Evidence map›Paper›PMID 37410126›Full record

ReviewAnalytical and bioanalytical chemistry2023

Recent progress in analytical strategies of arsenic-binding proteomes in living systems.

Jiahui Liu, Baowei Chen, Ruijia Zhang, Yizheng Li, Ruohong Chen, Siqi Zhu, Shijun Wen, Tiangang Luan

Abstract readReview
PubMed Publisher
In one paragraph

Review in Analytical and bioanalytical chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. The arsenic proteome in cancer: Unravelling molecular mechanisms of anticancer drugs.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Review
  2. Article
  3. Article
  4. Recent advances and future developments in ultrasensitive omics.Analytical and bioanalytical chemistry · 2023
    Article
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

8 authors at 3 institutions in 1 country.

Jiahui Liu *State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, 510275, China.
Baowei Chen *Southern Marine Science and Engineering Guangdong Laboratory, School of Marine Sciences, Sun Yat-sen University, Zhuhai, 519082, China.
Ruijia ZhangState Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, 510275, China.
Yizheng LiSouthern Marine Science and Engineering Guangdong Laboratory, School of Marine Sciences, Sun Yat-sen University, Zhuhai, 519082, China.
Ruohong ChenState Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, 510275, China.
Siqi ZhuState Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, 510275, China.
Shijun WenState Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center, Guangzhou, 510060, China.
Tiangang LuanState Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, 510275, China. cesltg@mail.sysu.edu.cn.
Sun Yat-sen University · CNSouthern Marine Science and Engineering Guangdong Laboratory (Guangzhou) · CNSun Yat-sen University Cancer Center · CN

Funding

National Natural Science Foundation of China 22127810National Natural Science Foundation of China 22276224
6 · The paper itself

Abstract

Arsenic (As) is one of the most concerning elements due to its high exposure risks to organisms and ecosystems. The interaction between arsenicals and proteins plays a pivotal role in inducing their biological effects on living systems, e.g., arsenicosis. In this review article, the recent advances in analytical techniques and methods of As-binding proteomes were well summarized and discussed, including chromatographic separation and purification, biotin-streptavidin pull-down probes, in situ imaging using novel fluorescent probes, and protein identification. These analytical technologies could provide a growing body of knowledge regarding the composition, level, and distribution of As-binding proteomes in both cells and biological samples, even at the organellar level. The perspectives on analysis of As-binding proteomes are also proposed, e.g., isolation and identification of minor proteins, in vivo targeted protein degradation (TPD) technologies, and spatial As-binding proteomics. The application and development of sensitive, accurate, and high-throughput methodologies of As-binding proteomics would enable us to address the key molecular mechanisms underlying the adverse health effects of arsenicals.

Indexed as

ArsenicArsenicalsBiotinEcosystemProteomeArsenicArsenicalsBiotinProteomeAs-binding proteomesBiotin-streptavidin pull-down methodsChromatography-based approachesImaging strategiesProtein identification

Identifiers

PMID37410126
OpenAlexW4383301659

What OpenQuestion 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 OpenQuestion graph.