hERG potassium channel gating is mediated by N- and C-terminal region interactions - Wikidata - awgldk - TriplyDB

hERG potassium channel gating is mediated by N- and C-terminal region interactions

hERG potassium channel gating is mediated by N- and C-terminal region interactions

http://www.wikidata.org/entity/Q34618908

about

Insight into the molecular interaction between the cyclic nucleotide-binding homology domain and the eag domain of the hERG channel Rescue of aberrant gating by a genetically encoded PAS (Per-Arnt-Sim) domain in several long QT syndrome mutant human ether-á-go-go-related gene potassium channels Structure of the carboxy-terminal region of a KCNH channel The S4–S5 Linker Acts as a Signal Integrator for hERG K+ Channel Activation and Deactivation Gating Structure of the C-terminal region of an ERG channel and functional implications Molecular Insights into the Mechanism of Calmodulin Inhibition of the EAG1 Potassium Channel Calmodulin Regulates Human Ether à Go-Go 1 (hEAG1) Potassium Channels through Interactions of the Eag Domain with the Cyclic Nucleotide Binding Homology Domain Molecular Cloning and Functional Expression of the Equine K+ Channel KV11.1 (Ether à Go-Go-Related/KCNH2 Gene) and the Regulatory Subunit KCNE2 from Equine Myocardium The subfamily-specific assembly of Eag and Erg K+ channels is determined by both the amino and the carboxyl recognition domains Molecular determinants of interactions between the N-terminal domain and the transmembrane core that modulate hERG K+ channel gating.An Interdomain KCNH2 Mutation Produces an Intermediate Long QT Syndrome Role of the cytoplasmic N-terminal Cap and Per-Arnt-Sim (PAS) domain in trafficking and stabilization of Kv11.1 channels.Concerted all-or-none subunit interactions mediate slow deactivation of human ether-à-go-go-related gene K+ channels Multiple interactions between cytoplasmic domains regulate slow deactivation of Kv11.1 channels.The Eag domain regulates the voltage-dependent inactivation of rat Eag1 K+ channels.The subfamily-specific interaction between Kv2.1 and Kv6.4 subunits is determined by interactions between the N- and C-termini.hERG1a N-terminal eag domain-containing polypeptides regulate homomeric hERG1b and heteromeric hERG1a/hERG1b channels: a possible mechanism for long QT syndrome.C-Linker Accounts for Differential Sensitivity of ERG1 and ERG2 K+ Channels to RPR260243-Induced Slow Deactivation.Cellular context and multiple channel domains determine cAMP sensitivity of HCN4 channels: ligand-independent relief of autoinhibition in HCN4.The eag domain regulates hERG channel inactivation gating via a direct interaction.Interactions between hERG and KCNQ1 α-subunits are mediated by their COOH termini and modulated by cAMP.Two structural components in CNGA3 support regulation of cone CNG channels by phosphoinositides.CNGA3 achromatopsia-associated mutation potentiates the phosphoinositide sensitivity of cone photoreceptor CNG channels by altering intersubunit interactions Crystal structure of the PAS domain of the hEAG potassium channel Domain-domain interactions in ion channels.Direct interaction of eag domains and cyclic nucleotide-binding homology domains regulate deactivation gating in hERG channels.A functional Kv1.2-hERG chimaeric channel expressed in Pichia pastoris Allocryptopine and benzyltetrahydropalmatine block hERG potassium channels expressed in HEK293 cells Pharmaceutical regulation of telomerase and its clinical potential Cytoplasmic domains and voltage-dependent potassium channel gating.HERG potassium channel regulation by the N-terminal eag domain.Insights into hERG K+ channel structure and function from NMR studies.Voltage-dependent gating of HERG potassium channels.The enigmatic cytoplasmic regions of KCNH channels.Getting to the heart of hERG K(+) channel gating.Molecular Basis of Cardiac Delayed Rectifier Potassium Channel Function and Pharmacology.Eag Domains Regulate LQT Mutant hERG Channels in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes Large-scale mutational analysis of Kv11.1 reveals molecular insights into type 2 long QT syndrome.Eag1 Voltage-Dependent Potassium Channels: Structure, Electrophysiological Characteristics, and Function in Cancer.The electric heart of hERG.

P2860

Q24299208-68A60D0B-05B2-4E7C-82C0-9393E543BF68 Q24301043-41E63423-B231-44AF-8502-E439B59CA4E6 Q27676656-831EFADA-39A4-4EFF-8D4B-434552A5CAEB Q27677437-B2C45788-8A61-4F5D-A39F-E3498C28CF67 Q27678809-E2A9B921-3F23-4993-A87A-9744E62C5DD5 Q27728045-00242D06-E0BF-44D2-BD0C-616229C3525D Q28119193-56525AF2-ADD5-477B-8A67-60A664F5A723 Q28548072-02E5176C-6E4D-4DBB-B971-52D4E95C2469 Q28568486-DADF92BE-DF8D-4C6E-BEF7-ED8DBD320B96 Q30474096-DB2FD845-7873-49D4-B618-67885F53D96B Q33165658-B14B2D49-A6F8-460F-8F2F-A7041ADD4C68 Q33619341-74D4E208-C606-4A36-A3F6-6AC3AD0CD7AC Q34141076-75626D11-9060-4FE4-878A-EC1A45EA227A Q34170800-731AA80D-1258-4535-90B5-3255C2AF2722 Q34379526-4BE7E8F1-6823-4F74-B0AB-50D2264B761E Q35182181-02EEC335-BF62-4665-8D8F-727DD71CE61E Q35581360-E091BF92-1CE7-495C-A97D-F3914B0A15AE Q35745902-AE00AD06-16B1-4CD4-8D70-E1E97B060F3E Q36353470-C6155256-69B8-4694-BE8D-AEE20B415528 Q36568494-45ECE25E-8576-4925-BE16-908A2B8FC840 Q36592986-E2D02CF5-E08C-4923-9236-A3DDDC413DA9 Q36715284-507B8567-CFB4-40B1-A17F-01917BB1DCC8 Q37051303-7C4F3FED-25CC-457A-9B03-F3C27A027B72 Q37151387-2CEC96BA-3A7F-401E-8B7C-A6AEED5745A3 Q37209181-F6272B19-3EBD-4E0E-8C2D-60F5D806CF57 Q37209213-23CBBC45-9AE6-452C-8C72-F1E457EADDDF Q37604013-7E4E7D07-E859-45B9-BD95-E6BFD5917221 Q37729074-822DC4F7-937E-4F61-BF58-86F56146E87A Q37942633-5DBF39C7-F151-4EBD-9D67-70D8E8E797A5 Q37999317-0D5E7C75-3750-4C38-B313-994302ACF0ED Q38004348-C4730D9A-3E44-4597-8A18-0F75BC9F2F9F Q38007114-5D1FD8F3-2582-4C8D-BA0B-A7725E01F159 Q38010173-DF26DB56-559D-4DDA-A5D5-26FACAD37B0E Q38243381-38EFF256-2D8A-4D64-9CCC-1113F93AC138 Q38395148-03B559FD-B8C1-46CC-BD4F-6983FAFA2FE1 Q38854244-88CFCD5A-4A1E-4E01-BE2F-5E1769BCA04B Q38881012-139EFDFF-6359-43E6-BD76-F66C50187F1B Q38938416-F70C7D8D-B341-4C88-986E-902C3B9C6BAB Q39119019-2894F49C-DD6C-44BB-BAD7-4F8ADB00F687 Q39286265-00361F46-D0B1-4D46-AA0A-794D9A987546

P2860

hERG potassium channel gating is mediated by N- and C-terminal region interactions

http://www.wikidata.org/entity/Q34618908

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մարտին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@ast

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@en

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@nl

type

label

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@ast

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@en

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@nl

prefLabel

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@ast

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@en

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@nl

P1433

Q34618908-F6B00072-FE24-4693-8961-137239FB0284

P1476

Q34618908-2F9332E0-F464-4455-8764-7D35667AE24B

P2093

Q34618908-3D5D9197-CD41-472F-BA39-B1D5D215ADD6

Q34618908-DBF76A58-B7B3-4013-8FD8-9F2435302837

P2860

Q34618908-0140DA0F-27FD-4A93-A7A5-ABC52A544B0C

Q34618908-042951E8-0088-49BC-A49C-65560BAD8D48

Q34618908-065DDAEF-042C-41BB-800B-A1310018DCDC

Q34618908-08160F5E-6637-41C7-9BB7-1FE63B3BFF37

Q34618908-08A698A3-7CCC-42AE-9A06-58DB1C702F42

Q34618908-0ACF3635-8AC8-4B00-92D2-9324510B77EE

Q34618908-1073EAE7-20C6-4653-9D6F-D1579188894A

Q34618908-1E7D7410-4A4F-436D-8C84-D7750C85973E

Q34618908-27643CC0-E5B0-46FE-A791-C7BB6C8821CB

Q34618908-2CB1B492-2899-4881-9224-63B9102169F7

P304

Q34618908-24E4215E-A483-4980-AD4E-58297F12A689

P31

Q34618908-6632FB36-CE8A-4E7B-A86B-E6F9DC7A495B

P356

Q34618908-848A636E-3066-4480-9745-174B2CADA86E

P433

Q34618908-22988377-D037-419B-958B-15DA8093745E

P478

Q34618908-4E2580E8-65E2-4F86-9084-BAF52A0452E5

P577

Q34618908-44AC502C-FBBD-413E-90E4-9F1081BE9F06

P5875

Q34618908-FFEE929C-7EC3-49E5-9777-B4D1D861DE12

P698

Q34618908-1D2BDB7B-8C14-4CAA-8250-42918BE0599E

P932

Q34618908-2F23FE5E-9300-4BA7-B615-1B1A262849AF

P356

P1433

The Journal of General Physiology

P1476

hERG potassium channel gating is mediated by N- and C-terminal region interactions

@en

P2093

Ahleah S Gustina

http://www.w3.org/2001/XMLSchema#string

Matthew C Trudeau

http://www.w3.org/2001/XMLSchema#string

P2860

A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel

A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome

HERG, a human inward rectifier in the voltage-gated potassium channel family

A novel role for HERG K+ channels: spike-frequency adaptation

A family of potassium channel genes related to eag in Drosophila and mammals

A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels

Structural basis for modulation and agonist specificity of HCN pacemaker channels

NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker

Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain

Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels revealed with fluorescence and electrophysiological methods

P304

315-325

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1085/JGP.201010582

http://www.w3.org/2001/XMLSchema#string

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

137

http://www.w3.org/2001/XMLSchema#string

P577

2011-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

50226837

http://www.w3.org/2001/XMLSchema#string

P698

21357734

http://www.w3.org/2001/XMLSchema#string

P932

3047612

http://www.w3.org/2001/XMLSchema#string