Evidence map›Paper›PMID 12034765›Full record

ArticleThe Journal of general physiology2002

Structural and functional determinants of conserved lipid interaction domains of inward rectifying Kir6.2 channels.

Catherine A Cukras, Iana Jeliazkova, Colin G Nichols

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. KATP Channels in the Cardiovascular System.Physiological reviews · 2016
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Channelopathies linked to plasma membrane phosphoinositides.Pflugers Archiv : European journal of physiology · 2010
    Review
  13. Article
  14. KirBac1.1: it's an inward rectifying potassium channel.The Journal of general physiology · 2009
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Interplay between PIP3 and calmodulin regulation of olfactory cyclic nucleotide-gated channels.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
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

3 authors at 1 institution in 1 country.

Catherine A CukrasDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Iana Jeliazkova
Colin G Nichols
Washington University in St. Louis · US

Funding

WU P&FP30DK020579 · NIDDK · WASHINGTON UNIVERSITY · PI Jennifer Lynn Powers Carson · 2013 to 2026
$27.1M
TRANSGENICS COREP60DK020579 · NIDDK · WASHINGTON UNIVERSITY · PI SCHAFFER, JEAN E. · 1986 to 2012
$25.2M
Rectification &Block of Ion Channel CurrentsR01HL054171 · NHLBI · WASHINGTON UNIVERSITY · PI NICHOLS, COLIN G · 1995 to 2017
$4.5M
NHLBI NIH HHS HL 54171NHLBI NIH HHS R01 HL054171NIDDK NIH HHS DK 20579NIDDK NIH HHS P30 DK020579NIDDK NIH HHS P60 DK020579
6 · The paper itself

Abstract

All members of the inward rectifiier K(+) (Kir) channel family are activated by phosphoinositides and other amphiphilic lipids. To further elucidate the mechanistic basis, we examined the membrane association of Kir6.2 fragments of K(ATP) channels, and the effects of site-directed mutations of these fragments and full-length Kir6.2 on membrane association and K(ATP) channel activity, respectively. GFP-tagged Kir6.2 COOH terminus and GFP-tagged pleckstrin homology domain from phospholipase C delta1 both associate with isolated membranes, and association of each is specifically reduced by muscarinic m1 receptor-mediated phospholipid depletion. Kir COOH termini are predicted to contain multiple beta-strands and a conserved alpha-helix (residues approximately 306-311 in Kir6.2). Systematic mutagenesis of D307-F315 reveals a critical role of E308, I309, W311 and F315, consistent with residues lying on one side of a alpha-helix. Together with systematic mutation of conserved charges, the results define critical determinants of a conserved domain that underlies phospholipid interaction in Kir channels.

Indexed as

AlanineAmino Acid SequenceAnimalsCell MembraneCOS CellsHydrogen-Ion ConcentrationIsoenzymesMolecular Sequence DataMutagenesisPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaPotassiumPotassium Channels, Inwardly RectifyingProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity RelationshipAlanineIsoenzymesPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaPotassiumPotassium Channels, Inwardly RectifyingType C Phospholipases

Identifiers

PMID12034765
PMCPMC2233865
OpenAlexW2085202839

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.