RYR1 and RYR3 have different roles in the assembly of calcium release units of skeletal muscle.
about
Multiple regions of RyR1 mediate functional and structural interactions with alpha(1S)-dihydropyridine receptors in skeletal muscleCa(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channelType 1 and type 3 ryanodine receptors generate different Ca(2+) release event activity in both intact and permeabilized myotubes.Ca2+ influx through alpha1S DHPR may play a role in regulating Ca2+ release from RyR1 in skeletal muscleReorganized stores and impaired calcium handling in skeletal muscle of mice lacking calsequestrin-1Structural and functional properties of ryanodine receptor type 3 in zebrafish tail muscle.Type 3 ryanodine receptors of skeletal muscle are segregated in a parajunctional position.Morphology and molecular composition of sarcoplasmic reticulum surface junctions in the absence of DHPR and RyR in mouse skeletal muscleThe structure of Ca(2+) release units in arthropod body muscle indicates an indirect mechanism for excitation-contraction couplingRyR1/RyR3 chimeras reveal that multiple domains of RyR1 are involved in skeletal-type E-C couplingDifferential effects of voltage-dependent inactivation and local anesthetics on kinetic phases of Ca2+ release in frog skeletal muscle.Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle.Ryanodine receptor point mutant E4032A reveals an allosteric interaction with ryanodine.Stac adaptor proteins regulate trafficking and function of muscle and neuronal L-type Ca2+ channelsBidirectional signaling between calcium channels of skeletal muscle requires multiple direct and indirect interactions.Ca(2+) sparks operated by membrane depolarization require isoform 3 ryanodine receptor channels in skeletal muscle.Regions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunitAccessibility of targeted DHPR sites to streptavidin and functional effects of binding on EC coupling.Evolution of skeletal type e-c coupling: a novel means of controlling calcium delivery.Alpha2delta1 dihydropyridine receptor subunit is a critical element for excitation-coupled calcium entry but not for formation of tetrads in skeletal myotubesEffects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.Ryanodine receptor luminal Ca2+ regulation: swapping calsequestrin and channel isoforms.Evidence for conformational coupling between two calcium channels.Conformational activation of Ca2+ entry by depolarization of skeletal myotubes.Differential contribution of skeletal and cardiac II-III loop sequences to the assembly of dihydropyridine-receptor arrays in skeletal muscle.Visualization of Ca²+ signaling during embryonic skeletal muscle formation in vertebrates.Knocking down type 2 but not type 1 calsequestrin reduces calcium sequestration and release in C2C12 skeletal muscle myotubes.Voltage-controlled Ca2+ release and entry flux in isolated adult muscle fibres of the mouse.All three ryanodine receptor isoforms generate rapid cooling responses in muscle cells.Observation of Network Dynamics of Ryanodine Receptors on Skeletal Muscle Sarcoplasmic Reticulum Membranes.A probable role of dihydropyridine receptors in repression of Ca2+ sparks demonstrated in cultured mammalian muscle.Nicotinic acid-adenine dinucleotide phosphate activates the skeletal muscle ryanodine receptor.RyR3 amplifies RyR1-mediated Ca(2+)-induced Ca(2+) release in neonatal mammalian skeletal muscle.Ca2+ sparks are initiated by Ca2+ entry in embryonic mouse skeletal muscle and decrease in frequency postnatally.Amino acids 1-1,680 of ryanodine receptor type 1 hold critical determinants of skeletal type for excitation-contraction coupling. Role of divergence domain D2.Localised calcium release events in cells from the muscle of guinea-pig gastric fundus.Ryanodine receptor oligomeric interaction: identification of a putative binding region.RyR1 exhibits lower gain of CICR activity than RyR3 in the SR: evidence for selective stabilization of RyR1 channel.External Ca(2+)-dependent excitation--contraction coupling in a population of ageing mouse skeletal muscle fibres.Endoplasmic Reticulum-Plasma Membrane Contacts Regulate Cellular Excitability.
P2860
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P2860
RYR1 and RYR3 have different roles in the assembly of calcium release units of skeletal muscle.
description
2000 nî lūn-bûn
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2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@ast
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@en
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@nl
type
label
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@ast
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@en
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@nl
prefLabel
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@ast
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@en
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@nl
P2093
P2860
P1433
P1476
RYR1 and RYR3 have different r ...... ease units of skeletal muscle.
@en
P2093
C Franzini-Armstrong
G Meissner
H Takekura
P2860
P304
P356
10.1016/S0006-3495(00)76491-5
P407
P577
2000-11-01T00:00:00Z