about
Four Ca2+ ions activate TRPM2 channels by binding in deep crevices near the pore but intracellularly of the gateThe ABC protein turned chloride channel whose failure causes cystic fibrosisThe proposed channel-enzyme transient receptor potential melastatin 2 does not possess ADP ribose hydrolase activityObligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerizationStrict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations.CFTR channel gating: incremental progress in irreversible steps.Rapid kinetic analysis of multichannel records by a simultaneous fit to all dwell-time histogramsStructure-activity analysis of a CFTR channel potentiator: Distinct molecular parts underlie dual gating effects.Putative chanzyme activity of TRPM2 cation channel is unrelated to pore gatingMutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gatingPore collapse underlies irreversible inactivation of TRPM2 cation channel currents.Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle.Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain.Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA.Severed molecules functionally define the boundaries of the cystic fibrosis transmembrane conductance regulator's NH(2)-terminal nucleotide binding domain.Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domainsA single active catalytic site is sufficient to promote transport in P-glycoproteinConformational changes in the catalytically inactive nucleotide-binding site of CFTR.Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanismsCatalyst-like modulation of transition states for CFTR channel opening and closing: new stimulation strategy exploits nonequilibrium gating.Mitoxantrone is expelled by the ABCG2 multidrug transporter directly from the plasma membrane.Ruling out pyridine dinucleotides as true TRPM2 channel activators reveals novel direct agonist ADP-ribose-2'-phosphate.Degenerate ABC composite site is stably glued together by trapped ATP.Ca(2+)- and voltage-dependent gating of Ca(2+)- and ATP-sensitive cationic channels in brain capillary endothelium.A new target for G protein signaling.Molecular Structure of the Human CFTR Ion Channel.CFTR gating: Invisible transitions made visible.A novel kinetic assay of mitochondrial ATP-ADP exchange rate mediated by the ANT.Identification of direct and indirect effectors of the transient receptor potential melastatin 2 (TRPM2) cation channel.Antagonistic regulation of native Ca2+- and ATP-sensitive cation channels in brain capillaries by nucleotides and decavanadate.Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions.Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2The twain shall meet: channels, transporters and things between. Meeting on Membrane Transport in Flux: the Ambiguous Interface Between Channels and Pumps.Ion channels as targets to treat cystic fibrosis lung disease.Electrophysiological, biochemical, and bioinformatic methods for studying CFTR channel gating and its regulation.The N-terminal transmembrane domain (TMD0) and a cytosolic linker (L0) of sulphonylurea receptor define the unique intrinsic gating of KATP channels.Timing of CFTR pore opening and structure of its transition state.Structure of a TRPM2 channel in complex with Ca2+ explains unique gating regulation.Enzyme activity and selectivity filter stability of ancient TRPM2 channels were simultaneously lost in early vertebratesCystic fibrosis drug ivacaftor stimulates CFTR channels at picomolar concentrations
P50
Q24655919-18C3F546-9DCE-4FCB-9234-058A6FA95AFDQ24657572-7C162707-8EE0-4C29-BBB6-0FC4B7746D59Q28116139-92AA281E-9364-44E9-9978-632B45B8A8C1Q28829296-1CE13E58-7B21-4B83-8DE0-2BBFAC42CE8EQ33666969-6178E5C3-DE56-4068-AD9F-6A271CA1189CQ33683078-08379897-7819-4703-9109-45687F08A6C5Q34172410-FC1BC26E-17C4-4BDD-9B11-19D9BBC9735CQ34262476-D3D5D882-68E8-4079-AFBE-8DAA2D1133AAQ34601119-EAF12CC3-C9C8-4CB8-942E-415E3D4ACA42Q35018175-57DBC5A0-5EB7-44C1-B949-2BA9F588D452Q36170779-D45E52D3-CEA4-4F0E-A8E7-001BCE704E5CQ36295891-14FCCAD6-06CD-418E-A85C-0156A98B035EQ36412577-80F308DD-8E3A-4B9B-A646-586D9990862AQ36412598-E8B13A03-374B-489C-A894-40EB5B239D5DQ36436335-36308315-AD7D-495E-B1B4-A62F192D17AEQ36444749-F30A1805-EE14-4FAD-BFE1-9E46D625C961Q36840944-1F0D5381-97F5-4E86-AF1A-54183C4EC101Q36951968-DAD90177-2823-4E41-A029-9C0E977AC106Q37280517-741628FF-FDCE-486F-8AE5-67F5CDA2EEB0Q37727045-E294477B-6270-433B-95AC-33313E20F853Q39670388-57D1FAB3-F7CF-4262-B985-6D42365F41BCQ39990488-F09CD704-91C8-4829-B6B4-F53ECAE316D7Q40226871-2F84D4A6-9F32-4B7A-8E52-94A9420A9A53Q40243075-586E54D1-3DF3-40F0-907F-AEC72CF89FFCQ41349949-9BBD2B44-25B4-4A85-93D3-1DD7C0315971Q41598483-EEBD054F-4A25-48E1-B445-56ACB96E37DEQ41851267-B570E6BA-C11E-4D36-AA67-8E71782859E3Q41863957-A8120BE0-5987-48CB-AB71-F2EF5146A7F1Q41923686-8C4257A0-B4AB-4584-B026-F40CEC603298Q41954014-141A8C6C-42D9-4532-927A-848D70084E6BQ42283021-C4B27300-D68B-469B-B830-0905CBF6D578Q42416978-46E1962A-2820-4947-8EDA-B937B87C103DQ43251824-8660069E-57D9-4E70-90B7-3B1D76647A91Q48611695-AAC50C09-8608-4D96-A1B1-E9E39D8D350FQ48673047-05802235-49ED-4BD9-8D18-599C931F106EQ51805285-C1A10A70-79D4-4D38-83C8-A8EB2FB68F48Q52664797-A357E147-24BE-4D40-819D-783DA6D42D01Q55063295-FE418E6D-685F-4BD5-BFBE-5CC181AC8DACQ64084155-6013950C-7522-4199-95E5-90C1B5D5B1DCQ83232187-6688E13A-E9FB-4F42-8856-F1CEE9BCA9CE
P50
description
(1971–) magyar biokémikus, kutató
@hu
biochemicus
@nl
hulumtues
@sq
researcher
@en
հետազոտող
@hy
name
Csanády László
@hu
László Csanády
@en
László Csanády
@es
László Csanády
@nl
László Csanády
@sl
type
label
Csanády László
@hu
László Csanády
@en
László Csanády
@es
László Csanády
@nl
László Csanády
@sl
prefLabel
Csanády László
@hu
László Csanády
@en
László Csanády
@es
László Csanády
@nl
László Csanády
@sl
P1153
6602477032
P19
P21
P2492
P27
P31
P3226
P496
0000-0002-6547-5889
P569
1971-07-29T00:00:00Z