Evidence map›Paper›PMID 42454224›Full record

ArticleNAR genomics and bioinformatics2026

ProteoMeter: a pipeline for integrating multi-PTM and limited proteolysis data to reveal modification-structure coupling at the residue level.

Jordan C Rozum, Amy C Sims, Xiaolu Li, Snigdha Sarkar, Tong Zhang, John T Melchior, Danielle Ciesielski, David D Pollock, H Steven Wiley, Wei-Jun Qian and 1 more

Abstract read
In one paragraph

Article in NAR genomics and bioinformatics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

11 authors.

Jordan C RozumBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0002-4356-9809
Amy C SimsNuclear, Chemical, and Biological Technologies Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.
Xiaolu LiBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0002-9845-1584
Snigdha SarkarBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0003-4551-0314
Tong ZhangBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0003-2540-2017
John T MelchiorBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0003-3781-2566
Danielle CiesielskiBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0003-0190-4530
David D PollockDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, CO 80045, United States.ORCID https://orcid.org/0000-0002-7627-4214
H Steven WileyEnvironmental Molecular Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0003-0232-6867
Wei-Jun QianBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0002-5393-2827
Song FengBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.ORCID https://orcid.org/0000-0003-3983-9009

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Systemic perturbations trigger extensive changes across the proteome-altering protein abundance, post-translational modifications (PTMs), conformational states, and complex assembly. Interpreting these effects demands computational pipelines capable of integrating diverse proteomics modalities, such as multi-PTM profiling, limited proteolysis mass spectrometry (LiP-MS), and cross-linking mass spectrometry (XL-MS), within a unified and interoperable framework. Because instrument data are quantified at the peptide level, mapping these measurements to individual residues or modification sites is essential for biologically meaningful interpretation. We introduce ProteoMeter, an open-source Python library designed to integrate multi-modal proteomics datasets and map them to single-residue resolution using a standardized coordinate framework. We showcase its capabilities in a combined multi-PTM and LiP-MS analysis profiling the proteomic response to human coronavirus 229e (HCoV-229E) infection. ProteoMeter is actively maintained and is freely available-including all source code and figure-generation scripts-at the following repository: https://github.com/PNNL-Predictive-Phenomics/ProteoMeter.

Indexed as

Protein Processing, Post-TranslationalProteomeProteomicsSoftwareHumansMass SpectrometryProteolysisProteome

Identifiers

PMID42454224
PMCPMC13365959

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.