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Martens, L.

Publications and source records attributed to Martens, L..

At least 19 recordsLinked to original sources

OmicsFM brings proteomics into the foundation model era

While foundation models have been shown to learn biological representations from large transcriptomic atlases, it remained unknown whether proteomics data allow the same. We here therefore introduce OmicsFM, a modality-agnostic transformer pretrained through masked abundance reconstruction on an unprecedented proteomics data corpus of 48,837 quality-filtered proteomics profiles from 1,397 reprocessed PRIDE projects. Interestingly, despite training on 14- to 93-fold fewer profiles than matched bulk- and single-cell transcriptomic models, respectively, our proteomics model rivals both. On held-out projects, OmicsFM attention networks recovered more molecular relationships than co-expression methods and existing single-cell foundation models across nine reference databases that reveal pathway-level organization. Sample-level embeddings preserved biological structure across independent studies, and its representations transferred successfully to cell-type classification, gene-essentiality prediction, and perturbation-response prediction, while consistently outperforming task-specific models. Moreover, our results show that proteomics and transcriptomics representations capture complementary biology. OmicsFM thus firmly establishes the possibility of training highly performant proteomics-based foundation models, and their importance in modelling and uncovering fundamental biology.

bioinformatics↗

Discovery of non-canonical proteins through modification-aware proteogenomics

ShortThe SwissProt database contains a stable 20,418 human protein-coding genes and 42,541 human protein sequences. Ribo-Seq suggests about 7,000 additional, non-canonical Open Reading Frames (ORFs) are present in humans, though only a few of them are confirmed by Mass Spectrometry (MS). Detecting these proteins requires extensive database searches, increasing computational load and inflating False Discovery Rates (FDR). Using the ionbot search engine with the OpenProt database allows for reliable detection of non-canonical proteins while controlling FDR. Ionbot surpasses the Trans-Proteomics Pipeline (TPP) in reproducibility, identifying more peptides and proteins supported by multiple spectra. In addition, open modification searches yield better PSMs compared to closed searches. This work highlights the importance of employing cutting-edge search engines in non-canonical protein research, as well as the value of open modification search in correcting errors in non-canonical protein detection. LongO_ST_ABSBackgroundC_ST_ABSThe SwissProt database reports a quite stable 20,418 human protein-coding genes and 42,541 human protein sequences, figures that have remained stable. New techniques like Ribo-Seq indicate that approximately 7,000 additional, non-canonical Open Reading Frames (ORFs) are translated in humans, few of which have been confirmed by Mass Spectrometry (MS). Detecting these non-canonical proteins requires comprehensive database searches, which increase computational load and False Discovery Rate (FDR). Here, we use the open search engine ionbot in combination with the OpenProt proteogenomics database to reproducibly detect non-canonical proteins while maintaining a well-controlled FDR. ResultsCompared to the current gold standard, the Trans-Proteomics Pipeline (TPP), ionbot shows higher reproducibility, with a higher number of peptides and proteins supported by multiple spectra, and across multiple samples. We observe that PSMs from the open modification search against OpenProt have higher fragment ion intensity correlation compared to PSMs obtained from the closed search, or by only searching canonical proteins. ConclusionsIn this work, we show the potential for open modification searching to correct potential mistakes in non-canonical proteins detection by preventing modified canonical peptides or variants from being incorrectly identified as non-canonical peptides. We also highlight the importance of assessing the FDR of non-canonical identifications separately from canonical ones, as global FDR calculations are biased by the scarcity of non-canonical identifications in each dataset.

molecular biology↗

Scop3P-Toolkit: executable structure-aware workflows linking PTMs, peptides, and mutations to protein function

Post-translational modifications (PTMs) and genetic variants regulate protein function, signalling, and disease, but their interpretation requires integration of sequence annotations with structural, interaction, and biophysical context. Although resources such as Scop3P, UniProt, the Protein Data Bank, and AlphaFold provide extensive annotations and structural information, integrating these data into reproducible structure-aware analyses still requires custom scripting and manual coordination between multiple independent tools. To address this challenge, we developed Scop3P-Toolkit, an open-source executable analytical environment for interactive analysis of PTMs, mutations, and proteomics-derived peptides in their structural context. The toolkit integrates protein annotation retrieval with structural mapping, residue interaction network analysis, comparative structural analysis, and residue-level biophysical profiling within a unified framework. Experimentally supported phosphosites, phosphopeptides, and phosphoproteomics evidence are provided for human proteins through Scop3P, with optional integration of curated UniProt PTM annotations. UniProt-derived PTMs, sequence features, and genetic variants are available for proteins from any species, extending the framework beyond the human phosphoproteome. Scop3P-Toolkit supports structure-centric analyses including interpretation of PTMs and disease-associated variants, analysis of residue interaction networks and their rewiring across alternative conformations, structural localisation of peptides, and exploration of protein-protein, protein-ligand, and host-pathogen interfaces. Interactive visualisation links sequence annotations, three-dimensional structures, residue interaction networks, and biophysical profiles, enabling coordinated exploration across multiple molecular representations. The toolkit is distributed as Jupyter notebooks, browser-based Voila applications, and a Galaxy interactive tool, providing transparent, accessible, and reproducible workflows for both computational and experimental researchers. By integrating biological annotation resources into executable, structure-aware workflows, Scop3P-Toolkit enables reproducible interpretation of PTMs, mutations, and proteomics data.

bioinformatics↗

Evaluating the use of non-linear models in data-driven rescoring of peptide-spectrum matches

In mass spectrometry (MS)-based proteomics, computational tools match acquired tandem MS spectra to peptides from a sequence database. Machine learning increasingly supports this task through peptide-spectrum match (PSM) rescoring, in which a classifier, typically a linear semi-supervised model, refines the initial matching score. However, Mokapot allows the user to choose among different machine learning algorithms of increasing complexity, from the default linear support vector machine (LSVM) to random forest and XGBoost. Here, we use an entrapment approach to assess the effect of this increasing complexity on PSM identification and the accuracy of the estimated false discovery rate (FDR). We show that, while more complex models increase the number of identified PSMs at a fixed FDR threshold, this gain reflects a bias towards random matches from the target proteome database rather than genuine identifications. Indeed, for the most complex model, the entrapment FDR reaches 6.3% instead of the estimated 1% decoy FDR. This bias thus yields overly optimistic FDR estimates, indicating that model complexity in PSM rescoring must be carefully balanced against this overfitting risk.

bioinformatics↗

Defining Quality Control Standards for Single-Cell Proteomics by Inter-Laboratory Benchmarking

Single-cell proteomics can quantify thousands of proteins from individual mammalian cells, yet the absence of community-wide quality control limits biological interpretability. Here, the HUPO Single Cell Initiative presents the first inter-laboratory single-cell proteomics benchmarking study across seven laboratories using standardized 384-well plates acquired on Orbitrap Astral and timsTOF Ultra2 instruments. Centralized analysis across six DIA software tools revealed that software choice impacts identification depth and quantitative accuracy more than instrument vendor. Multi-layered quality control enabled the detection of cell-leakage during sorting, LC misconfiguration, column degradation and site-specific pipetting failures. Inter-lab quantitative correlations were strongest between instruments of the same vendor relative to cross-platform comparisons. Sequential correction for plate identity and well position recovered clean cell-type separation for confident downstream differential expression analysis. This study provides a data-driven quality control framework spanning plate design to batch correction for reproducible single-cell proteomics across laboratories and platforms.

biochemistry↗

Scop3P in 2026: an expanded proteomics-informed resource contextualizing phosphorylation sites through sequence, structure, mutation, and experimental provenance

Protein phosphorylation is a central regulatory mechanism controlling protein activity, interactions, and cellular signalling, and its dysregulation is implicated in numerous diseases. Advances in mass spectrometry-based phosphoproteomics have led to a rapid expansion in the number of reported phosphorylation sites; however, interpretation of these data remains challenging due to fragmented evidence, limited structural context, and the lack of uniform experimental provenance across resources. Interpretation is further complicated by the fact that the biological meaning of reported phosphosites can vary substantially across tissues, cell lines, perturbations, and disease settings. Here, we present a major update of Scop3P, a proteomics-informed knowledgebase that contextualizes human phosphorylation sites within integrated sequence, structural, biophysical, evolutionary, and mutational frameworks. The current release incorporates uniformly reprocessed human phosphoproteomics data from 116 PRIDE datasets alongside curated UniProt annotations, retaining peptide-spectrum matches, site localization confidence, and direct links to primary mass spectrometry evidence via Universal Spectrum Identifiers. This integration yields 152,350 unique serine, threonine, and tyrosine phosphorylation sites across 16,533 human proteins, supported by full experimental provenance. Beyond site identification, Scop3P provides residue-level contextual annotations derived from experimentally determined protein structures and proteome-wide AlphaFold models, enabling near-complete structural coverage of phosphorylation sites. Structural context is further complemented by residue-level biophysical, evolutionary, and mutational annotations, supporting integrated assessment of phosphorylation in functional and disease-related settings. The current release also introduces residue interaction network representations derived from AlphaFold-predicted structures, capturing spatial connectivity and local interaction environments of phosphorylation and mutation sites. A redesigned web interface enables interactive exploration through coordinated 1D, 2D, 2.5D, and 3D visualizations, peptide-level coverage views, and direct access to original spectra via PRIDE. By bridging experimental phosphoproteomics with structural, functional, and disease-related context, Scop3P provides a scalable and provenance-aware resource for phosphosite interpretation, hypothesis generation, and data-driven modelling of phosphorylation-dependent regulation.

bioinformatics↗

HLiCA: An integrated cell atlas of the healthy human liver

The human liver is composed of a heterogeneous mix of cell types. How these distinct populations contribute individually and collectively to liver function remains poorly understood. Although single-cell technologies have advanced our understanding of liver biology, individual studies have often been limited by small donor cohorts and inconsistent cell type annotations. Integrating multiple datasets can overcome these challenges and better capture biological variability. We present the Human Liver Cell Atlas (HLiCA), an integrated reference of non-disease liver cells assembled from eight datasets across six research centers, encompassing more than 525,000 cells from 110 donors. Developed in collaboration with the Human Cell Atlas Liver Bionetwork, the HLiCA incorporates expert-curated cell annotations refined through community feedback and dedicated cell type annotation meetings. The HLiCA classifies cells into six lineages and expands the cell type resolution to include 47 distinct cell types. Starting from raw sequencing reads, we realigned all data and performed rigorous benchmarking to ensure robust integration across technical and biological variables. Genetic ancestry was inferred for all samples to evaluate the range of ancestral backgrounds represented in the atlas. The expanded cell type annotation enabled identification of previously unrecognized liver cell types, including NRXN1+ stromal cells. Their presence was validated using spatial transcriptomics, which localized NRXN1+ stromal cells to periportal regions. With the number of donors included in the HLiCA we were able to examine cell type specific associations with demographic covariates. In hepatocytes, drug metabolism genes showed differential expression between sexes, and in cholangiocytes, mucus-production genes varied with age. As the largest and most genetically diverse human liver cell atlas to date, the HLiCA provides a comprehensive, well-annotated reference for the field, annotated by expert consensus. This resource will enable deeper interrogation of liver cellular diversity, architecture, and function in the healthy human liver and serve as a reference to understand changes that occur with disease.

genomics↗

gamdid: generalized additive models for differential distributions in single cell experiments

Single-cell proteomics (SCP) generates protein abundance measurements across hundreds to thousands of individual cells, offering unprecedented resolution to study cellular heterogeneity. However, existing differential abundance (DA) methods are limited to detecting shifts in mean expression, leaving biologically relevant differences in shape undetected. Indeed, the specific power of SCP is to identify differences between individual cells in a population, which are typically only found as shape differences rather than in mean expression. We here therefore present gamdid (generalized additive models for differential distributions), a novel statistical framework and R package for differential distribution (DD) analysis in SCP data. gamdid is based on generalized additive models (GAMs) to flexibly model heterogeneous distributions, perform inference and provide interpretable visualizations. Through semi-synthetic benchmarking on two SCP datasets, gamdid demonstrates conservative false discovery rate control and substantially outperforms competing methods for differences in shape, while achieving comparable performance for mean shifts. A spike-in case study further demonstrates the utility of gamdid and its interpretable visualization. Uniquely among DD methods, gamdid supports omnibus testing across more than two groups, with post-hoc pairwise comparisons via stagewise testing, and is specifically tailored for proteomics abundance data.

genomics↗

Predicting and Elucidating Peptide Retention Mechanisms with Graph Attention Networks

Liquid chromatography (LC) is a key technology in bottom-up proteomics, separating proteolytic peptides to decrease sample complexity, enhance coverage, and increase the robustness of protein identification and quantification. Although high-resolution mass spectrometry has advanced significantly, comparable progress in LC has lagged, primarily due to a limited understanding of peptide-column interactions. To bridge this knowledge gap, we introduce a novel deep learning model (PeptideGNN) based on a Graph Neural Network (GNN) architecture to model and elucidate peptide behaviors across various separation conditions. Trained to accurately predict peptide retention times on ten diverse proteomic datasets, the model subsequently employed a saliency mapping technique to interpret the underlying retention mechanisms. Our model consistently outperformed existing retention-time predictors across multiple datasets, while the saliency mapping, importantly, revealed insights into peptide-stationary phase interactions, highlighting the effects of neighboring amino acids, post-translational modifications (PTMs), chromato-graphic columns, and mobile phase additives on peptide retention.

bioinformatics↗

Evaluation of Protein Reference Database Reduction and Its Impact on Peptide-Centric Metaproteomics

Metaproteomics identifies the proteins present in a microbial community and, from them, which organisms are active and what functions they carry out. Tools such as Unipept assign peptides to taxa and functions by matching them to UniProtKB proteins and taking the lowest common ancestor of the matching taxa, deriving functional annotations from the same matches. This analysis therefore depends directly on the content of UniProtKB, which was substantially restructured in 2025-2026, reducing it by more than 100 million protein entries. We investigated how these changes affect taxonomic interpretation and how restricting the database to sample-specific taxa identified by rRNA profiling modifies that effect. Fixed, non-redundant peptide lists from human-gut and marine-hatchery studies were reanalysed with Unipept against UniProtKB releases 2025_03, 2025_04, and 2026_02. Peptide mapping coverage fell from 85.9% to 73.3% (gut) and from 82.3% to 68.7% (marine) between release 2025_03 and 2026_02, yet dominant taxonomic profiles remained robust: family- and genus-level distributions changed little and all 15 dominant gut species were retained. Root-level assignments dropped from 18.7% to 7.0% (gut) and 25.8% to 14.3% (marine). Restricting UniProtKB 2026_02 to taxa detected by large-subunit ribosomal RNA (LSU rRNA) profiling reduced coverage to 64.4% (gut) and 41.8% (marine), while genus- and species-level proportions changed by less than one percentage point. The major UniProtKB restructuring of 2025-2026 therefore narrowed mapping breadth without destabilizing the dominant taxonomic profiles in these two datasets.

bioinformatics↗

LFQ Benchmark Dataset - Generation Beta: Assessing Modern Proteomics Instruments and Acquisition Workflows with High-Throughput LC Gradients

Recent advances in liquid chromatography-mass spectrometry (LC-MS) have accelerated the adoption of high-throughput workflows that deliver deep proteome coverage using minimal sample amounts. This trend is largely driven by clinical and single-cell proteomics, where sensitivity and reproducibility are essential. Here, we extend our previous benchmark dataset (PXD028735) using next-generation LC-MS platforms optimized for rapid proteome analysis. We generated an extensive DDA/DIA dataset using a human-yeast-E. coli hybrid proteome. The proteome sample was distributed across multiple laboratories together with standardized analytical protocols specifying two short LC gradients (5 and 15 min) and low sample input amounts. This dataset includes data acquired on four different platforms, and features new scanning quadrupole-based implementations, extending coverage across different instruments and acquisition strategies. Our comprehensive evaluation highlights how technological advances and reduced LC gradients may affect proteome depth, quantitative precision, and cross-instrument consistency. The release of this benchmark dataset via ProteomeXchange (PXD070049 and PXD071205), allows for the acceleration of cross-platform algorithm development, enhance data mining strategies, and supports standardization of short-gradient, high-throughput LC-MS-based proteomics.

bioinformatics↗

MoDPA: Inferring Modification-dependent Protein Associations from Uniformly Reprocessed Mass Spectrometry

MotivationPost-translational modifications (PTMs) are key regulators of protein function and cellular processes; however, the overall principles of PTM co-regulation and crosstalk remain to be fully understood. A major challenge in large-scale PTM crosstalk studies is the scarcity of data, which hampers the ability to reproducibly detect proteome-wide associations between modification sites. ResultsWe present a new computational framework, named Modification-Dependent Protein Associations (MoDPA). To overcome the extreme sparsity and heterogeneity of PTM calls across experiments, MoDPA utilizes a variational autoencoder (VAE) to embed per-site detection profiles into a low-dimensional latent space that preserves covariation while denoising missing data. A PTM association network is constructed by correlating latent representations across experiments. Benchmarking against pulsed SILAC data shows that MoDPA can correctly capture the correlation between heavy- and light-labelled peptides. We apply MoDPA to a large sample of reprocessed public datasets and identify clusters of modified proteins involved in distinct biological pathways, suggesting that some modifications may preferentially regulate specific biological processes, but not others. In particular, we find clusters enriched in lysine acetylation, lysine methylation, and arginine deamidation (citrullination) sites, which contain proteins involved in protein synthesis, neuron development, and cellular senescence. Availability and ImplementationAll code is freely available on GitHub (https://github.com/CompOmics/MoDPAv1.0) and Zenodo (10.5281/zenodo.18310674). The resulting MoDPA-derived PTM network is available via the TabloidProteome website at https://iomics.ugent.be/tabloidproteome. Contactenrico.massignani@ugent.be, lennart.martens@ugent.be

bioinformatics↗

quantms-rescoring enables deep proteome coverage across protein quantification, immunopeptidomics, and post-translational modifications experiments.

The growing volume of public proteomics datasets and the advent of novel machine learning (ML)-based methods create unprecedented opportunities for discovery through large-scale reanalysis. However, traditional desktop tools are increasingly insufficient for processing and integrating data at this scale. To address this challenge, we present a novel package, quantms-rescoring, that extends the cloud-native quantms workflow with a machine learning-based rescoring module. Unlike prior tools that rescore single-engine outputs, quantms-rescoring seamlessly integrates multiple search engines (SAGE, COMET, and MSGF+), performs automatic model selection, model fine-tuning, and scales reproducibly on cloud infrastructures. In quantms-rescoring, we rely on multiple fragment-ion intensity (AlphaPeptDeep and MS2PIP) and retention-time prediction (DeepLC) methods to improve results from multiple peptide database search engines. It features automatic model selection, fine-tuning, and retraining for MS/MS intensity and retention time prediction to select the best model for a given dataset. We applied the novel workflow to five representative datasets spanning DDA label-free quantification, TMT 10-plex isobaric labelling of tumor proteomics data, immunopeptidomics, phospho-proteomics, and unseen lysine malonylation experiments. We achieved a 16-22.8% increase in identified spectra, along with the quantification of 2191 additional phosphorylated peptides and 1337 phosphosites. In the tandem mass tag (TMT)-labeled clear cell renal cell carcinoma dataset, 76 novel differentially expressed multiple search engines identified proteins with quantms-rescoring. Additionally, novel 11,688 HLA-II potential binders were detected in the immunopeptidomics dataset by multiple search engines with quantms-rescoring. For unseen malonylation data, we reported more than 58.8% malonylation PSMs and 30.5% modification sites than COMET alone. Together, these results show that integrating multi-engine searches with machine learning-derived features can be combined in a scalable workflow that enhances identification, PTM localization, and quantification performance.

bioinformatics↗

ProteoBench: the community-curated platform for comparing proteomics data analysis workflows

Mass spectrometry (MS)-based proteomics is a well-established strategy for analyzing complex biological mixtures. Many MS instruments and data acquisition strategies are available, and the data they acquire differ substantially, thus requiring tailored analysis algorithms. Hence, many dedicated bioinformatics workflows are developed. These are in constant evolution, and the community lacks a centralized platform for comparing their performance. Here, we propose ProteoBench, a single platform that brings together software developers and software users to provide an ever-evolving comparison of state-of-the-art proteomics data processing tools. ProteoBench is an open-source resource that enables the community to evaluate data analysis workflows, develop benchmarking modules dedicated to specific comparisons, and discuss the best methods to compare software tools. The platform ensures that the benchmark evolves alongside advances in proteomics data analysis workflows. ProteoBench guides researchers towards the best-suited tool and parameters for their specific project and data according to their needs, and developers can test their newly developed tools or workflows privately, before adding them as public references. This community-driven effort will increase transparency and reproducibility between MS data analysis workflows, as well as facilitate the development and publication of software workflows in the field.

bioinformatics↗

iDeepLC: chemical structure information yields improved retention time prediction of peptides with unseen modifications

Deep learning has notably advanced the field of liquid chromatography-mass spectrometry-based proteomics. Accurate prediction of peptide retention times significantly enhances our ability to match LC-MS data with the correct peptides and proteins, especially for DIA data. While numerous models predict peptide LC retention times with high accuracy, few can accurately predict the retention times of chemically modified peptides, particularly those with modifications not encountered during model training. In our previously developed DeepLC model, accurate predictions could be made for unseen modifications by leveraging the chemical composition of (modified) residues. Here, however, we present a further enhancement of this model based on chemical structural information. The resulting model, called iDeepLC, shows overall more accurate predictions, and better generalization performance for predicting the retention time of unseen modifications than DeepLC. iDeepLC is freely available as open-source software under the Apache2 license and can be found at https://github.com/CompOmics/iDeepLC.

bioinformatics↗

The E. coli PeptideAtlas Build: Characterizing the observed Escherichia coli pan-proteome and its post-translational modifications

Escherichia coli is a widely used model organism in molecular biology. Despite its pivotal role, a comprehensive proteome resource covering the E. coli pan-proteome and its post-translational modifications (PTMs) has been lacking. Here we present the E. coli PeptideAtlas build, the first comprehensive pan-proteome analysis of E. coli, generated from 40 high-quality public and in-house datasets spanning a broad diversity of strains, sample types, and experimental conditions, and comprising over 73 million MS/MS spectra. All datasets were reprocessed using both a closed search (Trans-Proteomic Pipeline using MSFragger) and an open search (ionbot). The E. coli PeptideAtlas build provides evidence for 4,755 proteins, including 1,410 previously lacking protein-level support in UniProt. The resource offers protein coverage, modification sites, raw spectra with matched peptides, and manually annotated metadata for the E. coli pan proteome. PTM profiling identified over 10,000 modification sites, including phosphorylation (3,806), acetylation (754), methylation (730), glutathionylation (352) and phosphoribosylation (226). Analysis of the glutathionylation sites revealed potential links to metal binding regulation. We also detected proteins likely associated with phages, underscoring the value of pan-proteomic approaches for studying host-phage interactions. All identifications are publicly accessible and traceable through the PeptideAtlas interface. We expect that the E. coli PeptideAtlas build will provide a useful resource for the community, which supports, for example, targeted MS experiment design, PTM enrichment method development, and strain typing. It allows straightforward lookups of protein and peptide identifications and facilitates comparative proteomic analyses by enabling the assessment of protein presence and variability across different E. coli strains. The build is available at https://db.systemsbiology.net/sbeams/cgi/PeptideAtlas/buildDetails?atlas_build_id=585.

bioinformatics↗

Limitations of de novo sequencing in resolving sequence ambiguity

De novo peptide sequencing enables peptide identification from fragmentation spectra without relying on sequence databases. However, incomplete spectra create ambiguity, making unambiguous identification challenging. Recent deep learning advances have produced numerous de novo models that predict sequences and refine peptide-spectrum matches under such conditions. Yet, their relative strengths, weaknesses, and ability to handle spectrum ambiguity remain unclear. Here, we benchmark eight state-of-the-art models on three publicly available proteomics datasets, comparing performance using established metrics and quantifying inter-model agreement. We assess post-processing approaches, including iterative refinement, rescoring, and reranking, for their ability to improve identification accuracy, and perform an error analysis to identify common mispredictions and their causes. Model performance varied, with considerable overlap of correct identifications. Post-processing yielded no or only modest improvements. Most sequencing errors were model-independent and driven by limited fragment ion coverage, a limitation also observed in database searches with large search spaces.

bioinformatics↗

MLMarker: A machine learning framework for tissue inference and biomarker discovery

MLMarker is a machine learning tool that computes continuous tissue similarity scores for proteomics data, addressing the challenge of interpreting complex or sparse datasets. Trained on 34 healthy tissues, its Random Forest model generates probabilistic predictions with SHAP-based protein-level explanations. A penalty factor corrects for missing proteins, improving robustness for low-coverage samples. Across three public datasets, MLMarker revealed brain-like signatures in cerebral melanoma metastases, achieved high accuracy in a pan-cancer cohort, and identified brain and pituitary origins in biofluids. MLMarker provides an interpretable framework for tissue inference and hypothesis generation, available as a Python package and Streamlit app.

bioinformatics↗