Evidence map›Paper›PMID 27922185›Full record

ReviewBritish journal of pharmacology2017

Relaxin family peptides: structure-activity relationship studies.

Nitin A Patil, K Johan Rosengren, Frances Separovic, John D Wade, Ross A D Bathgate, Mohammed Akhter Hossain

Erratum issued Registry-linked trialAbstract readReview
In one paragraph

Review in British journal of pharmacology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. It is linked to trial NCT06808165 (Evaluation of Relaxin and Placental Volume in Placenta Accreta Spectrum Disorders), which is not on this map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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.

NCT06808165 completednot on this mapstarted 2022, after this paper: background citation

Evaluation of Relaxin and Placental Volume in Placenta Accreta Spectrum Disorders: A Case-Control Study

TypeobservationalSponsorBaşakşehir Çam & Sakura City HospitalRan2022 to 2023Enrolled40ConditionsPlacenta Accreta Spectrum, Placenta Accreta / PercretaArmsrelaxin
3 · Its place in the literature

Who cites it

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Relaxin-2 drives regenerative healing and suppresses scar formation.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Characterization of chickenAnimal biotechnology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Further Developments towards a Minimal Potent Derivative of Human Relaxin-2.International journal of molecular sciences · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Nitin A PatilThe Florey Institute of Neuroscience and Mental Health, University of Melbourne, Parkville, VIC, Australia.
K Johan RosengrenDepartment of Biochemistry and Molecular Biology, University of Melbourne, Parkville, VIC, Australia.
Frances SeparovicSchool of Chemistry, University of Melbourne, Parkville, VIC, Australia.ORCID 0000-0002-6484-2763
John D WadeThe Florey Institute of Neuroscience and Mental Health, University of Melbourne, Parkville, VIC, Australia.
Ross A D BathgateThe Florey Institute of Neuroscience and Mental Health, University of Melbourne, Parkville, VIC, Australia.
Mohammed Akhter HossainThe Florey Institute of Neuroscience and Mental Health, University of Melbourne, Parkville, VIC, Australia.ORCID 0000-0002-9961-0006

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human relaxin peptide family consists of seven cystine-rich peptides, four of which are known to signal through relaxin family peptide receptors, RXFP1-4. As these peptides play a vital role physiologically and in various diseases, they are of considerable importance for drug discovery and development. Detailed structure-activity relationship (SAR) studies towards understanding the role of important residues in each of these peptides have been reported over the years and utilized for the design of antagonists and minimized agonist variants. This review summarizes the current knowledge of the SAR of human relaxin 2 (H2 relaxin), human relaxin 3 (H3 relaxin), human insulin-like peptide 3 (INSL3) and human insulin-like peptide 5 (INSL5). LINKED ARTICLES: This article is part of a themed section on Recent Progress in the Understanding of Relaxin Family Peptides and their Receptors. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v174.10/issuetoc.

Indexed as

HumansInsulinModels, MolecularProteinsRelaxinStructure-Activity RelationshipInsulinLeydig insulin-like proteinProteinsRelaxinRLN2 protein, humanRLN3 protein, human

Identifiers

PMID27922185
PMCPMC5406294

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.