Evidence map›Paper›PMID 24692546›Full record

ArticleThe Journal of biological chemistry2014

Evidence for Follicle-stimulating Hormone Receptor as a Functional Trimer.

Xuliang Jiang, David Fischer, Xiaoyan Chen, Sean D McKenna, Heli Liu, Venkataraman Sriraman, Henry N Yu, Andreas Goutopoulos, Steve Arkinstall, Xiaolin He

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 5% 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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 104 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Allosteric modulation of gonadotropin receptors.Frontiers in endocrinology · 2023
    Review
  14. Article
  15. Review
  16. Human FSH Glycoform α-Subunit AsparagineFrontiers in endocrinology · 2022
    Article
  17. Article
  18. ERβ Regulation of Gonadotropin Responses during Folliculogenesis.International journal of molecular sciences · 2021
    Review
  19. Article
  20. 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

10 authors at 2 institutions in 2 countries.

Xuliang JiangFrom the EMD Serono Research and Development Institute, Billerica, Massachusetts 01821 and xuliang.jiang@emdserono.com.
David FischerFrom the EMD Serono Research and Development Institute, Billerica, Massachusetts 01821 and.
Xiaoyan Chenthe Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611.
Sean D McKennaFrom the EMD Serono Research and Development Institute, Billerica, Massachusetts 01821 and.
Heli Liuthe Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611.
Venkataraman SriramanFrom the EMD Serono Research and Development Institute, Billerica, Massachusetts 01821 and.
Henry N YuFrom the EMD Serono Research and Development Institute, Billerica, Massachusetts 01821 and.
Andreas GoutopoulosFrom the EMD Serono Research and Development Institute, Billerica, Massachusetts 01821 and.
Steve ArkinstallFrom the EMD Serono Research and Development Institute, Billerica, Massachusetts 01821 and.
Xiaolin Hethe Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611.
Merck Serono (Italy) · ITNorthwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
NCI NIH HHS P30 CA060553
6 · The paper itself

Abstract

Follicle-stimulating hormone receptor (FSHR), a G-protein coupled receptor, is an important drug target in the development of novel therapeutics for reproductive indications. The FSHR extracellular domains were observed in the crystal structure as a trimer, which enabled us to propose a novel model for the receptor activation mechanism. The model predicts that FSHR binds Asnα(52)-deglycosylated FSH at a 3-fold higher capacity than fully glycosylated FSH. It also predicts that, upon dissociation of the FSHR trimer into monomers, the binding of glycosylated FSH, but not deglycosylated FSH, would increase 3-fold, and that the dissociated monomers would in turn enhance FSHR binding and signaling activities by 3-fold. This study presents evidence confirming these predictions and provides crystallographic and mutagenesis data supporting the proposed model. The model also provides a mechanistic explanation to the agonist and antagonist activities of thyroid-stimulating hormone receptor autoantibodies. We conclude that FSHR exists as a functional trimer.

Indexed as

Protein MultimerizationAllosteric RegulationAnimalsCHO CellsCricetinaeCricetulusFollicle Stimulating HormoneHumansIntracellular SpaceModels, MolecularMutagenesisMutationProtein Structure, QuaternaryReceptors, FSHSignal TransductionFollicle Stimulating HormoneReceptors, FSHAllosteric RegulationArrestinCysteine-knot Growth FactorGlycoprotein HormonesG Protein-coupled Receptors (GPCR)Receptor Structure-functionReproduction

Identifiers

PMID24692546
PMCPMC4022893
OpenAlexW2055591390

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.