Evidence map›Paper›PMID 33208800›Full record

ArticleScientific reports2020

Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR.

Nan Wu, Naohiro Kobayashi, Kengo Tsuda, Satoru Unzai, Tomonori Saotome, Yutaka Kuroda, Toshio Yamazaki

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-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

36 citing papers in PubMed, 53 citations in OpenAlex.

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  13. A suicidal and extensively disordered luciferase with a bright luminescence.Protein science : a publication of the Protein Society · 2024
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  19. Bioluminescent imaging systems boosting near-infrared signals in mammalian cells.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  20. Article
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

7 authors at 5 institutions in 3 countries.

Nan WuCollege of Food and Bioengineering, Zhengzhou University of Light Industry, 136 Kexue Road, Zhengzhou, 450001, People's Republic of China.
Naohiro KobayashiNMR Science and Development Division, RSC, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama City, Kanagawa, 230-0045, Japan.
Kengo TsudaDivision of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama City, Kanagawa, 230-0045, Japan.
Satoru UnzaiDepartment of Frontier Bioscience, Faculty of Bioscience and Applied Chemistry, Hosei University, 3-7-2, Kajino-cho, Koganei-shi, Tokyo, 184-8584, Japan.
Tomonori SaotomeDepartment of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology (TUAT), 2-24-16 Nakamachi, Koganei-shi, Tokyo, 184-8588, Japan.
Yutaka KurodaDepartment of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology (TUAT), 2-24-16 Nakamachi, Koganei-shi, Tokyo, 184-8588, Japan. ykuroda@cc.tuat.ac.jp.
Toshio YamazakiNMR Science and Development Division, RSC, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama City, Kanagawa, 230-0045, Japan. toshio.yamazaki@riken.jp.
Tokyo University of Agriculture and Technology · JPCE Technologies (United Kingdom) · GBHosei University · JPRIKEN Center for Sustainable Resource Science · JPZhengzhou University of Light Industry · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gaussia luciferase (GLuc) is a small luciferase (18.2 kDa; 168 residues) and is thus attracting much attention as a reporter protein, but the lack of structural information is hampering further application. Here, we report the first solution structure of a fully active, recombinant GLuc determined by heteronuclear multidimensional NMR. We obtained a natively folded GLuc by bacterial expression and efficient refolding using a Solubility Enhancement Petide (SEP) tag. Almost perfect assignments of GLuc's

Indexed as

Amino Acid SequenceAnimalsCopepodaDisulfidesImidazolesLuciferasesNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein DomainsProtein FoldingPyrazinescoelenterazineDisulfidesImidazolesLuciferasesPyrazines

Identifiers

PMID33208800
PMCPMC7674443
OpenAlexW3106503083

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.