Evidence map›Paper›PMID 23415558›Full record

ArticleStructure (London, England : 1993)2013

Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility.

Manuel Etzkorn, Thomas Raschle, Franz Hagn, Vladimir Gelev, Amanda J Rice, Thomas Walz, Gerhard Wagner

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 109 citations in OpenAlex.

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  18. Journal of the American Chemical Society · 2017
    Article
  19. Article
  20. Solution NMR Spectroscopy in Target-Based Drug Discovery.Molecules (Basel, Switzerland) · 2017
    Review
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

7 authors at 1 institution in 1 country.

Manuel EtzkornDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Thomas Raschle
Franz Hagn
Vladimir Gelev
Amanda J Rice
Thomas Walz
Gerhard Wagner
Harvard University · US

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Project 4 (Goethe University of Frankfurt)U54GM094608 · NIGMS · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2014
$11.5M
800 MHz Triple Resonance Observe (TXO) Detection CryoProbeS10RR026417 · NCRR · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2010 to 2010
$359k
NCRR NIH HHS S10 RR026417NIBIB NIH HHS EB002026NIBIB NIH HHS P41 EB002026NIGMS NIH HHS GM047467NIGMS NIH HHS GM094608NIGMS NIH HHS P01 GM047467NIGMS NIH HHS U54 GM094608
6 · The paper itself

Abstract

Selecting a suitable membrane-mimicking environment is of fundamental importance for the investigation of membrane proteins. Nonconventional surfactants, such as amphipathic polymers (amphipols) and lipid bilayer nanodiscs, have been introduced as promising environments that may overcome intrinsic disadvantages of detergent micelle systems. However, structural insights into the effects of different environments on the embedded protein are limited. Here, we present a comparative study of the heptahelical membrane protein bacteriorhodopsin in detergent micelles, amphipols, and nanodiscs. Our results confirm that nonconventional environments can increase stability of functional bacteriorhodopsin, and demonstrate that well-folded heptahelical membrane proteins are, in principle, accessible by solution-NMR methods in amphipols and phospholipid nanodiscs. Our data distinguish regions of bacteriorhodopsin that mediate membrane/solvent contacts in the tested environments, whereas the protein's functional inner core remains almost unperturbed. The presented data allow comparing the investigated membrane mimetics in terms of NMR spectral quality and thermal stability required for structural studies.

Indexed as

Membranes, ArtificialBacteriorhodopsinsCulture MediaDetergentsEscherichia coliGene ExpressionHalobacterium salinarumLipid BilayersMembrane ProteinsMicellesModels, MolecularMolecular MimicryNuclear Magnetic Resonance, BiomolecularPhospholipidsProtein FoldingProtein StabilityBacteriorhodopsinsCulture MediaDetergentsLipid BilayersMembrane ProteinsMembranes, ArtificialMicellesPhospholipidsRecombinant Proteins

Identifiers

PMID23415558
PMCPMC3595385
OpenAlexW2009077514

What OpenQuestion holds

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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.