Cryoelectron microscopy resolves FK506-binding protein sites on the skeletal muscle ryanodine receptor.
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Further characterization of the type 3 ryanodine receptor (RyR3) purified from rabbit diaphragmIn situ modulation of the human cardiac ryanodine receptor (hRyR2) by FKBP12.6Single-Particle Cryo-EM of the Ryanodine Receptor Channel in an Aqueous EnvironmentCoordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gatingThree-dimensional reconstruction of the recombinant type 2 ryanodine receptor and localization of its divergent region 1Structure of glutaraldehyde cross-linked ryanodine receptorCryoelectron microscopy and image analysis of the cardiac ryanodine receptor.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.Subconductance states in single-channel activity of skeletal muscle ryanodine receptors after removal of FKBP12Ryanodine receptors: structure, expression, molecular details, and function in calcium release.The conserved sites for the FK506-binding proteins in ryanodine receptors and inositol 1,4,5-trisphosphate receptors are structurally and functionally different.Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12.Evidence for a role of the lumenal M3-M4 loop in skeletal muscle Ca(2+) release channel (ryanodine receptor) activity and conductance.Three-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptorSingle-particle cryo-EM of the ryanodine receptor channel in an aqueous environment.Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM.Caffeine-induced release of intracellular Ca2+ from Chinese hamster ovary cells expressing skeletal muscle ryanodine receptor. Effects on full-length and carboxyl-terminal portion of Ca2+ release channelsN-terminal and central segments of the type 1 ryanodine receptor mediate its interaction with FK506-binding proteinsThe structural biology of ryanodine receptors.The ryanodine receptor provides high throughput Ca2+-release but is precisely regulated by networks of associated proteins: a focus on proteins relevant to phosphorylation.Structures of the colossal RyR1 calcium release channel.Three-dimensional localization of divergent region 3 of the ryanodine receptor to the clamp-shaped structures adjacent to the FKBP binding sites.Mutation of divergent region 1 alters caffeine and Ca(2+) sensitivity of the skeletal muscle Ca(2+) release channel (ryanodine receptor).The role of FK506-binding proteins 12 and 12.6 in regulating cardiac function.Augmentation of SR Ca(2+) release by rapamycin and FK506 causes K(+)-channel activation and membrane hyperpolarization in bladder smooth muscle.Selectively suppressed Ca2+-induced Ca2+ release activity of alpha-ryanodine receptor (alpha-RyR) in frog skeletal muscle sarcoplasmic reticulum: potential distinct modes in Ca2+ release between alpha- and beta-RyR.Mechanisms of reduced SR Ca(2+) release induced by inorganic phosphate in rat skeletal muscle fibers.N-terminal region of FKBP12 is essential for binding to the skeletal ryanodine receptor.Acetaldehyde alters Ca2+-release channel gating and muscle contraction in a dose-dependent manner.Expression of FKBP12 and ryanodine receptors (RyRs) in the spinal cord of MND patients.The structural basis of ryanodine receptor ion channel function.Effects of ivermectin and midecamycin on ryanodine receptors and the Ca2+-ATPase in sarcoplasmic reticulum of rabbit and rat skeletal muscle.
P2860
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P2860
Cryoelectron microscopy resolves FK506-binding protein sites on the skeletal muscle ryanodine receptor.
description
1996 nî lūn-bûn
@nan
1996 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@ast
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@en
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@nl
type
label
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@ast
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@en
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@nl
prefLabel
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@ast
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@en
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@nl
P2093
P2860
P1433
P1476
Cryoelectron microscopy resolv ...... tal muscle ryanodine receptor.
@en
P2093
G J Wiederrecht
J Berkowitz
R Grassucci
S Fleischer
T Wagenknecht
P2860
P304
P356
10.1016/S0006-3495(96)79733-3
P407
P577
1996-04-01T00:00:00Z