Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle.
about
Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membraneStac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathyPI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins.Requirement for the ryanodine receptor type 3 for efficient contraction in neonatal skeletal muscles.Multiple regions of RyR1 mediate functional and structural interactions with alpha(1S)-dihydropyridine receptors in skeletal muscleAmphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in DrosophilaFunctional analysis of a frame-shift mutant of the dihydropyridine receptor pore subunit (alpha1S) expressing two complementary protein fragmentsRecent advances in understanding cardiac contractility in health and disease3D Structure of the Dihydropyridine Receptor of Skeletal MuscleCritical Role of Intracellular RyR1 Calcium Release Channels in Skeletal Muscle Function and DiseaseThe Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic PotentialThe endoplasmic reticulum: structure, function and response to cellular signalingCa(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channelThe junctophilin family of proteins: from bench to bedsideNanoscale patterning of STIM1 and Orai1 during store-operated Ca2+ entryStructural determination of the phosphorylation domain of the ryanodine receptorStructure of the voltage-gated calcium channel Cav1.1 complexChannelopathies of skeletal muscle excitabilityVoltage-gated calcium channelsS100A1 and calmodulin regulation of ryanodine receptor in striated muscleTwo domains in dihydropyridine receptor activate the skeletal muscle Ca(2+) release channel.A cardiac dihydropyridine receptor II-III loop peptide inhibits resting Ca(2+) sparks in ferret ventricular myocytesType 1 and type 3 ryanodine receptors generate different Ca(2+) release event activity in both intact and permeabilized myotubes.A component of excitation-contraction coupling triggered in the absence of the T671-L690 and L720-Q765 regions of the II-III loop of the dihydropyridine receptor alpha(1s) pore subunit.Spark- and ember-like elementary Ca2+ release events in skinned fibres of adult mammalian skeletal muscleFKBP12 modulation of the binding of the skeletal ryanodine receptor onto the II-III loop of the dihydropyridine receptor.Ca(2+)-induced Ca2+ release in myocytes from dyspedic mice lacking the type-1 ryanodine receptorCa2+ sparks in embryonic mouse skeletal muscle selectively deficient in dihydropyridine receptor alpha1S or beta1a subunits.Type 3 and type 1 ryanodine receptors are localized in triads of the same mammalian skeletal muscle fibersAn Ryr1I4895T mutation abolishes Ca2+ release channel function and delays development in homozygous offspring of a mutant mouse lineSkeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced Ca2+ release and contractilityReorganized stores and impaired calcium handling in skeletal muscle of mice lacking calsequestrin-1Congenital myopathy results from misregulation of a muscle Ca2+ channel by mutant Stac3.Domain cooperativity in the β1a subunit is essential for dihydropyridine receptor voltage sensing in skeletal muscle.What we don't know about the structure of ryanodine receptor calcium release channels.Structure of glutaraldehyde cross-linked ryanodine receptorElevated nuclear Foxo1 suppresses excitability of skeletal muscle fibersStructural and functional properties of ryanodine receptor type 3 in zebrafish tail muscle.Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution.Type 3 ryanodine receptors of skeletal muscle are segregated in a parajunctional position.
P2860
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P2860
Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
1988年學術文章
@zh
1988年學術文章
@zh-hant
name
Structural evidence for direct ...... m junction in skeletal muscle.
@ast
Structural evidence for direct ...... m junction in skeletal muscle.
@en
type
label
Structural evidence for direct ...... m junction in skeletal muscle.
@ast
Structural evidence for direct ...... m junction in skeletal muscle.
@en
prefLabel
Structural evidence for direct ...... m junction in skeletal muscle.
@ast
Structural evidence for direct ...... m junction in skeletal muscle.
@en
P2093
P2860
P356
P1476
Structural evidence for direct ...... m junction in skeletal muscle.
@en
P2093
C Franzini-Armstrong
K P Campbell
P2860
P304
P356
10.1083/JCB.107.6.2587
P407
P433
P577
1988-12-01T00:00:00Z