Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
about
Regulation of the cardiac muscle ryanodine receptor by glutathione transferasesCharacterization of the molecular architecture of human caveolin-3 and interaction with the skeletal muscle ryanodine receptorSingle-Particle Cryo-EM of the Ryanodine Receptor Channel in an Aqueous EnvironmentCoordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gatingDisease mutations in the ryanodine receptor N-terminal region couple to a mobile intersubunit interfaceStructural Basis for Gating and Activation of RyR1.Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptorSubnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channelCatecholaminergic polymorphic ventricular tachycardia is caused by mutation-linked defective conformational regulation of the ryanodine receptor.Structure of glutaraldehyde cross-linked ryanodine receptorImaging single cardiac ryanodine receptor Ca2+ fluxes in lipid bilayers.Interdomain interactions within ryanodine receptors regulate Ca2+ spark frequency in skeletal muscle.Localization of an NH(2)-terminal disease-causing mutation hot spot to the "clamp" region in the three-dimensional structure of the cardiac ryanodine receptor.Calcium transport across the sarcoplasmic reticulum: structure and function of Ca2+-ATPase and the ryanodine receptor.Ryanodine receptors: structure, expression, molecular details, and function in calcium release.Structure of the voltage-gated L-type Ca2+ channel by electron cryomicroscopyThree-dimensional structure of the type 1 inositol 1,4,5-trisphosphate receptor at 24 A resolution.Structural mapping of divergent regions in the type 1 ryanodine receptor using fluorescence resonance energy transfer.The skeletal muscle Ca2+ release channel has an oxidoreductase-like domainStructure of Ca2+ release channel at 14 A resolution.The pore structure of the closed RyR1 channel.Modulation of the oligomerization of isolated ryanodine receptors by their functional statesThree-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptorCalcium and arrhythmogenesis.Single-particle cryo-EM of the ryanodine receptor channel in an aqueous environment.Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminusEvolution of skeletal type e-c coupling: a novel means of controlling calcium delivery.Identification of ATP-binding regions in the RyR1 Ca²⁺ release channel.Ligand-dependent conformational changes in the clamp region of the cardiac ryanodine receptor.CLIC2-RyR1 interaction and structural characterization by cryo-electron microscopy.Ryanodine receptor-mediated arrhythmias and sudden cardiac death.Structural insights into Ca(2+)-activated long-range allosteric channel gating of RyR1.Ryanodine receptor structure: progress and challenges.Sarcoplasmic reticulum function in smooth muscle.The structural biology of ryanodine receptors.Calcium signaling in cardiac myocytes.ARVC-related mutations in divergent region 3 alter functional properties of the cardiac ryanodine receptor.All three ryanodine receptor isoforms generate rapid cooling responses in muscle cells.Three-dimensional localization of divergent region 3 of the ryanodine receptor to the clamp-shaped structures adjacent to the FKBP binding sites.The N-Terminal Region of the Ryanodine Receptor Affects Channel Activation.
P2860
Q24293209-3CAD4071-2E85-4F45-B7A1-8F2CD24D9238Q24608212-7B791120-7556-41EE-8558-D32DD8B2131CQ26766455-A5013598-FDBA-465A-B626-8AAE2AE14078Q27331094-1DC03237-B974-4659-847F-1B8DB1A0AD30Q27676474-51C6A54E-52E8-4987-A0A5-3CEDDEB848AEQ27728108-0B11783F-2DE0-41D6-8678-7F6E16138DF9Q28589538-0BE2A179-F330-4CE6-9165-ECA7FB6A3A85Q30482731-2F73498B-70D9-48A2-A3DC-3E3C5A1D90B8Q30494293-AB04859C-F812-4F55-ADC3-E36377763EF7Q30537162-F97FEB91-3928-4F3F-9260-E2A138D7AF9EQ31034373-A1646F08-8DDD-4340-9897-8DDB709A7CC5Q32054796-10279127-F0DF-4788-B069-1D4108F5C42EQ33565617-AD06E648-80AB-4B63-8563-FC6DF919BD3DQ34010108-A07E66F5-8461-4DA0-A141-3FFB717883CEQ34024377-5A8EC0E5-7F47-4944-9E5C-DF26F75B7FEBQ34074422-FF5B3728-7B13-426F-8971-80978C70B664Q34089878-ADA15DC8-F841-4994-9B9D-EF9B106864B6Q34143237-33524911-3F2A-459E-8A3A-DE9AAD7509AAQ34155483-7875EE3F-0DF1-4055-A65F-0BCE542FE321Q34298694-F2A093E2-213D-492D-A478-40AA2F73F0A3Q34318156-B3EBF403-B42A-49CB-BBA9-0A772C59F120Q34351078-3DA8C354-422F-49CA-BE20-BB381DC6A700Q34352742-36DA1AFB-19AE-46FC-93C0-ADE3A48B3930Q35095089-F2F3718B-5177-4ADD-8655-ED28C5D1D9C1Q35239728-84F9E18A-E9B0-40A4-A533-3AB99F639F60Q35930374-41A235BB-542D-44DF-8A3B-21546E93EDA9Q36321062-6BDAC49B-A5BA-45E6-94C9-9C502155AFDEQ36381016-68BACBFD-024D-4927-A63D-13766C19E6EFQ36596227-D71F2A55-DAAD-4648-934A-E399017B3276Q37155574-95D235AF-DBCD-4B92-87D8-2C22F12AB3BBQ37248371-2F68817E-C2EF-412C-B6C9-86A9EE849DB3Q37277630-3E5F0D43-57A3-4BF8-94CA-3DF387B4F0AFQ37300766-07B9DB9D-0A05-449E-9EA5-008BF2782CEAQ37677917-62C53B50-7CFC-4C2A-A1ED-5C08F01BC927Q37904888-F15B2748-8A4C-4286-9703-33EF69C2BD0EQ37923638-A17533FD-0213-47ED-A958-D57C3F15FC72Q38630423-25927CF4-A7F4-44AE-BB9D-8F430042DF3FQ40621036-5E9F045F-BB82-4F1D-B735-E9E527ED9521Q40671727-2A060AFC-7AE9-402A-B112-5386D866831FQ40995486-49FA5213-D14D-4668-929B-F431EFB12F01
P2860
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@ast
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@en
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@nl
type
label
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@ast
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@en
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@nl
prefLabel
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@ast
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@en
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@nl
P2093
P2860
P1433
P1476
Structure of the skeletal muscle calcium release channel activated with Ca2+ and AMP-PCP.
@en
P2093
I I Serysheva
M van Heel
S L Hamilton
P2860
P304
P356
10.1016/S0006-3495(99)77035-9
P407
P577
1999-10-01T00:00:00Z