Evidence map›Paper›PMID 26441827›Full record

ReviewFrontiers in endocrinology2015

In a Class of Their Own - RXFP1 and RXFP2 are Unique Members of the LGR Family.

Emma J Petrie, Samantha Lagaida, Ashish Sethi, Ross A D Bathgate, Paul R Gooley

Abstract readReview
In one paragraph

Review in Frontiers in endocrinology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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.

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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The Role of LGR4 (GPR48) in Normal and Cancer Processes.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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

5 authors.

Emma J PetrieDepartment of Biochemistry and Molecular Biology, University of Melbourne , Parkville, VIC , Australia ; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne , Parkville, VIC , Australia.
Samantha LagaidaDepartment of Biochemistry and Molecular Biology, University of Melbourne , Parkville, VIC , Australia ; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne , Parkville, VIC , Australia.
Ashish SethiDepartment of Biochemistry and Molecular Biology, University of Melbourne , Parkville, VIC , Australia ; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne , Parkville, VIC , Australia.
Ross A D BathgateDepartment of Biochemistry and Molecular Biology, University of Melbourne , Parkville, VIC , Australia ; Florey Institute of Neuroscience and Mental Health, University of Melbourne , Parkville, VIC , Australia.
Paul R GooleyDepartment of Biochemistry and Molecular Biology, University of Melbourne , Parkville, VIC , Australia ; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne , Parkville, VIC , Australia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The leucine-rich repeat-containing G protein-coupled receptors (LGRs) family consists of three groups: types A, B, and C and all contain a large extracellular domain (ECD) made up of the structural motif - the leucine-rich repeat (LRR). In the LGRs, the ECD binds the hormone or ligand, usually through the LRRs, that ultimately results in activation and signaling. Structures are available for the ECD of type A and B LGRs, but not the type C LGRs. This review discusses the structural features of LRR proteins, and describes the known structures of the type A and B LGRs and predictions that can be made for the type C LGRs. The mechanism of activation of the LGRs is discussed with a focus on the role of the low-density lipoprotein class A (LDLa) module, a unique feature of the type C LGRs. While the LDLa module is essential for activation of the type C LGRs, the molecular mechanism for this process is unknown. Experimental data for the potential interactions of the type C LGR ligands with the LRR domain, the transmembrane domain, and the LDLa module are summarized.

Indexed as

GPCRleucine-rich repeat-containing G protein-coupled receptorsLGRRXFP1RXFP2

Identifiers

PMID26441827
PMCPMC4561518

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Registered trials

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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.