Evidence map›Paper›PMID 18824232›Full record

ArticleProtein expression and purification2009

Mocr: a novel fusion tag for enhancing solubility that is compatible with structural biology applications.

James DelProposto, Chinmay Y Majmudar, Janet L Smith, William Clay Brown

Open access · greenAbstract read
In one paragraph

Article in Protein expression and purification, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.2field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 68 citations in OpenAlex.

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  5. Structure of a modular polyketide synthase reducing region.Structure (London, England : 1993) · 2023
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  6. Review
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  8. Article
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  12. Structural and dynamical rationale for fatty acid unsaturation inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. An Evolution-Based Approach to De Novo Protein Design.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  17. Current strategies for protein production and purification enabling membrane protein structural biology.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

James DelPropostoHigh-throughput Protein Lab, Center for Structural Biology, Life Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, Michigan 48109, USA.
Chinmay Y Majmudar
Janet L Smith
William Clay Brown
University of Michigan–Ann Arbor · USHigh Throughput Biology (United States) · US

Funding

STRUCTURE AND FUNCTION OF A PURINE BIOSYNTHETIC ENZYMER01DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1990 to 2024
$6.6M
Probing Transcriptional Activation at the Molecular Level - Equipment SupplementR01GM065330 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MAPP, ANNA K. · 2002 to 2019
$4.2M
NIDDK NIH HHS R01 DK042303NIGMS NIH HHS GM65330NIGMS NIH HHS R01 GM065330
6 · The paper itself

Abstract

A persistent problem in heterologous protein production is insolubility of the target protein when expressed to high level in the host cell. A widely employed strategy for overcoming this problem is the use of fusion tags. The best fusion tags promote solubility, may function as purification handles and either do not interfere with downstream applications or may be removed from the passenger protein preparation. A novel fusion tag is identified that meets these criteria. This fusion tag is a monomeric mutant of the Ocr protein (0.3 gene product) of bacteriophage T7. This fusion tag displays solubilizing activity with a variety of different passenger proteins. We show that it may be used as a purification handle similar to other fusion tags. Its small size and compact structure are compatible with its use in downstream applications of the passenger protein or it may be removed and purified away from the passenger protein. The use of monomeric Ocr (Mocr) as a complement to other fusion tags such as maltose-binding protein will provide greater flexibility in protein production and processing for a wide variety of protein applications.

Indexed as

Amino Acid SubstitutionChromatography, LiquidCloning, MolecularEthanolaminesPolymerase Chain ReactionProtein Array AnalysisProtein Structure, QuaternaryRecombinant Fusion ProteinsSequence Analysis, ProteinSolubilityViral Proteins2-diethylaminoethanolEthanolaminesOcr protein, bacteriophage T7Recombinant Fusion ProteinsViral Proteins

Identifiers

PMID18824232
PMCPMC2936452
OpenAlexW1965858950

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.