Kinetics of Drug Interaction with the Kv11.1 Potassium Channel

2014 ◽  
Vol 85 (5) ◽  
pp. 769-776 ◽  
Author(s):  
Adam P. Hill ◽  
Mark J. Perrin ◽  
Juliane Heide ◽  
Terence J. Campbell ◽  
Stefan A. Mann ◽  
...  
Keyword(s):  
Drug Interaction ◽  
Potassium Channel ◽  
Kinetics Of

scholarly journals Improving Trafficking and Kinetics of a Synthetic Light-Gated Potassium Channel

2017 ◽  
Vol 112 (3) ◽  
pp. 172a-173a
Author(s):  
Laura S. Alberio ◽  
Giordano Defranceschi ◽  
Federica Simeoni ◽  
Paolo Zuccolini ◽  
Gerhard Thiel ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Kinetics Of

Slow kinetics of a potassium channel inAcetabularia

1988 ◽  
Vol 102 (2) ◽  
pp. 141-152 ◽  
Author(s):  
A. Bertl ◽  
H. G. Klieber ◽  
D. Gradmann
Keyword(s):  
Potassium Channel ◽  
Slow Kinetics ◽  
Kinetics Of

scholarly journals Cloning and Expression of the Human Kv4.3 Potassium Channel

1999 ◽  
Vol 81 (4) ◽  
pp. 1974-1977 ◽  
Author(s):  
Daniel Dilks ◽  
Huai-Ping Ling ◽  
Mark Cockett ◽  
Patricia Sokol ◽  
Randy Numann
Keyword(s):  
Potassium Channel ◽  
Cloning And Expression ◽  
Short Version ◽  
Rt Pcr ◽  
Amino Acid Deletion ◽  
Inactivation Curve ◽  
Recovery From Inactivation ◽  
Window Current ◽  
Kinetics Of ◽  
The Brain

Cloning and expression of the human Kv4.3 potassium channel. We report on the cloning and expression of hKv4.3, a fast inactivating, transient, A-type potassium channel found in both heart and brain that is 91% homologous to the rat Kv4.3 channel. Two isoforms of hKv4.3 were cloned. One is full length (hKv4.3 long), and the other has a 19 amino acid deletion (hKv4.3 short). RT-PCR shows that the brain contains both forms of the channel RNA, whereas the heart predominantly has the longer version. Both versions of the channel were expressed in Xenopus oocytes, and both contain a significant window or noninactivating current seen near potentials of −30 to −40 mV. The inactivation curve for hKv4.3 short is shifted 10 mV positive relative to hKv4.3 long. This causes the peak window current for the short version to occur near −30 mV and the peak for the longer version to be at −40 mV. There was little difference in the recovery from inactivation or in the kinetics of inactivation between the two isoforms of the channel.

scholarly journals Drug Interaction at the Lipid Bilayer-Potassium Channel Interface

2017 ◽  
Vol 112 (3) ◽  
pp. 40a ◽  
Author(s):  
Nina Ottosson ◽  
Malin Silverå Ejneby ◽  
Xiongyu Wu ◽  
Samira Yazdi ◽  
Peter Konradsson ◽  
...  
Keyword(s):  
Drug Interaction ◽  
Potassium Channel ◽  
Lipid Bilayer

Blockers of potassium channels reduce the outward dark current in rod photoreceptor inner segments

1992 ◽  
Vol 8 (5) ◽  
pp. 479-481 ◽  
Author(s):  
Kun Yan ◽  
Gary Matthews
Keyword(s):  
Potassium Channel ◽  
Dark Current ◽  
Outer Segment ◽  
Light Response ◽  
Channel Blockers ◽  
Rod Photoreceptor ◽  
Potassium Channel Blockers ◽  
Internal Ph ◽  
Suction Electrode ◽  
Kinetics Of

AbstractThe dark current of single isolated toad rods was monitored by drawing either the inner segment or the outer segment into a suction electrode. The potassium-channel blockers tetraethylammonium (TEA) and 3,4-diaminopyridine (DAP) reduced the amplitude of the dark current when applied to the inner segment. Both drugs were less effective when applied to the outer segment, suggesting that they act at the inner segment to block part of the outward path for the dark current. In addition, DAP affected the kinetics of the light response, possibly by affecting internal pH.

scholarly journals Biochemical engineering of theN-acyl side chain of sialic acids alters the kinetics of a glycosylated potassium channel Kv3.1

FEBS Letters ◽  
2011 ◽  
Vol 585 (20) ◽  
pp. 3322-3327 ◽  
Author(s):  
M. Kristen Hall ◽  
Werner Reutter ◽  
Thisbe Lindhorst ◽  
Ruth A. Schwalbe
Keyword(s):  
Potassium Channel ◽  
Sialic Acids ◽  
Side Chain ◽  
Biochemical Engineering ◽  
Acyl Side Chain ◽  
Kinetics Of

Influence of protein surface charge on the bimolecular kinetics of a potassium channel peptide inhibitor

Biochemistry ◽  
1993 ◽  
Vol 32 (27) ◽  
pp. 6982-6987 ◽  
Author(s):  
Laura Escobar ◽  
Michael J. Root ◽  
Roderick MacKinnon
Keyword(s):  
Potassium Channel ◽  
Surface Charge ◽  
Peptide Inhibitor ◽  
Protein Surface ◽  
Kinetics Of

scholarly journals Folding and misfolding of potassium channel monomers during assembly and tetramerization

2021 ◽  
Vol 118 (34) ◽  
pp. e2103674118
Author(s):  
Kevin C. Song ◽  
Andrew V. Molina ◽  
Ruofan Chen ◽  
Isabelle A. Gagnon ◽  
Young Hoon Koh ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Disulfide Bridge ◽  
Transmembrane Helices ◽  
Dense Region ◽  
Nmr Studies ◽  
Dynamics Simulations ◽  
Pore Domain ◽  
Kinetics Of

The dynamics and folding of potassium channel pore domain monomers are connected to the kinetics of tetramer assembly. In all-atom molecular dynamics simulations of Kv1.2 and KcsA channels, monomers adopt multiple nonnative conformations while the three helices remain folded. Consistent with this picture, NMR studies also find the monomers to be dynamic and structurally heterogeneous. However, a KcsA construct with a disulfide bridge engineered between the two transmembrane helices has an NMR spectrum with well-dispersed peaks, suggesting that the monomer can be locked into a native-like conformation that is similar to that observed in the folded tetramer. During tetramerization, fluoresence resonance energy transfer (FRET) data indicate that monomers rapidly oligomerize upon insertion into liposomes, likely forming a protein-dense region. Folding within this region occurs along separate fast and slow routes, with τfold ∼40 and 1,500 s, respectively. In contrast, constructs bearing the disulfide bond mainly fold via the faster pathway, suggesting that maintaining the transmembrane helices in their native orientation reduces misfolding. Interestingly, folding is concentration independent despite the tetrameric nature of the channel, indicating that the rate-limiting step is unimolecular and occurs after monomer association in the protein-dense region. We propose that the rapid formation of protein-dense regions may help with the assembly of multimeric membrane proteins by bringing together the nascent components prior to assembly. Finally, despite its name, the addition of KcsA’s C-terminal “tetramerization” domain does not hasten the kinetics of tetramerization.

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