about
Activation of TxA2/PGH2 receptors and protein kinase C contribute to coronary dysfunction in superoxide treated rat hearts.A novel SCN5A mutation associated with long QT-3: altered inactivation kinetics and channel dysfunction.Insights into the molecular mechanisms of bradycardia-triggered arrhythmias in long QT-3 syndromeK+ channel structure-activity relationships and mechanisms of drug-induced QT prolongation.Coupling profile of the metabotropic glutamate receptor 1alpha is regulated by the C-terminal domain.A carboxyl-terminal hydrophobic interface is critical to sodium channel function. Relevance to inherited disorders.Characterization of bitter taste responses of intestinal STC-1 cells.Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor 1alpha.4-Phenyltetrahydroisoquinoline, but not nomifensine or cocaine, inhibits methamphetamine-induced dopamine release.Binding of Gq protein stabilizes the activated state of the muscarinic receptor type 1.Auto-oxidation products of epigallocatechin gallate activate TRPA1 and TRPV1 in sensory neurons.Methamphetamine antagonistic property of (+)- and (-)-4-phenyltetrahydroisoquinoline in rat anococcygeus muscle.Gi/o-coupled muscarinic receptors co-localize with GIRK channel for efficient channel activationActivated stellate (Ito) cells possess voltage-activated calcium currentSecondary structure of the human cardiac Na+ channel C terminus: evidence for a role of helical structures in modulation of channel inactivationAlcohol stimulates the expression of L-type voltage-operated Ca2+ channels in hepatic stellate cellsSustained beta-adrenergic stimulation increased L-type Ca2+ channel expression in cultured quiescent ventricular myocytes[FRET analysis of the activation of GPCR]Two mutations at different positions in the CNBH domain of the hERG channel accelerate deactivation and impair the interaction with the EAG domain
P50
Q31405299-17099B6D-990C-4564-9CAC-03EE87588705Q33148068-D8AA1C0C-CCE4-47C3-8BB4-3DBBBCAE8AB1Q34815219-07BFE384-BD3E-4BE1-AC0A-309B81A08EF8Q35050596-ABD6EBB7-9D55-4F3D-9DE4-4F0DBB34CE94Q40184554-F7FDAEB9-D8DA-4C20-9AAA-08132A4D866AQ40263023-540178C0-4260-4C4B-9611-1053671944EAQ40452069-59F21752-DC03-41B8-8B9C-AFD3E62B024FQ44927471-53F2B5A2-1501-4910-B7E5-0BB9A1697F31Q48233612-95239187-BB6F-479C-AFB0-92B541EB08E6Q48327965-0828F984-E9CA-46BF-B9F1-3BC51F3BDA16Q50445395-A507556B-C5D6-424C-90BF-4EBAE3477410Q51652998-A6601981-95E0-4618-9305-3F49FEA63718Q58707303-C42D3C96-DB89-4906-8DD5-7D29D241ED2DQ77343177-AAAA5379-DAC5-4F83-9BC7-C4DF5F4D87AAQ77347116-A94AA7DC-68B2-4A61-9513-D27BE38F1DF2Q77478419-9E1D7078-0EB0-4F85-971A-4EE66569333CQ79899028-207EC044-30AA-4A0B-A04E-5F8704D43E47Q87844959-DD12919C-184E-4CB3-837C-61A01D3E96ABQ90816746-B428FFF5-D633-4D82-B0F0-324FDBA966DE
P50
description
researcher
@en
wetenschapper
@nl
name
M Tateyama
@en
M Tateyama
@nl
type
label
M Tateyama
@en
M Tateyama
@nl
prefLabel
M Tateyama
@en
M Tateyama
@nl
P106
P31
P496
0000-0002-1514-976X