ArticleMethods in molecular biology (Clifton, N.J.)2025
LMPTMSite: A Platform for PTM Site Prediction in Proteins Leveraging Transformer-Based Protein Language Models.
Article in Methods in molecular biology (Clifton, N.J.), 2025. 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.
- Pool PaRTI: a PageRank-based pooling method for identifying critical residues and enhancing protein sequence representations.Bioinformatics (Oxford, England) · 2025Article
- Pool PaRTI: A PageRank-Based Pooling Method for Identifying Critical Residues and Enhancing Protein Sequence Representations.bioRxiv : the preprint server for biology · 2025Article
- A Survey of Biological Function Prediction Methods with Focus on Natural Language Processing (NLP) and Large Language Models (LLM).Methods in molecular biology (Clifton, N.J.) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Protein post-translational modifications (PTMs) introduce new functionalities and play a critical role in the regulation of protein functions. Characterizing these modifications, especially PTM sites, is essential for unraveling complex biological systems. However, traditional experimental approaches, such as mass spectrometry, are time-consuming and expensive. Machine learning and deep learning techniques offer promising alternatives for predicting PTM sites. In this chapter, we introduce our LMPTMSite (language model-based post-translational modification site predictor) platform, which emphasizes two transformer-based protein language model (pLM) approaches: pLMSNOSite and LMSuccSite, for the prediction of S-nitrosylation sites and succinylation sites in proteins, respectively. We highlight the various methods of using pLM-based sequence encoding, explain the underlying deep learning architectures, and discuss the superior efficacy of these tools compared to other state-of-the-art tools. Subsequently, we present an analysis of runtime and memory usage for pLMSNOSite, with a focus on CPU and RAM usage as the input sequence length is scaled up. Finally, we showcase a case study predicting succinylation sites in proteins active within the tricarboxylic acid (TCA) cycle pathway using LMSuccSite, demonstrating its potential utility and efficiency in real-world biological contexts. The LMPTMSite platform, inclusive of pLMSNOSite and LMSuccSite, is freely available both as a web server ( http://kcdukkalab.org/pLMSNOSite/ and http://kcdukkalab.org/LMSuccSite/ ) and as standalone packages ( https://github.com/KCLabMTU/pLMSNOSite and https://github.com/KCLabMTU/LMSuccSite ), providing valuable tools for researchers in the field.
Indexed as
Identifiers
39576587What 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.