Evidence map›Paper›PMID 23772397›Full record

ArticleFEBS open bio2013

Zinc-binding and structural properties of the histidine-rich loop of Arabidopsis thaliana vacuolar membrane zinc transporter MTP1.

Natsuki Tanaka, Miki Kawachi, Takashi Fujiwara, Masayoshi Maeshima

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 38 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Natsuki TanakaLaboratory of Cell Dynamics, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
Miki Kawachi
Takashi Fujiwara
Masayoshi Maeshima
Nagoya University · JPNagoya University Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The vacuolar Zn(2+)/H(+) antiporter of Arabidopsis thaliana, AtMTP1, has a cytosolic histidine-rich loop (His-loop). We characterized the structures and Zn(2+)-binding properties of the His-loop and other domains. Circular dichroism analyses revealed that the His-loop partly consists of a polyproline type II structure and that its conformational change is induced by Zn(2+) as well as the C-terminal domain. Isothermal titration calorimetry of the His-loop revealed a binding number of four Zn(2+) per molecule. Numbers of Ni and Co associated with the His-loop were approximately one ion per molecule and the thermodynamic parameters of the association with these ions were different from that of Zn(2+). These results suggest the involvement of the His-loop in sensing cytosolic Zn(2+) and in the regulation of zinc transport activity through Zn(2+)-induced structural change.

Indexed as

Circular dichroism spectroscopyCTD, carboxyl terminal domainHis-loop, histidine-rich loopHistidine-rich loopIsothermal titration calorimetryITC, isothermal titration calorimetryMetal tolerance proteinMTP, metal tolerant proteinNTD, amino terminal domainPPII, polyproline type IITFE, trifluoroethanolTM, transmembrane.Zinc bindingZinc transporter

Identifiers

PMID23772397
PMCPMC3668522
OpenAlexW2077695546

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.