Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
about
Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated musclesObscurin targets ankyrin-B and protein phosphatase 2A to the cardiac M-lineNav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Nav1.5 on the surface of cardiomyocytesObscurin is a ligand for small ankyrin 1 in skeletal muscleIdentification and characterization of two ankyrin-B isoforms in mammalian heart.Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal musclesRegulatory polymorphisms in the bovine Ankyrin 1 gene promoter are associated with tenderness and intramuscular fat contentThe hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin.Effects of streptozotocin-induced diabetes and physical training on gene expression of titin-based stretch-sensing complexes in mouse striated muscle.Exon organization and novel alternative splicing of the human ANK2 gene: implications for cardiac function and human cardiac diseaseExon organization and novel alternative splicing of Ank3 in mouse heartObscurin is required for ankyrinB-dependent dystrophin localization and sarcolemma integrity.Mechanisms of human arrhythmia syndromes: abnormal cardiac macromolecular interactions.Molecular evolution of ankyrin: gain of function in vertebrates by acquisition of an obscurin/titin-binding-related domain.Interactions between small ankyrin 1 and sarcolipin coordinately regulate activity of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA1).
P2860
Q24292672-F8F4E6AD-0389-4090-A19A-622CA8335323Q24311794-121A4106-9CF2-4541-9A4E-A6EA962C6694Q24319636-AF9B5B98-7F53-422C-AF83-4D9F71F6410AQ24554297-3E1AE36D-2475-403C-970E-BE771D9A1A93Q27302084-09FFE2B6-3C2A-4AF3-B5F3-E48E10010710Q28513853-6C022FE3-4C30-4310-A7FD-1C12AF160E63Q33772283-378500D5-9842-4C96-92C6-620497CDB29BQ34160104-6A52ED3E-BB75-4190-AE1B-4E8AA846921EQ34569151-F78FFB27-9B45-4F0F-BA54-BE9A3D01865BQ34827043-0BADF10F-DE1B-41D1-BA8C-A942A49B6CE2Q35665600-A8E3DD92-7D86-4D9A-8ADC-231A5D628D59Q36618905-7A540CEA-8C42-4F37-9066-C4F9CD2A338EQ36967654-197F2424-6181-4EC9-90C3-DCA28CA142E7Q39268979-05A22B15-69AE-4F61-82A8-A8B9DDACAD0BQ51012051-C79A540E-ADA0-4481-95D7-CB8536934350
P2860
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
@en
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
@nl
type
label
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
@en
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
@nl
prefLabel
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
@en
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
@nl
P2093
P2860
P356
P1476
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
@en
P2093
Christian Cognard
Christiane Deprette
Claire Gagelin
Ekaterini Kordeli
Guy Raymond
Jean Cartaud
Marie-Aline Ludosky
Michel Recouvreur
P2860
P304
12978-12987
P356
10.1074/JBC.M111299200
P407
P577
2002-01-16T00:00:00Z