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

Bone: Formation by Autoinduction

Urist, M. R. (1965) · Science · doi:10.1126/science.150.3698.893 · Cited by 5,529 · see citing works

Novel Regulators of Bone Formation: Molecular Clones and Activities

Wozney, J. M., Rosen, V., Celeste, A. J., Mitsock, L. M., Whitters, M. J., Kriz, R., Hewick, R. M., & Wang, E. A. (1988) · Science · doi:10.1126/science.3201241 · Cited by 3,874 · see citing works

TGFβ signalling in context

Massagué, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3434 · Cited by 3,130 · see citing works

Identification of Smad7, a TGFβ-inducible antagonist of TGF-β signalling

Nakao, A., Afrakhte, M., Morn, A., Nakayama, T., Christian, J. L., Heuchel, R. L., Itoh, S., Kawabata, M., Heldin, N., Heldin, C., et al. (1997) · Nature · doi:10.1038/39369 · Cited by 1,796 · see citing works

Bone morphogenetic protein-2 converts the differentiation pathway of C2C12 myoblasts into the osteoblast lineage [published erratum appears in J Cell Biol 1995 Feb;128(4):following 713]

Katagiri, T. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.6.1755 · Cited by 1,452 · see citing works

The MAD-Related Protein Smad7 Associates with the TGFβ Receptor and Functions as an Antagonist of TGFβ Signaling

Hayashi, H., Abdollah, S., Qiu, Y., Cai, J., Xu, Y., Grinnell, B. W., Richardson, M. A., Topper, J. N., Gimbrone, M. A., Wrana, J. L., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80303-7 · Cited by 1,322 · see citing works

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 · see citing works

Smad6 inhibits signalling by the TGF-β superfamily

Imamura, T., Takase, M., Nishihara, A., Oeda, E., Hanai, J., Kawabata, M., & Miyazono, K. (1997) · Nature · doi:10.1038/39355 · Cited by 1,023 · see citing works

Bone morphogenetic protein receptors and signal transduction

Miyazono, K., Kamiya, Y., & Morikawa, M. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp148 · Cited by 1,000 · see citing works

Identification and Functional Characterization of Distinct Critically Important Bone Morphogenetic Protein-specific Response Elements in the Id1 Promoter

Korchynskyi, O., & ten Dijke, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111023200 · Cited by 876 · see citing works

The regulation of TGFβ signal transduction

Moustakas, A., & Heldin, C. (2009) · Development · doi:10.1242/dev.030338 · Cited by 830 · see citing works

TGF-β Superfamily Signaling in Embryonic Development and Homeostasis

Wu, M., & Hill, C. S. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.02.012 · Cited by 743 · see citing works

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 · see citing works

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 635 · see citing works

Signal transduction of bone morphogenetic protein receptors

Nohe, A. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2003.08.011 · Cited by 514 · see citing works

Balancing BMP Signaling through Integrated Inputs into the Smad1 Linker

Sapkota, G. P., Alarcón, C. R., Spagnoli, F. M., Brivanlou, A. H., & Massagué, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.006 · Cited by 419 · see citing works

Roles of Bone Morphogenetic Protein Type I Receptors and Smad Proteins in Osteoblast and Chondroblast Differentiation

Fujii, M., Takeda, K., Imamura, T., Aoki, H., Sampath, T. K., ENOMOTO, S., Kawabata, M., Kato, M., Ichijo, H., & Miyazono, K. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.11.3801 · Cited by 411 · see citing works

Negative regulation of TGF-β receptor/Smad signal transduction

Itoh, S., & ten Dijke, P. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.02.015 · Cited by 387 · see citing works

Beyond TGFβ: roles of other TGFβ superfamily members in cancer

Wakefield, L. M., & Hill, C. S. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3500 · Cited by 373 · see citing works

Phospho-control of TGF-β superfamily signaling

Wrighton, K. H., Lin, X., & Feng, X. (2008) · Cell Research · doi:10.1038/cr.2008.327 · Cited by 366 · see citing works

Isolation of osteogenin, an extracellular matrix-associated, bone-inductive protein, by heparin affinity chromatography.

Sampath, T. K., Muthukumaran, N., & Reddi, A. H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.20.7109 · Cited by 333 · see citing works

Direct Binding of Smad1 and Smad4 to Two Distinct Motifs Mediates Bone Morphogenetic Protein-specific Transcriptional Activation ofId1 Gene

López-Rovira, T., Chalaux, E., Massagué, J., Rosa, J. L., & Ventura, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106826200 · Cited by 285 · see citing works

Promiscuity and specificity in BMP receptor activation

Mueller, T. D., & Nickel, J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.02.043 · Cited by 285 · see citing works

Identification of a BMP‐responsive element in Id1, the gene for inhibition of myogenesis

Katagiri, T., Imada, M., Yanai, T., Suda, T., Takahashi, N., & Kamijo, R. (2002) · Genes to Cells · doi:10.1046/j.1365-2443.2002.00573.x · Cited by 262 · see citing works

Constitutively Activated ALK2 and Increased SMAD1/5 Cooperatively Induce Bone Morphogenetic Protein Signaling in Fibrodysplasia Ossificans Progressiva

Fukuda, T., Kohda, M., Kanomata, K., Nojima, J., Nakamura, A., Kamizono, J., Noguchi, Y., IWAKIRI, K., Kondo, T., 黒瀬, 純., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801681200 · Cited by 205 · see citing works

Dynamics of TGF‐β/Smad signaling

Zi, Z., Chapnick, D. A., & Liu, X. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.063 · Cited by 203 · see citing works

Dose-dependent Smad1, Smad5 and Smad8 signaling in the early mouse embryo

Arnold, S. J., Maretto, S., Islam, A., Bikoff, E. K., & Robertson, E. J. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.04.442 · Cited by 163 · see citing works

Modifications of Vectors pEF-BOS, pcDNA1 and pcDNA3 Result in Improved Convenience and Expression

Goldman, L. A., Cutrone, E. C., Kotenko, S. V., Krause, C. D., & Langer, J. A. (1996) · BioTechniques · doi:10.2144/96216bm10 · Cited by 158 · see citing works

Smad6 as a Transcriptional Corepressor

Bai, S., Shi, X., Yang, X., & Cao, X. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8267 · Cited by 150 · see citing works

IN VIVO SOMATIC CELL GENE TRANSFER OF AN ENGINEERED NOGGIN MUTEIN PREVENTS BMP4-INDUCED HETEROTOPIC OSSIFICATION

Glaser, D. L., Economides, A. N., Wang, L., Liu, X., KIMBLE, R. D., Fandl, J. P., Wilson, J. M., Stahl, N., Kaplan, F. S., & Shore, E. M. (2003) · Journal of Bone and Joint Surgery · doi:10.2106/00004623-200312000-00010 · Cited by 143 · see citing works

Tumor Necrosis Factor α Represses Bone Morphogenetic Protein (BMP) Signaling by Interfering with the DNA Binding of Smads through the Activation of NF-κB

Yamazaki, M., Fukushima, H., Shin, M., Katagiri, T., Doi, T., Takahashi, T., & Jimi, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.070540 · Cited by 139 · see citing works

Smad6 Recruits Transcription Corepressor CtBP To Repress Bone Morphogenetic Protein-Induced Transcription

Lin, X., Liang, Y.-Y., Sun, B., Liang, M., Shi, Y. G., Brunicardi, F. C., Shi, Y., & Feng, X. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.24.9081-9093.2003 · Cited by 109 · see citing works

Structural Basis of Smad1 Activation by Receptor Kinase Phosphorylation

Qin, B. Y., Chacko, B. M., Lam, S. S., de Caestecker, M. P., Correia, J. J., & Lin, K. F. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00417-8 · Cited by 109 · see citing works

Constitutively Active BMP Type I Receptors Transduce BMP-2 Signals without the Ligand in C2C12 Myoblasts

Akiyama, S., Katagiri, T., Namiki, M., Yamaji, N., Yamamoto, N., Miyama, K., Shibuyà, H., Ueno, N., Wozney, J. M., & Suda, T. (1997) · Experimental Cell Research · doi:10.1006/excr.1997.3680 · Cited by 106 · see citing works

Fine‐tuning BMP7 signalling in adipogenesis by UBE2O/E2‐230K‐mediated monoubiquitination of SMAD6

Zhang, X., Zhang, J., Bauer, A., Zhang, L., Selinger, D. W., Lu, C., & ten Dijke, P. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.38 · Cited by 97 · see citing works

Phosphatases in SMAD regulation

Bruce, D. L., & Sapkota, G. P. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.02.001 · Cited by 86 · see citing works

Dual Roles of Smad Proteins in the Conversion from Myoblasts to Osteoblastic Cells by Bone Morphogenetic Proteins

Nojima, J., Kanomata, K., Takada, Y., Fukuda, T., Kokabu, S., Ohte, S., Takada, T., Tsukui, T., Yamamoto, T. S., Sasanuma, H., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028019 · Cited by 79 · see citing works

Purification and identification of a BMP-like factor from bovine serum

Kodaira, K., Imada, M., Goto, M., Tomoyasu, A., Fukuda, T., Kamijo, R., Suda, T., Higashio, K., & Katagiri, T. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.045 · Cited by 70 · see citing works

A unique mutation of ALK2, G356D, found in a patient with fibrodysplasia ossificans progressiva is a moderately activated BMP type I receptor

Fukuda, T., Kanomata, K., Nojima, J., Kokabu, S., Akita, M., Ikebuchi, K., Jimi, E., Komori, T., Maruki, Y., Matsuoka, M., et al. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.093 · Cited by 67 · see citing works

Autocrine BMP4 signalling regulates ID3 proto-oncogene expression in human ovarian cancer cells

Shepherd, T. G., Thériault, B. L., & Nachtigal, M. W. (2008) · Gene · doi:10.1016/j.gene.2008.02.015 · Cited by 66 · see citing works

The unique activity of bone morphogenetic proteins in bone: a critical role of the Smad signaling pathway

Katagiri, T., & Tsukamoto, S. (2013) · Biological Chemistry · doi:10.1515/hsz-2012-0310 · Cited by 59 · see citing works

A novel mutation of ALK2, L196P, found in the most benign case of fibrodysplasia ossificans progressiva activates BMP-specific intracellular signaling equivalent to a typical mutation, R206H

Ohte, S., Shin, M., Sasanuma, H., Yoneyama, K., Akita, M., Ikebuchi, K., Jimi, E., Maruki, Y., Matsuoka, M., Namba, A., et al. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.03.001 · Cited by 48 · see citing works

Phospho-control of TGF-β superfamily signaling

Katharine, Wrighton, Xia, Lin, , X., & Feng (2009) · Cell Research · Cited by 44 · see citing works

5 The Bone Morphogenetic ProteinsPreprint

Katagiri, T., Suda, T., & Miyazono, K. (2008) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969752.50.121 · Cited by 42 · see citing works

Recent Topics in Fibrodysplasia Ossificans Progressiva

Katagiri, T., Tsukamoto, S., Nakachi, Y., & Kuratani, M. (2018) · Endocrinology and Metabolism · doi:10.3803/enm.2018.33.3.331 · Cited by 38 · see citing works

ANA Deficiency Enhances Bone Morphogenetic Protein-induced Ectopic Bone Formation via Transcriptional Events

Miyai, K., Yoneda, M., Hasegawa, U., Toita, S., Izu, Y., Hemmi, H., Hayata, T., Ezura, Y., Mizutani, S., Miyazono, K., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807677200 · Cited by 25 · see citing works

Identification of a novel bone morphogenetic protein (BMP)-inducible transcript, BMP-inducible transcript-1, by utilizing the conserved BMP-responsive elements in the Id genes

Shin, M., Ohte, S., Fukuda, T., Sasanuma, H., Yoneyama, K., Kokabu, S., Miyamoto, A., Tsukamoto, S., Hohjoh, H., Jimi, E., et al. (2012) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-012-0381-1 · Cited by 22 · see citing works

BMP signaling is responsible for serum-induced Id2 expression

Kurooka, H., Nakahiro, T., Mori, K., Sano, K., & Yokota, Y. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.02.150 · Cited by 19 · see citing works

Identification and functional analysis of Zranb2 as a novel Smad‐binding protein that suppresses BMP signaling

Ohte, S., Kokabu, S., Iemura, S., Sasanuma, H., Yoneyama, K., Shin, M., Suzuki, S., Fukuda, T., Nakamura, Y., Jimi, E., et al. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23408 · Cited by 16 · see citing works

Role of Smad phosphatases in BMP-Smad signaling axis-induced osteoblast differentiation

Kokabu, S., Katagiri, T., Yoda, T., & Rosen, V. (2012) · Journal of Oral Biosciences · doi:10.1016/j.job.2012.02.003 · Cited by 14 · see citing works

Recent topics in fibrodysplasia ossificans progressiva

Katagiri, T. (2012) · Journal of Oral Biosciences · doi:10.1016/j.job.2012.03.004 · Cited by 14 · see citing works

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 848 · see citing works

Contextual determinants of TGFβ action in development, immunity and cancer

David, C. J., & Massagué, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0007-0 · Cited by 851 · see citing works

Bone Morphogenetic ProteinsPreprint

Katagiri, T., & Watabe, T. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021899 · Cited by 533 · see citing works

Immunoregulation by members of the TGFβ superfamily

Chen, W., & ten Dijke, P. (2016) · Nature reviews. Immunology · doi:10.1038/nri.2016.112 · Cited by 347 · see citing works

Life-Course Genome-wide Association Study Meta-analysis of Total Body BMD and Assessment of Age-Specific Effects

Medina‐Gómez, C., Kemp, J. P., Trajanoska, K., Luan, J., Chesi, A., Ahluwalia, T. S., Mook-Kanamori, D. O., Ham, A. C., Hartwig, F. P., Evans, D. S., et al. (2018) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.12.005 · Cited by 346 · see citing works

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 253 · see citing works

Simultaneous Multiplexed Measurement of RNA and Proteins in Single Cells

Darmanis, S., Gallant, C. J., Marinescu, V. D., Niklasson, M., Segerman, A., Flamourakis, G., Fredriksson, S., Assarsson, E., Lundberg, M., Nelander, S., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.021 · Cited by 219 · see citing works

TGF‐β signaling: A recap of SMAD‐independent and SMAD‐dependent pathways

Aashaq, S., Batool, A., Mir, S. A., Beigh, M. A., Andrabi, K. I., & Shah, Z. A. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30529 · Cited by 216 · see citing works

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 129 · see citing works

Hepcidin and the BMP-SMAD pathway: An unexpected liaison

Silvestri, L., Nai, A., Dulja, A., & Pagani, A. (2019) · Vitamins and hormones · doi:10.1016/bs.vh.2019.01.004 · Cited by 125 · see citing works

Smad1/5 is required for erythropoietin-mediated suppression of hepcidin in mice

Wang, C., Core, A. B., Canali, S., Zumbrennen‐Bullough, K. B., Özer, S., Umans, L., Zwijsen, A., & Babitt, J. L. (2017) · Blood · doi:10.1182/blood-2016-12-759423 · Cited by 86 · see citing works

The co-stimulatory molecule B7-H3 promotes the epithelial-mesenchymal transition in colorectal cancer

Jiang, B., Zhang, T., Liu, F., Sun, Z., Shi, H., Hua, D., & Yang, C. G. (2016) · Oncotarget · doi:10.18632/oncotarget.9035 · Cited by 82 · see citing works

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 · see citing works

Ligand-activated BMP signaling inhibits cell differentiation and death to promote melanoma

Venkatesan, A. M., Vyas, R., Gramann, A. K., Dresser, K., Gujja, S., Bhatnagar, S., Chhangawala, S., Gomes, C. B. F., Xi, H. S., Lian, C. G., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci92513 · Cited by 60 · see citing works

Apobec1 complementation factor overexpression promotes hepatic steatosis, fibrosis, and hepatocellular cancer

Blanc, V., Riordan, J. D., Soleymanjahi, S., Nadeau, J. H., Nalbantoglu, I., Xie, Y., Molitor, E. A., Madison, B., Brunt, E. M., Mills, J. C., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci138699 · Cited by 57 · see citing works

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 · see citing works

Estimates of linkage disequilibrium and effective population sizes in Chinese Merino (Xinjiang type) sheep by genome-wide SNPs

Liu, S., He, S., Chen, L., Li, W., Di, J., & Liu, M. (2017) · Genes & Genomics · doi:10.1007/s13258-017-0539-2 · Cited by 50 · see citing works

Canonical BMP signaling in tubular cells mediates recovery after acute kidney injury

Vigolo, E., Markó, L., Hinze, C., Müller, D. N., Schmidt‐Ullrich, R., & Schmidt-Ott, K. M. (2018) · Kidney International · doi:10.1016/j.kint.2018.08.028 · Cited by 49 · see citing works

Integrative genomic analyses identify candidate causal genes for calcific aortic valve stenosis involving tissue-specific regulation

Thériault, S., Li, Z., Abner, E., Luan, J., Manikpurage, H. D., Houessou, U., Zamani, P., Briend, M., Estonian Biobank Research Team, Boudreau, D. K., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46639-4 · Cited by 49 · see citing works

Genome data uncover four synergistic key regulators for extremely small body size in horses

Metzger, J., Rau, J., Naccache, F., Conn, L. B., Lindgren, G., & Distl, O. (2018) · BMC Genomics · doi:10.1186/s12864-018-4877-5 · Cited by 46 · see citing works

Ablation of Hepatocyte Smad1, Smad5, and Smad8 Causes Severe Tissue Iron Loading and Liver Fibrosis in Mice

Wang, C., Xiao, X., Bayer, A. L., Xu, Y., Dev, S., Canali, S., Nair, A. V., Masia, R., & Babitt, J. L. (2019) · Hepatology · doi:10.1002/hep.30780 · Cited by 45 · see citing works

A Rare Mutation in <i>SMAD9</i> 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 · see citing works

The effect of acute heat stress on the innate immune function of rainbow trout based on the transcriptome

Zhou, C., Ka, W., Yuan, W.-K., & Wang, J. (2021) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2021.102834 · Cited by 44 · see citing works

Homozygous GDF2 nonsense mutations result in a loss of circulating BMP9 and BMP10 and are associated with either PAH or an “HHT‐like” syndrome in children

Hodgson, J. M., Ruiz‐Llorente, L., McDonald, J., Quarrell, O., Ugonna, K., Bentham, J. R., Mason, R., Martin, J. M., Moore, D., Bergstrom, K. L., et al. (2021) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.1685 · Cited by 42 · see citing works

Genomic Signatures of Selection Associated With Litter Size Trait in Jining Gray Goat

Wang, J., Zhang, T., Chen, Q.-M., Zhang, R., Li, L., Cheng, S., Shen, W., & Lei, C. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00286 · Cited by 38 · see citing works

Recent Topics in Fibrodysplasia Ossificans Progressiva

Katagiri, T., Tsukamoto, S., Nakachi, Y., & Kuratani, M. (2018) · Endocrinology and Metabolism · doi:10.3803/enm.2018.33.3.331 · Cited by 38 · see citing works

A combination of genome-wide association study and selection signature analysis dissects the genetic architecture underlying bone traits in chickens

Li, Y. D., Liu, X., Li, Z., Wang, W. J., Li, Y. M., Cao, Z. P., Luan, P., Xiao, F., Gao, H., Guo, H., et al. (2021) · animal · doi:10.1016/j.animal.2021.100322 · Cited by 36 · see citing works

Fibrodysplasia ossificans progressiva: current concepts from bench to bedside

Kaliya-Perumal, A.-K., Carney, T. J., & Ingham, P. W. (2020) · Disease Models & Mechanisms · doi:10.1242/dmm.046441 · Cited by 35 · see citing works

The study of selection signature and its applications on identification of candidate genes using whole genome sequencing data in chicken—a review

Bello, S. F., Lawal, R. A., Adeola, A. C., & Nie, Q. (2023) · Poultry Science · doi:10.1016/j.psj.2023.102657 · Cited by 35 · see citing works

Integrated RNA-seq and DNase-seq analyses identify phenotype-specific BMP4 signaling in breast cancer

Ampuja, M., Rantapero, T., Rodriguez-Martinez, A., Palmroth, M., Alarmo, E., Nykter, M., & Kallioniemi, A. H. (2017) · BMC Genomics · doi:10.1186/s12864-016-3428-1 · Cited by 32 · see citing works

Identification of genetic factors underlying persistent pulmonary hypertension of newborns in a cohort of Chinese neonates

Liu, X., Mei, M., Chen, X., Lu, Y., Dong, X., Hu, L., Hu, X., Cheng, G., Cao, Y., Yang, L., et al. (2019) · Respiratory Research · doi:10.1186/s12931-019-1148-1 · Cited by 32 · see citing works

The Genetic Architecture of High Bone Mass

Gregson, C. L., & Duncan, E. L. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.595653 · Cited by 32 · see citing works

Effects of FKBP12 and type II BMP receptors on signal transduction by ALK2 activating mutations associated with genetic disorders

Machiya, A., Tsukamoto, S., Ohte, S., Kuratani, M., Fujimoto, M., Kumagai, K., Osawa, K., Suda, N., Bullock, A. N., & Katagiri, T. (2018) · Bone · doi:10.1016/j.bone.2018.03.015 · Cited by 31 · see citing works

Expression, Regulation, and Functions of the Galectin-16 Gene in Human Cells and Tissues

Kaminker, J. D., & Timoshenko, A. V. (2021) · Biomolecules · doi:10.3390/biom11121909 · Cited by 30 · see citing works

A comprehensive transcriptomic view on the role of SMAD4 gene by RNAi-mediated knockdown in porcine follicular granulosa cells

Zhang, L., Du, X., Wei, S., Li, D., & Li, Q. (2016) · Reproduction · doi:10.1530/rep-16-0034 · Cited by 29 · see citing works

Lefty-1 alleviates TGF-β1-induced fibroblast–myofibroblast transdifferentiation in NRK-49F cells

Zhang, J., Zhang, L., Zhou, X., Wang, W., Renping, Z., Wu, P., Hu, W., & Xu, C. (2015) · Drug Design Development and Therapy · doi:10.2147/dddt.s86770 · Cited by 29 · see citing works

RNAseq based transcriptomics study of SMCs from carotid atherosclerotic plaque: BMP2 and IDs proteins are crucial regulators of plaque stability

Alloza, I., Goikuria, H., Idro, J. L., Triviño, J. C., Fernández Velasco, J. M., Elizagaray, E., García-Barcina, M., Montoya-Murillo, G., Sarasola, E., Vega Manrique, R., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-03687-9 · Cited by 25 · see citing works

Artificial Neural Network With Composite Architectures for Prediction of Local Control in Radiotherapy

Cui, S., Luo, Y., Tseng, H.-H., Haken, R. K. T., & Naqa, I. E. (2018) · IEEE Transactions on Radiation and Plasma Medical Sciences · doi:10.1109/trpms.2018.2884134 · Cited by 25 · see citing works

Coxsackievirus B3 Infection Early in Pregnancy Induces Congenital Heart Defects Through Suppression of Fetal Cardiomyocyte Proliferation

Sharma, V., Goessling, L. S., Brar, A. K., Joshi, C. S., Mysorekar, I. U., & Eghtesady, P. (2021) · Journal of the American Heart Association · doi:10.1161/jaha.120.017995 · Cited by 24 · see citing works

The Role of Bone Morphogenetic Protein 4 in Ovarian Function and Diseases

Yang, D., Yang, X., Dai, F., Wang, Y., Yang, Y., Hu, M. S., & Cheng, Y. (2021) · Reproductive Sciences · doi:10.1007/s43032-021-00600-8 · Cited by 24 · see citing works

A novel miRNA-4484 is up-regulated on microarray and associated with increased MMP-21 expression in serum of systemic sclerosis patients

Rusek, M., Michalska-Jakubus, M. M., Kowal, M., Bełtowski, J., & Krasowska, D. (2019) · Scientific Reports · doi:10.1038/s41598-019-50695-y · Cited by 23 · see citing works

Transcriptional downregulation of FAM3C/ILEI in the Alzheimer’s brain

Watanabe, N., Nakano, M., Mitsuishi, Y., Hara, N., Mano, T., Iwata, A., Murayama, S., Suzuki, T., Ikeuchi, T., & Nishimura, M. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab226 · Cited by 23 · see citing works

Establishment of the TALE-code reveals aberrantly activated homeobox gene PBX1 in Hodgkin lymphoma

Nagel, S., Pommerenke, C., Meyer, C., MacLeod, R. A. F., & Drexler, H. G. (2021) · PLoS ONE · doi:10.1371/journal.pone.0246603 · Cited by 22 · see citing works

Smad8/9 Is Regulated Through the BMP Pathway

Katakawa, Y., Funaba, M., & Murakami, M. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25478 · Cited by 20 · see citing works

SMAD1/5 mediates bone morphogenetic protein 2-induced up-regulation of BAMBI expression in human granulosa-lutein cells

Bai, L., Chang, H., Cheng, J., Klausen, C., Chu, G., Leung, P. C. K., & Yang, G. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.05.017 · Cited by 20 · see citing works

Human neuron subtype programming via single-cell transcriptome-coupled patterning screens

Lin, H., Janssens, J., Eisinger, B. N., Hornauer, P., Kroell, A.-S. H., Santel, M., Pascual-Garcia, M., Okamoto, R., Karava, K., He, Z., et al. (2025) · Science · doi:10.1126/science.adn6121 · Cited by 19 · see citing works

An emerging class of new therapeutics targeting TGF , Activin, and BMP ligands in pulmonary arterial hypertension

Upton, P. D., Dunmore, B. J., Li, W., & Morrell, N. W. (2022) · Developmental Dynamics · doi:10.1002/dvdy.478 · Cited by 19 · see citing works

Gelatin-based 3D biomimetic scaffolds platform potentiates culture of cancer stem cells in esophageal squamous cell carcinoma

Wu, Y., Liang, H., Luo, A., Li, Y., Liu, Z., Liu, Z., Li, X., Li, W., Liang, K., Li, J., et al. (2023) · Biomaterials · doi:10.1016/j.biomaterials.2023.122323 · Cited by 18 · see citing works

An investigation of BMP-7 mediated alterations to BMP signalling components in human tenocyte-like cells

Klatte‐Schulz, F., Giese, G., Differ, C., Minkwitz, S., Ruschke, K., Puts, R., Knaus, P. I., & Wildemann, B. (2016) · Scientific Reports · doi:10.1038/srep29703 · Cited by 18 · see citing works

Myoneurin regulates BMP signaling by competing with Ppm1a for Smad binding

Yang, S., Ning, G., Hou, Y., Cao, Y., Xu, J., Wu, J., Zhang, T., & Wang, Q. (2022) · iScience · doi:10.1016/j.isci.2022.104495 · Cited by 17 · see citing works

High Bone Mass Disorders: New Insights From Connecting the Clinic and the Bench

Bergen, D. J. M., Maurizi, A., Formosa, M. M., McDonald, G. L. K., El‐Gazzar, A., Hassan, N., Brandi, M. L., Riancho, J. A., Rivadeneira, F., Ntzani, E., et al. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4715 · Cited by 16 · see citing works

Norepinephrine triggers an immediate-early regulatory network response in primary human white adipocytes

Higareda-Almaraz, J. C., Karbiener, M., Giroud, M., Pauler, F., Gerhalter, T., Herzig, S., & Scheideler, M. (2018) · BMC Genomics · doi:10.1186/s12864-018-5173-0 · Cited by 12 · see citing works

Reduction of miR-744 delivered by NSCLC cell-derived extracellular vesicles upregulates SUV39H1 to promote NSCLC progression via activation of the Smad9/BMP9 axis

Gao, L., Tian, Q., Wu, T., Shi, S., Yin, X., Liu, L., Zheng, L., Wang, P., Tian, Y., & Xu, S. (2021) · Journal of Translational Medicine · doi:10.1186/s12967-020-02654-9 · Cited by 16 · see citing works

New Anti-Müllerian Hormone Target Genes Involved in Granulosa Cell Survival in Women With Polycystic Ovary Syndrome

Racine, C., Genêt, C., Bourgneuf, C., Dupont, C., Plisson‐Petit, F., Sarry, J., Hennequet‐Antier, C., Vigouroux, C., d’Argent, E. M., Pierre, A., et al. (2020) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaa879 · Cited by 14 · see citing works

The expression of Smad signaling pathway in myocardium and potential therapeutic effects.

Duan, Y., Zhu, W., Liu, M., Ashraf, M., & Xu, M. (2017) · PubMed · doi:10.14670/hh-11-845 · Cited by 14 · see citing works

Smad8 Is Increased in Duchenne Muscular Dystrophy and Suppresses miR-1, miR-133a, and miR-133b

Lopez, M. A., Si, Y., Hu, X., Williams, V., Qushair, F., Carlyle, J., Alesce, L., Conklin, M. J., Gilbert, S. R., Bamman, M. M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147515 · Cited by 12 · see citing works

Effect of Thrombin on the Metabolism and Function of Murine Macrophages

Ukan, Ü., Lagos, F. D., Kempf, S., Günther, S., Siragusa, M., Fißlthaler, B., & Fleming, I. (2022) · Cells · doi:10.3390/cells11101718 · Cited by 13 · see citing works

Discovery of Heterotopic Bone-Inducing Activity in Hard Tissues and the TGF-β Superfamily

Katagiri, T., Tsukamoto, S., Nakachi, Y., & Kuratani, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113586 · Cited by 12 · see citing works

Role of the redox state of the Pirin-bound cofactor on interaction with the master regulators of inflammation and other pathways

Ahsan, T., Shoily, S. S., Ahmed, T., & Sajib, A. A. (2023) · PLoS ONE · doi:10.1371/journal.pone.0289158 · Cited by 11 · see citing works

A proteomics approach to study mouse long bones: examining baseline differences and mechanical loading-induced bone formation in young-adult and old mice

Chermside‐Scabbo, C. J., Shuster, J. T., Erdmann-Gilmore, P., Tycksen, E., Zhang, Q., Townsend, R. R., & Silva, M. J. (2024) · Aging · doi:10.18632/aging.206131 · Cited by 10 · see citing works

Cytoplasmic calcium increase via fusion with inactivated Sendai virus induces apoptosis in human multiple myeloma cells by downregulation of c-Myc oncogene

Jiang, Y., Saga, K., Miyamoto, Y., & Kaneda, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.9105 · Cited by 10 · see citing works

Prognostic value of small mother against decapentaplegic expression in human gastric cancer

Zhang, H., Guo, Y., Sun, L., Ni, F., & Xu, K. (2021) · Bioengineered · doi:10.1080/21655979.2021.1935192 · Cited by 9 · see citing works

A potential role for SMAD9 in goose follicular selection through regulation of mRNA levels of luteinizing hormone receptor

Yu, D., Zhang, L., Wang, H., Chen, F., Chen, J., Zhang, Z., Li, J., Xing, C., Li, H., Li, J., et al. (2018) · Theriogenology · doi:10.1016/j.theriogenology.2018.11.022 · Cited by 9 · see citing works

Amelotin is expressed in retinal pigment epithelium and localizes to hydroxyapatite deposits in dry age-related macular degeneration

Rajapakse, D., Peterson, K. M., Mishra, S., Fan, J., Lerner, J. E., Campos, M. M., & Wistow, G. J. (2020) · Translational research · doi:10.1016/j.trsl.2020.02.007 · Cited by 10 · see citing works

The effects of mouse ovarian granulosa cell function and related gene expression by suppressing BMP/Smad signaling pathway

Zhang, L., Wang, H., Yu, D., Chen, J., Xing, C., Li, J., Li, J., & Cai, Y. (2018) · Animal Cells and Systems · doi:10.1080/19768354.2018.1497706 · Cited by 9 · see citing works

A blocking monoclonal antibody reveals dimerization of intracellular domains of ALK2 associated with genetic disorders

Katagiri, T., Tsukamoto, S., Kuratani, M., Tsuji, S., Nakamura, K., Ohte, S., Kawaguchi, Y., & Takaishi, K. (2023) · Nature Communications · doi:10.1038/s41467-023-38746-5 · Cited by 8 · see citing works

MiR-122-5p as a potential regulator of pulmonary vascular wall cell in idiopathic pulmonary arterial hypertension

Zhao, H. Z., Duan, R., Wang, Q., Hu, X., Zhao, Q., Wu, W., Jiang, R., Gong, S., Wang, L., Liu, J., et al. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e22922 · Cited by 8 · see citing works

Drosophila glial system: an approach towards understanding molecular complexity of neurodegenerative diseases

Shweta, Sharma, K., Shakarad, M., Agrawal, N., & Maurya, S. K. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-10075-w · Cited by 8 · see citing works

A Computational Recognition Analysis of Promising Prognostic Biomarkers in Breast, Colon and Lung Cancer Patients

Bakheet, T. M., Al-Mutairi, N., Doubi, M., Al‐Ahmadi, W., Alhosaini, K. A., & Al-Zoghaibi, F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031017 · Cited by 8 · see citing works

Genome-wide association study identified six loci associated with adverse drug reactions to aripiprazole in schizophrenia patients

Wang, X., Mei, D., Lu, Z., Zhang, Y., Sun, Y., Lu, T., Yan, H., & Yue, W. (2023) · Schizophrenia · doi:10.1038/s41537-023-00369-6 · Cited by 7 · see citing works

PLGA-based control release of Noggin blocks the premature fusion of cranial sutures caused by retinoic acid

Wang, W., Zhou, C., Feng, Z., Li, H., Zhang, Y., Bao, B., Cai, B., Chen, M., & Huang, H. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9457-8 · Cited by 7 · see citing works

The TGF-β/UCHL5/Smad2 Axis Contributes to the Pathogenesis of Placenta Accreta

Hashimoto, K., Miyagawa, Y., Watanabe, S., Takasaki, K., Nishizawa, M., Yatsuki, K., Takahashi, Y. K., Kamata, H., Kihira, C., Hiraike, H., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813706 · Cited by 7 · see citing works

Active Components of Pueraria lobata through the MAPK/ERK Signaling Pathway Alleviate Iron Overload in Alcoholic Liver Disease

Li, X., Le, L., Wan, M., Gong, L., Su, J., & Xu, L. (2024) · Chemistry & Biodiversity · doi:10.1002/cbdv.202400005 · Cited by 7 · see citing works

Pharmacological Manipulation of Early Zebrafish Skeletal Development Shows an Important Role for Smad9 in Control of Skeletal Progenitor Populations

McDonald, G. L. K., Wang, M., Hammond, C. L., & Bergen, D. J. M. (2021) · Biomolecules · doi:10.3390/biom11020277 · Cited by 7 · see citing works

Human neuron subtype programming through combinatorial patterning with scRNA-seq readoutsPreprint

Lin, H., Janssens, J., Kroell, A.-S. H., Hornauer, P., Santel, M., Okamoto, R., Karava, K., Priouret, M., Pascual-Garcia, M., Schröter, M. S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.12.571318 · Cited by 7 · see citing works

Investigating the potential effect of Holothuria scabra extract on osteogenic differentiation in preosteoblast MC3T3-E1 cells

Songkoomkrong, S., Nonkhwao, S., Duangprom, S., Saetan, J., Manochantr, S., Sobhon, P., Kornthong, N., & Amonruttanapun, P. (2024) · Scientific Reports · doi:10.1038/s41598-024-77850-4 · Cited by 6 · see citing works

Integrated Transcriptome and Multiple Activated Pathways in Endometrial Cancer

Jin, Q., Jiang, X., Du, X., Hu, W., Bai, S., Wang, X., Xu, B., & Zhao, W. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.680331 · Cited by 6 · see citing works

ZSWIM4 regulates embryonic patterning and BMP signaling by promoting nuclear Smad1 degradation

Wang, C., Liu, Z., Zeng, Y., Zhou, L., Long, Q., Hassan, I. U., Zhang, Y., Qi, X., Cai, D., Mao, B., et al. (2024) · EMBO Reports · doi:10.1038/s44319-023-00046-w · Cited by 5 · see citing works

The innate immune response in fetal lung mesenchymal cells targets VEGFR2 expression and activity

Medal, R. M., Im, A. M., Yamamoto, Y., Lakhdari, O., Blackwell, T. S., Hoffman, H. M., Sahoo, D., & Prince, L. S. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00554.2016 · Cited by 5 · see citing works

Understanding Musculoskeletal Disorders Through Next-Generation Sequencing

Garg, B., Tomar, N., Biswas, A., Mehta, N. H., & Malhotra, R. (2022) · JBJS Reviews · doi:10.2106/jbjs.rvw.21.00165 · Cited by 5 · see citing works

Chondroitin polymerizing factor (CHPF) promotes the progression of colorectal cancer through ASB2-mediated ubiquitylation of SMAD9.

Zhao, J., Tang, X., & Zhu, H. (2024) · PubMed · doi:10.14670/hh-18-738 · Cited by 4 · see citing works

Effects of Triiodothyronine on Human Osteoblast-Like Cells: Novel Insights From a Global Transcriptome Analysis

Rodrigues, B., Mathias, L. S., Depra, I. D. C., Cury, S., de Oliveira, M., Olimpio, R., Sibio, M. D. D., Gonçalves, B. M., & Nogueira, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.886136 · Cited by 2 · see citing works

Current and emerging treatment modalities for fibrodysplasia ossificans progressiva

Gençel, D., Erbil, N. N., Demiryürek, Ş., & Demiryürek, A. T. (2024) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2024.2422548 · Cited by 4 · see citing works

Tril targets Smad7 for degradation to allow hematopoietic specification in Xenopus embryos

Green, Y. S., Kwon, S., Mimoto, M. S., Xie, Y., & Christian, J. L. (2016) · Development · doi:10.1242/dev.141812 · Cited by 4 · see citing works

Identification of novel fibroblast subsets in diffuse cutaneous systemic sclerosis

Rosendahl, A.-H., Bornikoel, A., Zeinert, I., Keufgens, L., Tellkamp, F., Kleinenkuhnen, N., Baar, T., Schönborn, K., Krüger, M., Tresch, A., et al. (2025) · Annals of the Rheumatic Diseases · doi:10.1016/j.ard.2025.11.027 · Cited by 3 · see citing works

MECoRank: cancer driver genes discovery simultaneously evaluating the impact of SNVs and differential expression on transcriptional networks

Hui, Y., Wei, P.-J., Xia, J., Wang, Y., & Zheng, C.-H. (2019) · BMC Medical Genomics · doi:10.1186/s12920-019-0582-8 · Cited by 3 · see citing works

Genome-wide analysis for nanofiber induced global gene expression profile: A study in MC3T3-E1 cells by RNA-Seq

Wang, P., Meng, X., Xue, J., Fan, C., & Wang, J. (2023) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2023.113143 · Cited by 3 · see citing works

Refolding, purification, and characterization of constitutive-active human-Smad8 produced as inclusion bodies in ClearColi® BL21 (DE3)

Segovia-Trinidad, C. L., Quaas, B., Li, Z., Lavrentieva, A. V., Roger, Y., Scheper, T. H., Hoffmann, A., & Rinas, U. (2021) · Protein Expression and Purification · doi:10.1016/j.pep.2021.105878 · Cited by 3 · see citing works

Smad9 is a key player of follicular selection in goose via keeping the balance of LHR transcriptionPreprint

Yu, D., Chen, F., Zhang, L., Wang, H., Chen, J., Zhang, Z., Li, J., Xing, C., Li, H., Li, J., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/213546 · Cited by 3 · see citing works

A primate-specific (GCC) repeat in SMAD9 undergoes natural selection in humans and harbors unambiguous genotypes in late-onset neurocognitive disorder.Preprint

Alizadeh, S., Khamse, S., Bernhart, S. H., Vahedi, M., Afshar, H., Rezaei, O., Delbari, A., & Ohadi, M. (2022) · Research Square · doi:10.21203/rs.3.rs-2144796/v1 · Cited by 4 · see citing works

Camphorataimide B suppresses the metastasis of human colorectal cancer cell by inhibiting Smad/FAK/Akt axis and promoting degradation of Snail/BMP4 complex

Huang, C., Hung, C.-H., Lee, Y., Tseng, T., Lee, Y., Kao, S., & Wang, C. (2022) · Journal of Food and Drug Analysis · doi:10.38212/2224-6614.3405 · Cited by 2 · see citing works

Hints on transcriptional control of essential players in heterotopic ossification of Fibrodysplasia Ossificans Progressiva

Ravazzolo, R., Cappato, S., & Bocciardi, R. (2017) · Bone · doi:10.1016/j.bone.2017.10.028 · Cited by 2 · see citing works

[The role of bone morphogenetic protein signaling pathway in tooth root development].

Liu, C., Zhou, Y., Yan, G., Shi, C., Zhang, X., Hu, Y., Hao, X., Zhao, H., & Sun, H. (2018) · PubMed Central · doi:10.7518/hxkq.2018.05.017 · Cited by 2 · see citing works

miR-10b-5p regulates adipocyte lineage commitment and adipogenesis via targeting of Gata6 and Tubby

Kalenderoglou, N., Dimitri, F., Gonzalez, C. N., Vidal‐Puig, A., Hobbs, J., Younis, A. Z., Christodoulides, C., Carobbio, S., & Christian, M. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02834-y · Cited by 1 · see citing works

The pathogenesis and intersecting mechanisms of monogenic bone mass disorders

Padidela, R., Hendrickx, G., Mortier, G. R., & Mäkitie, O. (2026) · Nature Reviews Endocrinology · doi:10.1038/s41574-026-01260-x · Cited by 1 · see citing works

The role of anti-Müllerian hormone as a therapeutic agent to preserve the ovarian follicle pool during chemotherapy

Peregrín-Álvarez, I., Zemet, R., Woodard, T. L., Schenk, L. M., McKenzie, L. J., Huang, J.-C., Sharif, M., & Detti, L. (2026) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-026-03941-y · Cited by 1 · see citing works

Receptor-regulated smads (R-Smads) in the liver fluke Fasciola gigantica: Characterization, comparative sequence analysis, and life stage-specific expression

Japa, O., Phuangsri, C., Klinbumrung, K., & Prakhammin, K. (2025) · Acta Tropica · doi:10.1016/j.actatropica.2025.107603 · Cited by 1 · see citing works

Novel In Vitro Assay Models to Study Osteogenesis and Chondrogenesis for Human Skeletal Disorders

Katagiri, T. (2017) · Springer eBooks · doi:10.1007/978-3-319-47507-3_5

Comparative Oncogenomics Identifies Novel Regulators and Clinical Relevance of Neural Crest Identities in Melanoma

Venkatesan, A. M. (2017) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/m20386

A rare SMAD9 mutation identifies the BMP signalling pathway as a potential osteoanabolic targetPreprint

Gregson, C. L., Bergen, D. J. M., Leo, P., Sessions, R. B., Wheeler, L., Hartley, A. E., Youlten, S. E., Croucher, P. I., McInerney-Leo, A. M., Fraser, W. D., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/560565

The role of Smads and related transcription factors in the signal transduction of bone morphogenetic protein

Zheng-me, L. (2008) · International Journal of Stomatology

The unique activity of bone morphogenetic proteins in bone: a critical role of the Smad signaling pathway

Katagiri, T., & Tsukamoto, S. (2013) · Biological Chemistry · doi:10.1515/hsz-2012-0310 · Cited by 59 · see citing works

Signal transduction by bone morphogenetic protein receptors: functional roles of Smad proteins

Miyazono, K. (1999) · Bone · doi:10.1016/s8756-3282(99)00113-1 · Cited by 191 · see citing works

Activation of Smad1-mediated transcription by p300/CBP

Pearson, K. L., Hunter, T. R., & Janknecht, R. (1999) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(99)00166-9 · Cited by 57 · see citing works

A human Mad protein acting as a BMP-regulated transcriptional activator

Liu, F., Hata, A., Baker, J. C., Doody, J. F., Cárcamo, J. M., Harland, R. M., & Massagué, J. (1996) · Nature · doi:10.1038/381620a0 · Cited by 673 · see citing works