Evidence map›Paper›PMID 10786817›Full record

ReviewEndocrine1999

Role of glycosylation in function of follicle-stimulating hormone.

A Ulloa-Aguirre, C Timossi, P Damián-Matsumura, J A Dias

Abstract readReview
PubMed Publisher
In one paragraph

Review in Endocrine, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

40 citing papers in PubMed, 156 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Review
  6. Crystal structure of LGR ligand α2/β5 fromProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. FSH for the Treatment of Male Infertility.International journal of molecular sciences · 2020
    Review
  15. Review
  16. Review
  17. Glycosylation Pattern andFrontiers in endocrinology · 2019
    Article
  18. Mouse models for the analysis of gonadotropin secretion and action.Best practice & research. Clinical endocrinology & metabolism · 2018
    Review
  19. Review
  20. Frontiers in endocrinology · 2018
    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

4 authors at 2 institutions in 2 countries.

A Ulloa-AguirreResearch Unit in Reproductive Medicine, Hospital de Gineco Obstetricia Luis Castelazo Ayala, Instituto Mexicano del Seguro Social, México DF. aulloaa@buzon.main.conacyt.mx
C Timossi
P Damián-Matsumura
J A Dias
Mexican Social Security Institute · MXWadsworth Center · US

Funding

STRUCTURE AND CELLULAR BIOLOGY OF GPH RECEPTORSR01HD018407 · NICHD · WADSWORTH CENTER · PI A, DIAS JAMES · 1985 to 2010
$2.4M
NICHD NIH HHS HD18407
6 · The paper itself

Abstract

The oligosaccharide structures of heterodimeric glycoprotein hormones, such as follicle-stimulating hormone (FSH), have been shown to play an important role in the biosynthesis, secretion, metabolic fate, and regulation of potency of the hormone. The oligosaccharide structures attached to each subunit of the protein seem to exhibit distinct roles in some of these functions. Glycans attached to the alpha-subunit are critical for dimer assembly, integrity, and secretion, as well as for signal transduction; although beta-subunit glycans are also important for dimer assembly and secretion, they play a crucial role in clearance of the dimer from the circulation. Alternative glycosylation on FSH and other glycoprotein hormones not only may affect the metabolic clearance and net in vivo biopotency of the hormone, but also offers the interesting possibility that some glycosylation variants of the hormone may provoke differential or even unique effects at the target cell level. Glycosylation of FSH is regulated by hypothalamic and/or end products from the glands under the control of this hormone. In particular, estrogens regulate terminal sialylation and thus some functional properties of the gonadotropin influenced by sialic acid. Through these extrapituitary inputs, the gonadotroph may regulate not only the amount but also the intensity of the gonadotropin signal to be secreted by the pituitary in a given physiological condition.

Indexed as

AnimalsDimerizationFemaleFollicle Stimulating HormoneGlycosylationHumansModels, MolecularOligosaccharidesReceptors, FSHSignal TransductionStructure-Activity RelationshipFollicle Stimulating HormoneOligosaccharidesReceptors, FSH

Identifiers

PMID10786817
OpenAlexW1988660122

What OpenQuestion holds

Textmetadata
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.