mean-field model describes time evolution and lipid reorganization.Membrane association of the PTEN tumor suppressor: molecular details of the protein-membrane complex from SPR binding studies and neutron reflectionElectrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfacesNuclear envelope remnants: fluid membranes enriched in sterols and polyphosphoinositidesHeterogeneous diffusion of a membrane-bound pHLIP peptide.Regulation of the putative TRPV1t salt taste receptor by phosphatidylinositol 4,5-bisphosphateKey role of polyphosphoinositides in dynamics of fusogenic nuclear membrane vesicles.Coupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3Fluorescence correlation spectroscopy, raster image correlation spectroscopy, and number and brightness on a commercial confocal laser scanning microscope with analog detectors (Nikon C1).Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction.Nanodomains in early and later phases of FcɛRI signalling.Membrane binding and subcellular localization of retroviral Gag proteins are differentially regulated by MA interactions with phosphatidylinositol-(4,5)-bisphosphate and RNA.Lipoprotein insertion into membranes of various complexity: lipid sorting, interfacial adsorption and protein clustering.Role of GAP-43 in sequestering phosphatidylinositol 4,5-bisphosphate to Raft bilayersInfectious Disease: Connecting Innate Immunity to Biocidal Polymers.Quantitative analysis of the binding of ezrin to large unilamellar vesicles containing phosphatidylinositol 4,5 bisphosphate.Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding.Diffusion coefficient of fluorescent phosphatidylinositol 4,5-bisphosphate in the plasma membrane of cellsPathogen destruction versus intracellular survival: the role of lipids as phagosomal fate determinants.Giant unilamellar vesicles containing phosphatidylinositol(4,5)bisphosphate: characterization and functionalityProfilin interaction with phosphatidylinositol (4,5)-bisphosphate destabilizes the membrane of giant unilamellar vesiclesEffects of Membrane Charge and Order on Membrane Binding of the Retroviral Structural Protein Gag.Modeling membrane deformations and lipid demixing upon protein-membrane interaction: the BAR dimer adsorption.Calcium-dependent lateral organization in phosphatidylinositol 4,5-bisphosphate (PIP2)- and cholesterol-containing monolayers.Polyamine effects on cell function: Possible central role of plasma membrane PI(4,5)P2.Defining the oligomerization state of γ-synuclein in solution and in cells.Calmodulin-mediated regulation of the epidermal growth factor receptor.Recent developments in fluorescence correlation spectroscopy for diffusion measurements in planar lipid membranes.Helix 8 of the angiotensin- II type 1A receptor interacts with phosphatidylinositol phosphates and modulates membrane insertion.Membrane nanodomains: contribution of curvature and interaction with proteins and cytoskeleton.Differential interference of chlorpromazine with the membrane interactions of oncogenic K-Ras and its effects on cell growth.Lateral dynamics of proteins with polybasic domain on anionic membranes: a dynamic Monte-Carlo study.Coupled diffusion of peripherally bound peptides along the outer and inner membrane leaflets.Divalent cation-induced cluster formation by polyphosphoinositides in model membranes.Simultaneous characterization of lateral lipid and prothrombin diffusion coefficients by z-scan fluorescence correlation spectroscopy.
P2860
Q26752446-CDE0FF82-7F9F-498E-9E28-91A097CD5B90Q27011678-A0B5936B-C3B5-4F3A-AEA1-33CB1A7C654CQ28114932-C697B842-FB7A-42C3-B25E-3FED0A9318EEQ30009259-920B48B8-A99E-414E-A7A9-F8C1FF8914EFQ30425982-C1C18848-0573-4984-97B2-01D5EFA9A57AQ30481454-1CDA47D1-366E-40F7-B41E-1A6897FF5A99Q31055274-6FD3F2C4-F101-46C2-A871-C617E81B1A49Q31110240-CF61379C-B13B-44A9-BF54-E1BB8818E6CDQ33402484-C6FFE6E5-D08A-4BEB-8D88-3F524F990ECAQ33908287-08C4B995-F981-4317-A3F1-DFE654EE355EQ33920858-39C86436-FF18-4EB6-8531-AFF51A366812Q34023173-CC6B9FE6-6399-4DCB-AC79-D7C79AE3CBE0Q34089040-8FACF5B6-E73E-4A30-A705-1A4BDE889FFDQ34401764-FA2FF8A8-DE10-4E3B-A2E5-29E947996FB2Q34698720-88BD3B0C-9BD6-4533-BAD2-1C3EE95CACDEQ35064036-68A02A46-2044-4467-8862-3AD598BD5AB1Q35072137-CB9894B0-56A9-4341-A3B2-922459027194Q35951636-C2184C3B-F9E6-4168-B897-838FE5DD1F65Q36259531-95A5FA31-1B91-4584-B3E2-E39C7C6A5FD6Q36298207-C6DCAF75-AAA4-4486-95C6-A1A47C86DA81Q36345022-424C88F5-59CB-46D0-845F-9A00A487CA30Q36483820-0BFA262A-AC3A-4F2B-AD24-35817E7A385FQ36536616-913390F0-598C-4751-B113-21791EF2BA22Q36677618-F837DB0F-3A4E-46B6-9258-0BE2465A91ECQ36938679-670B9B40-53BD-4EBF-B7AF-2520B24E09DEQ37265344-D4993CA6-464F-4B92-BE1C-71B481CF34F6Q37300342-D5F4917D-6764-4C27-8B98-E55A5FB4BCA3Q37359471-CC325B37-EB99-40F4-A9CB-005F12BF666CQ37415354-BD3B6945-E391-4CD8-B666-293EB72163FAQ37595417-78291FC9-34A3-4666-9B67-9E6C36922F23Q37598290-232D142B-C628-4DF4-81BB-8CA648174A5EQ37642081-F04F1B3D-8F12-4E61-BE5C-1D980D229E93Q37729842-5A8F99E9-E932-4C86-9682-43AFBFA0BED7Q37736201-B4700E6C-9404-4602-93EE-5945715E58B2Q38346513-1A9A99F9-E226-4F88-847F-634686D4FA49Q39951891-06EF127C-D980-4907-A4FE-82934E6166FAQ41866287-BE541D56-2787-421A-B21D-F8DD504FE1FBQ42102077-0D172FD5-5145-46C2-BB24-9421B8237A0CQ42325961-CA21FBF7-6B40-4435-8B62-03BAE99CCA05Q42630015-F22493E3-0438-45FA-BF42-B9AC51FE9887
P2860
Membrane-bound basic peptides sequester multivalent (PIP2), but not monovalent (PS), acidic lipids.
description
2006 nî lūn-bûn
@nan
2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@ast
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@en
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@nl
type
label
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@ast
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@en
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@nl
prefLabel
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@ast
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@en
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@nl
P2093
P2860
P1433
P1476
Membrane-bound basic peptides ...... onovalent (PS), acidic lipids.
@en
P2093
Alok Gambhir
Gyöngyi Hangyás-Mihályné
Irina Zaitseva
Joachim Rädler
Stuart McLaughlin
Urszula Golebiewska
P2860
P304
P356
10.1529/BIOPHYSJ.106.081562
P407
P577
2006-04-28T00:00:00Z