Evidence map›Paper›PMID 35983271›Full record

ArticleACS pharmacology & translational science2022

Matrix Metalloproteinase-14 as an Instigator of Fibrosis in Human Pterygium and Its Pharmacological Intervention.

Cesar Masitas, Zhihong Peng, Man Wang, Mohini Mohan Konai, Luis F Avila-Cobian, Leslie Lemieux, John Hovanesian, James E Grady, Shahriar Mobashery, Mayland Chang

Open access · greenAbstract read
In one paragraph

Article in ACS pharmacology & translational science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

7 citing papers in PubMed, 7 citations in OpenAlex.

  1. Matrix Metalloproteinase 14 in Corneal Neovascularization.International journal of molecular sciences · 2026
    Review
  2. Review
  3. Granzyme B Expression in Conjunctiva of Patients with Pterygium.International journal of molecular sciences · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. 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 2 institutions in 1 country.

Cesar MasitasDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Zhihong PengDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Man WangDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Mohini Mohan KonaiDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Luis F Avila-CobianDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Leslie LemieuxHarvard Eye Associates, Laguna Hills, California 92653, United States.
John HovanesianHarvard Eye Associates, Laguna Hills, California 92653, United States.
James E GradyDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.ORCID https://orcid.org/0000-0002-7695-7883
Mayland ChangDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.ORCID https://orcid.org/0000-0002-4333-3775
University of Notre Dame · USHarvard Eye Associates · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There exists a paucity of information on the pathogenesis of pterygium, a benign ocular tumor that scars the cornea and can lead to vision loss. The main recourse for pterygium is surgery; however, recurrence is observed. Matrix metalloproteinases (MMPs) are involved in the pathology of pterygium. The determination of the specific MMP involved among the 24 human enzymes has not been established due to challenges in MMP profiling. We used an affinity resin that binds specifically to the active forms of MMPs in the complex mixture of the cellular proteome. The proteomics analysis identified active MMP-14 and three related metalloproteinases, ADAM9, ADAM10, and ADAM17, in human pterygia. Inhibition of MMP-14 with the small-molecule inhibitor (

Identifiers

PMID35983271
PMCPMC9380204
OpenAlexW4285795336

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.