A divergent two-domain structure of the anti-Müllerian hormone prodomain.

TGFβ family ligands are synthesized as precursors consisting of an N-terminal prodomain and C-terminal growth factor (GF) signaling domain. After proteolytic processing, the prodomain typically remains noncovalently associated with the GF, sometimes forming a high-affinity latent procomplex that requires activation. For the TGFβ family ligand anti-Müllerian hormone (AMH), the prodomain maintains a high-affinity interaction with its GF that does not render it latent.

The experiences of podiatrists prescribing custom foot orthoses and patients using custom foot orthoses for foot pain management in the United Kingdom: A focus group study.

Introduction: Foot pain can be a significant burden for patients. Custom foot orthoses (CFOs) have been a mainstay in podiatry treatment for foot pain management and improving foot function. However, little is known about podiatrists' experience of prescribing CFOs or patient experience of using foot orthoses (FOs), including CFOs, for foot pain.

Structural Basis of Non-Latent Signaling by the Anti-Müllerian Hormone Procomplex.

Most TGFβ family ligands exist as procomplexes consisting of a prodomain noncovalently bound to a growth factor (GF); Whereas some prodomains confer latency, the Anti-Müllerian Hormone (AMH) prodomain maintains a remarkably high affinity for the GF yet remains active. Using single particle EM methods, we show the AMH prodomain consists of two subdomains: a vestigial TGFβ prodomain-like fold and a novel, helical bundle GF-binding domain, the result of an exon insertion 450 million years ago, that engages both receptor epitopes. When associated with the prodomain, the AMH GF is distorted into a strained, open conformation whose closure upon bivalent binding of AMHR2 displaces the prodomain through a conformational shift mechanism to allow for signaling.

Three derivatives of phenacyldiphenylphosphine oxide: influence of aromatic and alkyl substituents on the luminescence sensitization of four Ln(NO) salts.

A series of four β-carbonylphosphine oxide compounds have been synthesized, and their complexes with the nitrate salts of Sm, Eu, Tb and Dy have been characterized in solution and in the solid state. Analysis of the complexes using IR and NMR suggests that metal-ligand binding occurs mainly through the phosphine oxide group of the ligand, with some involvement of the carbonyl group. All 16 complexes luminesce in solutions of acetonitrile, albeit with varying degrees of intensity.

Characterization of erythroferrone oligomerization and its impact on BMP antagonism.

Hepcidin, a peptide hormone that negatively regulates iron metabolism, is expressed by bone morphogenetic protein (BMP) signaling. Erythroferrone (ERFE) is an extracellular protein that binds and inhibits BMP ligands, thus positively regulating iron import by indirectly suppressing hepcidin. This allows for rapid erythrocyte regeneration after blood loss.