Evidence map›Paper›PMID 26356202›Full record

ArticleACS chemical biology2015

Controlled Co-reconstitution of Multiple Membrane Proteins in Lipid Bilayer Nanodiscs Using DNA as a Scaffold.

Thomas Raschle, Chenxiang Lin, Ralf Jungmann, William M Shih, Gerhard Wagner

Abstract readLetter
In one paragraph

Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

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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

5 authors.

Thomas RaschleDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Chenxiang LinDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Ralf JungmannDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School , Boston, Massachusetts 02115, United States.
William M ShihDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Gerhard WagnerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School , Boston, Massachusetts 02115, United States.

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI LI, ZONGLI · 2001 to 2016
$23.7M
Structure and interactions of the Voltage-Dependent Anion Channel(VDAC)R01GM075879 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 2005 to 2013
$2.3M
NIGMS NIH HHS GM075879NIGMS NIH HHS P01 GM047467NIGMS NIH HHS P01 GM062580NIGMS NIH HHS P01 GM62580NIGMS NIH HHS R01 GM075879
6 · The paper itself

Abstract

Nanodiscs constitute a tool for the solubilization of membrane proteins in a lipid bilayer, thus offering a near-native membrane environment. Many membrane proteins interact with other membrane proteins; however, the co-reconstitution of multiple membrane proteins in a single nanodisc is a random process that is adversely affected by several factors, including protein aggregation. Here, we present an approach for the controlled co-reconstitution of multiple membrane proteins in a single nanodisc. The temporary attachment of designated oligonucleotides to individual membrane proteins enables the formation of stable, detergent-solubilized membrane protein complexes by base-pairing of complementary oligonucleotide sequences, thus facilitating the insertion of the membrane protein complex into nanodiscs with defined stoichiometry and composition. As a proof of principle, nanodiscs containing a heterodimeric and heterotrimeric membrane protein complex were reconstituted using a fluorescently labeled voltage-gated anion channel (VDAC) as a model system.

Indexed as

DNAFluorescent DyesIon ChannelsLipid BilayersMembrane ProteinsMicroscopy, FluorescenceModels, BiologicalNanostructuresNuclear MatrixDNAFluorescent DyesIon ChannelsLipid BilayersMembrane Proteins

Identifiers

PMID26356202
PMCPMC4769731

What OpenQuestion holds

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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.