Evidence map›Paper›PMID 35157454›Full record

ReviewJournal of medicinal chemistry2022

Advances in the Development of Nonpeptide Small Molecules Targeting Ghrelin Receptor.

Gianfabio Giorgioni, Fabio Del Bello, Wilma Quaglia, Luca Botticelli, Carlo Cifani, E Micioni Di Bonaventura, M V Micioni Di Bonaventura, Alessandro Piergentili

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of medicinal chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 20 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Gianfabio GiorgioniSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, Via Madonna delle Carceri, 62032 Camerino, Italy.ORCID 0000-0002-9576-6580
Fabio Del BelloSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, Via Madonna delle Carceri, 62032 Camerino, Italy.ORCID 0000-0001-6538-6029
Wilma QuagliaSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, Via Madonna delle Carceri, 62032 Camerino, Italy.ORCID 0000-0002-7708-0200
Luca BotticelliSchool of Pharmacy, Pharmacology Unit, University of Camerino, Via Madonna delle Carceri 9, 62032 Camerino, Italy.ORCID 0000-0002-5414-2368
Carlo CifaniSchool of Pharmacy, Pharmacology Unit, University of Camerino, Via Madonna delle Carceri 9, 62032 Camerino, Italy.ORCID 0000-0001-6180-828X
E Micioni Di BonaventuraSchool of Pharmacy, Pharmacology Unit, University of Camerino, Via Madonna delle Carceri 9, 62032 Camerino, Italy.ORCID 0000-0001-8484-7513
M V Micioni Di BonaventuraSchool of Pharmacy, Pharmacology Unit, University of Camerino, Via Madonna delle Carceri 9, 62032 Camerino, Italy.ORCID 0000-0002-8044-1206
Alessandro PiergentiliSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, Via Madonna delle Carceri, 62032 Camerino, Italy.ORCID 0000-0001-6135-6826
Università di Camerino · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ghrelin is an octanoylated peptide acting by the activation of the growth hormone secretagogue receptor, namely, GHS-R1a. The involvement of ghrelin in several physiological processes, including stimulation of food intake, gastric emptying, body energy balance, glucose homeostasis, reduction of insulin secretion, and lipogenesis validates the considerable interest in GHS-R1a as a promising target for the treatment of numerous disorders. Over the years, several GHS-R1a ligands have been identified and some of them have been extensively studied in clinical trials. The recently resolved structures of GHS-R1a bound to ghrelin or potent ligands have provided useful information for the design of new GHS-R1a drugs. This perspective is focused on the development of recent nonpeptide small molecules acting as GHS-R1a agonists, antagonists, and inverse agonists, bearing classical or new molecular scaffolds, as well as on radiolabeled GHS-R1a ligands developed for imaging. Moreover, the pharmacological effects of the most studied ligands have been discussed.

Indexed as

Drug DesignSmall Molecule LibrariesAnimalsGhrelinHomeostasisHumansLigandsReceptors, GhrelinGhrelinGHRL protein, humanLigandsReceptors, GhrelinSmall Molecule Libraries

Identifiers

PMID35157454
PMCPMC8883476
OpenAlexW4212969303

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.