Evidence map›Paper›PMID 25288495›Full record

ArticleBioorganic & medicinal chemistry2014

Peptidomimetics of Arg-Phe-NH2 as small molecule agonists of Mas-related gene C (MrgC) receptors.

Niyada Hin, Jesse Alt, Sarah C Zimmermann, Greg Delahanty, Dana V Ferraris, Camilo Rojas, Fengxian Li, Qin Liu, Xinzhong Dong, Barbara S Slusher and 1 more

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2014. 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
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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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

11 authors at 2 institutions in 1 country.

Niyada HinBrain Science Institute, Johns Hopkins University, Baltimore, MD 21205, United States.
Jesse AltBrain Science Institute, Johns Hopkins University, Baltimore, MD 21205, United States.
Sarah C ZimmermannDepartment of Neurology, Johns Hopkins University, Baltimore, MD 21205, United States.
Greg DelahantyBrain Science Institute, Johns Hopkins University, Baltimore, MD 21205, United States.
Dana V FerrarisBrain Science Institute, Johns Hopkins University, Baltimore, MD 21205, United States.
Camilo RojasBrain Science Institute, Johns Hopkins University, Baltimore, MD 21205, United States.
Fengxian LiCenter for the Study of Itch and Departments of Anesthesiology and Anatomy & Neurobiology, Washington University School of Medicine, St Louis, MO 63110, United States.
Qin LiuCenter for the Study of Itch and Departments of Anesthesiology and Anatomy & Neurobiology, Washington University School of Medicine, St Louis, MO 63110, United States.
Xinzhong DongThe Solomon H. Snyder Department of Neuroscience, Johns Hopkins University, Baltimore, MD 21205, United States.
Barbara S SlusherBrain Science Institute, Johns Hopkins University, Baltimore, MD 21205, United States; Department of Neurology, Johns Hopkins University, Baltimore, MD 21205, United States.
Takashi TsukamotoBrain Science Institute, Johns Hopkins University, Baltimore, MD 21205, United States; Department of Neurology, Johns Hopkins University, Baltimore, MD 21205, United States. Electronic address: ttsukamoto@jhmi.edu.
Johns Hopkins University · USWashington University in St. Louis · US

Funding

Functional analysis of the Mrg receptor family in pain sensationR01NS054791 · NINDS · JOHNS HOPKINS UNIVERSITY · PI DONG, XINZHONG · 2007 to 2020
$5.0M
NINDS NIH HHS 2R01NS054791NINDS NIH HHS R01 NS054791
6 · The paper itself

Abstract

A series of Arg-Phe-NH2 peptidomimetics containing an Arg mimetic were synthesized and tested as agonists of human MrgX1, rat MrgC, and mouse MrgC11 receptors. As predicted from the previously established species specificity, these peptidomimetics were found to be devoid of MrgX1 agonist activity. In contrast, these compounds acted as agonists of MrgC and/or MrgC11 with varying degrees of potency. These new peptidomimetics should complement the existing small molecule human MrgX1 agonists and enhance our ability to assess the therapeutic utility of targeting Mrg receptors in rodent models.

Indexed as

AnimalsHEK293 CellsHumansMiceNeuropeptidesPeptidomimeticsProtein BindingRatsReceptors, G-Protein-CoupledSmall Molecule LibrariesTransfectionarginylphenylalaninamidemas-related gene-X1 receptor, humanMrgprc protein, ratMrgprx1 protein, mouseNeuropeptidesPeptidomimeticsReceptors, G-Protein-CoupledSmall Molecule LibrariesAgonistArginine mimeticMas-related gene (Mrg) receptorsPeptidomimetic

Identifiers

PMID25288495
PMCPMC4254045
OpenAlexW2061978929

What OpenQuestion holds

Textmetadata
LicenceTDM
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.