Evidence map›Paper›PMID 33673639›Full record

ArticlePharmaceuticals (Basel, Switzerland)2021

Discovery and Optimization of Selective Inhibitors of Meprin α (Part II).

Chao Wang, Juan Diez, Hajeung Park, Timothy P Spicer, Louis D Scampavia, Christoph Becker-Pauly, Gregg B Fields, Dmitriy Minond, Thomas D Bannister

Abstract read
In one paragraph

Article in Pharmaceuticals (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. TyrosineACS chemical neuroscience · 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

9 authors.

Chao WangDepartment of Molecular Medicine, Scripps Research, Jupiter, FL 33458, USA.
Juan DiezRumbaugh-Goodwin Institute for Cancer Research, Nova Southeastern University, 3321 College Avenue, CCR r.605, Fort Lauderdale, FL 33314, USA.
Hajeung ParkDepartment of Molecular Medicine, Scripps Research, Jupiter, FL 33458, USA.
Timothy P SpicerDepartment of Molecular Medicine, Scripps Research, Jupiter, FL 33458, USA.
Louis D ScampaviaDepartment of Molecular Medicine, Scripps Research, Jupiter, FL 33458, USA.
Christoph Becker-PaulyUnit for Degradomics of the Protease Web, University of Kiel, Institute of Biochemistry, Rudolf-Höber-Str.1, 24118 Kiel, Germany.ORCID 0000-0002-5100-9916
Gregg B FieldsDepartment of Chemistry & Biochemistry and I-HEALTH, Florida Atlantic University, 5353 Parkside Drive, Jupiter, FL 33458, USA.ORCID 0000-0001-7126-1601
Dmitriy MinondDepartment of Chemistry, Scripps Research, Jupiter, FL 33458, USA.
Thomas D BannisterDepartment of Molecular Medicine, Scripps Research, Jupiter, FL 33458, USA.

Funding

HTS for selective inhibitors of Meprin alpha and betaR01AR066676 · NIAMS · TORREY PINES INST FOR MOLECULAR STUDIES · PI MINOND, DMITRIY, SCAMPAVIA, LOUIS DANIEL · 2015 to 2017
$1.0M
In vivo efficacy evaluation of novel melanoma activesR15CA249788 · NCI · NOVA SOUTHEASTERN UNIVERSITY · PI MINOND, DMITRIY · 2020 to 2020
$453k
Deutsche Forschungsgemeinschaft A9 and A15NCI NIH HHS CA249788NIAMS NIH HHS AR066676
6 · The paper itself

Abstract

Meprin α is a zinc metalloproteinase (metzincin) that has been implicated in multiple diseases, including fibrosis and cancers. It has proven difficult to find small molecules that are capable of selectively inhibiting meprin a, or its close relative meprin b, over numerous other metzincins which, if inhibited, would elicit unwanted effects. We recently identified possible molecular starting points for meprin a-specific inhibition through an HTS effort (see part I, preceding paper). Here, in part II, we report further efforts to optimize potency and selectivity. We hope that a hydroxamic acid meprin α inhibitor probe will help define the therapeutic potential for small molecule meprin a inhibition and spur further drug discovery efforts in the area of zinc metalloproteinase inhibition.

Indexed as

medicinal chemistrymeprin αmeprin βprobe developmentzinc metalloproteinase

Identifiers

PMID33673639
PMCPMC7997411

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.