Evidence map›Paper›PMID 21844195›Full record

ArticleThe Journal of biological chemistry2011

Engineering a prokaryotic Cys-loop receptor with a third functional domain.

Raman Goyal, Ahmed Abdullah Salahudeen, Michaela Jansen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 45 citations in OpenAlex.

  1. RIC-3 Interacts Directly with the 5-HTbioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Identification of a binding site for bupropion inbioRxiv : the preprint server for biology · 2023
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. A Novel Glycine Receptor Variant with Startle Disease Affects Syndapin I and Glycinergic Inhibition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
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  17. Review
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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

3 authors at 2 institutions in 2 countries.

Raman GoyalDepartment of Cell Physiology and Molecular Biophysics, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, Texas 79430, USA.
Ahmed Abdullah Salahudeen
Michaela Jansen
Texas Tech University · USInstitute of Molecular Biology and Biophysics · RU

Funding

Nicotinic Acetylcholine Receptor Structure, Thermal Motion and GatingR00NS059841 · NINDS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI JANSEN, MICHAELA · 2009 to 2011
$736k
Nicotinic Acetylcholine Receptor Structure, Thermal Motion and GatingK99NS059841 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI JANSEN, MICHAELA · 2007 to 2008
$180k
NINDS NIH HHS K99 NS059841NINDS NIH HHS NS059841NINDS NIH HHS R00 NS059841
6 · The paper itself

Abstract

Prokaryotic members of the Cys-loop receptor ligand-gated ion channel superfamily were recently identified. Previously, Cys-loop receptors were only known from multicellular organisms (metazoans). Contrary to the metazoan Cys-loop receptors, the prokaryotic ones consist of an extracellular (ECD) and a transmembrane domain (TMD), lacking the large intracellular domain (ICD) present in metazoa (between transmembrane segments M3 and M4). Using a chimera approach, we added the 115-amino acid ICD from mammalian serotonin type 3A receptors (5-HT(3A)) to the prokaryotic proton-activated Gloeobacter violaceus ligand-gated ion channel (GLIC). We created 12 GLIC-5-HT(3A)-ICD chimeras by replacing a variable number of amino acids in the short GLIC M3M4 linker with the entire 5-HT(3A)-ICD. Two-electrode voltage clamp recordings after expression in Xenopus laevis oocytes showed that only two chimeras were functional and produced currents upon acidification. The pH(50) was comparable with wild-type GLIC. 5-HT(3A) receptor expression can be inhibited by the chaperone protein RIC-3. We have shown previously that the 5-HT(3A)-ICD is required for the attenuation of 5-HT-induced currents when RIC-3 is co-expressed with 5-HT(3A) receptors in X. laevis oocytes. Expression of both functional 5-HT(3A) chimeras was inhibited by RIC-3 co-expression, indicating appropriate folding of the 5-HT(3A)-ICD in the chimeras. Our results indicate that the ICD can be considered a separate domain that can be removed from or added to the ECD and TMD while maintaining the overall structure and function of the ECD and TMD.

Indexed as

Amino AcidsAnimalsCyanobacteriaCysteineEscherichia coliHorsesHydrogen-Ion ConcentrationIonsLigandsLipid BilayersOocytesPatch-Clamp TechniquesPlasmidsProtein ConformationProtein EngineeringProtein Structure, TertiaryAmino AcidsCysteineIonsLigandsLipid BilayersReceptors, Serotonin, 5-HT3

Identifiers

PMID21844195
PMCPMC3186389
OpenAlexW2040228066

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.