Interactions controlling the membrane binding of basic protein domains: phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces.
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Membrane position of a basic aromatic peptide that sequesters phosphatidylinositol 4,5 bisphosphate determined by site-directed spin labeling and high-resolution NMRMyristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayersLocation and dynamics of basic peptides at the membrane interface: electron paramagnetic resonance spectroscopy of tetramethyl-piperidine-N-oxyl-4-amino-4-carboxylic acid-labeled peptidesPolylysine-induced 2H NMR-observable domains in phosphatidylserine/phosphatidylcholine lipid bilayers.The secretory carrier membrane protein family: structure and membrane topology.Location of the myristoylated alanine-rich C-kinase substrate (MARCKS) effector domain in negatively charged phospholipid bicelles.The SNARE motif of synaptobrevin exhibits an aqueous-interfacial partitioning that is modulated by membrane curvature.The calcium-dependent and calcium-independent membrane binding of synaptotagmin 1: two modes of C2B binding.Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins.The invariant phenylalanine of precursor proteins discloses the importance of Omp85 for protein translocation into cyanellesPolyanions decelerate the kinetics of positively charged gramicidin channels as shown by sensitized photoinactivation.Fluorescence correlation spectroscopy studies of Peptide and protein binding to phospholipid vesicles.Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer.Cross-talk unfolded: MARCKS proteins.Membrane-bound basic peptides sequester multivalent (PIP2), but not monovalent (PS), acidic lipids.Surface plasmon resonance spectroscopy: an emerging tool for the study of peptide-membrane interactions.Emerging Roles for SSeCKS/Gravin/AKAP12 in the Control of Cell Proliferation, Cancer Malignancy, and Barriergenesis.Plasma membrane phosphoinositide organization by protein electrostatics.Functional role of the interaction between polysialic acid and myristoylated alanine-rich C kinase substrate at the plasma membraneAsymmetry in the lipid affinity of bihelical amphipathic peptides. A structural determinant for the specificity of ABCA1-dependent cholesterol efflux by peptides.The intertransmembrane region of Kaposi's sarcoma-associated herpesvirus modulator of immune recognition 2 contributes to B7-2 downregulation.Noncovalent keystone interactions controlling biomembrane structure.The "electrostatic-switch" mechanism: Monte Carlo study of MARCKS-membrane interaction.Segregation of negatively charged phospholipids by the polycationic and farnesylated membrane anchor of Kras.Flexible charged macromolecules on mixed fluid lipid membranes: theory and Monte Carlo simulations.Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions.Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labeling.Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain.
P2860
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P2860
Interactions controlling the membrane binding of basic protein domains: phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces.
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Interactions controlling the m ...... bstrate protein to interfaces.
@ast
Interactions controlling the m ...... bstrate protein to interfaces.
@en
type
label
Interactions controlling the m ...... bstrate protein to interfaces.
@ast
Interactions controlling the m ...... bstrate protein to interfaces.
@en
prefLabel
Interactions controlling the m ...... bstrate protein to interfaces.
@ast
Interactions controlling the m ...... bstrate protein to interfaces.
@en
P2093
P356
P1433
P1476
Interactions controlling the m ...... bstrate protein to interfaces.
@en
P2093
P304
12527-12536
P356
10.1021/BI990847B
P407
P577
1999-09-01T00:00:00Z