Evidence map›Paper›PMID 39511177›Full record

ArticleNature communications2024

SSEmb: A joint embedding of protein sequence and structure enables robust variant effect predictions.

Lasse M Blaabjerg, Nicolas Jonsson, Wouter Boomsma, Amelie Stein, Kresten Lindorff-Larsen

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Evolutionary profiles for protein fitness prediction.Bioinformatics (Oxford, England) · 2026
    Article
  4. Review
  5. MAVISp: A modular structure-based framework for protein variant effects.Protein science : a publication of the Protein Society · 2026
    Article
  6. Article
  7. Predicting Protein-Protein Interactions from Machine-Learned Representations.Advances in experimental medicine and biology · 2026
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

5 authors.

Lasse M BlaabjergLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N, Denmark.
Nicolas JonssonLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N, Denmark.ORCID 0000-0002-7838-1814
Wouter BoomsmaCenter for Basic Machine Learning Research in Life Science, Department of Computer Science, University of Copenhagen, Copenhagen N, Denmark. wb@di.ku.dk.ORCID 0000-0002-8257-3827
Amelie SteinLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N, Denmark. amelie.stein@bio.ku.dk.ORCID 0000-0002-5862-1681
Kresten Lindorff-LarsenLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N, Denmark. lindorff@bio.ku.dk.ORCID 0000-0002-4750-6039

Funding

Carlsbergfondet (Carlsberg Foundation) CF21-0392Novo Nordisk Fonden (Novo Nordisk Foundation) NNF18OC0033950Novo Nordisk Fonden (Novo Nordisk Foundation) NNF20OC0062606
6 · The paper itself

Abstract

The ability to predict how amino acid changes affect proteins has a wide range of applications including in disease variant classification and protein engineering. Many existing methods focus on learning from patterns found in either protein sequences or protein structures. Here, we present a method for integrating information from sequence and structure in a single model that we term SSEmb (Sequence Structure Embedding). SSEmb combines a graph representation for the protein structure with a transformer model for processing multiple sequence alignments. We show that by integrating both types of information we obtain a variant effect prediction model that is robust when sequence information is scarce. We also show that SSEmb learns embeddings of the sequence and structure that are useful for other downstream tasks such as to predict protein-protein binding sites. We envisage that SSEmb may be useful both for variant effect predictions and as a representation for learning to predict protein properties that depend on sequence and structure.

Indexed as

ProteinsAlgorithmsAmino Acid SequenceBinding SitesComputational BiologyModels, MolecularProtein ConformationSequence AlignmentSequence Analysis, ProteinProteins

Identifiers

PMID39511177
PMCPMC11544099

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.