Evidence map›Paper›PMID 35337108›Full record

ArticlePharmaceuticals (Basel, Switzerland)2022

Rethinking Protein Drug Design with Highly Accurate Structure Prediction of Anti-CRISPR Proteins.

Ho-Min Park, Yunseol Park, Joris Vankerschaver, Arnout Van Messem, Wesley De Neve, Hyunjin Shim

Abstract read
In one paragraph

Article in Pharmaceuticals (Basel, Switzerland), 2022. 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
–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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. AcrDB update: Predicted 3D structures of anti-CRISPRs in human gut viromes.Protein science : a publication of the Protein Society · 2025
    Article
  7. FoldX force field revisited, an improved version.Bioinformatics (Oxford, England) · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. AlphaFold2 and its applications in the fields of biology and medicine.Signal transduction and targeted therapy · 2023
    Review
  12. Review
  13. Deep learning in CRISPR-Cas systems: a review of recent studies.Frontiers in bioengineering and biotechnology · 2023
    Review
  14. Article
  15. AlphaFold, Artificial Intelligence (AI), and Allostery.The journal of physical chemistry. B · 2022
    Review
  16. 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

6 authors.

Ho-Min ParkCenter for Biosystems and Biotech Data Science, Ghent University Global Campus, Incheon 21985, Korea.ORCID 0000-0001-9937-8617
Yunseol ParkCenter for Biosystems and Biotech Data Science, Ghent University Global Campus, Incheon 21985, Korea.ORCID 0000-0002-2005-1847
Joris VankerschaverCenter for Biosystems and Biotech Data Science, Ghent University Global Campus, Incheon 21985, Korea.ORCID 0000-0002-5813-5659
Arnout Van MessemDepartment of Mathematics, University of Liège, 4000 Liège, Belgium.ORCID 0000-0001-8545-7437
Wesley De NeveCenter for Biosystems and Biotech Data Science, Ghent University Global Campus, Incheon 21985, Korea.
Hyunjin ShimCenter for Biosystems and Biotech Data Science, Ghent University Global Campus, Incheon 21985, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein therapeutics play an important role in controlling the functions and activities of disease-causing proteins in modern medicine. Despite protein therapeutics having several advantages over traditional small-molecule therapeutics, further development has been hindered by drug complexity and delivery issues. However, recent progress in deep learning-based protein structure prediction approaches, such as AlphaFold2, opens new opportunities to exploit the complexity of these macro-biomolecules for highly specialised design to inhibit, regulate or even manipulate specific disease-causing proteins. Anti-CRISPR proteins are small proteins from bacteriophages that counter-defend against the prokaryotic adaptive immunity of CRISPR-Cas systems. They are unique examples of natural protein therapeutics that have been optimized by the host-parasite evolutionary arms race to inhibit a wide variety of host proteins. Here, we show that these anti-CRISPR proteins display diverse inhibition mechanisms through accurate structural prediction and functional analysis. We find that these phage-derived proteins are extremely distinct in structure, some of which have no homologues in the current protein structure domain. Furthermore, we find a novel family of anti-CRISPR proteins which are structurally similar to the recently discovered mechanism of manipulating host proteins through enzymatic activity, rather than through direct inference. Using highly accurate structure prediction, we present a wide variety of protein-manipulating strategies of anti-CRISPR proteins for future protein drug design.

Indexed as

AlphaFoldanti-CRISPR proteinsbacteriophagesin-silico drug designprokaryotic defence mechanismsprotein drugstructural biology

Identifiers

PMID35337108
PMCPMC8949011

What OpenQuestion holds

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Registered trials

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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.