Evidence map›Paper›PMID 30674983›Full record

ArticleScientific reports2019

An improved yeast surface display platform for the screening of nanobody immune libraries.

Tomasz Uchański, Thomas Zögg, Jie Yin, Daopeng Yuan, Alexandre Wohlkönig, Baptiste Fischer, Daniel M Rosenbaum, Brian K Kobilka, Els Pardon, Jan Steyaert

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

67 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Orally available designed miniproteins inhibit enterotoxigenicbioRxiv : the preprint server for biology · 2026
    Article
  3. EngineeringMicroorganisms · 2026
    Article
  4. Article
  5. KRASScience advances · 2026
    Article
  6. Review
  7. Review
  8. Yeast-mediated display: probingIranian journal of microbiology · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Epitope-directed selection of GPCR nanobody ligands with evolvable function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. A facile yeast-display approach for antibody mask discovery.Protein engineering, design & selection : PEDS · 2025
    Article
  17. Review
  18. Review
  19. Review
  20. Review

7 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 3 countries.

Tomasz UchańskiStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.ORCID 0000-0001-8456-4206
Thomas ZöggStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.ORCID 0000-0003-0454-4227
Jie YinDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390, USA.
Daopeng YuanBeijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Medicine, Tsinghua University, Beijing, 100084, China.
Alexandre WohlkönigStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.ORCID 0000-0003-3103-5022
Baptiste FischerStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.ORCID 0000-0001-9620-921X
Daniel M RosenbaumDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390, USA.
Brian K KobilkaBeijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Medicine, Tsinghua University, Beijing, 100084, China.
Els PardonStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.ORCID 0000-0002-2466-0172
Jan SteyaertStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium. jan.steyaert@vub.ac.be.ORCID 0000-0002-3825-874X
Vrije Universiteit Brussel · BECenter for Life Sciences · CNThe University of Texas Southwestern Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fusions to the C-terminal end of the Aga2p mating adhesion of Saccharomyces cerevisiae have been used in many studies for the selection of affinity reagents by yeast display followed by flow cytometric analysis. Here we present an improved yeast display system for the screening of Nanobody immune libraries where we fused the Nanobody to the N-terminal end of Aga2p to avoid steric hindrance between the fused Nanobody and the antigen. Moreover, the display level of a cloned Nanobody on the surface of an individual yeast cell can be monitored through a covalent fluorophore that is attached in a single enzymatic step to an orthogonal acyl carrier protein (ACP). Additionally, the displayed Nanobody can be easily released from the yeast surface and immobilised on solid surfaces for rapid analysis. To prove the generic nature of this novel Nanobody discovery platform, we conveniently selected Nanobodies against three different antigens, including two membrane proteins.

Indexed as

Cell Adhesion MoleculesGene LibrarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSingle-Domain AntibodiesAGA2 protein, S cerevisiaeCell Adhesion MoleculesSaccharomyces cerevisiae ProteinsSingle-Domain Antibodies

Identifiers

PMID30674983
PMCPMC6344588
OpenAlexW2913432304

What OpenQuestion holds

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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.