Evidence map›Paper›PMID 40243858›Full record

ArticleProteomics2025

Quantitative Top-Down Proteomics Reveals Significant Differences in Histone Proteoforms Between Metastatic and Nonmetastatic Colorectal Cancer Cells.

Fei Fang, Brian Fries, Zhige Wang, Xiaowen Liu, Amanda B Hummon, Liangliang Sun

Abstract read
In one paragraph

Article in Proteomics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. A Draft Map of E. coli Proteoforms.Analytical chemistry · 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

6 authors.

Fei FangDepartment of Chemistry, Michigan State University, East Lansing, Michigan, USA.
Brian FriesDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, Ohio, USA.
Zhige WangDepartment of Computer Science, School of Science & Engineering, Tulane University, New Orleans, Louisiana, USA.ORCID 0009-0002-1168-5597
Xiaowen LiuDeming Department of Medicine, School of Medicine, Tulane University, New Orleans, Louisiana, USA.ORCID 0000-0003-4139-1127
Amanda B HummonDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, Ohio, USA.ORCID 0000-0002-1969-9013
Liangliang SunDepartment of Chemistry, Michigan State University, East Lansing, Michigan, USA.ORCID 0000-0001-8939-5042

Funding

Quantitative top-down proteomics of human colorectal cancer cells and tumorsR01CA247863 · NCI · MICHIGAN STATE UNIVERSITY · PI HUMMON, AMANDA B., LIU, XIAOWEN · 2021 to 2025
$1.9M
Advancing top-down proteomics with capillary electrophoresis-mass spectrometryR35GM153479 · NIGMS · MICHIGAN STATE UNIVERSITY · PI Liangliang Sun · 2024 to 2026
$1.4M
NCI NIH HHS R01 CA247863NIGMS NIH HHS R35 GM153479
6 · The paper itself

Abstract

Colorectal cancer (CRC) development is closely associated with the accumulation of both genetic and epigenetic alterations. Many efforts have been made to investigate the role of epigenetic modifications in CRC metastasis. In this work, we present the quantitative top-down proteomics study focusing on histone proteoforms between metastatic (SW620) and nonmetastatic (SW480) CRC cells to reveal potentially critical histone proteoforms in CRC metastasis. We isolated histone proteins from CRC cells, fractionated them by sodium dodecyl-sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), and analyzed them by capillary zone electrophoresis (CZE)-tandem mass spectrometry (MS/MS). A total of 230 histone proteoforms were quantified in SW480 and SW620 cell lines, among which 34 proteoforms were significantly altered in abundance in the metastatic cells, indicating a significant transformation of histone proteoforms during metastasis. We observed a significant increase in abundance of all nine differentially expressed histone H4 proteoforms in metastatic SW620 cells compared to SW480 cells, while differentially expressed proteoforms of other histone proteins display diversified expression patterns. Additionally, two histone H2A proteoforms with a combination of N-terminal acetylation and phosphorylation were upregulated in the metastatic CRC cells. These differentially expressed histone proteoforms could be novel proteoform biomarkers of CRC metastasis.

Indexed as

Colorectal NeoplasmsHistonesProteomicsCell Line, TumorHumansNeoplasm MetastasisTandem Mass SpectrometryHistonescapillary electrophoresis‐mass spectrometrycolorectal cancer metastasishistone proteoformspost‐translational modificationstop‐down proteomics

Identifiers

PMID40243858
PMCPMC12716108

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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.