Evidence map›Paper›PMID 35813657›Full record

ReviewFrontiers in endocrinology2022

Molecular Mechanisms of AMH Signaling.

James A Howard, Kaitlin N Hart, Thomas B Thompson

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in endocrinology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
8.4field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Molecular Characterization and Functional Analysis ofInternational journal of molecular sciences · 2026
    Article
  4. Review
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  19. Yet another twist to the regulation of the TGF-β family ligands.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Role of epigenetic regulation in diminished ovarian reserve.Journal of assisted reproduction and genetics · 2025
    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

3 authors at 1 institution in 1 country.

James A HowardDepartment of Pharmacology & Systems Physiology, University of Cincinnati, Cincinnati, OH, United States.
Kaitlin N HartDepartment of Pharmacology & Systems Physiology, University of Cincinnati, Cincinnati, OH, United States.
Thomas B ThompsonDepartment of Molecular Genetics, Biochemistry, & Microbiology, University of Cincinnati, Cincinnati, OH, United States.
University of Cincinnati · US

Funding

ENVIRONMETAL CARCINOGENESIS AND MUTAGENESIST32ES007250 · NIEHS · UNIVERSITY OF CINCINNATI · PI MILLER, WILLIAM E · 1988 to 2024
$11.9M
Structure-function analysis of Mullerian Inhibiting Substance (MIS)R01HD105818 · NICHD · UNIVERSITY OF CINCINNATI · PI THOMAS B THOMPSON · 2021 to 2026
$2.6M
NICHD NIH HHS R01 HD105818NIEHS NIH HHS T32 ES007250
6 · The paper itself

Abstract

Anti-Müllerian Hormone (AMH) is a secreted glycoprotein hormone with critical roles in reproductive development and regulation. Its chemical and mechanistic similarities to members of the Transforming Growth Factor β (TGF-β) family have led to its placement within this signaling family. As a member of the TGF-β family, AMH exists as a noncovalent complex of a large N-terminal prodomain and smaller C-terminal mature signaling domain. To produce a signal, the mature domain will bind to the extracellular domains of two type I and two type II receptors which results in an intracellular SMAD signal. Interestingly, as will be discussed in this review, AMH possesses several unique characteristics which set it apart from other ligands within the TGF-β family. In particular, AMH has a dedicated type II receptor, Anti-Müllerian Hormone Receptor Type II (AMHR2), making this interaction intriguing mechanistically as well as therapeutically. Further, the prodomain of AMH has remained largely uncharacterized, despite being the largest prodomain within the family. Recent advancements in the field have provided valuable insight into the molecular mechanisms of AMH signaling, however there are still many areas of AMH signaling not understood. Herein, we will discuss what is known about the biochemistry of AMH and AMHR2, focusing on recent advances in understanding the unique characteristics of AMH signaling and the molecular mechanisms of receptor engagement.

Indexed as

Anti-Mullerian HormonePeptide HormonesProtein Serine-Threonine KinasesSignal TransductionTransforming Growth Factor betaAnti-Mullerian HormonePeptide HormonesProtein Serine-Threonine KinasesTransforming Growth Factor betaactivinanti-müllerian hormone (AMH)anti-müllerian hormone receptor type II (AMHR2)bone morphogenetic protein (BMP)cell signalingpersistent müllerian duct syndrome (PMDS)prodomaintransforming growth factor-β (TGF-β)

Identifiers

PMID35813657
PMCPMC9256959
OpenAlexW4283266826

What OpenQuestion holds

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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.