Evidence map›Paper›PMID 22760604›Full record

ArticleThe Journal of membrane biology2012

Connexin composition in apposed gap junction hemiplaques revealed by matched double-replica freeze-fracture replica immunogold labeling.

John E Rash, Naomi Kamasawa, Kimberly G V Davidson, Thomas Yasumura, Alberto E Pereda, James I Nagy

Open access · hybridAbstract read
In one paragraph

Article in The Journal of membrane biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

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  6. Connexins and Disease.Cold Spring Harbor perspectives in biology · 2018
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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

6 authors at 4 institutions in 2 countries.

John E RashDepartment of Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA. john.rash@colostate.edu
Naomi Kamasawa
Kimberly G V Davidson
Thomas Yasumura
Alberto E Pereda
James I Nagy
Colorado State University · USAlbert Einstein College of Medicine · USMax Planck Florida Institute for Neuroscience · USUniversity of Manitoba · CA

Funding

Connexins in Neuronal and Glial Gap Junctions in the Central Nervous SystemR01NS044395 · NINDS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI RASH, JOHN E · 2002 to 2012
$3.5M
Control of Junctional Conductance at Auditory AfferentsR01DC003186 · NIDCD · YESHIVA UNIVERSITY · PI PEREDA, ALBERTO E · 2002 to 2006
$1.7M
Control of Junctional Conductance at Auditory AfferentR56DC003186 · NIDCD · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI PEREDA, ALBERTO E · 2009 to 2009
$429k
Connexins in Neuronal and Glial Gap Junctions in the Central Nervous SystemR56NS044395 · NINDS · COLORADO STATE UNIVERSITY · PI RASH, JOHN E · 2007 to 2007
$360k
Zeiss LSM 510 Laser Scanning MicroscopeS10RR015706 · NCRR · COLORADO STATE UNIVERSITY-FORT COLLINS · PI RASH, JOHN E · 2002 to 2002
$341k
CONTROL OF JUNCTIONAL CONDUCTANCE AT AUDITORY AFFERENTSR29DC003186 · NIDCD · YESHIVA UNIVERSITY · PI PEREDA, ALBERTO E · 1997 to 2001
$238k
JEOL JFD-9010-CR FREEZE-FRACTURE MACHINES10RR008329 · NCRR · COLORADO STATE UNIVERSITY-FORT COLLINS · PI RASH, JOHN E · 1993 to 1993
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CIHRNCRR NIH HHS S10 RR015706NCRR NIH HHS S10 RR08329NIDCD NIH HHS DC03186NIDCD NIH HHS R01 DC003186NIDCD NIH HHS R29 DC003186NIDCD NIH HHS R56 DC003186NINDS NIH HHS NS044395NINDS NIH HHS NS0552827NINDS NIH HHS R01 NS044395NINDS NIH HHS R56 NS044395
6 · The paper itself

Abstract

Despite the combination of light-microscopic immunocytochemistry, histochemical mRNA detection techniques and protein reporter systems, progress in identifying the protein composition of neuronal versus glial gap junctions, determination of the differential localization of their constituent connexin proteins in two apposing membranes and understanding human neurological diseases caused by connexin mutations has been problematic due to ambiguities introduced in the cellular and subcellular assignment of connexins. Misassignments occurred primarily because membranes and their constituent proteins are below the limit of resolution of light microscopic imaging techniques. Currently, only serial thin-section transmission electron microscopy and freeze-fracture replica immunogold labeling have sufficient resolution to assign connexin proteins to either or both sides of gap junction plaques. However, freeze-fracture replica immunogold labeling has been limited because conventional freeze fracturing allows retrieval of only one of the two membrane fracture faces within a gap junction, making it difficult to identify connexin coupling partners in hemiplaques removed by fracturing. We now summarize progress in ascertaining the connexin composition of two coupled hemiplaques using matched double-replicas that are labeled simultaneously for multiple connexins. This approach allows unambiguous identification of connexins and determination of the membrane "sidedness" and the identities of connexin coupling partners in homotypic and heterotypic gap junctions of vertebrate neurons.

Indexed as

AnimalsAstrocytesConnexinsFreeze FracturingGap JunctionsHumansImmunohistochemistryNeuronsOligodendrogliaConnexins

Identifiers

PMID22760604
PMCPMC3401501
OpenAlexW2014074382

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.