ReviewQuantitative biology (Beijing, China)2026
A survey of downstream applications of evolutionary scale modeling protein language models.
Review in Quantitative biology (Beijing, China), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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.
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.
Who cites it
3 citing papers in PubMed.
- A survey of downstream applications of evolutionary scale modeling protein language models.Quantitative biology (Beijing, China) · 2026Review
- Pooling multimodal cancer data across unaligned embedding spaces maintains tumor of origin signal.Bioinformatics advances · 2026Article
- Machine learning for the prediction of gram-negative bacterial secreted effectors: advances and challenges.Frontiers in chemistry · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The evolutionary scale modeling (ESM) series is promising to revolutionize protein science and engineering through large language models (LLMs), providing a robust framework for understanding the relationships among sequences, structures, and functions of proteins. Trained on a large number of unlabeled protein sequences, ESM models are able to capture intricate patterns of mutation and conservation, yielding insights into the structural and functional properties of proteins. Despite a growing body of literature surrounding ESM, existing surveys often fail to comprehensively describe its advancements or applications in a focused manner. This survey covers the latest developments of ESM, categorizing them into techniques of using ESM and downstream applications. Approximately 100 papers are selected and analyzed, highlighting recognized and innovative studies that exemplify the impact of ESM. Furthermore, we critically discuss the strengths and limitations of ESM to envision future applications. This review provides a valuable resource for researchers seeking to explore the power of ESM models and the emerging applications of LLMs in biology and medicine.
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What OpenQuestion holds
Registered trials
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.