Evidence map›Paper›PMID 27652777›Full record

ArticleScientific reports2016

Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica.

Ae Kyung Park, Il-Sup Kim, Hackwon Do, Byung Wook Jeon, Chang Woo Lee, Soo Jung Roh, Seung Chul Shin, Hyun Park, Young-Saeng Kim, Yul-Ho Kim and 3 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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 70 citations in OpenAlex.

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  17. Overexpression of E3 Ubiquitin Ligase GeneFrontiers in plant science · 2017
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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

13 authors at 4 institutions in 1 country.

Ae Kyung ParkDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Il-Sup KimSchool of Life Sciences, BK21 Plus KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of Korea.
Hackwon DoDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Byung Wook JeonDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Chang Woo LeeDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Soo Jung RohDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Seung Chul ShinDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Hyun ParkDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Young-Saeng KimResearch Institute for Ulleung-do &Dok-do, Kyungpook National University, Daegu 41566, Republic of Korea.
Yul-Ho KimHighland Agriculture Research Institute, National Institute of Crop Science, Rural Development Administration, Pyeongchang 25342, Republic of Korea.
Ho-Sung YoonSchool of Life Sciences, BK21 Plus KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of Korea.
Jun Hyuck LeeDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Han-Woo KimDivision of Polar Life Sciences, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Korea Polar Research Institute · KRKorea University of Science and Technology · KRKyungpook National University · KRRural Development Administration · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ascorbic acid (AsA) maintains redox homeostasis by scavenging reactive oxygen species from prokaryotes to eukaryotes, especially plants. The enzyme monodehydroascorbate reductase (MDHAR) regenerates AsA by catalysing the reduction of monodehydroascorbate, using NADH or NADPH as an electron donor. The detailed recycling mechanism of MDHAR remains unclear due to lack of structural information. Here, we present the crystal structures of MDHAR in the presence of cofactors, nicotinamide adenine dinucleotide (NAD

Identifiers

PMID27652777
PMCPMC5031999
OpenAlexW2522203837

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.