Evidence map›Paper›PMID 36252041›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

A generic framework for hierarchical de novo protein design.

Zander Harteveld, Jaume Bonet, Stéphane Rosset, Che Yang, Fabian Sesterhenn, Bruno E Correia

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. The structural landscape of the immunoglobulin fold by large-scale de novo design.Protein science : a publication of the Protein Society · 2024
    Article
  3. Review
  4. Article
  5. De novo design of stable proteins that efficaciously inhibit oncogenic G proteins.Protein science : a publication of the Protein Society · 2023
    Article
  6. bioRxiv : the preprint server for biology · 2023
    Article
  7. Review
  8. De novo protein fold design through sequence-independent fragment assembly simulations.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. A generic framework for hierarchical de novo protein design.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. 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

6 authors.

Zander HarteveldInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, CH-1015, Switzerland.
Jaume BonetInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, CH-1015, Switzerland.
Stéphane RossetInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, CH-1015, Switzerland.ORCID 0000-0002-8443-6017
Che YangInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, CH-1015, Switzerland.ORCID 0000-0002-4591-5373
Fabian SesterhennInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, CH-1015, Switzerland.
Bruno E CorreiaInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, CH-1015, Switzerland.ORCID 0000-0002-7377-8636

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

De novo protein design enables the exploration of novel sequences and structures absent from the natural protein universe. De novo design also stands as a stringent test for our understanding of the underlying physical principles of protein folding and may lead to the development of proteins with unmatched functional characteristics. The first fundamental challenge of de novo design is to devise "designable" structural templates leading to sequences that will adopt the predicted fold. Here, we built on the TopoBuilder (TB) de novo design method, to automatically assemble structural templates with native-like features starting from string descriptors that capture the overall topology of proteins. Our framework eliminates the dependency of hand-crafted and fold-specific rules through an iterative, data-driven approach that extracts geometrical parameters from structural tertiary motifs. We evaluated the TopoBuilder framework by designing sequences for a set of five protein folds and experimental characterization revealed that several sequences were folded and stable in solution. The TopoBuilder de novo design framework will be broadly useful to guide the generation of artificial proteins with customized geometries, enabling the exploration of the protein universe.

Indexed as

Protein FoldingProteinsModels, MolecularProtein EngineeringProteinscomputational biologyde novo designprotein designprotein topological descriptors

Identifiers

PMID36252041
PMCPMC9618129

What OpenQuestion holds

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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.