A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva

Muscle injury activates resident fibro/adipogenic progenitors that facilitate myogenesis

Joe, A. W. B., Yi, L., Natarajan, A., Le Grand, F., So, L., Wang, J., Rudnicki, M. A., & Rossi, F. M. V. (2010) · Nature Cell Biology · doi:10.1038/ncb2015 · Cited by 1,690

TGF-β and BMP signaling in osteoblast, skeletal development, and bone formation, homeostasis and disease

Wu, M., Chen, G., & Li, Y.-P. (2016) · Bone Research · doi:10.1038/boneres.2016.9 · Cited by 1,553

Skeletal remodeling in health and disease

Zaidi, M. (2007) · Nature Medicine · doi:10.1038/nm1593 · Cited by 1,069

TGF-β signaling in health and disease

Massagué, J., & Sheppard, D. (2023) · Cell · doi:10.1016/j.cell.2023.07.036 · Cited by 890

BMP signalling in skeletal development, disease and repair

Salazar, V. S., Gamer, L. W., & Rosen, V. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.12 · Cited by 822

Signaling Receptors for TGF-β Family Members

Heldin, C.-H., & Moustakas, A. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022053 · Cited by 711

Genetic Control of Bone Formation

Karsenty, G., Kronenberg, H. M., & Settembre, C. (2009) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113308 · Cited by 667

Osteoimmunology: The conceptual framework unifying the immune and skeletal systems

Okamoto, K., Nakashima, T., Shinohara, M., Negishi-Koga, T., Komatsu, N., Terashima, A., Sawa, S., Nitta, T., & Takayanagi, H. (2017) · Physiological Reviews · doi:10.1152/physrev.00036.2016 · Cited by 534

Recurrent somatic mutations in ACVR1 in pediatric midline high-grade astrocytoma

Fontebasso, A. M., Papillon-Cavanagh, S., Schwartzentruber, J., Nikbakht, H., Gerges, N., Fiset, P.-O., Bechet, D., Faury, D., De Jay, N., Ramkissoon, L. A., et al. (2014) · Nature Genetics · doi:10.1038/ng.2950 · Cited by 465

ACVR1 R206H receptor mutation causes fibrodysplasia ossificans progressiva by imparting responsiveness to activin A

Hatsell, S. J., Idone, V., Wolken, D. M. A., Huang, L., Kim, H. J., Wang, L., Wen, X., Nannuru, K. C., Jimenez, J., Xie, L., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aac4358 · Cited by 446

Kinase mutations in human disease: interpreting genotype–phenotype relationships

Lahiry, P., Torkamani, A., Schork, N. J., & Hegele, R. A. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2707 · Cited by 420

Clinical research for rare disease: Opportunities, challenges, and solutions

Griggs, R. C., Batshaw, M., Dunkle, M., Gopal-Srivastava, R., Kaye, E., Krischer, J., Nguyen, T., Paulus, K., & Merkel, P. A. (2009) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2008.10.003 · Cited by 401

Skeletal stem cells

Bianco, P., & Robey, P. G. (2015) · Development · doi:10.1242/dev.102210 · Cited by 402

Wnt inhibitors Dkk1 and Sost are downstream targets of BMP signaling through the type IA receptor (BMPRIA) in osteoblasts

Kamiya, N., Kobayashi, T., Mochida, Y., Yu, P. B., Yamauchi, M., Kronenberg, H. M., & Mishina, Y. (2010) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.090806 · Cited by 198

Smad9 is a new type of transcriptional regulator in bone morphogenetic protein signaling

Tsukamoto, S., Mizuta, T., Fujimoto, M., Ohte, S., Osawa, K., Miyamoto, A., Yoneyama, K., Murata, E., Machiya, A., Jimi, E., et al. (2014) · Scientific Reports · doi:10.1038/srep07596 · Cited by 122

Molecular Communication from Skeletal Muscle to Bone: A Review for Muscle-Derived Myokines Regulating Bone Metabolism

Guo, B., Zhang, Z.-K., Liang, C., Li, J., Liu, J., Lu, A., Zhang, B.-T., & Zhang, G. (2017) · Calcified Tissue International · doi:10.1007/s00223-016-0209-4 · Cited by 96

Transferrin receptor 2 controls bone mass and pathological bone formation via BMP and Wnt signalling

Rauner, M., Baschant, U., Roetto, A., Pellegrino, R. M., Rother, S., Salbach-Hirsch, J., Weidner, H., Hintze, V., Campbell, G., Petzold, A., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-018-0005-8 · Cited by 87

Defective pulmonary vascular remodeling in Smad8 mutant mice

Huang, Z., Wang, D., Ihida-Stansbury, K., Jones, P. L., & Martin, J. F. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp214 · Cited by 81

Monoallelic BMP2 Variants Predicted to Result in Haploinsufficiency Cause Craniofacial, Skeletal, and Cardiac Features Overlapping Those of 20p12 Deletions

Tan, T. Y., Gonzaga-Jauregui, C., Bhoj, E. J., Strauss, K. A., Brigatti, K., Puffenberger, E., Li, D., Xie, L., Das, N., Skubas, I., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.10.006 · Cited by 55

Aspects of parasomnias in childhood and adolescence

Stores, G. (2009) · Archives of Disease in Childhood · doi:10.1136/adc.2007.131631 · Cited by 46

A Rare Mutation in SMAD9 Associated With High Bone Mass Identifies the SMAD-Dependent BMP Signaling Pathway as a Potential Anabolic Target for Osteoporosis

Gregson, C. L., Bergen, D. J. M., Leo, P., Sessions, R. B., Wheeler, L., Hartley, A., Youlten, S., Croucher, P. I., McInerney-Leo, A. M., Fraser, W., et al. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3875 · Cited by 44

CryoEM structure of ALK2:BMP6 reveals distinct mechanism that allow ALK2 to interact with both BMP and activin ligands

Goebel, E. J., Aykul, S., Hom, W. W., Saotome, K., Economides, A. N., Franklin, M. C., & Idone, V. J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2502788122 · Cited by 2