Evidence map›Paper›PMID 12547773›Full record

ArticleBiophysical journal2003

Permeant cations and blockers modulate pH gating of ROMK channels.

H Sackin, A Vasilyev, L G Palmer, M Krambis

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. A mathematical model of the rat kidney. IV. Whole kidney response to hyperkalemia.American journal of physiology. Renal physiology · 2022
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  5. Inhibition of ROMK channels by low extracellular K+ and oxidative stress.American journal of physiology. Renal physiology · 2013
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  7. Review
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  16. Review
  17. Functional characterization of a prokaryotic Kir channel.The Journal of biological chemistry · 2004
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  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

H SackinDepartment of Physiology and Biophysics, The Chicago Medical School, North Chicago, Illinois 60064, USA. sackinh@mis.finchcms.edu
A Vasilyev
L G Palmer
M Krambis
Rosalind Franklin University of Medicine and Science · US

Funding

MOLECULAR CLONING OF EPITHELIAL K CHANNELSR01DK046950 · NIDDK · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI SACKIN, HENRY · 1996 to 2017
$5.4M
MEMBRANE PROCESSES MEDIATING NACL TRANSPORTR01DK027847 · NIDDK · WEILL MEDICAL COLL OF CORNELL UNIV · PI PALMER, LAWRENCE G · 1986 to 2013
$4.8M
Molecular Cloning of Epithelial K ChannelsR56DK046950 · NIDDK · ROSALIND FRANKLIN UNIV OF MEDICINE & SCI · PI SACKIN, HENRY · 2008 to 2008
$231k
NIDDK NIH HHS DK27847NIDDK NIH HHS DK46950NIDDK NIH HHS R01 DK027847NIDDK NIH HHS R01 DK046950NIDDK NIH HHS R56 DK046950
6 · The paper itself

Abstract

External potassium (K) activates the inward rectifier ROMK (K(ir)1.1) by altering the pH gating of the channel. The present study examines this link between external K and internal pH sensitivity using both the two-electrode voltage clamp and the perfused, cut-open Xenopus oocyte preparation. Elevating extracellular K from 1 mM to 10 mM to 100 mM activated ROMK channels by shifting their apparent pK(a) from 7.2 +/- 0.1 (n = 6) in 1 mM K, to 6.9 +/- 0.02 (n = 5) in 10 mM K, and to 6.6 +/- 0.03 (n = 5) in 100 mM K. At any given internal pH, the number of active ROMK channels is a saturating function of external [K]. Extracellular Cs (which blocks almost all inward K current) also stimulated outward ROMK conductance (at constant 1 mM external K) by shifting the apparent pK(a) of ROMK from 7.2 +/- 0.1 (n = 6) in 1 mM K to 6.8 +/- 0.01 (n = 4) in 1 mM K + 104 mM Cs. Surprisingly, the binding and washout of the specific blocker, Tertiapin-Q, also activated ROMK in 1 mM K and caused a comparable shift in apparent pK(a). These results are interpreted in terms of both a three-state kinetic model and a two-gate structural model that is based on results with KcsA in which the selectivity filter can assume either a high or low K conformation. In this context, external K, Cs, and Tertiapin-Q activate ROMK by destabilizing the low-K (collapsed) configuration of the selectivity filter.

Indexed as

Potassium Channels, Inwardly RectifyingAnimalsBee VenomsCells, CulturedDose-Response Relationship, DrugElectric ConductivityFemaleHydrogen-Ion ConcentrationIon Channel GatingModels, BiologicalMutagenesis, Site-DirectedOocytesPotassiumPotassium ChannelsRecombinant ProteinsSensitivity and SpecificityBee VenomsPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingRecombinant Proteinstertiapin

Identifiers

PMID12547773
PMCPMC1302669
OpenAlexW2103362423

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.