Evidence map›Paper›PMID 41959267›Full record

ArticlebioRxiv : the preprint server for biology2026

Chemical Proteomic Profiling of the Histaminylation Proteome in Cancer Cells Unveils Uncharted Epigenetic Marks on Core Histones.

Xingyu Ma, Anne A Leaman, Zeng Lin, Huapeng Li, Zhengjun Cai, Kaiwaan Dalal, Md Shahadat Hossain, Venkatesh P Thirumalaikumar, Zhihong Wang, Valerie P O'Brien and 2 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

5 · Who and what money

Authors and funding

12 authors.

Xingyu Ma
Anne A Leaman
Zeng Lin
Huapeng Li
Zhengjun Cai
Kaiwaan Dalal
Md Shahadat Hossain
Venkatesh P Thirumalaikumar
Zhihong Wang
Valerie P O'Brien
W Andy Tao

Funding

Development of a Chemical Biology Toolbox to Investigate Histone MonoaminylationR35GM150676 · NIGMS · PURDUE UNIVERSITY · PI Qingfei Zheng · 2023 to 2026
$1.6M
NIGMS NIH HHS R35 GM150676
6 · The paper itself

Abstract

Histamine is a key signaling molecule in pathophysiology that can exhibit significant regulatory roles in diverse health and disease status. Besides the well-studied noncovalent interactions between histamine and its receptors, protein histaminylation is a recently discovered mode of action, through which histamine regulates cellular signaling pathways in a covalent-interaction manner. Histaminylation is an emerging protein post-translational modification, where an isopeptide bond is formed between the histamine primary amine and γ-carboxyl group of glutamine through a transamidation reaction catalyzed by transglutaminase 2 (TGM2). However, due to the lack of efficient pan-specific antibodies targeting histaminylated glutamine, the histaminylation proteome in cells remains poorly explored. Here, we report the design and development of a novel N

Identifiers

PMID41959267
PMCPMC13060797

What OpenQuestion holds

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Registered trials

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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.