Evidence map›Paper›PMID 27041595›Full record

ArticleStructure (London, England : 1993)2016

Manipulation of Subunit Stoichiometry in Heteromeric Membrane Proteins.

Claudio L Morales-Perez, Colleen M Noviello, Ryan E Hibbs

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing 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

107 citing papers in PubMed.

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  20. Structure of the human KNature structural & molecular biology · 2025
    Article

47 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Claudio L Morales-PerezDepartments of Neuroscience and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Colleen M NovielloDepartments of Neuroscience and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Ryan E HibbsDepartments of Neuroscience and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: ryan.hibbs@utsouthwestern.edu.

Funding

3D Structure and Function of Neuronal Nicotinic Acetylcholine ReceptorsR00NS077983 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2012 to 2014
$735k
The Cellular Biophysics of the Neuron Training ProgramT32NS069562 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI KAVALALI, EGE T · 2010 to 2014
$568k
Structural biology of the alpha4beta2 nicotinic acetylcholine receptorR21DA037492 · NIDA · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2014 to 2015
$368k
Howard Hughes Medical InstituteNIDA NIH HHS R21 DA037492NINDS NIH HHS R00 NS077983NINDS NIH HHS T32 NS069562
6 · The paper itself

Abstract

The ability of oligomeric membrane proteins to assemble in different functional ratios of subunits is a common feature across many systems. Recombinant expression of hetero-oligomeric proteins with defined stoichiometries facilitates detailed structural and functional analyses, but remains a major challenge. Here we present two methods for overcoming this challenge: one for rapid virus titration and another for stoichiometry determination. When these methods are coupled, they allow for efficient dissection of the heteromer stoichiometry problem and optimization of homogeneous protein expression. We demonstrate the utility of the methods in a system that to date has proved resistant to atomic-scale structural study, the nicotinic acetylcholine receptor. Leveraging these two methods, we have successfully expressed, purified, and grown diffraction-quality crystals of this challenging target.

Indexed as

Protein MultimerizationBaculoviridaeCrystallography, X-RayHEK293 CellsHumansProtein SubunitsReceptors, NicotinicProtein SubunitsReceptors, Nicotinic

Identifiers

PMID27041595
PMCPMC4856541

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Registered trials

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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.