Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
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Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fractionImpact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverinThe crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thalianaStabilizing Function for Myristoyl Group Revealed by the Crystal Structure of a Neuronal Calcium Sensor, Guanylate Cyclase-Activating Protein 1Role of N-Terminal Myristylation in the Structure and Regulation of cAMP-Dependent Protein KinaseA Highly Conserved Cysteine of Neuronal Calcium-sensing Proteins Controls Cooperative Binding of Ca2+ to RecoverinMolecular mechanics of calcium-myristoyl switchesCalcium-regulated DNA binding and oligomerization of the neuronal calcium-sensing protein, calsenilin/DREAM/KChIP3Structural insights for activation of retinal guanylate cyclase by GCAP1The EF-hand Ca(2+)-binding protein p22 associates with microtubules in an N-myristoylation-dependent mannerRecoverin regulates light-dependent phosphodiesterase activity in retinal rodsBiophysical and functional characterization of hippocalcin mutants responsible for human dystonia.Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3.Structural diversity of neuronal calcium sensor proteins and insights for activation of retinal guanylyl cyclase by GCAP1.Comparison of simulated and measured calcium sparks in intact skeletal muscle fibers of the frogApplication of surface plasmon resonance for analysis of protein-protein interactions in the G protein-mediated signal transduction pathway.Myristoylation and membrane binding regulate c-Src stability and kinase activityMolecular structure and target recognition of neuronal calcium sensor proteins.Structural analysis of Mg2+ and Ca2+ binding, myristoylation, and dimerization of the neuronal calcium sensor and visinin-like protein 1 (VILIP-1)Toward a unified model of vertebrate rod phototransductionPositive cooperativity without domains or subunits in a monomeric membrane channel.Onset of feedback reactions underlying vertebrate rod photoreceptor light adaptationCalcium-dependent membrane association of a flagellar calcium sensor does not require calcium binding.Crystal Structure of Recoverin with Calcium Ions Bound to Both Functional EF Hands.Regulatory subunit myristoylation antagonizes calcineurin phosphatase activation in yeastThe role of steady phosphodiesterase activity in the kinetics and sensitivity of the light-adapted salamander rod photoresponse.Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State.Effects of Ca2+, Mg2+, and myristoylation on guanylyl cyclase activating protein 1 structure and stabilityS100-annexin complexes--structural insights.The effect of recombinant recoverin on the photoresponse of truncated rod photoreceptors.Responses of the phototransduction cascade to dim light.N-myristoylated proteins, key components in intracellular signal transduction systems enabling rapid and flexible cell responses.Dual regulation of a chimeric plant serine/threonine kinase by calcium and calcium/calmodulin.Ca2+ and Mg2+ binding properties of GCAP-1. Evidence that Mg2+-bound form is the physiological activator of photoreceptor guanylyl cyclase.Secondary structure and Ca2+-induced conformational change of calexcitin, a learning-associated protein.A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes.The binding of myristoylated N-terminal nonapeptide from neuro-specific protein CAP-23/NAP-22 to calmodulin does not induce the globular structure observed for the calmodulin-nonmyristylated peptide complex.Dimerization of peptides by calcium ions: investigation of a calcium-binding motif.Conformational dynamics of recoverin's Ca2+-myristoyl switch probed by 15N NMR relaxation dispersion and chemical shift analysis.Double electron-electron resonance probes Ca²⁺-induced conformational changes and dimerization of recoverin.
P2860
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P2860
Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
@en
Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
@nl
type
label
Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
@en
Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
@nl
prefLabel
Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
@en
Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
@nl
P2093
P2860
P356
P1476
Amino-terminal myristoylation induces cooperative calcium binding to recoverin.
@en
P2093
P2860
P304
P356
10.1074/JBC.270.9.4526
P407
P577
1995-03-01T00:00:00Z