Evidence map›Paper›PMID 28483911›Full record

ArticleMolecular and cellular biology2017

CD99-Derived Agonist Ligands Inhibit Fibronectin-Induced Activation of β1 Integrin through the Protein Kinase A/SHP2/Extracellular Signal-Regulated Kinase/PTPN12/Focal Adhesion Kinase Signaling Pathway.

Kyoung-Jin Lee, Yuri Kim, Yeon Ho Yoo, Min-Seo Kim, Sun-Hee Lee, Chang-Gyum Kim, Kyeonghan Park, Dooil Jeoung, Hansoo Lee, In Young Ko and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. CD99 at the crossroads of physiology and pathology.Journal of cell communication and signaling · 2018
    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

11 authors at 1 institution in 1 country.

Kyoung-Jin LeeDepartment of Anatomy and Cell Biology, School of Medicine, Kangwon National University, Chuncheon, Republic of Korea.
Yuri KimDepartment of Anatomy and Cell Biology, School of Medicine, Kangwon National University, Chuncheon, Republic of Korea.
Yeon Ho YooDepartment of Anatomy and Cell Biology, School of Medicine, Kangwon National University, Chuncheon, Republic of Korea.
Min-Seo KimDepartment of Anatomy and Cell Biology, School of Medicine, Kangwon National University, Chuncheon, Republic of Korea.
Sun-Hee LeeDepartment of Anatomy and Cell Biology, School of Medicine, Kangwon National University, Chuncheon, Republic of Korea.
Chang-Gyum KimDepartment of Anatomy and Cell Biology, School of Medicine, Kangwon National University, Chuncheon, Republic of Korea.
Kyeonghan ParkDepartment of Anatomy and Cell Biology, School of Medicine, Kangwon National University, Chuncheon, Republic of Korea.
Dooil JeoungDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, Republic of Korea.
Hansoo LeeDepartment of Biological Sciences, College of Natural Sciences, Kangwon National University, Chuncheon, Republic of Korea.
In Young KoDepartment of Medical Biotechnology, College of Biomedical Science, Kangwon National University, Chuncheon, Republic of Korea.
Jang-Hee HahnDepartment of Anatomy and Cell Biology, School of Medicine, Kangwon National University, Chuncheon, Republic of Korea jhahn@kangwon.ac.kr.
Kangwon National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human CD99 protein is a 32-kDa glycosylated transmembrane protein that regulates various cellular responses, including cell adhesion and leukocyte extravasation. We previously reported that CD99 activation suppresses β1 integrin activity through dephosphorylation of focal adhesion kinase (FAK) at Y397. We explored a molecular mechanism underlying the suppression of β1 integrin activity by CD99 agonists and its relevance to tumor growth

Indexed as

Signal Transduction12E7 AntigenCell AdhesionCell Line, TumorCell MovementCyclic AMP-Dependent Protein KinasesExtracellular Signal-Regulated MAP KinasesFibronectinsFocal Adhesion Protein-Tyrosine KinasesHumansIntegrin beta ChainsLigandsPhosphorylationProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 1212E7 AntigenCD99 protein, humanCyclic AMP-Dependent Protein KinasesExtracellular Signal-Regulated MAP KinasesFibronectinsFocal Adhesion Protein-Tyrosine KinasesIntegrin beta ChainsLigandsProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 12PTPN12 protein, humanagonist ligandsCD99MCF-7 cellsPTPN12β1 integrin

Identifiers

PMID28483911
PMCPMC5492169
OpenAlexW2612947772

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.