Evidence map›Paper›PMID 39080256›Full record

ArticleNature communications2024

Sequence-to-sequence translation from mass spectra to peptides with a transformer model.

Melih Yilmaz, William E Fondrie, Wout Bittremieux, Carlo F Melendez, Rowan Nelson, Varun Ananth, Sewoong Oh, William Stafford Noble

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 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

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  18. Generalizable Direct Protein Sequencing With InstaNexus.Molecular & cellular proteomics : MCP · 2026
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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

8 authors.

Melih Yilmaz *Paul G. Allen School of Computer Science and Engineering, University of Washington, Seattle, USA.ORCID http://orcid.org/0000-0001-7473-4785
William E Fondrie *Talus Bioscience, Seattle, USA.
Wout Bittremieux *Department of Computer Science, University of Antwerp, Antwerp, Belgium.ORCID http://orcid.org/0000-0002-3105-1359
Carlo F MelendezDepartment of Genome Sciences, University of Washington, Seattle, USA.
Rowan NelsonDepartment of Genome Sciences, University of Washington, Seattle, USA.ORCID http://orcid.org/0000-0001-5084-3741
Varun AnanthPaul G. Allen School of Computer Science and Engineering, University of Washington, Seattle, USA.
Sewoong OhPaul G. Allen School of Computer Science and Engineering, University of Washington, Seattle, USA.
William Stafford NoblePaul G. Allen School of Computer Science and Engineering, University of Washington, Seattle, USA. William-noble@uw.edu.ORCID http://orcid.org/0000-0001-7283-4715

Funding

National Science Foundation (NSF) 2245300National Science Foundation (NSF) CCF-2019844
6 · The paper itself

Abstract

A fundamental challenge in mass spectrometry-based proteomics is the identification of the peptide that generated each acquired tandem mass spectrum. Approaches that leverage known peptide sequence databases cannot detect unexpected peptides and can be impractical or impossible to apply in some settings. Thus, the ability to assign peptide sequences to tandem mass spectra without prior information-de novo peptide sequencing-is valuable for tasks including antibody sequencing, immunopeptidomics, and metaproteomics. Although many methods have been developed to address this problem, it remains an outstanding challenge in part due to the difficulty of modeling the irregular data structure of tandem mass spectra. Here, we describe Casanovo, a machine learning model that uses a transformer neural network architecture to translate the sequence of peaks in a tandem mass spectrum into the sequence of amino acids that comprise the generating peptide. We train a Casanovo model from 30 million labeled spectra and demonstrate that the model outperforms several state-of-the-art methods on a cross-species benchmark dataset. We also develop a version of Casanovo that is fine-tuned for non-enzymatic peptides. Finally, we demonstrate that Casanovo's superior performance improves the analysis of immunopeptidomics and metaproteomics experiments and allows us to delve deeper into the dark proteome.

Indexed as

PeptidesProteomicsTandem Mass SpectrometryAlgorithmsAmino Acid SequenceDatabases, ProteinHumansMachine LearningNeural Networks, ComputerSequence Analysis, ProteinPeptides

Identifiers

PMID39080256
PMCPMC11289372

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.