Eileen M. Shore

TL;DR: Protein modeling predicts destabilization of the GS domain, consistent with constitutive activation of ACVR1 as the underlying cause of the ectopic chondrogenesis, osteogenesis and joint fusions seen in FOP.

TL;DR: Genotype‐phenotype correlation between some ACVR1 mutations and the age of onset of heterotopic ossification or on embryonic skeletal development is observed and protein structure homology modeling predicts that each of the amino acid substitutions activates the ACVR 1 protein to enhance receptor signaling.

TL;DR: Overexpression of a potent bone-inducing morphogen (bone morphogenetic protein 4) in lymphocytes is associated with the disabling ectopic osteogenesis of fibrodysplasia ossificans progressiva.

TL;DR: The recent discovery of overproduction of bone morphogenetic protein-4 in lesional cells and lymphocytic cells of affected patients provides a clue to both the underlying pathophysiology and potential therapy.

TL;DR: Examination of cell extracts for protein complexes containing the cell adhesion molecule uvomorulin indicates that separate complexes exist containing ankyrin and fodrin with either uvmorulin or Na+,K+-ATPase, and the presence of these proteins reflects direct molecular interactions which play roles in coordinating cell-cell contact and the assembly of the basal-lateral domain of the plasma membrane.