Activation and inhibition of ATP-sensitive K+ channels by fluorescein derivatives.

doi:10.1016/s0021-9258(18)42869-4

Paper

DOI: 10.1016/s0021-9258(18)42869-4

Activation and inhibition of ATP-sensitive K+ channels by fluorescein derivatives.

Published Mar 5, 1992 · J. D. de Weille, M. Müller, M. Lazdunski

The Journal of biological chemistry

Q1 SJR score

Citations

Influential Citations

Full textSemantic Scholar

Abstract

Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.

In Vitro Study

Study Snapshot

Fluorescein derivatives can both inhibit and reactivate ATP-sensitive K+ channels, making them resistant to classical blockers like glibenclamide.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Sign up to use Study Snapshot

Consensus is limited without an account. Create an account or sign in to get more searches and use the Study Snapshot.

Create an account

Full text analysis coming soon...

References

Citations

DOI: 10.1016/j.bmc.2010.06.069

Rose Bengal analogs and vesicular glutamate transporters (VGLUTs).

Rose Bengal analogs show potential as potent inhibitors of vesicular glutamate transporters, potentially aiding in glutamate/acetylcholine co-transmission studies.

2010·28citations·N. Pietrancosta et al.·Bioorganic & medicinal chemistry

Bioorganic & medicinal chemistry

DOI: 10.1016/J.ICS.2006.01.048

Lucifer Yellow CH modifies voltage-gated channels and a ligand-gated channel in a light-dependent manner

Lucifer Yellow CH (LY) increases the current magnitude of voltage-gated K+ channels and AMPA receptor channels in a light-dependent manner, but has no effect on HVA-Ca 2+, Cl, NMDA, kainite, and 5HT3 channels.

2006·0citations·Keita Takeuchi et al.

DOI: 10.1074/JBC.M108023200

Phloxine B Interacts with the Cystic Fibrosis Transmembrane Conductance Regulator at Multiple Sites to Modulate Channel Activity* 210

Phloxine B interacts directly with CFTR at multiple sites to modulate channel activity, potentially aiding in the development of new treatments for diseases caused by CFTR malfunction.

2002·57citations·Z. Cai et al.·The Journal of Biological Chemistry

The Journal of Biological Chemistry

DOI: 10.1007/s002100100410

Chromanol 293B, a blocker of the slow delayed rectifier K+ current (IKs), inhibits the CFTR Cl– current

Chromanol 293B, a blocker of the slow delayed rectifier K+ current in the heart, also inhibits the CFTR Cl- current, suggesting its potential role in cystic fibrosis treatment.

2001·24citations·A. Bachmann et al.·Naunyn-Schmiedeberg's Archives of Pharmacology

Naunyn-Schmiedeberg's Archives of Pharmacology

DOI: 10.1038/sj.bjp.0703600

Potent stimulation and inhibition of the CFTR Cl− current by phloxine B

Phloxine B increases CFTR channel activity and slows deactivation, with inhibition dominating at high concentrations, potentially mediated by direct interactions with CFTR from the inside of the cell.

2000·21citations·A. Bachmann et al.·British Journal of Pharmacology

British Journal of Pharmacology

DOI: 10.1038/sj.bjp.0703181

Pharmacology of human sulphonylurea receptor SUR1 and inward rectifier K+ channel Kir6.2 combination expressed in HEK‐293 cells

The pharmacological properties of SUR1 and Kir6.2 channels co-expressed in HEK-293 cells resemble those of native KATP channels in pancreatic and neuronal tissues.

2000·32citations·M. Gopalakrishnan et al.·British Journal of Pharmacology

British Journal of Pharmacology

DOI: 10.1210/EDRV.20.2.0361

Molecular biology of adenosine triphosphate-sensitive potassium channels.

KATP channels play a crucial role in regulating insulin secretion and glucose metabolism, with their loss leading to constitutive depolarization and continuous release of insulin in beta-cells.

1999·684citations·L. Aguilar-Bryan et al.·Endocrine reviews

Endocrine reviews

DOI: 10.2170/JJPHYSIOL.48.397

ATP-sensitive potassium channels: structures, functions, and pathophysiology.

ATP-sensitive potassium channels (KATP channels) play crucial roles in coupling cell metabolic status to electrical activity, with their molecular basis being a complex of the Kir6.0 subunit and the SUR subunit, and their functional diversity determined by a combination of these subunits.

1998·58citations·N. Inagaki et al.·The Japanese journal of physiology

The Japanese journal of physiology

DOI: 10.1038/sj.bjp.0701756

Binding of KATP channel modulators in rat cardiac membranes

Binding studies with [3H]-P1075 are feasible in rat heart membranes in the presence of MgATP and an ATP-regenerating system, with a pharmacological profile distinct from that expected for SUR2A and SUR2B.

1998·30citations·Cornelia Löffler-Walz et al.·British Journal of Pharmacology

British Journal of Pharmacology