Evidence map›Paper›PMID 14681015›Full record

ArticleCell communication & adhesion

Pore-lining residues identified by single channel SCAM studies in Cx46 hemichannels.

J Kronengold, E B Trexler, F F Bukauskas, T A Bargiello, V K Verselis

Abstract read
In one paragraph

Article in Cell communication & adhesion. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The NHAmerican journal of physiology. Cell physiology · 2017
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Functional effects of Cx50 mutations associated with congenital cataracts.American journal of physiology. Cell physiology · 2014
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors.

J KronengoldDepartment of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
E B Trexler
F F Bukauskas
T A Bargiello
V K Verselis

Funding

MECHANISMS OF GATING AND PERMEATION IN GAP JUNCTIONSR01GM054179 · NIGMS · YESHIVA UNIVERSITY · PI VERSELIS, VYTAUTAS K · 1996 to 2018
$5.3M
STRUCTURE/FUNCTION STUDIES OF GAP JUNCTIONSR01GM046889 · NIGMS · YESHIVA UNIVERSITY · PI BARGIELLO, THADDEUS ANDREW · 1992 to 2009
$3.8M
MECHANISMS OF INTERCELLULAR COMMUNICATIONT32NS007439 · NINDS · YESHIVA UNIVERSITY · PI VERSELIS, VYTAUTAS K · 1998 to 2013
$2.7M
Gap Junction Channels Formation and GatingR01NS036706 · NINDS · YESHIVA UNIVERSITY · PI BUKAUSKAS, FELIKSAS · 1999 to 2007
$2.3M
NIGMS NIH HHS GM54179NIGMS NIH HHS R01 GM046889NIGMS NIH HHS R01 GM054179NINDS NIH HHS R01 NS036706NINDS NIH HHS T32 NS007439NINDS NIH HHS TS-NS07439
6 · The paper itself

Abstract

The substituted cysteine accessibility method was applied to single Cx46 hemichannels to identify residues that participate in lining the aqueous pore of channels formed of connexins. Criteria for assignment to the pore included reactivity to sulfydryl-specific methanethiosulfonate (MTS) reagents from both sides of an open hemichannel and observable effects on open channel properties. We demonstrate reactivity to MTS reagents over a stretch of seventeen amino acids, D51 through L35, that constitute segments of E1 and TM1. Qualitatively, the nature of the effects caused by the Cys substitutions alone and their modification with MTS reagents of either charge indicate side chain valence is most influential in determining single channel properties with D51 and L35 defining the extracellular and intracellular limits, respectively, of the identified pore-lining region. A number of Cys substitutions beyond L35 in TM1 caused severe alterations in hemichannel function and precluded assignment to the pore. Although all six subunits can be modified by smaller MTS reagents, modifications appear limited to fewer subunits with larger reagents.

Indexed as

Amino Acid SubstitutionAnimalsConnexinsGap JunctionsIon ChannelsMesylatesModels, MolecularOocytesPatch-Clamp TechniquesProtein ConformationXenopus laevisConnexinsGJA3 protein, humanIon ChannelsMesylatesmethanethiosulfonate

Identifiers

PMID14681015
PMCPMC4516056

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.