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.
about
3D Mapping of the SPRY2 domain of ryanodine receptor 1 by single-particle cryo-EM.Myoplasmic resting Ca2+ regulation by ryanodine receptors is under the control of a novel Ca2+-binding region of the receptor.Calcium Dynamics Mediated by the Endoplasmic/Sarcoplasmic Reticulum and Related Diseases.Ryanodine receptors: structure, expression, molecular details, and function in calcium release.Structural mapping of divergent regions in the type 1 ryanodine receptor using fluorescence resonance energy transfer.Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle.Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interactionLocalization of a disease-associated mutation site in the three-dimensional structure of the cardiac muscle ryanodine receptorBidirectional signaling between calcium channels of skeletal muscle requires multiple direct and indirect interactions.Distinct Components of Retrograde Ca(V)1.1-RyR1 Coupling Revealed by a Lethal Mutation in RyR1.CLIC2-RyR1 interaction and structural characterization by cryo-electron microscopy.Allosterically coupled calcium and magnesium binding sites are unmasked by ryanodine receptor chimeras.The Central domain of RyR1 is the transducer for long-range allosteric gating of channel openingEvidence for conformational coupling between two calcium channels.Dominant and recessive RYR1 mutations in adults with core lesions and mild muscle symptoms.The structural biology of ryanodine receptors.Crystal structures of wild type and disease mutant forms of the ryanodine receptor SPRY2 domain.Effects of peptide C corresponding to the Glu724-Pro760 region of the II-III loop of the DHP (dihydropyridine) receptor alpha1 subunit on the domain- switch-mediated activation of RyR1 (ryanodine receptor 1) Ca2+ channels.Maurocalcine and domain A of the II-III loop of the dihydropyridine receptor Cav 1.1 subunit share common binding sites on the skeletal ryanodine receptor.Molecular cloning and characterization of a ryanodine receptor gene in brown planthopper (BPH), Nilaparvata lugens (Stål).Conformation-dependent stability of junctophilin 1 (JP1) and ryanodine receptor type 1 (RyR1) channel complex is mediated by their hyper-reactive thiols.Ryanodine receptor type 1 (RyR1) mutations C4958S and C4961S reveal excitation-coupled calcium entry (ECCE) is independent of sarcoplasmic reticulum store depletion.Ryanodine receptors
P2860
Q31037327-BAF180CC-2AFD-4B56-91D2-C2862B5D0E71Q33606502-2C78BEEF-75FF-4B2D-8F42-EF5E32EEBC89Q33755195-503E70E0-AFE1-4D58-BB3C-401ED423E6FDQ34024377-CF1C89C1-2EB7-4FB8-A1B1-9C107C1A5D90Q34143237-9CF75AC8-E740-4002-8525-8385872A4ED8Q34368667-415E4E4D-854F-463A-8E64-D372C76AF581Q34642130-7D65D8B4-DE2F-4DAB-8074-B69E72639C86Q34642817-6C8BC9DC-B8F6-4426-8220-E21D16173CD0Q35544373-2CFE33E4-EEE4-4B0F-86C2-17746246A0C1Q36644359-DD3B4067-002F-4AF4-A5E1-992A9AA19206Q37155574-668FBC85-B3D8-4C24-A94A-FB1B95B26325Q37219796-9DBAB546-7DB3-4209-9C3A-9F6FEF02C7C4Q37277612-3B49068E-F3AA-404E-9B40-7E798319F8A5Q37494384-0F72B9FF-9D6E-4BCE-871A-DFF1FB54FA6AQ37889772-97BB4897-A202-481B-B75C-C0B932DDB089Q37904888-D5BC28EA-6044-4299-8A2E-482ADDF99039Q41607050-F5A6BA2E-2687-406F-B3CA-E1A0AB574E4AQ41806986-B810B242-9D0D-433A-A4D6-89F5CADDC450Q42018621-74EF06BC-A44B-48EF-B4B1-C46D8BAC7CFDQ42611173-F265585B-65F4-40E8-AA13-D22F560DE6E1Q46192991-5195B52F-52E5-4A56-9412-941E8859B217Q46667699-AE73D1C4-58F6-436C-B626-2CAE05400B0EQ59270311-C5CB15F0-556C-4E2A-B915-BC7991971764
P2860
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.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Amino acids 1-1,680 of ryanodi ...... Role of divergence domain D2.
@en
Amino acids 1-1,680 of ryanodi ...... Role of divergence domain D2.
@nl
type
label
Amino acids 1-1,680 of ryanodi ...... Role of divergence domain D2.
@en
Amino acids 1-1,680 of ryanodi ...... Role of divergence domain D2.
@nl
prefLabel
Amino acids 1-1,680 of ryanodi ...... Role of divergence domain D2.
@en
Amino acids 1-1,680 of ryanodi ...... Role of divergence domain D2.
@nl
P2093
P2860
P356
P1476
Amino acids 1-1,680 of ryanodi ...... Role of divergence domain D2.
@en
P2093
Claudio F Perez
Paul D Allen
Santwana Mukherjee
P2860
P304
39644-39652
P356
10.1074/JBC.M305160200
P407
P577
2003-08-04T00:00:00Z