Docking phospholipase A2 on membranes using electrostatic potential-modulated spin relaxation magnetic resonance.
about
The role of hydrophobic interactions in positioning of peripheral proteins in membranesCrystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranesDiscovery of novel membrane binding structures and functionsConformation and membrane position of the region linking the two C2 domains in synaptotagmin 1 by site-directed spin labeling.Data-driven docking for the study of biomolecular complexes.Lipid interaction networks of peripheral membrane proteins revealed by data-driven micelle dockingCharacterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics.Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domainsProbing the interaction of brain fatty acid binding protein (B-FABP) with model membranesAccelerating membrane insertion of peripheral proteins with a novel membrane mimetic model.Structure and function of a membrane-bound murine MHC class I moleculeInterfacial membrane docking of cytosolic phospholipase A2 C2 domain using electrostatic potential-modulated spin relaxation magnetic resonance.A paramagnetic molecular voltmeter.Using hydrogen/deuterium exchange mass spectrometry to define the specific interactions of the phospholipase A2 superfamily with lipid substrates, inhibitors, and membranes.Atomic-level description of protein-lipid interactions using an accelerated membrane model.Phospholipase A2 structure/function, mechanism, and signaling.Action of human group IIa secreted phospholipase A2 on cell membranes. Vesicle but not heparinoid binding determines rate of fatty acid release by exogenously added enzyme.Substrate efflux propensity plays a key role in the specificity of secretory A-type phospholipases.Topography of the prostaglandin endoperoxide H2 synthase-2 in membranes.Phenylalanine-24 in the N-terminal region of ammodytoxins is important for both enzymic activity and presynaptic toxicity.On the binding preference of human groups IIA and X phospholipases A2 for membranes with anionic phospholipids.How a G protein binds a membrane.Unusual mode of binding of human group IIA secreted phospholipase A2 to anionic interfaces as studied by continuous wave and time domain electron paramagnetic resonance spectroscopy.A model for hydrophobic protrusions on peripheral membrane proteins
P2860
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P2860
Docking phospholipase A2 on membranes using electrostatic potential-modulated spin relaxation magnetic resonance.
description
1998 nî lūn-bûn
@nan
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Docking phospholipase A2 on me ...... relaxation magnetic resonance.
@ast
Docking phospholipase A2 on me ...... relaxation magnetic resonance.
@en
type
label
Docking phospholipase A2 on me ...... relaxation magnetic resonance.
@ast
Docking phospholipase A2 on me ...... relaxation magnetic resonance.
@en
prefLabel
Docking phospholipase A2 on me ...... relaxation magnetic resonance.
@ast
Docking phospholipase A2 on me ...... relaxation magnetic resonance.
@en
P2093
P2860
P1433
P1476
Docking phospholipase A2 on me ...... relaxation magnetic resonance.
@en
P2093
B H Robinson
W L Hubbell
P2860
P304
P356
10.1126/SCIENCE.279.5358.1925
P407
P577
1998-03-01T00:00:00Z