Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
about
A novel biological activity of praziquantel requiring voltage-operated Ca2+ channel beta subunits: subversion of flatworm regenerative polarityOrientation of the calcium channel beta relative to the alpha(1)2.2 subunit is critical for its regulation of channel activityGuanylate kinase domains of the MAGUK family scaffold proteins as specific phospho-protein-binding modulesSolution structure of the N-terminal A domain of the human voltage-gated Ca2+channel beta4a subunitA short history of voltage-gated calcium channelsThe importance of occupancy rather than affinity of CaV(beta) subunits for the calcium channel I-II linker in relation to calcium channel functionThe Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic PotentialL-type calcium channel targeting and local signalling in cardiac myocytesStructure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channelsThe dynamic architecture of photoreceptor ribbon synapses: cytoskeletal, extracellular matrix, and intramembrane proteinsStructure of the voltage-gated calcium channel Cav1.1 complexBeta-cell CaV channel regulation in physiology and pathophysiology.Direct interaction of CaVβ with actin up-regulates L-type calcium currents in HL-1 cardiomyocytesVoltage-gated calcium channelsNew short splice variants of the human cardiac Cavbeta2 subunit: redefining the major functional motifs implemented in modulation of the Cav1.2 channelCritical role for the beta regulatory subunits of Cav channels in T lymphocyte function.BARP suppresses voltage-gated calcium channel activity and Ca2+-evoked exocytosisCacnb4 directly couples electrical activity to gene expression, a process defective in juvenile epilepsyThe junctional SR protein JP-45 affects the functional expression of the voltage-dependent Ca2+ channel Cav1.1The VGL-Chanome: A Protein Superfamily Specialized for Electrical Signaling and Ionic HomeostasisStructural and biophysical analyses of the skeletal dihydropyridine receptor β subunit β1a reveal critical roles of domain interactions for stability.¹H, ¹³C, and ¹⁵N backbone resonance assignments of the 37 kDa voltage-gated Ca²⁺ channel β4 subunit core SH3-GK domains.Domain cooperativity in the β1a subunit is essential for dihydropyridine receptor voltage sensing in skeletal muscle.Characterization of the first honeybee Ca²⁺ channel subunit reveals two novel species- and splicing-specific modes of regulation of channel inactivation.Interaction of bestrophin-1 and Ca2+ channel β-subunits: identification of new binding domains on the bestrophin-1 C-terminusHomodimerization of the Src homology 3 domain of the calcium channel β-subunit drives dynamin-dependent endocytosis.The ß subunit of voltage-gated Ca2+ channelsFunctional dissection of the intramolecular Src homology 3-guanylate kinase domain coupling in voltage-gated Ca2+ channel beta-subunits.Determinants of the voltage dependence of G protein modulation within calcium channel beta subunits.The calcium channel beta2 (CACNB2) subunit repertoire in teleosts.Functional modularity of the beta-subunit of voltage-gated Ca2+ channels.A CaVbeta SH3/guanylate kinase domain interaction regulates multiple properties of voltage-gated Ca2+ channels.The N-terminal domain tethers the voltage-gated calcium channel β2e-subunit to the plasma membrane via electrostatic and hydrophobic interactionsEmerging evidence for specific neuronal functions of auxiliary calcium channel α₂δ subunits.Orientation of palmitoylated CaVbeta2a relative to CaV2.2 is critical for slow pathway modulation of N-type Ca2+ current by tachykinin receptor activation.Transfer of beta subunit regulation from high to low voltage-gated Ca2+ channels.The best disease-linked Cl- channel hBest1 regulates Ca V 1 (L-type) Ca2+ channels via src-homology-binding domains.Facilitation versus depression in cultured hippocampal neurons determined by targeting of Ca2+ channel Cavbeta4 versus Cavbeta2 subunits to synaptic terminalsNegatively charged residues in the N-terminal of the AID helix confer slow voltage dependent inactivation gating to CaV1.2.Ablation of Ca2+ channel beta3 subunit leads to enhanced N-methyl-D-aspartate receptor-dependent long term potentiation and improved long term memory
P2860
Q21092297-1FDDE1AF-B727-47E2-B249-B8C11F5B4647Q21144219-DDB23635-B5F0-4A8A-89BA-DDB36E1F1FB5Q24298323-52B05A90-BFA6-41AB-AA81-5C1E17F9BB9FQ24300054-A3414DE5-38C5-4A13-AE4B-A91D275BFCBAQ24670360-E3B19B2E-D016-4D69-87ED-1506F9C343AAQ24682120-DBBDD5EF-036E-47D2-BF0D-00DD3BA78B20Q26781422-B050D79A-1CA2-44A1-BE38-82186E8CF127Q26853101-C47A3B7E-AD5B-4C44-9EC2-80085CF2B6A6Q26864613-BF0B9CC7-D58B-4386-B7E5-FC14266FD76EQ26865168-A7B349A1-C214-410D-9105-848D56893E93Q27703151-D7334A51-C7C9-4344-B76A-CCD84759836CQ27863802-70003DAE-8A10-4D4E-B856-9B2514B7700CQ28119053-44CD1F83-FF81-4B45-B3E2-BF8DD5BB99D4Q28242997-76F0B542-4FD9-4A3B-9129-79C7581518E8Q28279950-A59CE920-4922-4465-AD10-E55CBB569F01Q28505265-719B68A3-2835-4ED0-8E61-7C602FA64CFBQ28512209-763DABFA-8507-4BB7-B705-1C6712E4541CQ28574061-352187E4-A67D-4DB1-962A-4192A0439340Q28587534-C5E73EE1-6860-4D4E-B67C-EF8AB8A1B181Q29032115-13942B73-D775-4CAD-AEC4-9CAA1CDAC324Q30008756-18F31CF1-A72A-4135-9F81-37CF6F881C49Q30009846-8930EFA4-6977-48E2-B220-9728B3B856E8Q30009869-9A66BF2A-EB4A-414F-A9CD-DB621E98C83CQ30009875-4C6DCAFC-6116-48FF-979A-35F1E0921F1BQ30155551-10D20B54-2AD3-4137-991F-4A5EA2FA66FAQ30155579-8C620F71-14F3-44D2-9E79-FDE14A661B36Q30155988-428C1698-ECBE-421E-86B8-DA9F22E2DBD4Q30157263-FF68BB0B-C295-4692-B9B9-8CD3E4DCE68AQ30157629-D18F9E60-A012-4867-8755-20713D5CD8C7Q30157705-422FCFD9-0B42-4777-AC96-44496ABEEFCFQ30157978-6FE17923-ACFF-4857-BBFD-178D79A462C2Q30160124-2F97EFBC-025C-437C-8385-C7B4F98340E3Q30405831-6B8E9573-DC31-456C-A12A-124E108BC966Q30407837-754F786D-5C4C-4109-B479-75438675226BQ30436277-F9BEA196-C701-412C-8710-5CEEF108DE04Q30437245-587AFCB6-4EC2-4024-B0B9-371464BF87A1Q30440755-B3ACC4A3-2D60-4AB9-BFA8-189687DBCE21Q30443807-6CBD85D7-E597-47BA-AABD-33A98B91F84EQ30447395-14A772D1-D37D-4B15-B196-F8D49840A45BQ30448457-F3578C87-FE75-487E-86D7-230E9071DBF1
P2860
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
name
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@ast
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@en
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@nl
type
label
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@ast
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@en
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@nl
prefLabel
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@ast
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@en
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@nl
P2093
P2860
P3181
P356
P1433
P1476
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels
@en
P2093
Aileen Fitzmaurice
Hailong Zhang
Lin-Ling He
Ming-Hui Li
Yoichi Yamada
Yu-Hang Chen
P2860
P2888
P304
P3181
P356
10.1038/NATURE02641
P407
P50
P577
2004-05-30T00:00:00Z
P6179
1012183770