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

A new logic for DNA engineering using recombination in Escherichia coli

Zhang, Y., Buchholz, F., Muyrers, J. P. P., & Stewart, A. F. (1998) · Nature Genetics · doi:10.1038/2417 · Cited by 1,228

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

Shore, E. M., Xu, M., Feldman, G. J., Fenstermacher, D., Cho, T., Choi, I. H., Connor, J. M., Delai, P. L. R., Glaser, D. L., Merrer, M. F. L., et al. (2006) · Nature Genetics · doi:10.1038/ng1783 · Cited by 1,215

GS domain mutations that constitutively activate T beta R‐I, the downstream signaling component in the TGF‐beta receptor complex.

Wieser, R., Wrana, J. L., & Massagué, J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07214.x · Cited by 689

BMP type I receptor inhibition reduces heterotopic ossification

Yu, P. B., Deng, D. Y., Lai, C. S. C., Hong, C. C., Cuny, G. D., Bouxsein, M., Hong, D. W., McManus, P. M., Katagiri, T., Sachidanandan, C., et al. (2008) · Nature Medicine · doi:10.1038/nm.1888 · Cited by 641

Identification of human activin and TGFβ type I receptors that form heteromeric kinase complexes with type II receptors

Attisano, L. (1993) · Cell · doi:10.1016/0092-8674(93)90488-c · Cited by 639

High-throughput engineering of the mouse genome coupled with high-resolution expression analysis

Valenzuela, D. M., Murphy, A. J., Frendewey, D. A., Gale, N. W., Economides, A. N., Auerbach, W., Poueymirou, W. T., Adams, N. C., Rojas, J., Yasenchak, J., et al. (2003) · Nature Biotechnology · doi:10.1038/nbt822 · Cited by 583

Specific Activation of Smad1 Signaling Pathways by the BMP7 Type I Receptor, ALK2

Macías‐Silva, M., Hoodless, P. A., Tang, S. J., Buchwald, M., & Wrana, J. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25628 · Cited by 476

Mice with megabase humanization of their immunoglobulin genes generate antibodies as efficiently as normal mice

Murphy, A. J., Macdonald, L. E., Stevens, S. G., Karow, M. L., Dore, A. T., Pobursky, K. J., Huang, T. T., Poueymirou, W. T., Esau, L., Meola, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324022111 · Cited by 469

A directional strategy for monitoring Cre-mediated recombination at the cellular level in the mouse

Schnütgen, F., Doerflinger, N., Calleja, C., Wendling, O., Chambon, P., & Ghyselinck, N. B. (2003) · Nature Biotechnology · doi:10.1038/nbt811 · Cited by 401

Precise and in situ genetic humanization of 6 Mb of mouse immunoglobulin genes

Macdonald, L. E., Karow, M. L., Stevens, S. G., Auerbach, W., Poueymirou, W. T., Yasenchak, J., Frendewey, D. A., Valenzuela, D. M., Giallourakis, C. C., Alt, F. W., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1323896111 · Cited by 396

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

Heterotopic Ossification: A Comprehensive Review

Meyers, C. A., Lisiecki, J. L., Miller, S., Levin, A. S., Fayad, L. M., Ding, C., Sono, T., McCarthy, E. F., Lévi, B., & James, A. W. (2019) · JBMR Plus · doi:10.1002/jbm4.10172 · Cited by 536

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

Bone Morphogenetic ProteinsPreprint

Katagiri, T., & Watabe, T. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021899 · Cited by 561

The roles and regulatory mechanisms of TGF-β and BMP signaling in bone and cartilage development, homeostasis and disease

Wu, M., Wu, S., Chen, W., & Li, Y.-P. (2024) · Cell Research · doi:10.1038/s41422-023-00918-9 · Cited by 445

Immunoregulation by members of the TGFβ superfamily

Chen, W., & ten Dijke, P. (2016) · Nature reviews. Immunology · doi:10.1038/nri.2016.112 · Cited by 360

Neofunction of ACVR1 in fibrodysplasia ossificans progressiva

Hino, K., Ikeya, M., Horigome, K., Matsumoto, Y., Ebise, H., Nishio, M., Sekiguchi, K., Shibata, M., Nagata, S., Matsuda, S., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510540112 · Cited by 319

TGF-β Family Signaling in Mesenchymal DifferentiationPreprint

Grafe, I., Alexander, S., Peterson, J. R., Snider, T. N., Lévi, B., Lee, B., & Mishina, Y. M. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022202 · Cited by 278

Combinatorial Signal Perception in the BMP Pathway

Antebi, Y. E., Linton, J. M., Klumpe, H. E., Bintu, B., Gong, M., Su, C. J., McCardell, R. D., & Elowitz, M. B. (2017) · Cell · doi:10.1016/j.cell.2017.08.015 · Cited by 272

The BMP Pathway and Its Inhibitors in the Skeleton

Lowery, J. W., & Rosen, V. (2018) · Physiological Reviews · doi:10.1152/physrev.00028.2017 · Cited by 263

Targeting TGF-β Signaling for Therapeutic GainPreprint

Akhurst, R. J. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022301 · Cited by 255

Bone morphogenetic protein receptor signal transduction in human disease

Gomez‐Puerto, M. C., Iyengar, P. V., de Vinuesa, A. G., ten Dijke, P., & Sánchez‐Duffhues, G. (2018) · The Journal of Pathology · doi:10.1002/path.5170 · Cited by 239

Activin-dependent signaling in fibro/adipogenic progenitors causes fibrodysplasia ossificans progressiva

Lees‐Shepard, J. B., Yamamoto, M., Biswas, A. A., Stoessel, S. J., Nicholas, S.-A. E., Cogswell, C. A., Devarakonda, P. M., Schneider, M. J., Cummins, S. M., Legendre, N. P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-02872-2 · Cited by 228

TGF-β uses a novel mode of receptor activation to phosphorylate SMAD1/5 and induce epithelial-to-mesenchymal transition

Ramachandran, A., Vizán, P., Das, D., Chakravarty, P., Vogt, J., Rogers, K. W., Müller, P., Hinck, A. P., Sapkota, G. P., & Hill, C. S. (2018) · eLife · doi:10.7554/elife.31756 · Cited by 204

Two tissue-resident progenitor lineages drive distinct phenotypes of heterotopic ossification

Dey, D., Bagarova, J., Hatsell, S. J., Armstrong, K. A., Huang, L., Ermann, J., Vonner, A. J., Shen, Y., Mohedas, A. H., Lee, A. M., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf1090 · Cited by 195

Osteoimmunology: A Current Update of the Interplay Between Bone and the Immune System

Guder, C., Gravius, S., Burger, C., Wirtz, D. C., & Schildberg, F. A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00058 · Cited by 199

Palovarotene Inhibits Heterotopic Ossification and Maintains Limb Mobility and Growth in Mice With the Human ACVR1R206H Fibrodysplasia Ossificans Progressiva (FOP) Mutation

Chakkalakal, S. A., Uchibe, K., Convente, M. R., Zhang, D., Economides, A. N., Kaplan, F. S., Pacifici, M., Iwamoto, M., & Shore, E. M. (2016) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2820 · Cited by 174

Depletion of Mast Cells and Macrophages Impairs Heterotopic Ossification in an Acvr1R206H Mouse Model of Fibrodysplasia Ossificans Progressiva

Convente, M. R., Chakkalakal, S. A., Yang, E.-J., Caron, R., Zhang, D., Kambayashi, T., Kaplan, F., & Shore, E. (2018) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3304 · Cited by 144

Activin-A enhances mTOR signaling to promote aberrant chondrogenesis in fibrodysplasia ossificans progressiva

Hino, K., Horigome, K., Nishio, M., Komura, S., Nagata, S., Zhao, C., Jin, Y., Kawakami, K., Yamada, Y., Ohta, A., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci93521 · Cited by 168

Bone Morphogenetic Proteins in Vascular Homeostasis and DiseasePreprint

Goumans, M., Zwijsen, A., ten Dijke, P., & Bailly, S. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a031989 · Cited by 173

Transforming Growth Factor-β Family Ligands Can Function as Antagonists by Competing for Type II Receptor Binding

Aykul, S., & Martinez-Hackert, E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.713487 · Cited by 143

Endothelial‐to‐mesenchymal transition in cardiovascular diseases: Developmental signaling pathways gone awry

Sánchez‐Duffhues, G., de Vinuesa, A. G., & ten Dijke, P. (2017) · Developmental Dynamics · doi:10.1002/dvdy.24589 · Cited by 145

BMPR2 acts as a gatekeeper to protect endothelial cells from increased TGFβ responses and altered cell mechanics

Hiepen, C., Jatzlau, J., Hildebrandt, S., Kampfrath, B., Goktas, M., Murgai, A., Cuellar‐Camacho, J. L., Haag, R., Ruppert, C., Sengle, G., et al. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000557 · Cited by 148

Influence of the TGF-β Superfamily on Osteoclasts/Osteoblasts Balance in Physiological and Pathological Bone Conditions

Jann, J., Gascon, S., Roux, S., & Faucheux, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207597 · Cited by 133

ACVR1 R206H cooperates with H3.1K27M in promoting diffuse intrinsic pontine glioma pathogenesis

Hoeman, C. M., Cordero, F. J., Hu, G., Misuraca, K., Romero, M. M., Cardona, H. J., Nazarian, J., Hashizume, R., McLendon, R. E., Yu, P. B., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08823-9 · Cited by 133

Cellular Hypoxia Promotes Heterotopic Ossification by Amplifying BMP Signaling

Wang, H., Lindborg, C. M., Lounev, V. Y., Kim, J., McCarrick-Walmsley, R., Xu, M., Mangiavini, L., Groppe, J. C., Shore, E. M., Schipani, E., et al. (2016) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2848 · Cited by 128

The role of bone morphogenetic protein signaling in vascular calcification

Yang, P. B., Troncone, L., Augur, Z. M., Kim, S. S., McNeil, M. E., & Yu, P. B. (2020) · Bone · doi:10.1016/j.bone.2020.115542 · Cited by 127

ALK2 inhibitors display beneficial effects in preclinical models of ACVR1 mutant diffuse intrinsic pontine glioma

Carvalho, D. M., Taylor, K. R., Olaciregui, N. G., Molinari, V., Clarke, M., Mackay, A. G., Ruddle, R. R., Henley, A. T., Valenti, M. R., Hayes, A., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0420-8 · Cited by 127

TGF-β Family Signaling in Connective Tissue and Skeletal DiseasesPreprint

MacFarlane, E. G., Haupt, J., Dietz, H. C., & Shore, E. M. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022269 · Cited by 125

Contemporary perspectives on heterotopic ossification

Hwang, C. D., Pagani, C. A., Nunez, J. H., Cherief, M., Qin, Q., Gomez-Salazar, M. A., Kadaikal, B., Kang, H., Chowdary, A. R., Patel, N., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.158996 · Cited by 110

NF-κB/MAPK activation underlies ACVR1-mediated inflammation in human heterotopic ossification

Barruet, E., Morales, B. M., Cain, C. J., Ton, A. N., Wentworth, K. L., Chan, T. V., Moody, T. A., Haks, M. C., Ottenhoff, T. H. M., Hellman, J., et al. (2018) · JCI Insight · doi:10.1172/jci.insight.122958 · Cited by 107

Principles of Genetic Engineering

Lanigan, T. M., Kopera, H. C., & Saunders, T. L. (2020) · Genes · doi:10.3390/genes11030291 · Cited by 114

BMP-SMAD-ID promotes reprogramming to pluripotency by inhibiting p16/INK4A-dependent senescence

Hayashi, Y., Hsiao, E. C., Sami, S., Lancero, M., Schlieve, C. R., Nguyen, T., Yano, K., Nagahashi, A., Ikeya, M., Matsumoto, Y., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603668113 · Cited by 105

Mutant ACVR1 Arrests Glial Cell Differentiation to Drive Tumorigenesis in Pediatric Gliomas

Fortin, J., Tian, R., Zarrabi, I., Hill, G., Williams, E., Sánchez‐Duffhues, G., Thorikay, M., Ramachandran, P., Siddaway, R., Wong, J. F., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.02.002 · Cited by 103

Heterotopic ossification of tendon and ligament

Zhang, Q., Zhou, D., Wang, H., & Tan, J. H. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15240 · Cited by 97

Endometrial receptivity and implantation require uterine BMP signaling through an ACVR2A-SMAD1/SMAD5 axis

Monsivais, D., Nagashima, T., Prunskaite‐Hyyryläinen, R., Nozawa, K., Shimada, K., Tang, S., Hamor, C., Agno, J. E., Chen, F., Masand, R. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23571-5 · Cited by 95

Structural Basis of Intracellular TGF-β Signaling: Receptors and SmadsPreprint

Chaikuad, A., & Bullock, A. N. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022111 · Cited by 95

Macrophages in heterotopic ossification: from mechanisms to therapy

Huang, Y., Wang, X., Zhou, D., Zhou, W., Dai, F., & Lin, H. (2021) · npj Regenerative Medicine · doi:10.1038/s41536-021-00178-4 · Cited by 94

ACVR1 Function in Health and Disease

Valer, J. A., Sánchez‐de‐Diego, C., Pimenta-Lopes, C., Rosa, J. L., & Ventura, F. (2019) · Cells · doi:10.3390/cells8111366 · Cited by 96

Receptor binding competition: A paradigm for regulating TGF-β family action

Martı́nez-Hackert, E., Sundan, A., & Holien, T. (2020) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2020.09.003 · Cited by 93

Ligand-receptor promiscuity enables cellular addressing

Su, C. J., Murugan, A., Linton, J. M., Yeluri, A., Bois, J. S., Klumpe, H. E., Langley, M. A., Antebi, Y. E., & Elowitz, M. B. (2022) · Cell Systems · doi:10.1016/j.cels.2022.03.001 · Cited by 92

Tumor-Suppressor Inactivation of GDF11 Occurs by Precursor Sequestration in Triple-Negative Breast Cancer

Bajikar, S. S., Wang, C., Borten, M. A., Pereira, E. J., Atkins, K. A., & Janes, K. A. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.10.027 · Cited by 87

Signaling pathways regulating cartilage growth plate formation and activity

Samsa, W. E., Zhou, X., & Zhou, G. D. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.07.008 · Cited by 91

Bone Morphogenetic Protein–Based Therapeutic ApproachesPreprint

Lowery, J. W., & Rosen, V. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022327 · Cited by 85

Heterotopic ossification and the elucidation of pathologic differentiation

Cholok, D. J., Chung, M. T., Ranganathan, K., Ucer, S., Day, D., Davis, T. A., Mishina, Y. M., & Lévi, B. (2017) · Bone · doi:10.1016/j.bone.2017.09.019 · Cited by 82

Bone morphogenetic proteins in inflammation, glucose homeostasis and adipose tissue energy metabolism

Grgurević, L., Christensen, G. L., Schulz, T. J., & Vukičević, S. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.12.009 · Cited by 84

The obligatory role of Activin A in the formation of heterotopic bone in Fibrodysplasia Ossificans Progressiva

Wolken, D. M. A., Idone, V. J., Hatsell, S. J., Yu, P. B., & Economides, A. N. (2017) · Bone · doi:10.1016/j.bone.2017.06.011 · Cited by 78

Activin A forms a non-signaling complex with ACVR1 and type II Activin/BMP receptors via its finger 2 tip loop

Aykul, S., Corpina, R. A., Goebel, E. J., Cunanan, C. J., Dimitriou, A., Kim, H. J., Zhang, Q., Rafique, A., Leidich, R., Wang, X., et al. (2020) · eLife · doi:10.7554/elife.54582 · Cited by 78

Heterotopic ossification: Mechanistic insights and clinical challenges

Xu, R., Hu, J., Zhou, X., & Yang, Y. (2017) · Bone · doi:10.1016/j.bone.2017.08.025 · Cited by 76

Structural biology of betaglycan and endoglin, membrane-bound co-receptors of the TGF-beta family

Kim, S. K., Henen, M. A., & Hinck, A. P. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219881160 · Cited by 79

Bioprinted constructs that simulate nerve–bone crosstalk to improve microenvironment for bone repair

Wang, T., Li, W., Zhang, Y., Xu, X., Qiang, L., Miao, W., Yue, X., Jiao, X., Zhou, X., Ma, Z., et al. (2023) · Bioactive Materials · doi:10.1016/j.bioactmat.2023.02.013 · Cited by 73

The Expansion of Heterotopic Bone in Fibrodysplasia Ossificans Progressiva Is Activin A-Dependent

Upadhyay, J., Xie, L., Huang, L., Das, N., Stewart, R. C., Lyon, M. C., Palmer, K., Rajamani, S., Graul, C., Lobo, M., et al. (2017) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3235 · Cited by 73

Role of Signal Transduction Pathways and Transcription Factors in Cartilage and Joint Diseases

Nishimura, R., Hata, K., Takahata, Y., Murakami, T., Nakamura, E., Ohkawa, M., & Ruengsinpinya, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041340 · Cited by 73

Saracatinib is an efficacious clinical candidate for fibrodysplasia ossificans progressiva

Williams, E., Bagarova, J., Kerr, G., Xia, D.-D., Place, E., Dey, D., Shen, Y., Bocobo, G. A., Mohedas, A. H., Huang, X., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.95042 · Cited by 71

Role of the NF-kB signalling pathway in heterotopic ossification: biological and therapeutic significance

Liu, F., Zhao, Y., Pei, Y., Lian, F., & Lin, H. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01533-w · Cited by 76

Strategic Targeting of Multiple BMP Receptors Prevents Trauma-Induced Heterotopic Ossification

Agarwal, S., Loder, S. J., Breuler, C. J., Li, J., Cholok, D. J., Brownley, C., Peterson, J. R., Hsieh, H. H. S., Drake, J., Ranganathan, K., et al. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2017.01.008 · Cited by 71

A BMP/activin A chimera is superior to native BMPs and induces bone repair in nonhuman primates when delivered in a composite matrix

Seeherman, H. J., Berasi, S. P., Brown, C. T., Martinez, R., Juo, Z. S., Jelinsky, S. A., Cain, M., Grode, J., Tumelty, K. E., Bohner, M., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aar4953 · Cited by 69

Inflammation in Fibrodysplasia Ossificans Progressiva and Other Forms of Heterotopic Ossification

Matsuo, K., Chavez, R. D., Barruet, E., & Hsiao, E. C. (2019) · Current Osteoporosis Reports · doi:10.1007/s11914-019-00541-x · Cited by 68

Garetosmab in fibrodysplasia ossificans progressiva: a randomized, double-blind, placebo-controlled phase 2 trial

Rocco, M. D., Forleo‐Neto, E., Pignolo, R. J., Keen, R. W., Orcel, P., Funck‐Brentano, T., Roux, C., Kolta, S., Madeo, A., Bubbear, J. S., et al. (2023) · Nature Medicine · doi:10.1038/s41591-023-02561-8 · Cited by 68

Common mutations in ALK2/ACVR1, a multi-faceted receptor, have roles in distinct pediatric musculoskeletal and neural orphan disorders

Pacifici, M., & Shore, E. M. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.12.007 · Cited by 68

Bone Morphogenetic Protein Signaling in Cancer; Some Topics in the Recent 10 Years

Ehata, S., & Miyazono, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.883523 · Cited by 67

Therapeutic advances for blocking heterotopic ossification in fibrodysplasia ossificans progressiva

Wentworth, K. L., Masharani, U. B., & Hsiao, E. C. (2018) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.13823 · Cited by 67

Palovarotene reduces heterotopic ossification in juvenile FOP mice but exhibits pronounced skeletal toxicity

Lees‐Shepard, J. B., Nicholas, S.-A. E., Stoessel, S. J., Devarakonda, P. M., Schneider, M. J., Yamamoto, M., & Goldhamer, D. J. (2018) · eLife · doi:10.7554/elife.40814 · Cited by 69

Granting immunity to FOP and catching heterotopic ossification in the Act

Kaplan, F. S., Pignolo, R. J., & Shore, E. M. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.12.013 · Cited by 65

The activin receptor is stimulated in the skeleton, vasculature, heart, and kidney during chronic kidney disease

Williams, M. J., Sugatani, T., Agapova, O. A., Fang, Y., Gaut, J. P., Monier‐Faugere, M., Malluche, H. H., & Hruska, K. A. (2017) · Kidney International · doi:10.1016/j.kint.2017.06.016 · Cited by 63

Stem cells and heterotopic ossification: Lessons from animal models

Lees‐Shepard, J. B., & Goldhamer, D. J. (2018) · Bone · doi:10.1016/j.bone.2018.01.029 · Cited by 63

The immunophilin FKBP12 inhibits hepcidin expression by binding the BMP type I receptor ALK2 in hepatocytes

Colucci, S., Pagani, A., Pettinato, M., Artuso, I., Nai, A., Camaschella, C., & Silvestri, L. (2017) · Blood · doi:10.1182/blood-2017-04-780692 · Cited by 62

Context-dependent TGFβ family signalling in cell fate regulation

Richardson, L., Wilcockson, S. G., Guglielmi, L., & Hill, C. S. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00638-3 · Cited by 63

Induced Pluripotent Stem Cells to Model Human Fibrodysplasia Ossificans Progressiva

Cai, J., Orlova, V. V., Cai, X., Eekhoff, E. M. W., Zhang, K., Pei, D., Pan, G., Mummery, C. L., & ten Dijke, P. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.10.020 · Cited by 60

An mTOR Signaling Modulator Suppressed Heterotopic Ossification of Fibrodysplasia Ossificans Progressiva

Hino, K., Zhao, C., Horigome, K., Nishio, M., Okanishi, Y., Nagata, S., Komura, S., Yamada, Y., Toguchida, J., Ohta, A., et al. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.10.007 · Cited by 60

The effect of type 2 diabetes mellitus and obesity on muscle progenitor cell function

Teng, S., & Huang, P. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1186-0 · Cited by 63

Activins as Dual Specificity TGF-β Family Molecules: SMAD-Activation via Activin- and BMP-Type 1 Receptors

Olsen, O. E., Hella, H., Elsaadi, S., Jacobi, C., Martı́nez-Hackert, E., & Holien, T. (2020) · Biomolecules · doi:10.3390/biom10040519 · Cited by 61

Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization

Agnew, C., Ayaz, P., Kashima, R., Loving, H. S., Ghatpande, P., Kung, J. E., Underbakke, E. S., Shan, Y., Shaw, D. E., Hata, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25248-5 · Cited by 58

Anti-ACVR1 antibodies exacerbate heterotopic ossification in fibrodysplasia ossificans progressiva (FOP) by activating FOP-mutant ACVR1

Aykul, S., Huang, L., Wang, L., Das, N., Reisman, S., Ray, Y., Zhang, Q., Rothman, N. J., Nannuru, K. C., Kamat, V., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci153792 · Cited by 57

TGF-β family ligands exhibit distinct signalling dynamics that are driven by receptor localisation

Miller, D. S. J., Schmierer, B., & Hill, C. S. (2019) · Journal of Cell Science · doi:10.1242/jcs.234039 · Cited by 56

Retinoid roles and action in skeletal development and growth provide the rationale for an ongoing heterotopic ossification prevention trial

Pacifici, M. (2017) · Bone · doi:10.1016/j.bone.2017.08.010 · Cited by 56

BMPR2 inhibits activin and BMP signaling via wild-type ALK2

Olsen, O. E., Sankar, M., Elsaadi, S., Hella, H., Buene, G., Darvekar, S. R., Misund, K., Katagiri, T., Knaus, P. I., & Holien, T. (2018) · Journal of Cell Science · doi:10.1242/jcs.213512 · Cited by 56

GDF8 and activin A blockade protects against GLP-1–induced muscle loss while enhancing fat loss in obese male mice and non-human primates

Mastaitis, J. W., Gomez, D., Raya, J. G., Li, D., Min, S., Stec, M., Kleiner, S., McWilliams, T., Altarejos, J. Y., Murphy, A. J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59485-9 · Cited by 53

The ACVR1 R206H mutation found in fibrodysplasia ossificans progressiva increases human induced pluripotent stem cell-derived endothelial cell formation and collagen production through BMP-mediated SMAD1/5/8 signaling

Barruet, E., Morales, B. M., Lwin, W. W., White, M. P., Theodoris, C. V., Kim, H., Urrutia, A., Wong, S. A., Srivastava, D., & Hsiao, E. C. (2016) · Stem Cell Research & Therapy · doi:10.1186/s13287-016-0372-6 · Cited by 54

Smad-dependent mechanisms of inflammatory bone destruction

Fennen, M., Pap, T., & Dankbar, B. (2016) · Arthritis Research & Therapy · doi:10.1186/s13075-016-1187-7 · Cited by 54

Matters of context guide future research in TGFβ superfamily signaling

Akhurst, R. J., & Padgett, R. W. (2015) · Science Signaling · doi:10.1126/scisignal.aad0416 · Cited by 52

A self-amplifying loop of YAP and SHH drives formation and expansion of heterotopic ossification

Cong, Q., Liu, Y., Zhou, T., Zhou, Y., Xu, R., Cheng, C., Chung, H. S., Yan, M., Zhou, H., Liao, Z., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abb2233 · Cited by 52

Variable signaling activity by FOP ACVR1 mutations

Haupt, J., Xu, M., & Shore, E. M. (2017) · Bone · doi:10.1016/j.bone.2017.10.027 · Cited by 52

Repurposing Vandetanib plus Everolimus for the Treatment of ACVR1 -Mutant Diffuse Intrinsic Pontine Glioma

Carvalho, D. M., Richardson, P. J., Olaciregui, N., Stankunaite, R., Lavarino, C. E., Molinari, V., Corley, E. A., Smith, D. P., Ruddle, R. R., Donovan, A., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-1201 · Cited by 54

Inhibition of TGFβ signaling decreases osteogenic differentiation of fibrodysplasia ossificans progressiva fibroblasts in a novel in vitro model of the disease

Micha, D., Voermans, E., Eekhoff, E. M. W., van Essen, H. W., Zandieh‐Doulabi, B., Netelenbos, J. C., Rustemeyer, T., Sistermans, E. A., Pals, G., & Bravenboer, N. (2016) · Bone · doi:10.1016/j.bone.2016.01.004 · Cited by 51

Heterotopic bone induction via BMP signaling: Potential therapeutic targets for fibrodysplasia ossificans progressiva

Katagiri, T., Tsukamoto, S., & Kuratani, M. (2017) · Bone · doi:10.1016/j.bone.2017.07.024 · Cited by 51

Early clinical observations on the use of imatinib mesylate in FOP: A report of seven cases

Kaplan, F. S., Andolina, J. R., Adamson, P. C., Teachey, D. T., Finklestein, J. Z., Ebb, D. H., Whitehead, B., Jacobs, B., Siegel, D. M., Keen, R. W., et al. (2017) · Bone · doi:10.1016/j.bone.2017.07.019 · Cited by 51

Pathogenic ACVR1R206H activation by Activin A‐induced receptor clustering and autophosphorylation

Ramachandran, A., Mehić, M., Wasim, L., Malinova, D., Gori, I., Blaszczyk, B. K., Carvalho, D. M., Shore, E. M., Jones, C., Hyvönen, M., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106317 · Cited by 51

Pharmacokinetics and Pharmacodynamics of Garetosmab (Anti‐Activin A): Results From a First‐in‐Human Phase 1 Study

Vanhoutte, F. P., Liang, S., Ruddy, M. K., Zhao, A., Drewery, T., Wang, Y., DelGizzi, R., Forleo‐Neto, E., Rajadhyaksha, M., Herman, G. A., et al. (2020) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.1638 · Cited by 49

Tendon mineralization is progressive and associated with deterioration of tendon biomechanical properties, and requires BMP-Smad signaling in the mouse Achilles tendon injury model

Zhang, K., Asai, S., Hast, M. W., Liu, M., Usami, Y., Iwamoto, M., Soslowsky, L. J., & Enomoto‐Iwamoto, M. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.01.015 · Cited by 48

Shaping the bone through iron and iron-related proteins

Ledesma-Colunga, M. G., Weidner, H., Spasić, M. V., Hofbauer, L. C., Baschant, U., & Rauner, M. (2021) · Seminars in Hematology · doi:10.1053/j.seminhematol.2021.06.002 · Cited by 50

ACVR1R206HFOP mutation alters mechanosensing and tissue stiffness during heterotopic ossification

Haupt, J., Stanley, A. K., McLeod, C. M., Cosgrove, B. D., Culbert, A. L., Wang, L., Mourkioti, F., Mauck, R. L., & Shore, E. M. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-05-0311 · Cited by 48

Biology of bone morphogenetic protein in bone repair and regeneration: A role for autologous blood coagulum as carrier

Sampath, T. K., & Vukičević, S. (2020) · Bone · doi:10.1016/j.bone.2020.115602 · Cited by 46

Conserved signaling pathways underlying heterotopic ossification

Chen, K., Chen, L., Hu, Y., Ding, N., Lu, H., Li, Y., Kessler, J. A., & Kan, L. (2017) · Bone · doi:10.1016/j.bone.2017.04.014 · Cited by 46

Activin A amplifies dysregulated BMP signaling and induces chondro-osseous differentiation of primary connective tissue progenitor cells in patients with fibrodysplasia ossificans progressiva (FOP)

Wang, H., Shore, E. M., Pignolo, R. J., & Kaplan, F. S. (2017) · Bone · doi:10.1016/j.bone.2017.11.014 · Cited by 46

Elevated BMP and Mechanical Signaling Through YAP1/RhoA Poises FOP Mesenchymal Progenitors for Osteogenesis

Stanley, A. K., Heo, S.-J., Mauck, R. L., Mourkioti, F., & Shore, E. M. (2019) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3760 · Cited by 48

Fibrodysplasia ossificans progressiva (FOP): A disorder of osteochondrogenesis

Kaplan, F. S., Mukaddam, M. A., Stanley, A. K., Towler, O. W., & Shore, E. M. (2020) · Bone · doi:10.1016/j.bone.2020.115539 · Cited by 46

Fibrodysplasia Ossificans Progressiva: What Have We Achieved and Where Are We Now? Follow-up to the 2015 Lorentz Workshop

de Ruiter, R. D., Smilde, B. J., Pals, G., Bravenboer, N., Knaus, P. I., Schoenmaker, T., Botman, E., Sánchez‐Duffhues, G., Pacifici, M., Pignolo, R. J., et al. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.732728 · Cited by 45

Osteogenic potential of alpha smooth muscle actin expressing muscle resident progenitor cells

Matthews, B. G., Torreggiani, E., Roeder, E., Matić, I., Grčević, D., & Kalajzić, I. (2015) · Bone · doi:10.1016/j.bone.2015.12.010 · Cited by 45

The Fibrodysplasia Ossificans Progressiva (FOP) mutation p.R206H in ACVR1 confers an altered ligand response

Hildebrand, L., Stange, K., Deichsel, A., Gossen, M., & Seemann, P. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.10.001 · Cited by 37

Activin-dependent signaling in fibro/adipogenic progenitors causes fibrodysplasia ossificans progressiva

Lees‐Shepard, J. B., Yamamoto, M., Biswas, A. A., Stoessel, S. J., Nicholas, S.-A. E., Cogswell, C. A., Devarakonda, P. M., Schneider, M. J., Cummins, S. M., Legendre, N. P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-02872-2 · Cited by 228

An anti-ACVR1 antibody exacerbates heterotopic ossification by fibro-adipogenic progenitors in fibrodysplasia ossificans progressiva mice

Lees-Shepard, J. B., Stoessel, S. J., Chandler, J., Bouchard, K., Bento, P., Apuzzo, L. N., Devarakonda, P. M., Hunter, J. W., & Goldhamer, D. J. (2022) · Journal of Clinical Investigation · doi:10.1172/jci153795 · Cited by 41

The obligatory role of Activin A in the formation of heterotopic bone in Fibrodysplasia Ossificans Progressiva

Wolken, D. M. A., Idone, V. J., Hatsell, S. J., Yu, P. B., & Economides, A. N. (2017) · Bone · doi:10.1016/j.bone.2017.06.011 · Cited by 78

Molecular Consequences of the ACVR1R206H Mutation of Fibrodysplasia Ossificans Progressiva

Song, G.-A., Kim, H., Woo, K. M., Baek, J., Kim, G.-S., Choi, J., & Ryoo, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.094557 · Cited by 114