Evidence map›Paper›PMID 26569224›Full record

ArticleInternational journal of molecular sciences2015

Identification of Arsenic Direct-Binding Proteins in Acute Promyelocytic Leukaemia Cells.

Tao Zhang, Haojie Lu, Weijun Li, Ronggui Hu, Zi Chen

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

11 citing papers in PubMed, 20 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
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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

5 authors at 3 institutions in 1 country.

Tao ZhangDepartment of Laboratory Medicine, Huashan Hospital, Fudan University, 12 Central Urumqi Road, Shanghai 200040, China. shmuzt@126.com.
Haojie LuShanghai Cancer Center and Key Laboratory of Glycoconjugates Research Ministry of Public Health, Fudan University, Shanghai 200032, China. luhaojie@fudan.edu.cn.
Weijun LiState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China. drchenzi2@163.com.
Ronggui HuState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China. coryhu@sibs.ac.cn.
Zi ChenDepartment of Hematology, Huashan Hospital, Fudan University, Shanghai 200040, China. drchenzi@tom.com.
Fudan University · CNCenter for Excellence in Molecular Cell Science · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The identification of arsenic direct-binding proteins is essential for determining the mechanism by which arsenic trioxide achieves its chemotherapeutic effects. At least two cysteines close together in the amino acid sequence are crucial to the binding of arsenic and essential to the identification of arsenic-binding proteins. In the present study, arsenic binding proteins were pulled down with streptavidin and identified using a liquid chromatograph-mass spectrometer (LC-MS/MS). More than 40 arsenic-binding proteins were separated, and redox-related proteins, glutathione S-transferase P1 (GSTP1), heat shock 70 kDa protein 9 (HSPA9) and pyruvate kinase M2 (PKM2), were further studied using binding assays in vitro. Notably, PKM2 has a high affinity for arsenic. In contrast to PKM2, GSTP1and HSPA9 did not combine with arsenic directly in vitro. These observations suggest that arsenic-mediated acute promyelocytic leukaemia (APL) suppressive effects involve PKM2. In summary, we identified several arsenic binding proteins in APL cells and investigated the therapeutic mechanisms of arsenic trioxide for APL. Further investigation into specific signal pathways by which PKM2 mediates APL developments may lead to a better understanding of arsenic effects on APL.

Indexed as

Antineoplastic AgentsArsenicalsArsenic TrioxideBiotinBiotinylationCarrier ProteinsCell Line, TumorChromatography, LiquidGlutathione S-Transferase piHSP70 Heat-Shock ProteinsHumansLeukemia, Promyelocytic, AcuteMembrane ProteinsMitochondrial ProteinsNeoplasm ProteinsOxidesAntineoplastic AgentsArsenicalsArsenic TrioxideBiotinCarrier ProteinsGlutathione S-Transferase piGSTP1 protein, humanHSP70 Heat-Shock ProteinsHSPA9 protein, humanMembrane ProteinsMitochondrial ProteinsNeoplasm ProteinsOxidesStreptavidinThyroid Hormone-Binding ProteinsThyroid Hormonesacute promyelocytic leukaemiaarsenic-binding proteinarsenic-biotinLC-MS/MSpyruvate kinase M2

Identifiers

PMID26569224
PMCPMC4661853
OpenAlexW2100241300

What OpenQuestion holds

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LicenceCC BY
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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.