Endogenous BMP2/7 and BMP4/7 heterodimers form in vivo, and are the predominant functional ligand in many, if not all, tissues of developing mouse embryos.

A periosteal Bmp2 signaling center couples bone length to bone width during development and must be reactivated by clinical bone anabolic therapies to reduce fracture risk and accelerate fracture repair.

ChIP-seq analysis reveals BMP signaling targets in a cnidarian and identifies ZSWIM4-6 as a dampener of the pSMAD1/5 gradient and a potential conveyor of the BMP-mediated gene repression.

SMOC inhibits BMP signaling locally, but also expands the range of BMP signaling by competing for heparan sulfate binding sites.

Members of the BMP family of growth factors act as a reiterative code of distinct activities to direct the identities of different classes of sensory neurons in the spinal cord.

Optogenetic manipulation of BMP signaling indicates that diversity in BMP-dependent gene expression is not well explained by differential responses to BMP, and combinatorial signaling is a major driver of diversity.

Embryo-wide quantitative analysis of BMP signaling in zebrafish embryos, combined with a mathematical model-based computational screen, challenges the prevailing model of an antagonist counter-gradient shaping the gastrula BMP morphogen gradient and supports an antagonist sink with BMP diffusion mechanism.

BMP-dependent retinoic acid signaling is responsible for the separation of central from peripheral lineages during neural development.

A protein called Megf8 regulates the activity of key signaling molecules involved in the development of the peripheral nervous system.

Attaching a molecule of adenosine mono-phosphate (AMP) to the BiP protein at threonine 518 regulates its chaperone activity in the endoplasmic reticulum.