Evidence map›Paper›PMID 37405651›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Affinity Maturation of the Natural Ligand (B7-H6) for Natural Cytotoxicity Receptor NKp30 by Yeast Surface Display.

Stefan Zielonka, Simon Krah, Paul Arras, Britta Lipinski, Jasmin Zimmermann, Ammelie Svea Boje, Katja Klausz, Matthias Peipp, Lukas Pekar

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. NKp30: A Key Membrane Molecule in the Fight Against Cancer and Infection.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    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

9 authors at 3 institutions in 1 country.

Stefan ZielonkaProtein Engineering and Antibody Technologies (PEAT), Merck Healthcare KGaA, Darmstadt, Germany.
Simon KrahProtein Engineering and Antibody Technologies (PEAT), Merck Healthcare KGaA, Darmstadt, Germany.
Paul ArrasProtein Engineering and Antibody Technologies (PEAT), Merck Healthcare KGaA, Darmstadt, Germany.
Britta LipinskiProtein Engineering and Antibody Technologies (PEAT), Merck Healthcare KGaA, Darmstadt, Germany.
Jasmin ZimmermannProtein Engineering and Antibody Technologies (PEAT), Merck Healthcare KGaA, Darmstadt, Germany.
Ammelie Svea BojeStem Cell Transplantation and Immunotherapy, Division of Antibody-Based Immunotherapy, Department of Medicine II, Christian Albrechts University Kiel and University Medical Center Schleswig-Holstein, Kiel, Germany.
Katja KlauszStem Cell Transplantation and Immunotherapy, Division of Antibody-Based Immunotherapy, Department of Medicine II, Christian Albrechts University Kiel and University Medical Center Schleswig-Holstein, Kiel, Germany.
Matthias PeippStem Cell Transplantation and Immunotherapy, Division of Antibody-Based Immunotherapy, Department of Medicine II, Christian Albrechts University Kiel and University Medical Center Schleswig-Holstein, Kiel, Germany.
Lukas PekarProtein Engineering and Antibody Technologies (PEAT), Merck Healthcare KGaA, Darmstadt, Germany. Lukas.pekar@merckgroup.com.
Merck (Germany) · DEKiel University · DETechnical University of Darmstadt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years, the development of bispecific antibodies (bsAbs) has experienced tremendous progress for disease treatment, and consequently, a plethora of bsAbs is currently scrutinized in clinical trials. Besides antibody scaffolds, multifunctional molecules referred to as immunoligands have been developed. These molecules typically harbor a natural ligand entity for the engagement of a specific receptor, while binding to the additional antigen is facilitated by an antibody-derived paratope. Immunoligands can be exploited to conditionally activate immune cells, e.g., natural killer (NK) cells, in the presence of tumor cells, ultimately causing target-dependent tumor cell lysis. However, many ligands naturally show only moderate affinities toward their cognate receptor, potentially hampering killing capacities of immunoligands. Herein, we provide protocols for yeast surface display-based affinity maturation of B7-H6, the natural ligand of NK cell-activating receptor NKp30.

Indexed as

NeoplasmsSaccharomyces cerevisiaeB7 AntigensHumansKiller Cells, NaturalLigandsNatural Cytotoxicity Triggering Receptor 3B7 AntigensLigandsNatural Cytotoxicity Triggering Receptor 3Affinity maturationB7-H6BispecificsFluorescence-activated cell sortingImmunoligandNKp30Protein engineeringYeast surface display

Identifiers

PMID37405651
OpenAlexW4383186639

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.