Evidence map›Paper›PMID 33294281›Full record

ArticleAmerican journal of cancer research2020

Exposure of the cryptic de-adhesive site FNIII14 in fibronectin molecule and its binding to membrane-type eEF1A induce migration and invasion of cancer cells via β1-integrin inactivation.

Keisuke Itagaki, Manabu Sasada, Satoru Miyazaki, Takuya Iyoda, Takahiro Imaizumi, Makoto Haga, Akira Kuga, Hiroki Inomata, Yosuke Kondo, Satoshi Osada and 3 more

Open access · greenAbstract read
In one paragraph

Article in American journal of cancer research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
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

13 authors at 2 institutions in 1 country.

Keisuke ItagakiDepartment of Molecular Pathophysiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Manabu SasadaDepartment of Molecular Pathophysiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Satoru MiyazakiDepartment of Medical and Life Science, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Takuya IyodaDepartment of Molecular Pathophysiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Takahiro ImaizumiDepartment of Molecular Pathophysiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Makoto HagaDepartment of Molecular Pathophysiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Akira KugaDepartment of Molecular Pathophysiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Hiroki InomataDepartment of Molecular Pathophysiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Yosuke KondoDepartment of Medical and Life Science, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Satoshi OsadaDepartment of Biochemistry, Faculty of Science and Engineering, Saga University 1 Honjo-machi, Saga 840-8502, Japan.
Hiroaki KodamaDepartment of Biochemistry, Faculty of Science and Engineering, Saga University 1 Honjo-machi, Saga 840-8502, Japan.
Yoshikazu HigamiDepartment of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Fumio FukaiDepartment of Molecular Pathophysiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science 2641 Yamazaki, Noda-Shi, Chiba 278-8510, Japan.
Tokyo University of Science · JPSaga University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell migration is a highly coordinated process that involves not only integrin-mediated adhesion but also de-adhesion. We previously found that a cryptic de-adhesive site within fibronectin molecule, termed FNIII14, weakens cell adhesion to the extracellular matrix by inactivating β1-integrins. Surprisingly, eukaryotic translation elongation factor-1A (eEF1A), an essential factor during protein biosynthesis, was identified as a membrane receptor that mediates the de-adhesive effect of FNIII14. Here, we demonstrate that FNIII14-mediated de-adhesion causes enhanced migration and invasion in two types of highly invasive/metastatic cancer cells, resulting in the initiation of metastasis. Both

Indexed as

de-adhesioneukaryotic translation elongation factor 1Aextracellular matrixfibronectinIntegrinmetastasis

Identifiers

PMID33294281
PMCPMC7716165
OpenAlexW3112394648

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.