Evidence map›Paper›PMID 30337538›Full record

ArticleNature communications2018

Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility.

Mizuho Kajikawa, Toyoyuki Ose, Yuko Fukunaga, Yuki Okabe, Naoki Matsumoto, Kento Yonezawa, Nobutaka Shimizu, Simon Kollnberger, Masanori Kasahara, Katsumi Maenaka

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

10 authors at 5 institutions in 2 countries.

Mizuho KajikawaLaboratory of Microbiology, Showa Pharmaceutical University, Machida, Tokyo, 190-8543, Japan.
Toyoyuki OseLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, 060-0812, Japan.
Yuko FukunagaMedical Institute of Bioregulation, Kyushu University, Fukuoka, 812-8582, Japan.
Yuki OkabeMedical Institute of Bioregulation, Kyushu University, Fukuoka, 812-8582, Japan.
Naoki MatsumotoDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, 277-8562, Japan.
Kento YonezawaPhoton Factory, High Energy Accelerator Research Organization, Tsukuba, Ibaraki, 305-0801, Japan.
Nobutaka ShimizuPhoton Factory, High Energy Accelerator Research Organization, Tsukuba, Ibaraki, 305-0801, Japan.
Simon KollnbergerCardiff Institute of Infection & Immunity, University of Cardiff, Henry Wellcome Building, Heath Park, Cardiff, CF14 4XN, UK.
Masanori KasaharaDepartment of Pathology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo, 060-8638, Japan.
Katsumi MaenakaMedical Institute of Bioregulation, Kyushu University, Fukuoka, 812-8582, Japan. maenaka@pharm.hokudai.ac.jp.ORCID http://orcid.org/0000-0002-5459-521X
Kyushu University · JPHigh Energy Accelerator Research Organization · JPHokkaido University · JPCardiff University · GBThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The MILL family, composed of MILL1 and MILL2, is a group of nonclassical MHC class I molecules that occur in some orders of mammals. It has been reported that mouse MILL2 is involved in wound healing; however, the molecular mechanisms remain unknown. Here, we determine the crystal structure of MILL2 at 2.15 Å resolution, revealing an organization similar to classical MHC class I. However, the α1-α2 domains are not tightly fixed on the α3-β

Indexed as

AnimalsHeparan SulfateHistocompatibility Antigens Class IMembrane GlycoproteinsMiceModels, MolecularProtein BindingProtein DomainsProtein Structure, SecondaryRecombinant ProteinsHeparan SulfateHistocompatibility Antigens Class IMembrane GlycoproteinsMill2 protein, mouseRecombinant Proteins

Identifiers

PMID30337538
PMCPMC6193965
OpenAlexW2897793539

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.