Evidence map›Paper›PMID 20394823›Full record

ArticleJournal of structural biology2010

High-throughput expression and purification of membrane proteins.

Filippo Mancia, James Love

Abstract read
In one paragraph

Article in Journal of structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 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

2 authors.

Filippo ManciaDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY, USA.
James Love

Funding

Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI GOUAUX, JAMES E · 2005 to 2009
$16.8M
NIGMS NIH HHS GM075026NIGMS NIH HHS U54 GM075026
6 · The paper itself

Abstract

High-throughput (HT) methodologies have had a tremendous impact on structural biology of soluble proteins. High-resolution structure determination relies on the ability of the macromolecule to form ordered crystals that diffract X-rays. While crystallization remains somewhat empirical, for a given protein, success is proportional to the number of conditions screened and to the number of variants trialed. HT techniques have greatly increased the number of targets that can be trialed and the rate at which these can be produced. In terms of number of structures solved, membrane proteins appear to be lagging many years behind their soluble counterparts. Likewise, HT methodologies for production and characterization of these hydrophobic macromolecules are only now emerging. Presented here is an HT platform designed exclusively for membrane proteins that has processed over 5000 targets.

Indexed as

Bacterial ProteinsCrystallography, X-RayDetergentsElectrophoresis, Polyacrylamide GelMembrane ProteinsProkaryotic CellsProtein StabilityProteomicsRecombinant ProteinsSpectrophotometry, UltravioletBacterial ProteinsDetergentsMembrane ProteinsRecombinant Proteins

Identifiers

PMID20394823
PMCPMC2933282

What OpenQuestion holds

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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.