Identification of a bone morphogenetic protein type 2 receptor neutralizing antibody

Newby, Jordan B.; Hum, Julia M.; Gorrell, Ruthann; Schoerning, Laura; Lowery, Jonathan W.; Lawless, Warren; Totten, Madeline; Geyman, Logan J.

doi:10.1186/s13104-019-4367-0

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Identification of a bone morphogenetic protein type 2 receptor neutralizing antibody

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MLA citation style (9th ed.)

Newby, Jordan B, et al. Identification of a Bone Morphogenetic Protein Type 2 Receptor Neutralizing Antibody. . 6112. mushare.marian.edu/concern/generic_works/7b5ff80f-0f93-4d10-b331-054d2bb09235?locale=es.

APA citation style (7th ed.)

N. J. B, H. J. M, G. Ruthann, S. Laura, L. J. W, L. Warren, T. Madeline, & G. L. J. (6112). Identification of a bone morphogenetic protein type 2 receptor neutralizing antibody. https://mushare.marian.edu/concern/generic_works/7b5ff80f-0f93-4d10-b331-054d2bb09235?locale=es

Chicago citation style (CMOS 17, author-date)

Newby, Jordan B., Hum, Julia M., Gorrell, Ruthann, Schoerning, Laura, Lowery, Jonathan W., Lawless, Warren, Totten, Madeline et al. Identification of a Bone Morphogenetic Protein Type 2 Receptor Neutralizing Antibody. 6112. https://mushare.marian.edu/concern/generic_works/7b5ff80f-0f93-4d10-b331-054d2bb09235?locale=es.

Note: These citations are programmatically generated and may be incomplete.

The bone morphogenetic protein (BMP) signaling pathway comprises the largest subdivision of the transforming growth factor (TGF?) superfamily. BMP signaling plays essential roles in both embryonic development and postnatal tissue homeostasis. Dysregulated BMP signaling underlies human pathologies ranging from pulmonary arterial hypertension to heterotopic ossification. Thus, understanding the basic mechanisms and regulation of BMP signaling may yield translational opportunities. Unfortunately, limited tools are available to evaluate this pathway, and genetic approaches are frequently confounded by developmental requirements or ability of pathway components to compensate for one another. Specific inhibitors for type 2 receptors are poorly represented. Thus, we sought to identify and validate an antibody that neutralizes the ligand-binding function of BMP receptor type 2 (BMPR2) extracellular domain (ECD).

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