Evidence map›Paper›PMID 28767110›Full record

ArticleLab on a chip2017

Microfluidic platform for efficient Nanodisc assembly, membrane protein incorporation, and purification.

James H Wade, Joshua D Jones, Ivan L Lenov, Colleen M Riordan, Stephen G Sligar, Ryan C Bailey

Open access · greenAbstract read
In one paragraph

Article in Lab on a chip, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Reconstituted HDL as a therapeutic delivery device.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
  6. DNA-Mediated Stack Formation of Nanodiscs.Molecules (Basel, Switzerland) · 2021
    Article
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 2 institutions in 1 country.

James H WadeDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Joshua D Jones
Ivan L Lenov
Colleen M Riordan
Stephen G Sligar
Ryan C Bailey
University of Illinois Urbana-Champaign · USUniversity of Michigan · US

Funding

Multiplexed Platform to Probe Interactions at the Model Cell Membrane InterfaceR01GM110432 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BAILEY, RYAN C · 2014 to 2017
$1.1M
Meso-plex miRNA and protein profiling for cancer diagnostics using chip-integrateR33CA177462 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BAILEY, RYAN C, JOHNSON, MARK D · 2013 to 2015
$984k
NCI NIH HHS R33 CA177462NIGMS NIH HHS R01 GM110432
6 · The paper itself

Abstract

The characterization of integral membrane proteins presents numerous analytical challenges on account of their poor activity under non-native conditions, limited solubility in aqueous solutions, and low expression in most cell culture systems. Nanodiscs are synthetic model membrane constructs that offer many advantages for studying membrane protein function by offering a native-like phospholipid bilayer environment. The successful incorporation of membrane proteins within Nanodiscs requires experimental optimization of conditions. Standard protocols for Nanodisc formation can require large amounts of time and input material, limiting the facile screening of formation conditions. Capitalizing on the miniaturization and efficient mass transport inherent to microfluidics, we have developed a microfluidic platform for efficient Nanodisc assembly and purification, and demonstrated the ability to incorporate functional membrane proteins into the resulting Nanodiscs. In addition to working with reduced sample volumes, this platform simplifies membrane protein incorporation from a multi-stage protocol requiring several hours or days into a single platform that outputs purified Nanodiscs in less than one hour. To demonstrate the utility of this platform, we incorporated Cytochrome P450 into Nanodiscs of variable size and lipid composition, and present spectroscopic evidence for the functional active site of the membrane protein. This platform is a promising new tool for membrane protein biology and biochemistry that enables tremendous versatility for optimizing the incorporation of membrane proteins using microfluidic gradients to screen across diverse formation conditions.

Indexed as

Membranes, ArtificialModels, BiologicalEquipment DesignMembrane ProteinsMicrofluidic Analytical TechniquesNanostructuresPhospholipidsMembrane ProteinsMembranes, ArtificialPhospholipids

Identifiers

PMID28767110
PMCPMC5589448
OpenAlexW2736534968

What OpenQuestion holds

Textmetadata
LicenceTDM
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.