Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling.
about
Junctin - the quiet achieverMalignant hyperthermia: a reviewPharmGKB summary: very important pharmacogene information for RYR1Review of RyR1 pathway and associated pathomechanismsAltered expression of triadin 95 causes parallel changes in localized Ca2+ release events and global Ca2+ signals in skeletal muscle cells in cultureThe excitation-contraction coupling mechanism in skeletal muscle.Ablation of skeletal muscle triadin impairs FKBP12/RyR1 channel interactions essential for maintaining resting cytoplasmic Ca2+A skeletal muscle ryanodine receptor interaction domain in triadinMonovalent cationic channel activity in the inner membrane of nuclei from skeletal muscle fibers.Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interactionMalignant hyperthermia: a pharmacogenetic disorder.The elusive role of the SPRY2 domain in RyR1.A new cytoplasmic interaction between junctin and ryanodine receptor Ca2+ release channels.On the footsteps of Triadin and its role in skeletal muscleRegions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunitAltered stored calcium release in skeletal myotubes deficient of triadin and junctin.Assembly and dynamics of proteins of the longitudinal and junctional sarcoplasmic reticulum in skeletal muscle cellsJunctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin.Triadin: what possible function 20 years later?Triadin, not essential, but useful.A chemical chaperone improves muscle function in mice with a RyR1 mutation.Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Proteins within the intracellular calcium store determine cardiac RyR channel activity and cardiac output.Regulation of RYR2 by sarcoplasmic reticulum Ca(2+).Characterization of Ca(2+)-Dependent Protein-Protein Interactions within the Ca(2+) Release Units of Cardiac Sarcoplasmic Reticulum.Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Calsequestrin interacts directly with the cardiac ryanodine receptor luminal domain.RYR1-Related Myopathies: Clinical, Histopathologic and Genetic Heterogeneity Among 17 Patients from a Portuguese Tertiary Centre.Core skeletal muscle ryanodine receptor calcium release complex.Silencing genes of sarcoplasmic reticulum proteins clarifies their roles in excitation-contraction coupling.Observation of the molecular organization of calcium release sites in fast- and slow-twitch skeletal muscle with nanoscale imagingInteraction of ions with the luminal sides of wild-type and mutated skeletal muscle ryanodine receptors.The structural basis of ryanodine receptor ion channel function.Ryanodine receptors
P2860
Q24309384-05298919-A457-4E1D-AF9D-0B6761283390Q26799652-BBBBE4AA-D8AA-47AD-936B-86A3FE3D90DCQ28074804-4252FBBF-52F3-45C1-B997-19381D5399B1Q28078420-F14792E4-172B-413D-88FA-9C9464CD8CB1Q28578879-965B864C-3D5B-4E00-BCB8-7EF5262E21CFQ33659321-6AF54BB4-7628-45CB-A379-CD50B452E5BEQ34352263-E20114CB-D709-406A-836D-05A480964A18Q34399431-D9EBFF40-8FAA-48FB-A1F2-1319767FD127Q34467099-77617A39-ED7D-4305-A59D-967F43417675Q34642130-31165BA6-F266-4FE1-934E-B83356906DD0Q34883560-038DCC58-A1F4-42F6-9E55-EED7C75B6A8FQ35079050-2D648D38-72A5-4332-B454-574F4C23E8CBQ35126961-9EDF611C-B1CE-4D10-9EFB-97AC3F732939Q35193342-11B52227-FE9D-4140-B217-DE2660C41A13Q35878200-3E3E48DF-3838-41C7-8487-AACB919D651BQ37060519-35720B66-C4E5-4271-BCEE-7BD1BEF9FF20Q37140160-82B1187A-5B25-4B8B-8212-199C2D34B0B0Q37422708-F5C2F4D5-E9F9-4E31-962B-F915A840E818Q37464481-AC4AB9B9-0973-4D35-B253-B890F22591B3Q37536611-6F978317-BD39-4F7E-A7A0-E02C537C5EDFQ37733865-D405A06D-D028-4450-A67C-8B0F3B8D8191Q37945102-245384CD-E043-45EA-8170-1D44FAEEB66AQ38004648-9B7D0D23-EB1F-48A8-B2E3-F1F7F6109325Q38325324-05099699-B18A-4232-923A-C6C9400ACDA4Q38541159-9895CA0B-3579-454B-877C-4175C66B5870Q38587629-5E5381FB-B3B9-4069-A94A-614E1C83B2E9Q38734361-564F4715-0FEF-4FD4-8C08-169941C4C09FQ38749268-CAD4A848-9F73-4A3D-BEFE-FEB130805608Q38970694-DFD514F5-E0D9-4262-932A-39738C1F3D99Q39830880-D108163E-3B5B-4EB5-842A-F26CD1E79F29Q41778232-996E14FB-53E4-48CB-A884-9494C831F049Q46609010-EC4DF7FA-72C8-4BBD-876D-B2D898E819BAQ47419234-E4E023DB-233D-46EE-9389-F9AE81B50A5CQ59270311-39D9BF7C-6809-4587-A794-8C9F2EC35280
P2860
Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Triadin binding to the C-termi ...... citation contraction coupling.
@ast
Triadin binding to the C-termi ...... citation contraction coupling.
@en
type
label
Triadin binding to the C-termi ...... citation contraction coupling.
@ast
Triadin binding to the C-termi ...... citation contraction coupling.
@en
prefLabel
Triadin binding to the C-termi ...... citation contraction coupling.
@ast
Triadin binding to the C-termi ...... citation contraction coupling.
@en
P2093
P2860
P356
P1476
Triadin binding to the C-termi ...... citation contraction coupling.
@en
P2093
Alla D Lyfenko
Andrew Rosenfeld
Angela F Dulhunty
Isabelle Marty
Linda Groom
Nicole A Beard
Robert T Dirksen
Sanjeewa A Goonasekera
Takashi Kimura
P2860
P304
P356
10.1085/JGP.200709790
P577
2007-09-10T00:00:00Z