Evidence map›Paper›PMID 25620679›Full record

ArticleChembiochem : a European journal of chemical biology2015

Shear-stress-mediated refolding of proteins from aggregates and inclusion bodies.

Tom Z Yuan, Callum F G Ormonde, Stephan T Kudlacek, Sameeran Kunche, Joshua N Smith, William A Brown, Kaitlin M Pugliese, Tivoli J Olsen, Mariam Iftikhar, Colin L Raston and 1 more

Open access · greenAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 94 citations in OpenAlex.

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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

11 authors at 3 institutions in 2 countries.

Tom Z YuanUniversity of California, Irvine, Department of Molecular Biology and Biochemistry, Irvine, CA, 92697-2025 (USA).
Callum F G Ormonde
Stephan T Kudlacek
Sameeran Kunche
Joshua N Smith
William A Brown
Kaitlin M Pugliese
Tivoli J Olsen
Mariam Iftikhar
Colin L Raston
Gregory A Weiss
University of California, Irvine · USFlinders University · AUUniversity of Western Australia · AU

Funding

Membrane Protein Co- Crystallization with Highly Crystalline and Soluble ProteinsR01GM100700 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WEISS, GREGORY A. · 2012 to 2015
$1.1M
NIGMS NIH HHS R01 GM100700NIGMS NIH HHS R01 GM100700-01
6 · The paper itself

Abstract

Recombinant protein overexpression of large proteins in bacteria often results in insoluble and misfolded proteins directed to inclusion bodies. We report the application of shear stress in micrometer-wide, thin fluid films to refold boiled hen egg white lysozyme, recombinant hen egg white lysozyme, and recombinant caveolin-1. Furthermore, the approach allowed refolding of a much larger protein, cAMP-dependent protein kinase A (PKA). The reported methods require only minutes, which is more than 100 times faster than conventional overnight dialysis. This rapid refolding technique could significantly shorten times, lower costs, and reduce waste streams associated with protein expression for a wide range of industrial and research applications.

Indexed as

Green Chemistry TechnologyProtein RefoldingCatalytic DomainCaveolin 1Cyclic AMP-Dependent Protein KinasesEquipment DesignInclusion BodiesMuramidaseProtein Structure, SecondaryRecombinant ProteinsCaveolin 1Cyclic AMP-Dependent Protein Kinaseshen egg lysozymeMuramidaseRecombinant Proteinsgreen chemistryprotein expressionprotein foldingshear stress

Identifiers

PMID25620679
PMCPMC4388321
OpenAlexW2022713185

What OpenQuestion holds

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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.