Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling.
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The role of hydrophobic interactions in positioning of peripheral proteins in membranesMembrane position of a basic aromatic peptide that sequesters phosphatidylinositol 4,5 bisphosphate determined by site-directed spin labeling and high-resolution NMRContrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domainsC2 domains of protein kinase C isoforms alpha, beta, and gamma: activation parameters and calcium stoichiometries of the membrane-bound statePtdInsP2 and PtdSer cooperate to trap synaptotagmin-1 to the plasma membrane in the presence of calcium.Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfacesDiscovery of novel membrane binding structures and functionsBCL::MP-fold: Membrane protein structure prediction guided by EPR restraintsCooperative Substrate-Cofactor Interactions and Membrane Localization of the Bacterial Phospholipase A2 (PLA2) Enzyme, ExoU.The SNARE motif of synaptobrevin exhibits an aqueous-interfacial partitioning that is modulated by membrane curvature.Phosphatidylinositol 4,5-bisphosphate alters synaptotagmin 1 membrane docking and drives opposing bilayers closer together.Synaptotagmin 1 and SNAREs form a complex that is structurally heterogeneous.Solution and membrane-bound conformations of the tandem C2A and C2B domains of synaptotagmin 1: Evidence for bilayer bridgingThe calcium-dependent and calcium-independent membrane binding of synaptotagmin 1: two modes of C2B binding.Conformation and membrane position of the region linking the two C2 domains in synaptotagmin 1 by site-directed spin labeling.Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion.Spin-diffusion couples proton relaxation rates for proteins in exchange with a membrane interfaceThe calcium binding loops of the cytosolic phospholipase A2 C2 domain specify targeting to Golgi and ER in live cellsStructural refinement of membrane proteins by restrained molecular dynamics and solvent accessibility data.Probing Structural Dynamics and Topology of the KCNE1 Membrane Protein in Lipid Bilayers via Site-Directed Spin Labeling and Electron Paramagnetic Resonance Spectroscopy.Lipid interaction networks of peripheral membrane proteins revealed by data-driven micelle dockingRoles of amphipathic helices and the bin/amphiphysin/rvs (BAR) domain of endophilin in membrane curvature generationThe cytosolic domain of Fis1 binds and reversibly clusters lipid vesicles.Mechanism of specific membrane targeting by C2 domains: localized pools of target lipids enhance Ca2+ affinity.Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domainsMembrane docking geometry of GRP1 PH domain bound to a target lipid bilayer: an EPR site-directed spin-labeling and relaxation study.X-ray reflectivity studies of cPLA2{alpha}-C2 domains adsorbed onto Langmuir monolayers of SOPCDeimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope.Molecular mechanism of membrane binding of the GRP1 PH domain.Capturing spontaneous partitioning of peripheral proteins using a biphasic membrane-mimetic model.Self-induced docking site of a deeply embedded peripheral membrane proteinReconstitution of KCNE1 into lipid bilayers: comparing the structural, dynamic, and activity differences in micelle and vesicle environmentsMembrane-bending proteinsThe molecular basis of ceramide-1-phosphate recognition by C2 domains.Investigation of the binding geometry of a peripheral membrane protein.Ca2+ activation of the cPLA2 C2 domain: ordered binding of two Ca2+ ions with positive cooperativity.Cellular membranes and lipid-binding domains as attractive targets for drug development.Interactions of the GM2 activator protein with phosphatidylcholine bilayers: a site-directed spin-labeling power saturation study.Perturbations of the straight transmembrane α-helical structure of the amyloid precursor protein affect its processing by γ-secretase.The PICM chemical scanning method for identifying domain-domain and protein-protein interfaces: applications to the core signaling complex of E. coli chemotaxis.
P2860
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P2860
Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Membrane orientation and posit ...... y site-directed spin labeling.
@ast
Membrane orientation and posit ...... y site-directed spin labeling.
@en
type
label
Membrane orientation and posit ...... y site-directed spin labeling.
@ast
Membrane orientation and posit ...... y site-directed spin labeling.
@en
prefLabel
Membrane orientation and posit ...... y site-directed spin labeling.
@ast
Membrane orientation and posit ...... y site-directed spin labeling.
@en
P2093
P356
P1433
P1476
Membrane orientation and posit ...... y site-directed spin labeling.
@en
P2093
April A Frazier
David S Cafiso
Eric A Nalefski
Gail E Fanucci
Joseph J Falke
Kenneth G Victor
Mark A Wisner
Nathan J Malmberg
P304
P356
10.1021/BI0160821
P407
P577
2002-05-01T00:00:00Z