Evidence map›Paper›PMID 39107330›Full record

ArticleNature communications2024

Post-translational modification prediction via prompt-based fine-tuning of a GPT-2 model.

Palistha Shrestha, Jeevan Kandel, Hilal Tayara, Kil To Chong

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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. CLASPP: A unified model for predicting post-translational modifications.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. ANYI: The ANnotated Yeast Interactome.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Review
  12. Large language models for bioinformatics.Quantitative biology (Beijing, China) · 2026
    Review
  13. Review
  14. Review
  15. Article
  16. Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome.Journal of cardiovascular development and disease · 2026
    Review
  17. Review
  18. Review
  19. Review
  20. AI4Protein: transforming the future of protein design.Science China. Life sciences · 2025
    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

4 authors.

Palistha Shrestha *Department of Electronics and Information Engineering, Jeonbuk National University, Jeonju, Jeollabuk-do, Republic of Korea.ORCID 0009-0001-3660-0150
Jeevan Kandel *Graduate School of Integrated Energy-AI, Jeonbuk National University, Jeonju, Jeollabuk-do, Republic of Korea.ORCID 0000-0001-5223-355X
Hilal TayaraSchool of International Engineering and Science, Jeonbuk National University, Jeonju, Jeollabuk-do, Republic of Korea. hilaltayara@jbnu.ac.kr.ORCID 0000-0001-5678-3479
Kil To ChongDepartment of Electronics and Information Engineering, Jeonbuk National University, Jeonju, Jeollabuk-do, Republic of Korea. kitchong@jbnu.ac.kr.ORCID 0000-0002-1952-0001

Funding

Ministry of Knowledge Economy | Korea Institute of Energy Technology Evaluation and Planning (KETEP) 20204010600470National Research Foundation of Korea (NRF) 2020R1A2C2005612National Research Foundation of Korea (NRF) 2022R1G1A1004613
6 · The paper itself

Abstract

Post-translational modifications (PTMs) are pivotal in modulating protein functions and influencing cellular processes like signaling, localization, and degradation. The complexity of these biological interactions necessitates efficient predictive methodologies. In this work, we introduce PTMGPT2, an interpretable protein language model that utilizes prompt-based fine-tuning to improve its accuracy in precisely predicting PTMs. Drawing inspiration from recent advancements in GPT-based architectures, PTMGPT2 adopts unsupervised learning to identify PTMs. It utilizes a custom prompt to guide the model through the subtle linguistic patterns encoded in amino acid sequences, generating tokens indicative of PTM sites. To provide interpretability, we visualize attention profiles from the model's final decoder layer to elucidate sequence motifs essential for molecular recognition and analyze the effects of mutations at or near PTM sites to offer deeper insights into protein functionality. Comparative assessments reveal that PTMGPT2 outperforms existing methods across 19 PTM types, underscoring its potential in identifying disease associations and drug targets.

Indexed as

Protein Processing, Post-TranslationalAlgorithmsAmino Acid SequenceComputational BiologyDatabases, ProteinHumansProteinsProteins

Identifiers

PMID39107330
PMCPMC11303401

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.