Evidence map›Paper›PMID 20454838›Full record

ArticlePharmaceutical research2010

Novel cyclopeptides for the design of MMP directed delivery devices: a novel smart delivery paradigm.

El-Farouck Moustoifa, Mohamed-Anis Alouini, Arnaud Salaün, Thomas Berthelot, Aghleb Bartegi, Sandra Albenque-Rubio, Gérard Déléris

Abstract read
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In one paragraph

Article in Pharmaceutical research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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

7 authors at 4 institutions in 1 country.

El-Farouck MoustoifaUniversité Victor Segalen Bordeaux 2, CNRS UMR 5084 Bio-Organic Chemistry Group, 146 rue Léo Saignat, F-33076, Bordeaux Cedex, France.
Mohamed-Anis Alouini
Arnaud Salaün
Thomas Berthelot
Aghleb Bartegi
Sandra Albenque-Rubio
Gérard Déléris
Bioénergétique et Ingénierie des Protéines · FRCentre National de la Recherche Scientifique · FRUniversité de Bordeaux · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeMatrix metalloproteinases (MMP) are a family of proteolytic enzymes, the expression of which in a key step of tumor progression has been better defined recently. The studies highlighted the ongoing need for very specific inhibitors, substrates or release devices designed to be selective for one or at least very few MMPs.

methodsThis report deals with the design, synthesis and in vitro evaluation of linear and especially novel cyclic peptidic moieties, embodying MMP cleavable sequences designed to answer these questions. FRET (fluorescence resonance energy transfer) labelling via chromophore-modified amino-acids was used to give access to enzyme kinetics.

resultsEvaluation of these peptides showed that cyclisation gives rise to high specificity for certain MMP, suggesting that this approach could provide very specific MMP substrate. Moreover, cyclic structures present a very good plasma stability.

conclusionsThese original derivatives could allow the design of MMP-controlled delivery devices, the specificity of which will be retained in complex biological media and in vivo.

Indexed as

Drug Delivery SystemsDrug DesignMatrix Metalloproteinase InhibitorsAmino Acid SequenceCyclizationFluorescence Resonance Energy TransferHumansKineticsMolecular Sequence DataPeptidesMatrix Metalloproteinase InhibitorsPeptides

Identifiers

PMID20454838
OpenAlexW2082172339

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.