Evidence map›Paper›PMID 29632820›Full record

ArticleFEBS open bio2018

Crystal structures of FMN-bound and FMN-free forms of dihydroorotate dehydrogenase from

Tomomi Kubota, Osamu Tani, Tomohiko Yamaguchi, Ichiji Namatame, Hitoshi Sakashita, Koji Furukawa, Kazuhiko Yamasaki

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Complementing machine learning-based structure predictions with native mass spectrometry.Protein science : a publication of the Protein Society · 2022
    Article
  4. Article
  5. 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 2 institutions in 1 country.

Tomomi KubotaBiomedical Research Institute National Institute of Advanced Industrial Science and Technology (AIST) Tsukuba Japan.
Osamu TaniBiomedical Research Institute National Institute of Advanced Industrial Science and Technology (AIST) Tsukuba Japan.
Tomohiko YamaguchiDrug Discovery Research Astellas Pharma Inc. Tsukuba Japan.
Ichiji NamatameDrug Discovery Research Astellas Pharma Inc. Tsukuba Japan.
Hitoshi SakashitaBiomedical Research Institute National Institute of Advanced Industrial Science and Technology (AIST) Tsukuba Japan.
Koji FurukawaBiomedical Research Institute National Institute of Advanced Industrial Science and Technology (AIST) Tsukuba Japan.
Kazuhiko YamasakiBiomedical Research Institute National Institute of Advanced Industrial Science and Technology (AIST) Tsukuba Japan.
National Institute of Advanced Industrial Science and Technology · JPAstellas Pharma (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dihydroorotate dehydrogenase (DHODH) is a flavin-binding enzyme essential for pyrimidine biosynthesis, which converts dihydroorotate to orotate. Three-dimensional structures of cytosolic DHODH of parasitic protozoa are of interest in drug discovery for neglected tropical diseases, especially because these enzymes possess significantly different structural and functional properties from the membrane-associated human enzyme. The existing crystal structures of the flavin mononucleotide (FMN)-bound DHODHs reveal a number of interactions stabilizing FMN. However, to understand the binding mechanism correctly, it is necessary to compare the structures of the FMN-bound and FMN-free forms, because the protein moiety of the former is not necessarily the same as the latter. Here, we prepared the FMN-free DHODH of

Indexed as

apoformconformational flexibilityflavin‐binding enzymeneglected tropical diseasepeptide flippingTrypanosoma bruceiX‐ray crystallography

Identifiers

PMID29632820
PMCPMC5881531
OpenAlexW2789709390

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.