Evidence map›Paper›PMID 25664783›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

Preliminary X-ray analysis of the binding domain of the soybean vacuolar sorting receptor complexed with a sorting determinant of a seed storage protein.

Nobuyuki Maruyama, Tomohiro Goshi, Shigeru Sugiyama, Mayumi Niiyama, Hiroaki Adachi, Kazufumi Takano, Satoshi Murakami, Tsuyoshi Inoue, Yusuke Mori, Hiroyoshi Matsumura and 1 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.0field-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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

11 authors at 4 institutions in 1 country.

Nobuyuki MaruyamaLaboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Gokasho, Uji 611-0011, Japan.
Tomohiro GoshiLaboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Gokasho, Uji 611-0011, Japan.
Shigeru SugiyamaGraduate School of Science, Osaka University, Machikaneyama 1-3, Toyonaka, Osaka 560-8531, Japan.
Mayumi NiiyamaGraduate School of Engineering, Osaka University, Yamadaoka 2-1, Suita, Osaka 565-0871, Japan.
Hiroaki AdachiSOSHO Inc., 313 Photonics Center Building, Yamadaoka 2-1, Suita, Osaka 565-0871, Japan.
Kazufumi TakanoSOSHO Inc., 313 Photonics Center Building, Yamadaoka 2-1, Suita, Osaka 565-0871, Japan.
Satoshi MurakamiSOSHO Inc., 313 Photonics Center Building, Yamadaoka 2-1, Suita, Osaka 565-0871, Japan.
Tsuyoshi InoueGraduate School of Engineering, Osaka University, Yamadaoka 2-1, Suita, Osaka 565-0871, Japan.
Yusuke MoriGraduate School of Engineering, Osaka University, Yamadaoka 2-1, Suita, Osaka 565-0871, Japan.
Hiroyoshi MatsumuraGraduate School of Engineering, Osaka University, Yamadaoka 2-1, Suita, Osaka 565-0871, Japan.
Bunzo MikamiLaboratory of Applied Structural Biology, Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
Osaka University · JPKyoto University · JPTaisho Pharmaceutical (Japan) · JPKyoto Prefectural University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Conglycinin is a major seed storage protein in soybeans, which are an important source of protein. The major subunits (α, α' and β) of β-conglycinin are sorted to protein-storage vacuoles in seed cells. Vacuolar sorting receptor (VSR) is an integral membrane protein that recognizes the sorting determinant of vacuolar proteins, including β-conglycinin, and regulates their sorting process. Vacuolar sorting determinants of the α' and β subunits of β-conglycinin exist in their C-terminal peptides. Here, the preliminary X-ray diffraction analysis of the binding domain of soybean VSR crystallized with the peptide responsible for the sorting determinant in β-conglycinin is reported. X-ray diffraction data were collected to a resolution of 3.5 Å. The crystals belonged to space group P3121, with unit-cell parameters a = b = 116.4, c = 86.1 Å.

Indexed as

Antigens, PlantCrystallizationCrystallography, X-RayElectrophoresis, Polyacrylamide GelGlobulinsGlycine maxPeptidesProtein Structure, TertiaryProtein TransportReceptors, Cell SurfaceSeed Storage ProteinsSoybean ProteinsVacuolesAntigens, Plantbeta-conglycinin protein, Glycine maxGlobulinsPeptidesReceptors, Cell SurfaceSeed Storage ProteinsSoybean Proteinsseed storage proteinsoybeanvacuolar sorting receptorβ-conglycinin

Identifiers

PMID25664783
PMCPMC4321463
OpenAlexW2047987781

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.