Evidence map›Paper›PMID 28488120›Full record

ArticleApplied biochemistry and biotechnology2017

Efficient Antibody Assembly in E. coli Periplasm by Disulfide Bond Folding Factor Co-expression and Culture Optimization.

Carlos Rodriguez, Dong Hyun Nam, Evan Kruchowy, Xin Ge

Open access · greenAbstract read
In one paragraph

Article in Applied biochemistry and biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 26 citations in OpenAlex.

  1. Achieving protease substrate-specific inhibition by mAb dual functional selections.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Article
  4. Substrate derived sequences act as subsite-blocking motifs in protease inhibitory antibodies.Protein science : a publication of the Protein Society · 2023
    Article
  5. Article
  6. Article
  7. Evolution ofInternational journal of molecular sciences · 2020
    Review
  8. Article
  9. Article
  10. 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 1 institution in 1 country.

Carlos RodriguezDepartment of Chemical and Environmental Engineering, University of California, Riverside, 900 University Ave., Riverside, CA, 92521, USA.
Dong Hyun NamDepartment of Chemical and Environmental Engineering, University of California, Riverside, 900 University Ave., Riverside, CA, 92521, USA.
Evan KruchowyDepartment of Chemical and Environmental Engineering, University of California, Riverside, 900 University Ave., Riverside, CA, 92521, USA.
Xin GeDepartment of Chemical and Environmental Engineering, University of California, Riverside, 900 University Ave., Riverside, CA, 92521, USA. xge@engr.ucr.edu.ORCID http://orcid.org/0000-0001-7491-7805
University of California, Riverside · US

Funding

Structure-based design of camel-like human selective mAbs against MMPs in diseaseR01GM115672 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI GE, XIN · 2016 to 2020
$1.5M
Division of Chemical, Bioengineering, Environmental, and Transport Systems (US) 1453645National Institute of General Medical Sciences R01GM115672NIGMS NIH HHS R01 GM115672
6 · The paper itself

Abstract

Molecular chaperones and protein folding factors of bacterial periplasmic space play important roles in assisting disulfide bond formation and proper protein folding. In this study, effects of disulfide bond protein (Dsb) families were investigated on assembly of 3F3 Fab, an antibody inhibitor targeting matrix metalloproteinase-14 (MMP-14). By optimizing DsbA/C co-expression, promoter for 3F3 Fab, host strains, and culture media and conditions, a high yield of 30-mg purified 3F3 Fab per liter culture was achieved. Produced 3F3 Fab exhibited binding affinity of 34 nM and inhibition potency of 970 nM. This established method of DsbA/C co-expression can be applied to produce other important disulfide bond-dependent recombinant proteins in E. coli periplasm.

Indexed as

Protein FoldingEscherichia coliEscherichia coli ProteinsHumansImmunoglobulin Fab FragmentsPeriplasmProtein Disulfide-IsomerasesRecombinant ProteinsdsbA protein, E colidsbC protein, E coliEscherichia coli ProteinsImmunoglobulin Fab FragmentsProtein Disulfide-IsomerasesRecombinant ProteinsDsbADsbCFabIgGOver-expressionPeriplasmProtein folding factor

Identifiers

PMID28488120
PMCPMC5898612
OpenAlexW2613086300

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.