Evidence map›Paper›PMID 33815292›Full record

ReviewFrontiers in endocrinology2021

New Human Follitropin Preparations: How Glycan Structural Differences May Affect Biochemical and Biological Function and Clinical Effect.

James A Dias, Alfredo Ulloa-Aguirre

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in endocrinology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 3 pooled it
5.0field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 3 syntheses or guidelines pooled it, 35 citations in OpenAlex.

  1. Pooled it
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  13. Frontiers in veterinary science · 2025
    Article
  14. Observational
  15. Current Insights in Prolactin Signaling and Ovulatory Function.International journal of molecular sciences · 2024
    Review
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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

2 authors at 2 institutions in 2 countries.

James A DiasDepartment of Biomedical Sciences, State University of New York at Albany, Albany, NY, United States.
Alfredo Ulloa-AguirreRed de Apoyo a la Investigación, National University of Mexico-Instituto Nacional de Ciencias Médicas y Nutrición SZ., Mexico City, Mexico.
Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán · MXUniversity at Albany, State University of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is well accepted that pituitary follitropin is secreted into the circulation as a mixture of variants, which differ not in primary structure but rather at the level of glycosylation. These glycosidic forms vary in the number of glycosylation sites filled, complexity of glycosidic chains, and sialylation and sulfation. It is generally agreed that high sialylation, 2,3 sialic acid capping of terminal N-acetyl galactosamine or galactose leads to longer circulating half-life, by blocking binding of asialoglycoprotein receptor (ASGPR) in the liver. In contrast, 2,6 sialic acid found in humans does not prevent recognition of galactose and N-acetyl galactosamine by ASGPR. Few studies on clinical outcomes comparing differences in sialylation of follitropin found in commercially available preparations are available. Thus, there is a clear need for a consortium of open data to address this unmet need. Recently, FSH glycosylation, primarily on the β-subunit, which varies as women age, has emerged as a key modifier of follitropin action, with profound biological effects

Indexed as

AcetylgalactosamineAnimalsAsialoglycoprotein ReceptorCHO CellsCricetulusFemaleFollicle Stimulating HormoneFollicle Stimulating Hormone, HumanGlycoproteinsGlycosylationHumansLiverMaleMiceN-Acetylneuraminic AcidPolysaccharidesAcetylgalactosamineAsialoglycoprotein ReceptorFollicle Stimulating HormoneFollicle Stimulating Hormone, HumanGlycoproteinsN-Acetylneuraminic AcidPolysaccharidesProtein IsoformsRecombinant Proteinsfollitropinglycoproteinglycosylationpharmacokineticspharmocodynamicstherapeutics

Identifiers

PMID33815292
PMCPMC8018285
OpenAlexW3138983025

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.