Evidence map›Paper›PMID 42542530›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Combining SDS-PAGE with Capillary Zone Electrophoresis-Tandem Mass Spectrometry for Top-Down Proteomics Analysis of Intact Histone Proteoforms.

Fei Fang, Liangliang Sun

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 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

2 authors.

Fei FangDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, MI, 48824, USA.
Liangliang SunDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, MI, 48824, USA. lsun@chemistry.msu.edu.

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

Mass spectrometry (MS)-based top-down proteomics (TDP) analysis of histone proteoforms provides critical information about combinatorial posttranslational modifications (PTMs), which is vital for pursuing a better understanding of epigenetic regulation of gene expression. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) separates histone proteins (H1, H2, H3, and H4) based on their molecular weight, while capillary zone electrophoresis (CZE) provides additional separation of proteoforms of each histone protein based on their electrophoretic mobility, which is affected by PTMs, e.g., acetylation and phosphorylation. Here, we describe the combination of SDS-PAGE-based protein fractionation with CZE-tandem MS (MS/MS) for high-resolution characterization of histone proteoforms. Over 200 histone proteoforms from a commercial calf thymus histone sample were identified with good reproducibility.

Indexed as

Electrophoresis, Polyacrylamide GelHistonesProteomicsTandem Mass SpectrometryAnimalsCattleElectrophoresis, CapillaryProtein Processing, Post-TranslationalHistonesCapillary electrophoresis-mass spectrometryHistone proteoformPosttranslational modificationsSDS-PAGETop-down proteomics

Identifiers

What Socratic 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 Socratic graph.