Evidence map›Paper›PMID 22027370›Full record

ArticleNew biotechnology2012

Expressing the human proteome for affinity proteomics: optimising expression of soluble protein domains and in vivo biotinylation.

Tracy Keates, Christopher D O Cooper, Pavel Savitsky, Charles K Allerston, Claire Phillips, Martin Hammarström, Neha Daga, Georgina Berridge, Pravin Mahajan, Nicola A Burgess-Brown and 3 more

Abstract read
In one paragraph

Article in New biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
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  13. Several affinity tags commonly used in chromatographic purification.Journal of analytical methods in chemistry · 2013
    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

13 authors.

Tracy KeatesThe Structural Genomics Consortium, University of Oxford, ORCRB, Roosevelt Drive, Oxford OX3 7DQ, United Kingdom.
Christopher D O Cooper
Pavel Savitsky
Charles K Allerston
Claire Phillips
Martin Hammarström
Neha Daga
Georgina Berridge
Pravin Mahajan
Nicola A Burgess-Brown
Susanne Müller
Susanne Gräslund
Opher Gileadi

Funding

CIHRWellcome Trust 092809
6 · The paper itself

Abstract

The generation of affinity reagents to large numbers of human proteins depends on the ability to express the target proteins as high-quality antigens. The Structural Genomics Consortium (SGC) focuses on the production and structure determination of human proteins. In a 7-year period, the SGC has deposited crystal structures of >800 human protein domains, and has additionally expressed and purified a similar number of protein domains that have not yet been crystallised. The targets include a diversity of protein domains, with an attempt to provide high coverage of protein families. The family approach provides an excellent basis for characterising the selectivity of affinity reagents. We present a summary of the approaches used to generate purified human proteins or protein domains, a test case demonstrating the ability to rapidly generate new proteins, and an optimisation study on the modification of >70 proteins by biotinylation in vivo. These results provide a unique synergy between large-scale structural projects and the recent efforts to produce a wide coverage of affinity reagents to the human proteome.

Indexed as

AnimalsBiotinBiotinylationChromatography, AffinityCrystallizationCulture MediaGenesHumansMass SpectrometryPlasmidsProtein Structure, TertiaryProteomeProteomicsSolubilityBiotinCulture MediaProteome

Identifiers

PMID22027370
PMCPMC3383991

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.