ArticleThe Journal of biological chemistry2022
The anti-Müllerian hormone prodomain is displaced from the hormone/prodomain complex upon bivalent binding to the hormone receptor.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Molecular mechanisms and multi-organ regulatory roles of anti-Müllerian hormone in female reproduction.Communications biology · 2026Review
- Anti-Müllerian hormone in PCOS: Molecular regulation and emerging therapeutic strategies.Biomolecules & biomedicine · 2025Review
- Gene therapy with feline anti-Müllerian hormone analogs disrupts folliculogenesis and induces pregnancy loss in female domestic cats.Nature communications · 2025Article
- A divergent two-domain structure of the anti-Müllerian hormone prodomain.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural Basis of Non-Latent Signaling by the Anti-Müllerian Hormone Procomplex.bioRxiv : the preprint server for biology · 2024Article
- Characterization of the molecular mechanisms that govern anti-Müllerian hormone synthesis and activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- Anti-Müllerian hormone, testicular descent and cryptorchidism.Frontiers in endocrinology · 2024Review
- AMH Regulation by Steroids in the Mammalian Testis: Underlying Mechanisms and Clinical Implications.Frontiers in endocrinology · 2022Review
- Molecular Mechanisms of AMH Signaling.Frontiers in endocrinology · 2022Review
- Anti-Müllerian Hormone Signal Transduction involved in Müllerian Duct Regression.Frontiers in endocrinology · 2022Review
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Noncovalent complexes of transforming growth factor-β family growth/differentiation factors with their prodomains are classified as latent or active, depending on whether the complexes can bind their respective receptors. For the anti-Müllerian hormone (AMH), the hormone-prodomain complex is active, and the prodomain is displaced upon binding to its type II receptor, AMH receptor type-2 (AMHR2), on the cell surface. However, the mechanism by which this displacement occurs is unclear. Here, we used ELISA assays to measure the dependence of prodomain displacement on AMH concentration and analyzed results with respect to the behavior expected for reversible binding in combination with ligand-induced receptor dimerization. We found that, in solution, the prodomain has a high affinity for the growth factor (GF) (K
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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.