Evidence map›Paper›PMID 39012010›Full record

ArticleProtein science : a publication of the Protein Society2024

Miniprotein engineering for inhibition of PD-1/PD-L1 interaction.

Agnieszka Ciesiołkiewicz, Juan Lizandra Perez, Lukasz Skalniak, Paweł Noceń, Łukasz Berlicki

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Miniprotein engineering for inhibition of PD-1/PD-L1 interaction.Protein science : a publication of the Protein Society · 2024
    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

5 authors.

Agnieszka CiesiołkiewiczDepartment of Bioorganic Chemistry, Wrocław University of Science and Technology, Wrocław, Poland.
Juan Lizandra PerezDepartment of Bioorganic Chemistry, Wrocław University of Science and Technology, Wrocław, Poland.
Lukasz SkalniakFaculty of Chemistry, Jagiellonian University, Kraków, Poland.
Paweł NoceńDepartment of Bioorganic Chemistry, Wrocław University of Science and Technology, Wrocław, Poland.
Łukasz BerlickiDepartment of Bioorganic Chemistry, Wrocław University of Science and Technology, Wrocław, Poland.ORCID 0000-0003-0318-4944

Funding

National Science Centre, Poland 2018/31/B/ST5/02631
6 · The paper itself

Abstract

Miniproteins constitute an excellent basis for the development of structurally demanding functional molecules. The engrailed homeodomain, a three-helix-containing miniprotein, was applied as a scaffold for constructing programmed cell death protein 1/programmed death-ligand 1 (PD-1/PD-L1) interaction inhibitors. PD-L1 binders were initially designed using the computer-aided approach and subsequently optimized iteratively. The conformational stability was assessed for each obtained miniprotein using circular dichroism spectroscopy, indicating that numerous mutations could be introduced. The formation of a sizable hydrophobic surface at the inhibitor that fits the molecular target imposed the necessity for the incorporation of additional charged amino acid residues to retain its appropriate solubility. Finally, the miniprotein effectively binding to PD-L1 (K

Indexed as

B7-H1 AntigenProgrammed Cell Death 1 ReceptorProtein EngineeringHomeodomain ProteinsHumansModels, MolecularProtein BindingB7-H1 AntigenCD274 protein, humanHomeodomain ProteinsPDCD1 protein, humanProgrammed Cell Death 1 Receptorcancercircular dichroismimmunotherapypeptidesprotein–protein interactions

Identifiers

PMID39012010
PMCPMC11250529

What OpenQuestion holds

Textmetadata
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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.