Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.
about
Ca2+-dependent modulation of voltage-gated Ca2+ channelsMultiple C-terminal tail Ca(2+)/CaMs regulate Ca(V)1.2 function but do not mediate channel dimerizationSolution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5Solution NMR structure of the C-terminal EF-hand domain of human cardiac sodium channel NaV1.5IQ-motif selectivity in human IQGAP2 and IQGAP3: binding of calmodulin and myosin essential light chainThe diversity of calcium sensor proteins in the regulation of neuronal functionPEP-19, an intrinsically disordered regulator of calmodulin signalingCalmodulin regulation (calmodulation) of voltage-gated calcium channelsL-type calcium channel targeting and local signalling in cardiac myocytesTowards a Unified Theory of Calmodulin Regulation (Calmodulation) of Voltage-Gated Calcium and Sodium ChannelsThe calmodulin-binding, short linear motif, NSCaTE is conserved in L-type channel ancestors of vertebrate Cav1.2 and Cav1.3 channelsCrystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition featuresStructures of CaV2 Ca2+/CaM-IQ Domain Complexes Reveal Binding Modes that Underlie Calcium-Dependent Inactivation and FacilitationSolution Structure of the NaV1.2 C-terminal EF-hand DomainCrystal structure of dimeric cardiac L-type calcium channel regulatory domains bridged by Ca2+* calmodulinsDeterminants in CaV1 Channels That Regulate the Ca2+ Sensitivity of Bound CalmodulinStructural Studies of Soybean Calmodulin Isoform 4 Bound to the Calmodulin-binding Domain of Tobacco Mitogen-activated Protein Kinase Phosphatase-1 Provide Insights into a Sequential Target Binding ModeStructural Basis for the Differential Effects of CaBP1 and Calmodulin on CaV1.2 Calcium-Dependent InactivationNMR Structure of Calmodulin Complexed to an N-Terminally Acetylated α-Synuclein PeptideStructural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca2+-calmodulinStructural Insights into Calmodulin-regulated L-selectin Ectodomain SheddingCaldendrin, a neuron-specific modulator of Cav/1.2 (L-type) Ca2+ channelsThe calmodulin regulator protein, PEP-19, sensitizes ATP-induced Ca2+ releaseMyoscape controls cardiac calcium cycling and contractility via regulation of L-type calcium channel surface expression.The neurobiologist's guide to structural biology: a primer on why macromolecular structure matters and how to evaluate structural data.Reduction of CaV channel activities by Ca2+-CaM: inactivation or deactivation?Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation.Energetics of calmodulin domain interactions with the calmodulin binding domain of CaMKII.Continuously tunable Ca(2+) regulation of RNA-edited CaV1.3 channels.The structural biology of voltage-gated calcium channel function and regulationCalcium-dependent regulation of the voltage-gated sodium channel hH1: intrinsic and extrinsic sensors use a common molecular switchA molecular dynamics study and free energy analysis of complexes between the Mlc1p protein and two IQ motif peptidesCalmodulin overexpression does not alter Cav1.2 function or oligomerization state.Competition between α-actinin and Ca²⁺-calmodulin controls surface retention of the L-type Ca²⁺ channel Ca(V)1.2.Calmodulin and CaMKII as molecular switches for cardiac ion channels.Localized calcineurin confers Ca2+-dependent inactivation on neuronal L-type Ca2+ channels.Acidic/IQ motif regulator of calmodulinCalcium channels and short-term synaptic plasticity.Competitive and non-competitive regulation of calcium-dependent inactivation in CaV1.2 L-type Ca2+ channels by calmodulin and Ca2+-binding protein 1The Timothy syndrome mutation differentially affects voltage- and calcium-dependent inactivation of CaV1.2 L-type calcium channels.
P2860
Q21564049-EBBE3061-4CFB-440D-9866-EF4C35A6724EQ24303653-8C38D724-AA8C-4B2E-B332-65062C3FD7A6Q24317459-D2E6376F-7ABF-45DF-870B-7907C9AC5AC9Q24324607-8A2D4D3A-B648-472B-B6C8-D5CBF8CD2928Q24339401-35EF6AC3-60FE-4638-B79D-ADEDD3B2B488Q24604134-085EB07B-3535-4C76-BEBD-D0F4D7EBD22BQ24655495-27B60C73-09F3-4BB1-A849-8FCE7F9A1D6FQ26827282-5F6F9752-D865-4DCE-BA8C-EE8B9E77E8E4Q26853101-C8F7079A-AC50-4B10-86C0-B46B6CE8B36EQ27002550-B796B05D-7138-4AD4-B834-E40E43B5F812Q27324221-8A4348BF-5A0E-4692-9FFC-73A22CAA9202Q27643231-AD699FC1-4F45-4CA1-8313-A03857677FA4Q27652588-6CDD43DC-D7F8-4514-A34B-4B83330338E2Q27653359-54FF7AC9-EBF1-41F8-9477-B8980DB6FF3DQ27654070-688E546D-C349-4A48-A2DA-5BB80009AA5BQ27655638-30443636-A031-4354-843E-8F5B6DC9D50CQ27656954-C5961B39-01ED-49CA-840F-0B988B39B139Q27666196-746E18F1-A0C5-45E6-921A-144F2E4E755BQ27677491-8C9C124C-D43B-4ADE-8837-F69D00B397FCQ27678630-43CEAF8E-D5B3-4D40-A078-5E19FD72242BQ27681231-7A38904A-CD8C-44B7-8317-0E7D530F02E1Q28583948-1CF30EB2-8723-44D4-B5FC-2E68D212153DQ30668614-EE397DD2-9236-4664-8B07-FFEF020253D7Q30852031-35196EE9-F7B9-45FA-8841-D1C82767A462Q31113565-AC6F50EC-16D3-4ACF-BA40-695410BB53BEQ33763162-2E5D45B5-16FF-4751-8BF7-649C4FD94CD3Q33765534-5FC3568D-2182-4845-9BF5-A95D44FAEB84Q34074679-B175E4BA-A087-4A4A-84E6-1FC5B1606866Q34377391-70E7C5B9-F37A-4654-A2DC-250F7984546EQ34440686-2836FF8A-FCA2-4E58-B173-A1349F3824CFQ34574396-CFFD2201-448E-44D5-AC86-0014285998D8Q35021351-C26CC7FF-0008-4D6C-90D5-0968EB7C4273Q35577694-0974DF6B-8AC9-4E6B-BF04-084132F0F7CFQ36062292-BCB922BE-3973-4CB9-93D3-C0A38BF474C9Q36669731-8C19E11B-A557-46DE-BC85-60CAC0C78F5DQ36672587-8312E40B-2B5A-45E6-8913-57DB95A06361Q36741596-3F1F9AE5-0DC9-41A2-AD19-3AC1119C1D6EQ36760394-6A9DD36E-82CC-4A72-BD6B-7012827F1ABEQ36812386-209A536A-7403-4E66-A2CC-1286C7948C58Q36883128-7717E2CC-D7FF-4CC5-B7FA-3581EA11EB15
P2860
Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca
@nl
Structure of calmodulin bound ...... diac Ca(v)1.2 calcium channel.
@en
type
label
Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca
@nl
Structure of calmodulin bound ...... diac Ca(v)1.2 calcium channel.
@en
prefLabel
Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca
@nl
Structure of calmodulin bound ...... diac Ca(v)1.2 calcium channel.
@en
P2093
P1433
P1476
Structure of calmodulin bound ...... diac Ca(v)1.2 calcium channel.
@en
P2093
D Brent Halling
Florante A Quiocho
Jennifer L Fallon
Susan L Hamilton
P304
P356
10.1016/J.STR.2005.09.021
P577
2005-12-01T00:00:00Z