Evidence map›Paper›PMID 37094433›Full record

ArticleBioorganic & medicinal chemistry2023

Identification of small molecule inhibitors against MMP-14 via High-Throughput screening.

Hyun Lee, Isoo Youn, Robel Demissie, Tasneem M Vaid, Chun-Tao Che, Dimitri T Azar, Kyu-Yeon Han

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
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  4. Recent Updates on Protease Zymography.Methods in molecular biology (Clifton, N.J.) · 2025
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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

7 authors at 1 institution in 1 country.

Hyun LeeDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60607, USA; Biophysics Core at Research Resource Center, University of Illinois at Chicago, Chicago, IL 60607, USA.
Isoo YounDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60607, USA.
Robel DemissieDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60607, USA; Biophysics Core at Research Resource Center, University of Illinois at Chicago, Chicago, IL 60607, USA.
Tasneem M VaidDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60607, USA.
Chun-Tao CheDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60607, USA.
Dimitri T AzarDepartment of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, University of Illinois at Chicago, Chicago, IL 60612, USA.
Kyu-Yeon HanDepartment of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, University of Illinois at Chicago, Chicago, IL 60612, USA. Electronic address: biohan72@uic.edu.
University of Illinois Chicago · US

Funding

METALLOPROTEINASE EXPRESSION IN CORNEAL WOUNDSR01EY010101 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI AZAR, DIMITRI T · 1999 to 2020
$6.5M
Identification of a new role of membrane‐type 1 matrix metalloproteinases in corneal neovascularizationR01EY033758 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI Kyuyeon Han · 2023 to 2026
$1.6M
NEI NIH HHS R01 EY010101NEI NIH HHS R01 EY033758
6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) are involved in various cellular events in physiology and pathophysiology through endopeptidases activity. The expression levels and activities of most MMPs remain minimal in the normal conditions, whereas some MMPs are significantly activated in pathological conditions such as cancer and neovascularization. Hence, MMPs are considered as both diagnostic markers and potential targets for therapeutic agents. Twenty-three known human MMPs share a similar active site structure with a zinc-binding motif, resulting in lack of specificity. Therefore, the enhancement of target specificity is a primary goal for the development of specific MMP inhibitors. MMP-14 regulates VEGFA/VEGFR2-system through cleavage of the non-functional VEGFR1 in vascular angiogenesis. In this study, we developed a fluorescence-based enzymatic assay using a specific MMP-14 substrate generated from VEGFR1 cleavage site. This well optimized assay was used as a primary screen method to identify MMP-14 specific inhibitors from 1,200 Prestwick FDA-approved drug library. Of ten initial hits, two compounds showed IC

Indexed as

ClioquinolHigh-Throughput Screening AssaysHumansMatrix Metalloproteinase 14Matrix Metalloproteinase InhibitorsMatrix MetalloproteinasesClioquinolMatrix Metalloproteinase 14Matrix Metalloproteinase InhibitorsMatrix MetalloproteinasesHigh-throughput screeningMatrix metalloproteinasesMembrane-type 1 MMP (MMP-14)Small molecule inhibitor

Identifiers

PMID37094433
PMCPMC10167624
OpenAlexW4366134150

What OpenQuestion holds

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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.