GRP1 pleckstrin homology domain: activation parameters and novel search mechanism for rare target lipid.
about
Myo1e binds anionic phospholipids with high affinityBiophysical methods for the characterization of PTEN/lipid bilayer interactionsPTEN hopping on the cell membrane is regulated via a positively-charged C2 domainLateral diffusion of proteins on supported lipid bilayers: additive friction of synaptotagmin 7 C2A-C2B tandem domains.Structural Basis for the Golgi Association by the Pleckstrin Homology Domain of the Ceramide Trafficking Protein (CERT)Crystal structure of the pleckstrin homology domain from the ceramide transfer protein: implications for conformational change upon ligand bindingPhosphatidylinositol 4,5-bisphosphate-specific AKT1 is oncogenic.Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domainsMolecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of the AKT1 PH domain.Membrane docking geometry of GRP1 PH domain bound to a target lipid bilayer: an EPR site-directed spin-labeling and relaxation study.Single molecule diffusion of membrane-bound proteins: window into lipid contacts and bilayer dynamics.Solvent-Free, Highly Coarse-Grained Models for Charged Lipid Systems.Molecular mechanism of membrane binding of the GRP1 PH domain.Phosphatidylserine is a critical modulator for Akt activation.Biophysical and computational studies of membrane penetration by the GRP1 pleckstrin homology domain.Polyphosphoinositide binding domains: Key to inositol lipid biology.Mechanism for phosphoinositide selectivity and activation of TRPV1 ion channels.Lipid targeting domain with dual-membrane specificity that expands the diversity of intracellular targeting reactions.Phosphatidylserine binding is essential for plasma membrane recruitment and signaling function of 3-phosphoinositide-dependent kinase-1.Assembly of membrane-bound protein complexes: detection and analysis by single molecule diffusion.Segregation of PIP2 and PIP3 into distinct nanoscale regions within the plasma membraneDetermining selectivity of phosphoinositide-binding domainsPleckstrin homology (PH) domains and phosphoinositides.Molecular mechanism of membrane targeting by the GRP1 PH domainKinetics of endophilin N-BAR domain dimerization and membrane interactions.Regulation of PI3K by PKC and MARCKS: Single-Molecule Analysis of a Reconstituted Signaling PathwayStrange kinetics of bulk-mediated diffusion on lipid bilayers.Reversible binding and rapid diffusion of proteins in complex with inositol lipids serves to coordinate free movement with spatial informationSingle-molecule fluorescence studies of a PH domain: new insights into the membrane docking reaction.Kinetics of the interaction of myo1c with phosphoinositides.Quantification of protein-lipid selectivity using FRET.Interplay between phosphoinositide lipids and calcium signals at the leading edge of chemotaxing ameboid cells.Hydrophobic contributions to the membrane docking of synaptotagmin 7 C2A domain: mechanistic contrast between isoforms 1 and 7The GRP1 PH domain, like the AKT1 PH domain, possesses a sentry glutamate residue essential for specific targeting to plasma membrane PI(3,4,5)P(3).Interactions of Pleckstrin Homology Domains with Membranes: Adding Back the Bilayer via High-Throughput Molecular Dynamics.Phosphatidylinositol-(4,5)-bisphosphate enables efficient secretion of HIV-1 Tat by infected T-cells.Association of Peripheral Membrane Proteins with Membranes: Free Energy of Binding of GRP1 PH Domain with Phosphatidylinositol Phosphate-Containing Model Bilayers.The C2 domains of granuphilin are high-affinity sensors for plasma membrane lipids.The PH domain of phosphoinositide-dependent kinase-1 exhibits a novel, phospho-regulated monomer-dimer equilibrium with important implications for kinase domain activation: single-molecule and ensemble studiesMembrane Recruitment as a Cancer Mechanism: A Case Study of Akt PH Domain.
P2860
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P2860
GRP1 pleckstrin homology domain: activation parameters and novel search mechanism for rare target lipid.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
GRP1 pleckstrin homology domai ...... chanism for rare target lipid.
@en
GRP1 pleckstrin homology domai ...... chanism for rare target lipid.
@nl
type
label
GRP1 pleckstrin homology domai ...... chanism for rare target lipid.
@en
GRP1 pleckstrin homology domai ...... chanism for rare target lipid.
@nl
prefLabel
GRP1 pleckstrin homology domai ...... chanism for rare target lipid.
@en
GRP1 pleckstrin homology domai ...... chanism for rare target lipid.
@nl
P2093
P2860
P356
P1433
P1476
GRP1 pleckstrin homology domai ...... chanism for rare target lipid.
@en
P2093
John A Corbin
Joseph J Falke
Ronald A Dirkx
P2860
P304
16161-16173
P356
10.1021/BI049017A
P407
P577
2004-12-01T00:00:00Z