Evidence map›Paper›PMID 28299901›Full record

ArticleBiotechnology journal2017

Dual display of proteins on the yeast cell surface simplifies quantification of binding interactions and enzymatic bioconjugation reactions.

Sungwon Lim, Jeff E Glasgow, Maria Filsinger Interrante, Erica M Storm, Jennifer R Cochran

Open access · greenAbstract read
In one paragraph

Article in Biotechnology journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. A Rapid Antibody Enhancement Platform inACS synthetic biology · 2023
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  10. Article
  11. Article
  12. Review
  13. Article
  14. Engineered ACE2 receptor traps potently neutralize SARS-CoV-2.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Engineered ACE2 receptor traps potently neutralize SARS-CoV-2.bioRxiv : the preprint server for biology · 2020
    Article
  16. 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

5 authors at 3 institutions in 1 country.

Sungwon LimDept. of Bioengineering, Schools of Engineering and Medicine, Stanford University, Stanford, California, USA.
Jeff E GlasgowDept. of Bioengineering, Schools of Engineering and Medicine, Stanford University, Stanford, California, USA.
Maria Filsinger InterranteDept. of Bioengineering, Schools of Engineering and Medicine, Stanford University, Stanford, California, USA.
Erica M StormSchool of Medicine, Stanford University, Stanford, California, USA.
Jennifer R CochranDept. of Bioengineering, Schools of Engineering and Medicine, Stanford University, Stanford, California, USA.
Stanford Medicine · USStanford University · USPhysical Measurement Laboratory · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007365 · NIGMS · STANFORD UNIVERSITY · PI CHUA, KATRIN F · 1985 to 2021
$33.8M
Engineered HGF-NK1 antagonists for Met-targeted cancer imaging and therapyR01CA151706 · NCI · STANFORD UNIVERSITY · PI COCHRAN, JENNIFER R · 2010 to 2014
$1.6M
NCI NIH HHS R01 CA151706NIGMS NIH HHS T32 GM007365
6 · The paper itself

Abstract

Yeast surface display, a well-established technology for protein analysis and engineering, involves expressing a protein of interest as a genetic fusion to either the N- or C-terminus of the yeast Aga2p mating protein. Historically, yeast-displayed protein variants are flanked by peptide epitope tags that enable flow cytometric measurement of construct expression using fluorescent primary or secondary antibodies. Here, we built upon this technology to develop a new yeast display strategy that comprises fusion of two different proteins to Aga2p, one to the N-terminus and one to the C-terminus. This approach allows an antibody fragment, ligand, or receptor to be directly coupled to expression of a fluorescent protein readout, eliminating the need for antibody-staining of epitope tags to quantify yeast protein expression levels. We show that this system simplifies quantification of protein-protein binding interactions measured on the yeast cell surface. Moreover, we show that this system facilitates co-expression of a bioconjugation enzyme and its corresponding peptide substrate on the same Aga2p construct, enabling enzyme expression and catalytic activity to be measured on the surface of yeast.

Indexed as

AminoacyltransferasesBacterial ProteinsCell Adhesion MoleculesCell Surface Display TechniquesCysteine EndopeptidasesEnzyme AssaysGreen Fluorescent ProteinsModels, MolecularProtein BindingRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsAGA2 protein, S cerevisiaeAminoacyltransferasesBacterial ProteinsCell Adhesion MoleculesCysteine EndopeptidasesGreen Fluorescent ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteinssortase ABinding assayBioconjugationFluorescent proteinSortaseYeast surface display

Identifiers

PMID28299901
PMCPMC5708543
OpenAlexW2595111200

What OpenQuestion holds

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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.