Evidence map›Paper›PMID 35482190›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Affinity and Stability Analysis of Yeast Displayed Proteins.

Charlotte U Zajc, Magdalena Teufl, Michael W Traxlmayr

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
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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

3 authors.

Charlotte U ZajcDepartment of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Magdalena TeuflDepartment of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Michael W TraxlmayrDepartment of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences, Vienna, Austria. michael.traxlmayr@boku.ac.at.

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Yeast surface display is a powerful protein engineering technology that is extensively used to improve various properties of proteins, including affinity, specificity, and stability or even to add novel functions (usually ligand binding). Apart from its robustness and versatility as an engineering tool, yeast display offers a further critical advantage: Once the selection campaign is finished, usually resulting in an oligoclonal pool, these enriched protein variants can be analyzed individually on the surface of yeast without the need for any sub-cloning, soluble expression, and purification. Here, we provide detailed protocols for determining both the affinity and the thermal stability of yeast displayed proteins. In addition, we discuss the advantages, challenges, and potential pitfalls associated with affinity and stability analysis using yeast surface display.

Indexed as

Fungal ProteinsSaccharomyces cerevisiaeProtein EngineeringFungal ProteinsAffinity analysisLigand depletionProtein engineeringProtein stabilityThermal stability

Identifiers

What OpenQuestion holds

Textmetadata
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.