Evidence map›Paper›PMID 42695249›Full record

ReviewMass spectrometry reviews2026

Proteoforms in Disease: Biomedical Applications of Top-Down Proteomics.

Holden T Rogers, Zachery R Gregorich, Megan S Gant, Zhan Gao, Julia Chamot-Rooke, Ying Ge

Abstract readReview
In one paragraph

Review in Mass spectrometry reviews, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

6 authors.

Holden T RogersDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.ORCID https://orcid.org/0000-0003-0870-0127
Zachery R GregorichDepartment of Cell and Regenerative Biology, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Megan S GantInstitut Pasteur, CNRS UAR2024, Université Paris Cité, Paris, France.ORCID https://orcid.org/0009-0002-6037-9959
Zhan GaoDepartment of Cell and Regenerative Biology, University of Wisconsin-Madison, Madison, Wisconsin, USA.ORCID https://orcid.org/0009-0009-0677-9653
Julia Chamot-RookeInstitut Pasteur, CNRS UAR2024, Université Paris Cité, Paris, France.ORCID https://orcid.org/0000-0002-9427-543X
Ying GeDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.ORCID https://orcid.org/0000-0001-5211-6812

Funding

Training Program in Translational Cardiovascular Science (TPTCS)T32HL007936 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Lee Lochbaum Eckhardt, Gail A Robertson · 2001 to 2026
$11.6M
Deciphering Myofilament Modifications in Ischemic CardiomyopathyR01HL109810 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2013 to 2024
$3.5M
Defining the Multi-Omics Landscape of Phospholamban-induced Cardiomyopathy for Precision MedicineR01HL181422 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Ying Ge · 2026 to 2026
$747k
Role of Cardiac Proteoform Alterations in the Pathogenesis of Phospholamban R14del CardiomyopathyF31HL178305 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI ROGERS, HOLDEN TYLER · 2025 to 2025
$38k
French Proteomic Infrastructure ANR-10-INBS-08French Proteomic Infrastructure ANR-24-INBS-0015NHLBI NIH HHS F31 HL178305NHLBI NIH HHS F31HL178305NHLBI NIH HHS R01 HL109810NHLBI NIH HHS R01HL109810NHLBI NIH HHS R01 HL181422NHLBI NIH HHS R01HL181422NHLBI NIH HHS T32 HL007936NHLBI NIH HHS T32HL007936
6 · The paper itself

Abstract

The proteome is a dynamic landscape of proteoforms arising from genetic mutations, alternative splicing, and post-translational modifications (PTMs), which collectively drive biological function and disease phenotypes. Mass spectrometry (MS)-based proteomics has emerged as an essential technique for elucidating this molecular complexity. Although bottom-up proteomics enables deep protein identification and quantification through peptide-level analysis, it disrupts molecular connectivity and introduces a peptide-to-protein inference problem, which is suboptimal for proteoform analysis. Top-down proteomics (TDP) offers a complementary approach by analyzing intact proteins, preserving molecular connectivity, and enabling direct characterization and quantification of proteoforms. This capability is increasingly vital for understanding heterogeneous human diseases. Here, we review the evolving role of TDP in biomedical research, highlighting studies that revealed proteoform-level alterations, identified candidate biomarkers, and advanced our understanding of the roles of proteoforms in human diseases.

Indexed as

biomedical applicationsdiseasemass spectrometryproteoformstop‐down proteomics

Identifiers

PMID42695249
PMCPMC13691920

What OpenQuestion holds

Textmetadata
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.