Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium.
about
Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulumOn the role of junctin in cardiac Ca2+ handling, contractility, and heart failureHistidine-rich Ca-binding protein interacts with sarcoplasmic reticulum Ca-ATPaseAbsence of triadin, a protein of the calcium release complex, is responsible for cardiac arrhythmia with sudden death in humanProtein protein interactions between triadin and calsequestrin are involved in modulation of sarcoplasmic reticulum calcium release in cardiac myocytesThe role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium.Triadin regulation of the ryanodine receptor complexCardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1Calsequestrin mutations and catecholaminergic polymorphic ventricular tachycardiaAblation of triadin causes loss of cardiac Ca2+ release units, impaired excitation-contraction coupling, and cardiac arrhythmiashnRNP U protein is required for normal pre-mRNA splicing and postnatal heart development and functionTrisk 32 regulates IP(3) receptors in rat skeletal myoblastsCloning and characterization of a new isoform of skeletal muscle triadinTriadin (Trisk 95) overexpression blocks excitation-contraction coupling in rat skeletal myotubesCasq2 deletion causes sarcoplasmic reticulum volume increase, premature Ca2+ release, and catecholaminergic polymorphic ventricular tachycardiaNew Family With Catecholaminergic Polymorphic Ventricular Tachycardia Linked to the Triadin Gene.Dysregulated sarcoplasmic reticulum calcium release: potential pharmacological target in cardiac disease.Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction.Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.Triadin/Junctin double null mouse reveals a differential role for Triadin and Junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis.A skeletal muscle ryanodine receptor interaction domain in triadinCardiac function is regulated by B56α-mediated targeting of protein phosphatase 2A (PP2A) to contractile relevant substrates.Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interactionOn the footsteps of Triadin and its role in skeletal muscleTransitions of protein traffic from cardiac ER to junctional SRImpaired calcium-calmodulin-dependent inactivation of Cav1.2 contributes to loss of sarcoplasmic reticulum calcium release refractoriness in mice lacking calsequestrin 2.Calsequestrin accumulation in rough endoplasmic reticulum promotes perinuclear Ca2+ releaseTriadin regulates cardiac muscle couplon structure and microdomain Ca(2+) signalling: a path towards ventricular arrhythmias.Altered stored calcium release in skeletal myotubes deficient of triadin and junctin.Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin.Triadin deletion induces impaired skeletal muscle functionTriadin: what possible function 20 years later?New roles of calsequestrin and triadin in cardiac muscle.Triadin, not essential, but useful.Sarcoplasmic reticulum function in smooth muscle.Microarchitecture of the dyad.Modeling CICR in rat ventricular myocytes: voltage clamp studies.Mass spectrometry of cardiac calsequestrin characterizes microheterogeneity unique to heart and indicative of complex intracellular transit.Triadins are not triad-specific proteins: two new skeletal muscle triadins possibly involved in the architecture of sarcoplasmic reticulumModulation of SR Ca2+ release by the triadin-to-calsequestrin ratio in ventricular myocytes.
P2860
Q24291561-0FD1395F-FE9D-49C1-9187-0F0D2ABC39C0Q24301449-6F36494B-C3E2-4A49-AA6B-40E033803719Q24307062-6CDB789F-2920-4323-BF4B-45CC21EAADD9Q24307681-49D6D1B4-2163-49CF-B377-CBB1523B45AFQ24310819-4EBB98AD-375D-406A-A44A-A19283BDC5B5Q24319842-337FE429-489C-4D23-8F42-611FD7152A16Q26801317-84453887-EFFC-4F9B-8194-DCBF4003325CQ28143329-42D4B956-6EF8-4622-A8B3-877214878AA4Q28262015-80E46921-36AF-4144-B0AD-EA6A26052434Q28511129-569CDC04-A806-463E-963F-E19D4330DE81Q28513728-AF6468E3-EB44-4EF7-82F0-05E0C2548E27Q28571894-A8629BD6-9955-46C7-B353-B51D1FA22784Q28575170-4CFD8812-D907-45D8-BE7E-B973922B25E6Q28576225-3F015CA9-F7EE-431C-A5E1-AEC209B7BA4CQ28589230-EA952E70-9252-45AC-8E0F-17776D06A087Q30982059-91696EC8-75AA-471D-A387-E0B93CCE9AC7Q33559348-92959887-36BA-4BB3-8128-59054443E7E4Q33896739-56433415-10D8-43F8-B7BE-9C2EC602F6F0Q34279088-19B3C878-94EC-4167-BE13-658A434A50DEQ34329037-12EF92FE-42E8-4340-BC92-C62AB425117EQ34399431-4452FACF-4E80-41F1-8E91-7A5F1E39368FQ34634141-4906FAAE-5DE0-41B3-BF58-BE2944792A9DQ34642130-6BA6D2B3-5B80-43E2-9A1B-1F8A947A76EFQ35193342-EBD1E070-B7F0-4065-86D6-9BD3372E3BC3Q35386157-39252135-4AAA-4361-B2F4-34DF13D96B0BQ35514666-7F10553D-4EF0-4C51-97EE-BBCFCC700ECDQ35956759-1610762D-C4A5-4FF0-8430-3B53DA5A9D2BQ36786528-D7830B78-EF90-4876-938B-53ED9D4AC41EQ37060519-4BF2E592-E2C8-4957-A55D-B9F2E8539EC2Q37422708-73B3689A-5056-469E-BBA4-1ECC7DE31077Q37454303-1663008C-BB82-496F-916B-28995ACE5508Q37464481-E8CA3007-C23F-4D93-91A6-1EDF23B13893Q37487250-FF8897DE-5081-45D5-829E-C9DF5992FAEDQ37536611-9C6569CF-3751-4E96-9A06-0F2E4BD5B33FQ37677917-0D337229-AD4D-4ADD-BC86-051198D31F22Q38080767-FACB3351-DB22-4D44-94EA-A67815FE24CBQ39981612-27BDD325-8069-4E0D-B4B7-66065949FE63Q40714615-EB20F8AB-CA16-4F14-8651-6C471C01B549Q41975814-030A5DCF-D291-47A8-BBC9-73B9EBC7F37CQ42503629-281D29BE-41F3-4F46-B527-85201C06142D
P2860
Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium.
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
Identification of triadin 1 as ...... essed in mammalian myocardium.
@ast
Identification of triadin 1 as ...... essed in mammalian myocardium.
@en
type
label
Identification of triadin 1 as ...... essed in mammalian myocardium.
@ast
Identification of triadin 1 as ...... essed in mammalian myocardium.
@en
prefLabel
Identification of triadin 1 as ...... essed in mammalian myocardium.
@ast
Identification of triadin 1 as ...... essed in mammalian myocardium.
@en
P2860
P356
P1476
Identification of triadin 1 as ...... essed in mammalian myocardium.
@en
P2093
Kobayashi YM
P2860
P304
28660-28668
P356
10.1074/JBC.274.40.28660
P407
P577
1999-10-01T00:00:00Z