ArticleJournal of proteome research2025
Linker H1 Histone Direct Top-Down Proteoform Analysis.
Article in Journal of proteome research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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.
Who cites it
2 citing papers in PubMed.
- Exercise-induced protein lactylation: From molecular mechanisms to precision health applications.iScience · 2026Review
- A Proteoform-Resolved Atlas of Human Cardiac Histones.Research square · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors.
Funding
Abstract
Linker H1 histones are highly susceptible to a variety of post-translational modifications (PTMs) that play a critical role in chromatin dynamics and gene expression. In the present work, trapped ion mobility spectrometry in tandem with ultraviolet photodissociation followed by ultrahigh resolution mass measurements, provided by a Fourier transform ion cyclotron mass spectrometer (TIMS-q-UVPD-FT-ICR MS/MS), enabled direct characterization of the linker H1 histone proteoforms. The proposed method takes advantage of the mobility and mass preseparation of core and linker histones proteoforms prior to UVPD fragmentation and consequent high mass accuracy detection in the FT-ICR MS of the fragment ions for efficient PTM assignment. The application to a bovine histone extraction resulted in the annotation of four H1 variants (H1.2, H1.3, H1.5, and H1.4V), together with their PTM distribution with high sequence coverages (up to 60%); in particular, the H1.4V variant sequence was identified via
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Registered trials
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.