Evidence map›Paper›PMID 29050309›Full record

ArticleOncotarget2017

Fibronectin in cell adhesion and migration via N-glycosylation.

Cheng-Te Hsiao, Hung-Wei Cheng, Chi-Ming Huang, Hao-Ru Li, Meng-Hsin Ou, Jie-Rong Huang, Kay-Hooi Khoo, Helen Wenshin Yu, Yin-Quan Chen, Yang-Kao Wang and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

72 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
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  12. Pharmacological blocking of microfibrillar-associated protein 4 reduces retinal neoangiogenesis and vascular leakage.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  13. Review
  14. Article
  15. Vascular Extracellular Matrix in Atherosclerosis.International journal of molecular sciences · 2024
    Review
  16. Mutations in fibronectin dysregulate chondrogenesis in skeletal dysplasia.Cellular and molecular life sciences : CMLS · 2024
    Article
  17. Review
  18. Article
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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

12 authors at 4 institutions in 1 country.

Cheng-Te HsiaoInstitute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan.
Hung-Wei ChengInstitute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan.
Chi-Ming HuangInstitute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan.
Hao-Ru LiInstitute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan.
Meng-Hsin OuInstitute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan.
Jie-Rong HuangInstitute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan.
Kay-Hooi KhooInstitute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan.
Helen Wenshin YuBiophotonics and Molecular Imaging Research Center, National Yang-Ming University, Taipei 11221, Taiwan.
Yin-Quan ChenBiophotonics and Molecular Imaging Research Center, National Yang-Ming University, Taipei 11221, Taiwan.
Yang-Kao WangDepartment of Cell Biology and Anatomy, National Cheng Kung University, Tainan 70101, Taiwan.
Arthur ChiouBiophotonics and Molecular Imaging Research Center, National Yang-Ming University, Taipei 11221, Taiwan.
Jean-Cheng KuoInstitute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan.
National Yang Ming Chiao Tung University · TWNational Yang Ming Chiao Tung University · TWNational Taiwan University · TWNational Cheng Kung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Directed cell migration is an important step in effective wound healing and requires the dynamic control of the formation of cell-extracellular matrix interactions. Plasma fibronectin is an extracellular matrix glycoprotein present in blood plasma that plays crucial roles in modulating cellular adhesion and migration and thereby helping to mediate all steps of wound healing. In order to seek safe sources of plasma fibronectin for its practical use in wound dressing, we isolated fibronectin from human (homo) and porcine plasma and demonstrated that both have a similar ability as a suitable substrate for the stimulation of cell adhesion and for directing cell migration. In addition, we also defined the N-glycosylation sites and N-glycans present on homo and porcine plasma fibronectin. These N-glycosylation modifications of the plasma fibronectin synergistically support the integrin-mediated signals to bring about mediating cellular adhesion and directed cell migration. This study not only determines the important function of N-glycans in both homo and porcine plasma fibronectin-mediated cell adhesion and directed cell migration, but also reveals the potential applications of porcine plasma fibronectin if it was applied as a material for clinical wound healing and tissue repair.

Indexed as

cell migrationfibronectinglycoproteomicsintegrin signalsN-glycans

Identifiers

PMID29050309
PMCPMC5642584
OpenAlexW2743465912

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.