Evidence map›Paper›PMID 28337319›Full record

ArticleACS medicinal chemistry letters2017

Bifunctional Inhibitors as a New Tool To Reduce Cancer Cell Invasion by Impairing MMP-9 Homodimerization.

Elisa Nuti, Lea Rosalia, Doretta Cuffaro, Caterina Camodeca, Chiara Giacomelli, Eleonora Da Pozzo, Tiziano Tuccinardi, Barbara Costa, Claudia Antoni, Laura Vera and 7 more

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

5 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Development of a fluorogenic ADAMTS-7 substrate.Journal of enzyme inhibition and medicinal chemistry · 2021
    Article
  3. Article
  4. Article
  5. 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

17 authors at 2 institutions in 2 countries.

Elisa NutiDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Lea RosaliaDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Doretta CuffaroDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Caterina CamodecaDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Chiara GiacomelliDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Eleonora Da PozzoDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Tiziano TuccinardiDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Barbara CostaDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Claudia AntoniDipartimento di Farmacia, Università di Pisa, Via Bonanno 6, 56126 Pisa, Italy; CEA, iBiTec-S, Service d'Ingenierie Moleculaire des Proteines, CE-Saclay, 91191 Gif sur Yvette Cedex, France.
Laura VeraCEA, iBiTec-S , Service d'Ingenierie Moleculaire des Proteines, CE-Saclay, 91191 Gif sur Yvette Cedex, France.
Lidia CicconeDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Elisabetta OrlandiniDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Susanna NencettiDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Vincent DiveCEA, iBiTec-S , Service d'Ingenierie Moleculaire des Proteines, CE-Saclay, 91191 Gif sur Yvette Cedex, France.
Claudia MartiniDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
Enrico A SturaCEA, iBiTec-S , Service d'Ingenierie Moleculaire des Proteines, CE-Saclay, 91191 Gif sur Yvette Cedex, France.
Armando RosselloDipartimento di Farmacia, Università di Pisa , Via Bonanno 6, 56126 Pisa, Italy.
University of Pisa · ITCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein homodimers play important roles in physiological and pathological processes, including cancer invasion and metastasis. Recently, MMP-9 natural homodimerization via the PEX domain has been correlated with high migration rates of aggressive cancer cells. Here we propose that bifunctional MMP-9 inhibitors designed to impair natural MMP-9 homodimerization promoted by PEX-PEX interactions might be an effective tool to fight cancer cell invasion. Elaborating a previously described dimeric hydroxamate inhibitor

Indexed as

Bifunctional inhibitorsglioblastoma multiformeMMP-9 homodimerizationX-ray crystallography

Identifiers

PMID28337319
PMCPMC5346986
OpenAlexW2586679635

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.