Negatively charged residues in the N-terminal of the AID helix confer slow voltage dependent inactivation gating to CaV1.2.
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The role of distal S6 hydrophobic residues in the voltage-dependent gating of CaV2.3 channels.Molecular endpoints of Ca2+/calmodulin- and voltage-dependent inactivation of Ca(v)1.3 channelsKinetic properties of the cardiac L-type Ca2+ channel and its role in myocyte electrophysiology: a theoretical investigation.An autism-associated mutation in CaV1.3 channels has opposing effects on voltage- and Ca(2+)-dependent regulation.Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation.Roscovitine, a cyclin-dependent kinase inhibitor, affects several gating mechanisms to inhibit cardiac L-type (Ca(V)1.2) calcium channels.Alanine-scanning mutagenesis defines a conserved energetic hotspot in the CaValpha1 AID-CaVbeta interaction site that is critical for channel modulation.Mutations of nonconserved residues within the calcium channel alpha1-interaction domain inhibit beta-subunit potentiation.Ca2+-binding protein 2 inhibits Ca2+-channel inactivation in mouse inner hair cells.Calmodulin mutations associated with long QT syndrome prevent inactivation of cardiac L-type Ca(2+) currents and promote proarrhythmic behavior in ventricular myocytes.The C-terminal residues in the alpha-interacting domain (AID) helix anchor CaV beta subunit interaction and modulation of CaV2.3 channels.The role of the GX9GX3G motif in the gating of high voltage-activated Ca2+ channels.Inherited Ventricular Arrhythmias: The Role of the Multi-Subunit Structure of the L-Type Calcium Channel Complex.
P2860
Q27865194-387396C4-672D-4721-815D-0608265CD6A2Q33530299-6FF5017C-D25D-456D-BD69-F5533DE8FC34Q35632946-70FDD0C6-5C0B-4DB3-93CA-3E8348548EA2Q36964814-FBF3A457-DBCC-446C-9FF4-719DB406F0D3Q37124244-82405EB2-78E2-462C-8669-E82E545CE938Q40093407-C01B65DF-A0E5-4605-9E6B-1C13A47AEA22Q41869908-3E86F650-9865-435D-841B-39D7137246E2Q41911426-61A20348-F595-4CC8-8407-AF825FA9E301Q42318112-A7C26083-9694-4DA1-98D6-C8E4755B38CDQ42551776-6904B2FC-540D-4F7E-AE87-3D62A7013C71Q45126653-B66609EE-CC6C-4C94-A42C-95C22C36FAD8Q50643833-7EEB9022-9674-4FC0-AC40-51D219C0F1ADQ51094903-32D9D69D-32E5-415D-A781-996212097A39
P2860
Negatively charged residues in the N-terminal of the AID helix confer slow voltage dependent inactivation gating to CaV1.2.
description
2004 nî lūn-bûn
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2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2004 թվականի օգոստոսին հրատարակված գիտական հոդված
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name
Negatively charged residues in ...... inactivation gating to CaV1.2.
@ast
Negatively charged residues in ...... inactivation gating to CaV1.2.
@en
type
label
Negatively charged residues in ...... inactivation gating to CaV1.2.
@ast
Negatively charged residues in ...... inactivation gating to CaV1.2.
@en
prefLabel
Negatively charged residues in ...... inactivation gating to CaV1.2.
@ast
Negatively charged residues in ...... inactivation gating to CaV1.2.
@en
P2093
P2860
P1433
P1476
Negatively charged residues in ...... inactivation gating to CaV1.2.
@en
P2093
Alexandra Raybaud
Laurent Berrou
Lucie Parent
Rémy Sauvé
Yolaine Dodier
P2860
P304
P356
10.1529/BIOPHYSJ.104.045559
P407
P577
2004-08-31T00:00:00Z