Evidence map›Paper›PMID 38565617›Full record

ReviewNature reviews. Molecular cell biology2024

Opportunities and challenges in design and optimization of protein function.

Dina Listov, Casper A Goverde, Bruno E Correia, Sarel Jacob Fleishman

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
53.3field-weighted citation impact, top 1% 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

74 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
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  8. Evolutionary and physics-guided modulation of CaJournal of molecular modeling · 2026
    Article
  9. Article
  10. Review
  11. Review
  12. De novo design of RNA pseudoknots with deep learning.bioRxiv : the preprint server for biology · 2026
    Article
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  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
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14 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

Dina ListovDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.ORCID http://orcid.org/0000-0002-7378-1771
Casper A GoverdeInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
Bruno E CorreiaInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland. bruno.correia@epfl.ch.ORCID http://orcid.org/0000-0002-7377-8636
Sarel Jacob FleishmanDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel. sarel@weizmann.ac.il.ORCID http://orcid.org/0000-0003-3177-7560
École Polytechnique Fédérale de Lausanne · CHWeizmann Institute of Science · IL

Funding

European Research Council 815379
6 · The paper itself

Abstract

The field of protein design has made remarkable progress over the past decade. Historically, the low reliability of purely structure-based design methods limited their application, but recent strategies that combine structure-based and sequence-based calculations, as well as machine learning tools, have dramatically improved protein engineering and design. In this Review, we discuss how these methods have enabled the design of increasingly complex structures and therapeutically relevant activities. Additionally, protein optimization methods have improved the stability and activity of complex eukaryotic proteins. Thanks to their increased reliability, computational design methods have been applied to improve therapeutics and enzymes for green chemistry and have generated vaccine antigens, antivirals and drug-delivery nano-vehicles. Moreover, the high success of design methods reflects an increased understanding of basic rules that govern the relationships among protein sequence, structure and function. However, de novo design is still limited mostly to α-helix bundles, restricting its potential to generate sophisticated enzymes and diverse protein and small-molecule binders. Designing complex protein structures is a challenging but necessary next step if we are to realize our objective of generating new-to-nature activities.

Indexed as

Protein EngineeringProteinsAnimalsHumansModels, MolecularProtein ConformationProteins

Identifiers

PMID38565617
PMCPMC7616297
OpenAlexW4393552888

What OpenQuestion holds

Textmetadata
LicenceTDM
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.