Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
about
Multiple regions of RyR1 mediate functional and structural interactions with alpha(1S)-dihydropyridine receptors in skeletal muscle3D Structure of the Dihydropyridine Receptor of Skeletal MuscleCa(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channelFrog alpha- and beta-ryanodine receptors provide distinct intracellular Ca2+ signals in a myogenic cell lineTwo domains in dihydropyridine receptor activate the skeletal muscle Ca(2+) release channel.Type 1 and type 3 ryanodine receptors generate different Ca(2+) release event activity in both intact and permeabilized myotubes.Minding the calcium store: Ryanodine receptor activation as a convergent mechanism of PCB toxicityReorganized 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.Relationship between L-type Ca2+ current and unitary sarcoplasmic reticulum Ca2+ release events in rat ventricular myocytes.Expression of ryanodine receptor RyR3 produces Ca2+ sparks in dyspedic myotubes.Functional expression of transgenic 1sDHPR channels in adult mammalian skeletal muscle fibres.RyR1-mediated Ca2+ leak and Ca2+ entry determine resting intracellular Ca2+ in skeletal myotubes.Ryanodine receptors: structure, expression, molecular details, and function in calcium release.The beta 1a subunit is essential for the assembly of dihydropyridine-receptor arrays in skeletal muscle.RYR1 and RYR3 have different roles in the assembly of calcium release units of skeletal muscle.Divergent functional properties of ryanodine receptor types 1 and 3 expressed in a myogenic cell line.Ca2+ activation of RyR1 is not necessary for the initiation of skeletal-type excitation-contraction coupling.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 couplingCa2+ current and charge movements in skeletal myotubes promoted by the beta-subunit of the dihydropyridine receptor in the absence of ryanodine receptor type 1.Location of ryanodine and dihydropyridine receptors in frog myocardiumOrganization of Ca2+ release units in excitable smooth muscle of the guinea-pig urinary bladderMultiple loops of the dihydropyridine receptor pore subunit are required for full-scale excitation-contraction coupling in skeletal muscle.Ryanodine receptor point mutant E4032A reveals an allosteric interaction with ryanodine.Thyroid hormones differentially regulate the distribution of rabbit skeletal muscle Ca(2+)-ATPase (SERCA) isoforms in light and heavy sarcoplasmic reticulum.Amino 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 receptorOrthograde dihydropyridine receptor signal regulates ryanodine receptor passive leakStac adaptor proteins regulate trafficking and function of muscle and neuronal L-type Ca2+ channelsDifferential effect of calsequestrin ablation on structure and function of fast and slow skeletal muscle fibers.Mice expressing T4826I-RYR1 are viable but exhibit sex- and genotype-dependent susceptibility to malignant hyperthermia and muscle damageComparative Transcriptomic Study of Muscle Provides New Insights into the Growth Superiority of a Novel Grouper Hybrid.A transgenic myogenic cell line lacking ryanodine receptor protein for homologous expression studies: reconstitution of Ry1R protein and function.Accessibility of targeted DHPR sites to streptavidin and functional effects of binding on EC coupling.Fluorescence 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.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.The Central domain of RyR1 is the transducer for long-range allosteric gating of channel openingDifferential contribution of skeletal and cardiac II-III loop sequences to the assembly of dihydropyridine-receptor arrays in skeletal muscle.Core skeletal muscle ryanodine receptor calcium release complex.
P2860
Q24537576-130B9A2D-3C66-49BA-AEC0-1466B787B32DQ26766447-E1FF262B-B696-4D19-8583-27C190EE9057Q26866428-11533ED1-8B1B-4A35-A4A9-0E5EFD8040F2Q27323938-721BCD81-1FEA-432F-A513-593E4C819D06Q28346157-A59D2538-5BBB-42A8-95C8-AC3D3D23C491Q28365115-F2254C79-76B1-4C1A-BFC7-0BEC7FE7B278Q28393648-1984AD0A-A506-4593-A905-59B0274BE9CAQ28589478-B17D5B19-948A-4697-A7A7-5F2E9A5DFC8AQ30621019-639D0CD1-8A55-4ADE-8DBE-6D870D3BD343Q30653247-A188B274-F8B6-4632-A717-FFF125BA97C4Q30870690-1C3E13EE-5C1E-44B6-A4E2-7592F116E94FQ33801924-62CA3036-E712-4969-BCF8-4AF4F8B57D52Q33810099-AC8856C4-A48C-42ED-9D55-46191C90ED08Q34024377-352F9182-0856-4036-A730-53343C8DD58AQ34144818-B2280F48-76FA-4E35-B7DD-B041091F8216Q34174273-4FB20898-4C6B-4499-82E7-753FC330B3B2Q34174280-328903E8-120A-4391-AEC1-EEC66C25E7F3Q34177806-F157E98A-96BB-4E3C-A00E-85FC15E757DFQ34178117-37E1EC7C-9688-409A-B947-0DB58EEBBBD1Q34179200-9D0D1FBE-7345-476F-AC6D-317C9D64E3EFQ34180386-E9543ED4-83AB-44A9-9453-879EF9D4BFB6Q34180431-6D05FD83-EE20-4945-9BF0-96D0862831C5Q34187097-DCAD0F8C-D375-4C38-A980-EE0A0139E85DQ34350397-7D13130D-A161-408D-BF79-FB3111BB3577Q34501318-ACB8A872-A1B8-4046-84B8-BCD40784A973Q34651458-181EA1BC-082B-4243-AA94-EA99C645482FQ34774544-F9A1399C-77DF-4CFC-BB63-B2C6DB722B23Q34880821-F6964A83-90C9-4996-98C0-FFA3381948B6Q34985729-95EA7478-5EBF-4753-92E7-6E06B4AFF95DQ35214748-96F89B48-8B1F-4C90-B7C8-2B9315417E2EQ35787753-3FFBA088-A0A0-42CC-8719-217D8CEA6A55Q36231521-0AD6EA6A-7040-41C0-A356-301A5989993FQ36276697-6CBB074C-F5AB-4B67-B465-631311CACAAAQ36296090-3F9BE3ED-94AF-495A-B260-CEE89BD781C7Q36436167-7BDDFF5D-08C7-4B0E-BD84-49808FA56331Q36510485-AFC7ED83-F7A2-4F55-9DA1-C61350EAF44BQ37267658-D16A5571-F4F5-42EF-8B6F-50C14B6E7C29Q37277612-FD6F7947-1B9E-4AC4-BE82-F1F4C45E808AQ37657281-B768F68C-7E4C-4A4E-BE4C-4EBB4B01C0EAQ38970694-CA710486-C1D1-4DAB-A5EC-224CEB86732C
P2860
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
@ast
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
@en
type
label
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
@ast
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
@en
prefLabel
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
@ast
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
@en
P2093
P2860
P356
P1476
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
@en
P2093
C Franzini-Armstrong
P2860
P304
P356
10.1083/JCB.140.4.831
P407
P577
1998-02-01T00:00:00Z