A new conformation in sarcoplasmic reticulum calcium pump and plasma membrane Ca2+ pumps revealed by a photoactivatable phospholipidic probe.
about
Modulation of plasma membrane Ca2+-ATPase by neutral phospholipids: effect of the micelle-vesicle transition and the bilayer thickness.Determination of the dissociation constants for Ca2+ and calmodulin from the plasma membrane Ca2+ pump by a lipid probe that senses membrane domain changes.Plasma membrane calcium pump (PMCA) differential exposure of hydrophobic domains after calmodulin and phosphatidic acid activation.Plasma membrane calcium ATPase activity is regulated by actin oligomers through direct interaction.Conformational changes produced by ATP binding to the plasma membrane calcium pump.Autoinhibition mechanism of the plasma membrane calcium pump isoforms 2 and 4 studied through lipid-protein interactionDiving Into the Lipid Bilayer to Investigate the Transmembrane Organization and Conformational State Transitions of P-type Ion ATPases.Stabilization of the α2 isoform of Na,K-ATPase by mutations in a phospholipid binding pocket.Differential effects of G- and F-actin on the plasma membrane calcium pump activity.Single point mutations in the small cytoplasmic loop of ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana, generate partially deregulated pumps.Selectivity of plasma membrane calcium ATPase (PMCA)-mediated extrusion of toxic divalent cations in vitro and in cultured cells.Dynamic lipid-protein stoichiometry onE1andE2conformations of the Na+/K+-ATPase
P2860
Q30370945-60A31CA4-A969-4553-B526-D2EEDFCFF5B8Q33581158-B51AE355-96E6-41C6-9E74-8665E3D26FC1Q34628074-350EA07A-61C6-43FF-86EC-72675B0BF94BQ34653596-F2FAF059-608F-4B8E-9336-CD26190B5912Q34656000-B14612A2-8436-48AC-B5E2-552D755A4412Q37585093-BE2653A1-3F4A-4857-9A1C-75911299B70AQ37892353-D472F244-869D-4D20-B9FC-E774E0BBF309Q39708587-FE6A19DC-72DC-44B2-9C66-B31E1AB6E322Q41877176-B135C565-012E-404C-9F12-D72C7B27CC19Q42660996-3118728F-0840-4FED-877A-D779172DD002Q50882975-C84FC84E-7298-46A1-B649-2A899357E2DEQ57834702-B5F02F69-D9D9-41E0-962B-3E1AAF15C1DC
P2860
A new conformation in sarcoplasmic reticulum calcium pump and plasma membrane Ca2+ pumps revealed by a photoactivatable phospholipidic probe.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
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2008年學術文章
@zh-hant
name
A new conformation in sarcopla ...... ivatable phospholipidic probe.
@en
A new conformation in sarcopla ...... ivatable phospholipidic probe.
@nl
type
label
A new conformation in sarcopla ...... ivatable phospholipidic probe.
@en
A new conformation in sarcopla ...... ivatable phospholipidic probe.
@nl
prefLabel
A new conformation in sarcopla ...... ivatable phospholipidic probe.
@en
A new conformation in sarcopla ...... ivatable phospholipidic probe.
@nl
P2093
P2860
P356
P1476
A new conformation in sarcopla ...... ivatable phospholipidic probe.
@en
P2093
Ana María Villamil Giraldo
Ariel J Caride
Cristina Marino Buslje
Irene Mangialavori
Mariela Ferreira Gomes
P2860
P304
P356
10.1074/JBC.M806912200
P407
P577
2008-12-12T00:00:00Z