Evidence map›Paper›PMID 16284078›Full record

ArticleThe Journal of physiology2006

An amino-terminal lysine residue of rat connexin40 that is required for spermine block.

Xianming Lin, Edward Fenn, Richard D Veenstra

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  9. Review
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  13. Biological and biophysical properties of vascular connexin channels.International review of cell and molecular biology · 2009
    Review
  14. Article
  15. 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.

Xianming LinDepartment of Pharmacology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Edward Fenn
Richard D Veenstra
SUNY Upstate Medical University · US

Funding

GAP JUNCTIONS AND IONIC CURRENTS IN DEVELOPING HEARTR01HL042220 · NHLBI · UPSTATE MEDICAL UNIVERSITY · PI VEENSTRA, RICHARD DAVID, YANG, JENNY J. · 1988 to 2013
$3.1M
INTERCELLULAR COMMUNICATION IN THE HEARTR01HL045466 · NHLBI · WASHINGTON UNIVERSITY · PI BEYER, ERIC C · 1990 to 2003
$1.4M
NHLBI NIH HHS HL-42220NHLBI NIH HHS HL-45466NHLBI NIH HHS R01 HL042220NHLBI NIH HHS R01 HL045466
6 · The paper itself

Abstract

Spermine blocks connexin40 (Cx40) gap junctions, and two cytoplasmic amino-terminal domain glutamate residues are essential for this inhibitory activity. To further examine the molecular basis for block, we mutated a portion of a basic amino acid (HKH) motif on the Cx40 amino-terminal domain. Replacement of the Cx40 H15 + K16 residues with the Q15 + A16 sequence native to spermine-insensitive connexin43 (Cx43) gap junctions increased the equilibrium dissociation constant (K(d)) and reduced the maximum inhibition by spermine. The corresponding electrical distance (delta) approximation was decreased by about 50%. The transjunctional voltage (V(j))-dependent gating of homotypic Cx40 H15Q + K16A mutant gap junctions was also significantly reduced. The minimum normalized steady-state junctional conductance (G(min)) increased from 0.17 to 0.72, with an increase in the half-inactivation voltage from 48 to 60 mV. However, the unitary junctional conductance (gamma(j); 160 pS) was only slightly altered, and the relative cation/anion conductance and permeability ratios were unchanged from wild-type Cx40 gap junction channels. The relative K(+)/Cl(-) permeability (P(K)/P(Cl)) ratio increased from six to ten when [KCl] was reduced to 25% of normal. These data suggest that the HKH motif at positions 15-17 is important to the conformational structure of the putative voltage sensor and spermine receptor of Cx40, without causing significant alteration of the electrostatic surface charge potentials that contribute to the ion selectivity of this gap junction channel.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCell Line, TumorCell Membrane PermeabilityConnexin 43ConnexinsGap Junction alpha-5 ProteinGap JunctionsIon Channel GatingIon-Selective ElectrodesLysineMembrane PotentialsMiceMolecular Sequence DataMutationConnexin 43ConnexinsGap Junction alpha-5 ProteinLysineSpermine

Identifiers

PMID16284078
PMCPMC1464307
OpenAlexW2036525327

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.