Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
about
Structural changes in the cytoplasmic pore of the Kir1.1 channel during pHi-gating probed by FRETTransition metal ion FRET to measure short-range distances at the intracellular surface of the plasma membrane.Differential regulation by cyclic nucleotides of the CNGA4 and CNGB1b subunits in olfactory cyclic nucleotide-gated channelsFluorescence applications in molecular neurobiologyMapping membrane protein structure with fluorescence.Generation of functional fluorescent BK channels by random insertion of GFP variantsThe bile acid-sensitive ion channel (BASIC) is activated by alterations of its membrane environmentRegulation of TRPV1 ion channel by phosphoinositide (4,5)-bisphosphate: the role of membrane asymmetryMolecular mechanism of voltage-dependent potentiation of KCNH potassium channelsTwo distinct aspects of coupling between Gα(i) protein and G protein-activated K+ channel (GIRK) revealed by fluorescently labeled Gα(i3) protein subunitsShort-range molecular rearrangements in ion channels detected by tryptophan quenching of bimane fluorescence.Conformational Flip of Nonactivated HCN2 Channel Subunits Evoked by Cyclic Nucleotides.Patch fluorometry: shedding new light on ion channels.Dynamics of Ca2+-calmodulin-dependent inhibition of rod cyclic nucleotide-gated channels measured by patch-clamp fluorometry.State-dependent FRET reports calcium- and voltage-dependent gating-ring motions in BK channelsPatch-clamp fluorometry-based channel counting to determine HCN channel conductance.Structural rearrangement of the intracellular domains during AMPA receptor activation.Hysteresis of ligand binding in CNGA2 ion channelsConformational changes associated with proton-dependent gating of ASIC1a.Interactions of divalent cations with calcium binding sites of BK channels reveal independent motions within the gating ringEmerging approaches to probing ion channel structure and function.Patch-clamp fluorometry: electrophysiology meets fluorescence.Deciphering the function of the CNGB1b subunit in olfactory CNG channels.State-dependent cAMP binding to functioning HCN channels studied by patch-clamp fluorometry.
P2860
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P2860
Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
description
2003 nî lūn-bûn
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name
Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
@en
Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
@nl
type
label
Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
@en
Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
@nl
prefLabel
Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
@en
Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
@nl
P2860
P1476
Patch-clamp fluorometry recording of conformational rearrangements of ion channels.
@en
P2093
William N Zagotta
P2860
P356
10.1126/STKE.2003.176.PL7
P577
2003-04-01T00:00:00Z