Ca2+ binding to site I of the cardiac Ca2+ pump is sufficient to dissociate phospholamban.
about
Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathyA separate pool of cardiac phospholemman that does not regulate or associate with the sodium pump: multimers of phospholemman in ventricular muscleSuperinhibitory phospholamban mutants compete with Ca2+ for binding to SERCA2a by stabilizing a unique nucleotide-dependent conformational state.Phospholamban binds with differential affinity to calcium pump conformersAtomic-level mechanisms for phospholamban regulation of the calcium pump.The N Terminus of Sarcolipin Plays an Important Role in Uncoupling Sarco-endoplasmic Reticulum Ca2+-ATPase (SERCA) ATP Hydrolysis from Ca2+ TransportSarcolipin protein interaction with sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump.Sarco(endo)plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail.Phosphorylated phospholamban stabilizes a compact conformation of the cardiac calcium-ATPase.Structural dynamics of muscle protein phosphorylation.Phospholamban and sarcolipin: Are they functionally redundant or distinct regulators of the Sarco(Endo)Plasmic Reticulum Calcium ATPase?Secondary structure, backbone dynamics, and structural topology of phospholamban and its phosphorylated and Arg9Cys-mutated forms in phospholipid bilayers utilizing 13C and 15N solid-state NMR spectroscopy.Phospholamban mutants compete with wild type for SERCA binding in living cells.Time-resolved FRET reveals the structural mechanism of SERCA-PLB regulation.Probing the interaction of Arg9Cys mutated phospholamban with phospholipid bilayers by solid-state NMR spectroscopy.A phospholamban-tethered cardiac Ca2+ pump reveals stoichiometry and dynamic interactions between the two proteins.
P2860
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P2860
Ca2+ binding to site I of the cardiac Ca2+ pump is sufficient to dissociate phospholamban.
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Ca2+ binding to site I of the ...... t to dissociate phospholamban.
@ast
Ca2+ binding to site I of the ...... t to dissociate phospholamban.
@en
type
label
Ca2+ binding to site I of the ...... t to dissociate phospholamban.
@ast
Ca2+ binding to site I of the ...... t to dissociate phospholamban.
@en
prefLabel
Ca2+ binding to site I of the ...... t to dissociate phospholamban.
@ast
Ca2+ binding to site I of the ...... t to dissociate phospholamban.
@en
P2093
P2860
P356
P1476
Ca2+ binding to site I of the ...... t to dissociate phospholamban.
@en
P2093
Brandy L Akin
Larry R Jones
Zhenhui Chen
P2860
P304
P356
10.1074/JBC.M109.080820
P407
P577
2009-11-30T00:00:00Z