Evidence map›Paper›PMID 27922079›Full record

ArticleScientific reports2016

Proteomic profiling reveals that collismycin A is an iron chelator.

Makoto Kawatani, Makoto Muroi, Akira Wada, Gyo Inoue, Yushi Futamura, Harumi Aono, Kenshirou Shimizu, Takeshi Shimizu, Yasuhiro Igarashi, Naoko Takahashi-Ando and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

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  15. Anti-MRSA Activity of Actinomycin XFrontiers in microbiology · 2020
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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

11 authors at 3 institutions in 1 country.

Makoto KawataniChemical Biology Research Group, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Makoto MuroiChemical Biology Research Group, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Akira WadaNonnatural Amino Acid Technology Team, RIKEN CLST, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Gyo InoueDepartment of Applied Chemistry, Faculty of Science and Engineering, Toyo University, 2100 Kujirai, Kawagoe, Saitama 350-0815, Japan.
Yushi FutamuraChemical Biology Research Group, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Harumi AonoChemical Biology Research Group, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Kenshirou ShimizuChemical Biology Research Group, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Takeshi ShimizuChemical Biology Research Group, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Yasuhiro IgarashiBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
Naoko Takahashi-AndoDepartment of Applied Chemistry, Faculty of Science and Engineering, Toyo University, 2100 Kujirai, Kawagoe, Saitama 350-0815, Japan.
Hiroyuki OsadaChemical Biology Research Group, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
RIKEN · JPToyo University · JPToyama Prefectural University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collismycin A (CMA), a microbial product, has anti-proliferative activity against cancer cells, but the mechanism of its action remains unknown. Here, we report the identification of the molecular target of CMA by ChemProteoBase, a proteome-based approach for drug target identification. ChemProteoBase profiling showed that CMA is closely clustered with di-2-pyridylketone 4,4-dimethyl-3-thiosemicarbazone, an iron chelator. CMA bound to both Fe(II) and Fe(III) ions and formed a 2:1 chelator-iron complex with a redox-inactive center. CMA-induced cell growth inhibition was completely canceled by Fe(II) and Fe(III) ions, but not by other metal ions such as Zn(II) or Cu(II). Proteomic and transcriptomic analyses showed that CMA affects the glycolytic pathway due to the accumulation of HIF-1α. These results suggest that CMA acts as a specific iron chelator, leading to the inhibition of cancer cell growth.

Indexed as

Transcriptome2,2'-DipyridylA549 CellsAntineoplastic AgentsCell Cycle CheckpointsCell Line, TumorCell ProliferationCoordination ComplexesDatabases, ChemicalGlycolysisHeLa CellsHigh-Throughput Screening AssaysHumansHypoxia-Inducible Factor 1, alpha SubunitIronIron Chelating Agents2,2'-DipyridylAntineoplastic Agentscollismycin ACoordination ComplexesHIF1A protein, humanHypoxia-Inducible Factor 1, alpha SubunitIronIron Chelating AgentsThiosemicarbazones

Identifiers

PMID27922079
PMCPMC5138588
OpenAlexW2560329598

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.