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ProteomicsTop Down Histone H4 - SUM159 Butyrate
Proteins physiologically exist and function as ‘proteoforms’ that arise from one gene but acquire additional function by further variation such as post-translational modification (PTM). When multiple PTMs coexist on single protein molecules top down proteomics becomes the only feasible method; howev...
ORGANISM(S): Homo sapiens (Human) 
2019-11-22 | PXD013766 | Pride
Top-down Histone h4 
ProteomicsMus musculus brown adipose tissue histone proteoforms
Histones were isolated from brown adipose tissue and liver from mice housed at 28, 22, or 8 C. Quantitative top- or middle-down approaches were used to quantitate histone H4 and H3.2 proteoforms. See published article for complimentary RNA-seq and RRBS datasets.
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2023-06-05 | MSV000092105 | MassIVE
ProteomicsForebrain Hindbrain histone H4 Mus musculus P25 P47
Quantitative top down analysis of histone H4 proteoforms in the mouse forebrain and hindbrain at 25 and 47 days of age.
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
MSV000090249 | MassIVE
ProteomicsEvaluation of Protein Ion Relative Ratio Quantification in Top-down Electrospray Ionization–Mass Spectrometry Using Site-Specific Acetylated Recombinant Histone H3 Proteoforms
Electrospray ionization (ESI)-mass spectrometry (MS) provides a crucial platform for analyzing post-translationally modified proteins. With continuous advances in MS instruments and data analysis approaches, analyzing intact proteoforms using a “top-down” approach has become highly feasible. To quan...
ORGANISM(S): Homo sapiens (Human) 
2025-09-29 | PXD064777 | Pride
Proteoforms Top-down proteomics Histone h3 Quantitative proteomics Protein ion relative ratio 
ProteomicsCoupling SDS-PAGE to capillary zone electrophoresis-tandem mass spectrometry for high-resolution top-down proteomics analysis of intact histone proteoforms
Top-down mass spectrometry (TDMS) is a powerful tool to reveal the mechanism of epigenetic regulation by histones. However, the high similarity of histone variants and their highly dynamic post-translational modifications (PTMs) make them as on-going challenge analytes for separation with traditiona...
ORGANISM(S): Bos taurus (Bovine) 
2024-10-15 | PXD048061 | Pride
Sds-page Top-down proteomics Post-translational modifications Histone proteoform Cze-ms/ms 
ProteomicsCapillary Zone Electrophoresis-High Field Asymmetric Ion Mobility Spectrometry-Tandem Mass Spectrometry for Top-down Characterization of Histone Proteoforms
Characterization of histone proteoforms with various post-translational modifications (PTMs) is critical for a better understanding of functions of histone proteoforms in epigenetic control of gene expression. Mass spectrometry (MS)-based top-down proteomics (TDP) is a valuable approach for delineat...
ORGANISM(S): Bos taurus (Bovine) 
2023-12-07 | PXD041357 | Pride
Histone Top-down proteomics High-field asymmetric waveform ion mobility spectrometry Post-translational modification Capillary zone electrophoresis 
UnknownLinker H1 Histone Direct Top-Down Proteoform Analysis.
Not available
S-EPMC12869901 | biostudies-literature
ProteomicsQuantitative top-down proteomics reveals significant differences in histone proteoforms between metastatic and nonmetastatic colorectal cancer cells
As one of the leading causes of cancer deaths worldwide, 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 pre...
ORGANISM(S): Homo sapiens (Human) 
2025-11-21 | PXD060160 | Pride
Top-down proteomics Post-translational modifications Capillary electrophoresis-mass spectrometry Colorectal cancer metastasis Histone proteoforms 
GenomicsBrown adipose tissue histone proteoform analysis reveals an epigenetic response to cold stress
Brown adipose tissue histone proteoform analysis reveals an epigenetic response to cold stress
PRJNA982098 | ENA
UnknownEarly butyrate induced acetylation of histone H4 is proteoform specific and linked to methylation state.
Not available
S-EPMC6140813 | biostudies-literature
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