Evidence map›Paper›PMID 38361074›Full record

ReviewNature biotechnology2024

Machine learning for functional protein design.

Pascal Notin, Nathan Rollins, Yarin Gal, Chris Sander, Debora Marks

Abstract readReview
In one paragraph

Review in Nature biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing 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

105 citing papers in PubMed.

  1. Artificial intelligence catalyzes antimicrobial peptide design.Synthetic and systems biotechnology · 2027
    Review
  2. Article
  3. Review
  4. Artificial intelligence-assisted lead optimization in drug discovery: bridging computational advances and translational challenges.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Evolutionary profiles for protein fitness prediction.Bioinformatics (Oxford, England) · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Genuine Directed Evolution In Test Tube (GENie).bioRxiv : the preprint server for biology · 2026
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Direct evidence of acid-driven protein desolvation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  19. Article
  20. Peptide-functionalized nanoparticles for brain-targeted therapeutics.Drug delivery and translational research · 2026
    Review

45 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

5 authors.

Pascal Notin *Department of Systems Biology, Harvard Medical School, Boston, MA, USA. pascal_notin@hms.harvard.edu.
Nathan Rollins *Seismic Therapeutic, Cambridge, MA, USA. nrollins.home@gmail.com.
Yarin GalDepartment of Computer Science, University of Oxford, Oxford, UK.
Chris SanderDepartment of Systems Biology, Harvard Medical School, Boston, MA, USA.
Debora MarksDepartment of Systems Biology, Harvard Medical School, Boston, MA, USA. debbie@hms.harvard.edu.ORCID http://orcid.org/0000-0001-9388-2281

Funding

TR&D 3 - Network Guided Machine LearningP41GM103504 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI IDEKER, TREY · 2012 to 2024
$17.3M
Making antibody generation rapid, scalable, and democratic through machine learning and continuous evolutionR01CA260415 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI KRUSE, ANDREW, LIU, CHANG C · 2020 to 2024
$8.4M
GlaxoSmithKline (GlaxoSmithKline plc.) 18000077NCI NIH HHS R01 CA260415NIGMS NIH HHS P41 GM103504RCUK | Engineering and Physical Sciences Research Council (EPSRC) 18000077RCUK | Engineering and Physical Sciences Research Council (EPSRC) V030302/1U.S. Department of Energy (DOE) DE-SC0022024U.S. Department of Health & Human Services | National Institutes of Health (NIH) 1R01CA260415
6 · The paper itself

Abstract

Recent breakthroughs in AI coupled with the rapid accumulation of protein sequence and structure data have radically transformed computational protein design. New methods promise to escape the constraints of natural and laboratory evolution, accelerating the generation of proteins for applications in biotechnology and medicine. To make sense of the exploding diversity of machine learning approaches, we introduce a unifying framework that classifies models on the basis of their use of three core data modalities: sequences, structures and functional labels. We discuss the new capabilities and outstanding challenges for the practical design of enzymes, antibodies, vaccines, nanomachines and more. We then highlight trends shaping the future of this field, from large-scale assays to more robust benchmarks, multimodal foundation models, enhanced sampling strategies and laboratory automation.

Indexed as

Machine LearningProteinsAmino Acid SequenceAntibodiesBiotechnologyAntibodiesProteins

Identifiers

PMID38361074
PMCPMC13159571

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.