Evidence map›Paper›PMID 30068923›Full record

ArticleScientific reports2018

Identification, Characterization, and X-ray Crystallographic Analysis of a Novel Type of Lectin AJLec from the Sea Anemone Anthopleura japonica.

Hideaki Unno, Azusa Nakamura, Shingo Mori, Shuichiro Goda, Kenichi Yamaguchi, Keiko Hiemori, Hiroaki Tateno, Tomomitsu Hatakeyama

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
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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

8 authors at 3 institutions in 1 country.

Hideaki UnnoGraduate School of Engineering, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, 852-8521, Japan. unno@nagasaki-u.ac.jp.ORCID 0000-0001-5917-269X
Azusa NakamuraGraduate School of Engineering, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, 852-8521, Japan.
Shingo MoriGraduate School of Engineering, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, 852-8521, Japan.
Shuichiro GodaGraduate School of Engineering, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, 852-8521, Japan.
Kenichi YamaguchiFaculty of Fisheries, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, 852-8521, Japan.
Keiko HiemoriResearch Center for Medical Glycosciences, National Institute of Advanced Industrial Science and Technology, Tsukuba, 305-8568, Japan.
Hiroaki TatenoResearch Center for Medical Glycosciences, National Institute of Advanced Industrial Science and Technology, Tsukuba, 305-8568, Japan.
Tomomitsu HatakeyamaGraduate School of Engineering, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, 852-8521, Japan.
Nagasaki University · JPNational Institute of Advanced Industrial Science and Technology · JPUniversity of Nagasaki · JP

Funding

Japan Society for the Promotion of Science (JSPS) 15K06977Japan Society for the Promotion of Science (JSPS) 23580137Japan Society for the Promotion of Science (JSPS) 25450133Japan Society for the Promotion of Science (JSPS) 26450128
6 · The paper itself

Abstract

A novel galactose-specific lectin, AJLec (18.5 kDa), was isolated from the sea anemone, Anthopleura japonica. AJLec was characterized using the hemagglutination assay, isothermal titration calorimetry (ITC), and glycoconjugate microarray analysis and we found that AJLec has a specificity for galactose monomers and β-linked terminal galactose residues in complex carbohydrates, but not for N-acetylgalactosamine (GalNAc), which is commonly recognized by galactose-binding lectins. The primary structure of AJLec did not show homology with known lectins, and a crystal structural analysis also revealed a unique homodimeric structure. The crystal structure of AJLec complexed with lactose was solved by measuring the sulfur single-wavelength anomalous diffraction (S-SAD) phasing with an in-house Cu Kα source method. This analysis revealed that the galactose residue in lactose was recognized via its O2, O3, and O4 hydroxyl groups and ring oxygen by calcium coordination and two hydrogen bonds with residues in the carbohydrate-binding site, which demonstrated strict specificity for the β-linked terminal galactose in this lectin.

Indexed as

AnimalsBiological FactorsCalorimetryCrystallography, X-RayHemagglutinationLectinsModels, MolecularMolecular WeightPolysaccharidesProtein BindingProtein ConformationSea AnemonesSubstrate SpecificityBiological FactorsLectinsPolysaccharides

Identifiers

PMID30068923
PMCPMC6070535
OpenAlexW2884453537

What OpenQuestion holds

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Registered trials

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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.