Proper restoration of excitation-contraction coupling in the dihydropyridine receptor beta1-null zebrafish relaxed is an exclusive function of the beta1a subunit.
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Defects of the Glycinergic Synapse in Zebrafish.Ca(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channelRbfox-regulated alternative splicing is critical for zebrafish cardiac and skeletal muscle functionsStructural and biophysical analyses of the skeletal dihydropyridine receptor β subunit β1a reveal critical roles of domain interactions for stability.Congenital myopathy results from misregulation of a muscle Ca2+ channel by mutant Stac3.Stac3 has a direct role in skeletal muscle-type excitation-contraction coupling that is disrupted by a myopathy-causing mutation.Domain cooperativity in the β1a subunit is essential for dihydropyridine receptor voltage sensing in skeletal muscle.The ß subunit of voltage-gated Ca2+ channelsDefective glycinergic synaptic transmission in zebrafish motility mutants.Non-Ca2+-conducting Ca2+ channels in fish skeletal muscle excitation-contraction coupling.The Cavβ1a subunit regulates gene expression and suppresses myogenin in muscle progenitor cells.Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond.The β(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and activates the channel via its 35-residue C-terminal tailAmino acid residues 489-503 of dihydropyridine receptor (DHPR) β1a subunit are critical for structural communication between the skeletal muscle DHPR complex and type 1 ryanodine receptorThe alpha1 subunit EGL-19, the alpha2/delta subunit UNC-36, and the beta subunit CCB-1 underlie voltage-dependent calcium currents in Caenorhabditis elegans striated muscle.Rem uncouples excitation-contraction coupling in adult skeletal muscle fibers.Regions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunitFluorescence resonance energy transfer (FRET) indicates that association with the type I ryanodine receptor (RyR1) causes reorientation of multiple cytoplasmic domains of the dihydropyridine receptor (DHPR) α(1S) subunit.Three-dimensional localization of the α and β subunits and of the II-III loop in the skeletal muscle L-type Ca2+ channel.Fluorescence Resonance Energy Transfer-based Structural Analysis of the Dihydropyridine Receptor α1S Subunit Reveals Conformational Differences Induced by Binding of the β1a Subunit.Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.β1a490-508, a 19-residue peptide from C-terminal tail of Cav1.1 β1a subunit, potentiates voltage-dependent calcium release in adult skeletal muscle fibers.Analysis of embryonic and larval zebrafish skeletal myofibers from dissociated preparations.Structure and function of the β subunit of voltage-gated Ca²⁺ channels.Zebrafish muscular disease models towards drug discovery.The mammalian skeletal muscle DHPR has larger Ca2+ conductance and is phylogenetically ancient to the early ray-finned fish sterlet (Acipenser ruthenus).NO-sGC Pathway Modulates Ca2+ Release and Muscle Contraction in Zebrafish Skeletal Muscle.Divergent biophysical properties, gating mechanisms, and possible functions of the two skeletal muscle Ca(V)1.1 calcium channel splice variantsSkeletal muscle excitation-contraction coupling is independent of a conserved heptad repeat motif in the C-terminus of the DHPRbeta(1a) subunit.The Qgamma component of intra-membrane charge movement is present in mammalian muscle fibres, but suppressed in the absence of S100A1.De novo reconstitution reveals the proteins required for skeletal muscle voltage-induced Ca2+ release.Transport of the alpha subunit of the voltage gated L-type calcium channel through the sarcoplasmic reticulum occurs prior to localization to triads and requires the beta subunit but not Stac3 in skeletal muscles.Stac proteins associate with the critical domain for excitation-contraction coupling in the II-III loop of CaV1.1.
P2860
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P2860
Proper restoration of excitation-contraction coupling in the dihydropyridine receptor beta1-null zebrafish relaxed is an exclusive function of the beta1a subunit.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Proper restoration of excitati ...... unction of the beta1a subunit.
@en
type
label
Proper restoration of excitati ...... unction of the beta1a subunit.
@en
prefLabel
Proper restoration of excitati ...... unction of the beta1a subunit.
@en
P2093
P2860
P356
P1476
Proper restoration of excitati ...... unction of the beta1a subunit.
@en
P2093
Anamika Dayal
Johann Schredelseker
Manfred Grabner
P2860
P304
P356
10.1074/JBC.M807767200
P407
P577
2008-11-13T00:00:00Z