Evidence map›Paper›PMID 27226609›Full record

ArticleThe Journal of biological chemistry2016

Direct Comparison of Manganese Detoxification/Efflux Proteins and Molecular Characterization of ZnT10 Protein as a Manganese Transporter.

Yukina Nishito, Natsuko Tsuji, Hitomi Fujishiro, Taka-Aki Takeda, Tomohiro Yamazaki, Fumie Teranishi, Fumiko Okazaki, Ayu Matsunaga, Karin Tuschl, Rajini Rao and 5 more

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 94 citations in OpenAlex.

  1. Review
  2. Article
  3. Removal of Toxic Metabolites-Chelation: Manganese Disorders.Journal of inherited metabolic disease · 2025
    Review
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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

15 authors at 6 institutions in 3 countries.

Yukina NishitoFrom the Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan.
Natsuko TsujiFrom the Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan.
Hitomi Fujishirothe Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima 770-8514, Japan.
Taka-Aki TakedaFrom the Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan.
Tomohiro YamazakiFrom the Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan.
Fumie TeranishiFrom the Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan.
Fumiko Okazakithe Department of Food Science, Kyoto Women's University, Kyoto 605-8501, Japan.
Ayu Matsunagathe Department of Food Science, Kyoto Women's University, Kyoto 605-8501, Japan.
Karin Tuschlthe Clinical and Molecular Genetics Unit, University College London Institute of Child Health, London WC1N 1EH, United Kingdom.
Rajini Raothe Department of Physiology, School of Medicine, The Johns Hopkins University, Baltimore, Maryland 21205, and.
Satoshi Konothe First Department of Medicine, Hamamatsu University School of Medicine, Hamamatsu 431-3192, Japan.
Hiroaki Miyajimathe First Department of Medicine, Hamamatsu University School of Medicine, Hamamatsu 431-3192, Japan.
Hiroshi Naritathe Department of Food Science, Kyoto Women's University, Kyoto 605-8501, Japan.
Seiichiro Himenothe Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima 770-8514, Japan.
Taiho KambeFrom the Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan, kambe1@kais.kyoto-u.ac.jp.
Kyoto University · JPKyoto Women's University · JPHamamatsu University School of Medicine · JPTokushima Bunri University · JPJohns Hopkins Medicine · USUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Manganese homeostasis involves coordinated regulation of specific proteins involved in manganese influx and efflux. However, the proteins that are involved in detoxification/efflux have not been completely resolved nor has the basis by which they select their metal substrate. Here, we compared six proteins, which were reported to be involved in manganese detoxification/efflux, by evaluating their ability to reduce manganese toxicity in chicken DT40 cells, finding that human ZnT10 (hZnT10) was the most significant contributor. A domain swapping and substitution analysis between hZnT10 and the zinc-specific transporter hZnT1 showed that residue Asn(43), which corresponds to the His residue constituting the potential intramembranous zinc coordination site in other ZnT transporters, is necessary to impart hZnT10's unique manganese mobilization activity; residues Cys(52) and Leu(242) in transmembrane domains II and V play a subtler role in controlling the metal specificity of hZnT10. Interestingly, the His → Asn reversion mutant in hZnT1 conferred manganese transport activity and loss of zinc transport activity. These results provide important information about manganese detoxification/efflux mechanisms in vertebrate cells as well as the molecular characterization of hZnT10 as a manganese transporter.

Indexed as

Amino Acid SequenceAnimalsCation Transport ProteinsCell LineGene Knockdown TechniquesManganeseSequence Homology, Amino AcidCation Transport ProteinsManganeseATP13A family proteineffluxferroportinmanganesemetal homeostasisSPCA1substrate specificitytransporterzinc

Identifiers

PMID27226609
PMCPMC4938194
OpenAlexW2373868424

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.