Evidence map›Paper›PMID 28887577›Full record

ReviewCellular and molecular life sciences : CMLS2017

Periostin and its interacting proteins in the construction of extracellular architectures.

Isao Kii, Harumi Ito

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Temporal and spatial expression analysis of periostin in mice periodontitis model.Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2024
    Article
  12. The role of periostin in cardiac fibrosis.Heart failure reviews · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Periostin: an emerging activator of multiple signaling pathways.Journal of cell communication and signaling · 2022
    Review
  18. Article
  19. Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022
    Review
  20. A single injection of periostin decreases cardiac voltage-gated NaThe Journal of veterinary medical science · 2021
    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

2 authors at 1 institution in 2 countries.

Isao KiiCommon Facilities Unit, Integrated Research Group, Compass to Healthy Life Research Complex Program, RIKEN Cluster for Science and Technology Hub, 6-7-3 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo, 650-0047, Japan. isao.kii@riken.jp.
Harumi ItoPathophysiological and Health Science Team, Imaging Platform and Innovation Group, Division of Bio-Function Dynamics Imaging, RIKEN Center for Life Science Technologies, 6-7-3 Minatojima-minamimachi, Chuo-ku, Kobe, 650-0047, Japan.
RIKEN Center for Biosystems Dynamics Research · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (Collagen type I and V, fibronectin, tenascin, and laminin), matricellular proteins (CCN3 and βig-h3), and enzymes that catalyze covalent crosslinking between extracellular matrix proteins (lysyl oxidase and BMP-1). Adjacent binding sites on periostin have been suggested to put the interacting proteins in close proximity, promoting intermolecular interactions between each protein, and leading to their assembly into extracellular architectures. These extracellular architectures determine the mechanochemical properties of connective tissues, in which periostin plays an important role in physiological homeostasis and disease progression. In this review, we introduce the proteins that interact with periostin, and discuss how the multi-domain structure of periostin functions as a scaffold for the assembly of interacting proteins, and how it underlies construction of highly sophisticated extracellular architectures.

Indexed as

Protein Interaction Domains and MotifsProtein Interaction MappingBone Morphogenetic Protein 1Cell Adhesion MoleculesCollagenConnective TissueFibronectinsGene ExpressionHumansLamininNephroblastoma Overexpressed ProteinProtein BindingProtein IsoformsProteoglycansSignal TransductionTenascinBMP1 protein, humanBone Morphogenetic Protein 1CCN3 protein, humanCell Adhesion MoleculesCollagenFibronectinsLAMC2 protein, humanLamininNephroblastoma Overexpressed ProteinPOSTN protein, humanProtein IsoformsProteoglycansTenascinBMP-1CollagenEMIFAS 1FibronectinTenascin

Identifiers

PMID28887577
PMCPMC11107766
OpenAlexW2754439280

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.