TGF-β and the TGF-β family: context-dependent roles in cell and tissue physiology

Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega

Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576 · see citing works

A genetic model for colorectal tumorigenesis

Fearon, E. R., & Vogelstein, B. (1990) · Cell · doi:10.1016/0092-8674(90)90186-i · Cited by 12,132 · see citing works

The basics of epithelial-mesenchymal transition

Kalluri, R., & Weinberg, R. A. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39104 · Cited by 10,196 · see citing works

The Epithelial-Mesenchymal Transition Generates Cells with Properties of Stem Cells

Mani, S. A., Guo, W., Liao, M.-J., Eaton, E. N., Ayyanan, A., Zhou, A. Y., Brooks, M. W., Reinhard, F., Zhang, C. C., Shipitsin, M. V., et al. (2008) · Cell · doi:10.1016/j.cell.2008.03.027 · Cited by 8,679 · see citing works

Cancer Genome Landscapes

Vogelstein, B., Papadopoulos, N., Velculescu, V. E., Zhou, S., Diaz, L. A., & Kinzler, K. W. (2013) · Science · doi:10.1126/science.1235122 · Cited by 7,863 · see citing works

Conversion of Peripheral CD4+CD25− Naive T Cells to CD4+CD25+ Regulatory T Cells by TGF-β Induction of Transcription Factor Foxp3

Chen, W., Jin, W., Hardegen, N. J., Lei, K.-J., Li, L., Marinos, N. J., McGrady, G., & Wahl, S. M. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030152 · Cited by 4,678 · see citing works

The Role of Tumoral FOXP3 on Cell Proliferation, Migration, and Invasion in Gastric Cancer

Zhang, L., Xu, J., Zhang, X., Zhang, Y., Wang, L., Huang, X., & Xu, Z. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479442 · Cited by 4,090 · see citing works

Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member

McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013 · see citing works

The miR-200 family and miR-205 regulate epithelial to mesenchymal transition by targeting ZEB1 and SIP1

Gregory, P. A., Bert, A. G., Paterson, E. L., Barry, S. C., Tsykin, A., Farshid, G., Vadas, M. A., Khew‐Goodall, Y., & Goodall, G. J. (2008) · Nature Cell Biology · doi:10.1038/ncb1722 · Cited by 3,852 · see citing works

TGFβ in the Context of an Inflammatory Cytokine Milieu Supports De Novo Differentiation of IL-17-Producing T Cells

Veldhoen, M., Hocking, R. J., Atkins, C. J., Locksley, R. M., & Stockinger, B. (2006) · Immunity · doi:10.1016/j.immuni.2006.01.001 · Cited by 3,605 · see citing works

Targeted disruption of the mouse transforming growth factor-β1 gene results in multifocal inflammatory disease

Shull, M. M., Ormsby, I., Kier, A. B., Pawlowski, S., Diebold, R. J., Yin, M., Allen, R., Sidman, C., Proetzel, G., Calvin, D., et al. (1992) · Nature · doi:10.1038/359693a0 · Cited by 2,985 · see citing works

Transforming growth factor type beta: rapid induction of fibrosis and angiogenesis in vivo and stimulation of collagen formation in vitro.

Roberts, A. B., Sporn, M. B., Assoian, R. K., Smith, J. M., Roche, N. S., Wakefield, L. M., Heine, U., Liotta, L. A., Falanga, V., & Kehrl, J. H. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.12.4167 · Cited by 2,867 · see citing works

Disruption of a new forkhead/winged-helix protein, scurfin, results in the fatal lymphoproliferative disorder of the scurfy mouse

Brunkow, M. E., Jeffery, E. W., Hjerrild, K. A., Paeper, B. W., Clark, L. B., Yasayko, S.-A., Wilkinson, J. E., Galas, D. J., Ziegler, S. F., & Ramsdell, F. (2001) · Nature Genetics · doi:10.1038/83784 · Cited by 2,628 · see citing works

Transforming growth factor-beta stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix.

Ignotz, R. A., & Massagué, J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35666-1 · Cited by 2,492 · see citing works

Integration of External Signaling Pathways with the Core Transcriptional Network in Embryonic Stem Cells

Chen, X., Han, X., Yuan, P., Fang, F., Huss, M., Vega, V. B., Wong, E., Orlov, Y. L., Zhang, W., Jiang, J., et al. (2008) · Cell · doi:10.1016/j.cell.2008.04.043 · Cited by 2,474 · see citing works

<i>DPC4</i> , A Candidate Tumor Suppressor Gene at Human Chromosome 18q21.1

Hahn, S. A., Schutte, M., Shamsul Hoque, A. T. M., Moskaluk, C. A., da Costa, L. T., Rozenblum, E., Weinstein, C. L., Fischer, A., Yeo, C. J., Hruban, R. H., et al. (1996) · Science · doi:10.1126/science.271.5247.350 · Cited by 2,337 · see citing works

The miR-200 family determines the epithelial phenotype of cancer cells by targeting the E-cadherin repressors ZEB1 and ZEB2

Park, S.-M., Gaur, A. B., Lengyel, E., & Peter, M. E. (2008) · Genes &amp; Development · doi:10.1101/gad.1640608 · Cited by 2,272 · see citing works

Inactivation of the Type II TGF-β Receptor in Colon Cancer Cells with Microsatellite Instability

Markowitz, S. D., Wang, J., Myeroff, L. L., Parsons, R. E., Sun, L., Lutterbaugh, J., Fan, R. S., Zborowska, E., Kinzler, K. W., Vogelstein, B., et al. (1995) · Science · doi:10.1126/science.7761852 · Cited by 2,267 · see citing works

Transforming growth factor-beta 1 induces alpha-smooth muscle actin expression in granulation tissue myofibroblasts and in quiescent and growing cultured fibroblasts

Desmoulière, A., Geinoz, A., Gabbiani, F., & Gabbiani, G. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.1.103 · Cited by 2,226 · see citing works

Endothelial-to-mesenchymal transition contributes to cardiac fibrosis

Zeisberg, E. M., Tarnavski, O., Zeisberg, M., Dorfman, A. L., McMullen, J. R., Gustafsson, E., Chandraker, A. K., Yuan, X., Pu, W. T., Roberts, A. B., et al. (2007) · Nature Medicine · doi:10.1038/nm1613 · Cited by 2,224 · see citing works

A Mechanism for Regulating Pulmonary Inflammation and Fibrosis: The Integrin αvβ6 Binds and Activates Latent TGF β1

Munger, J. S., Huang, X., Kawakatsu, H., Griffiths, M. J. D., Dalton, S. L., Wu, J., Pittet, J.-F., Kaminski, N., Garat, C., Matthay, M. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80545-0 · Cited by 2,076 · see citing works

Double muscling in cattle due to mutations in the myostatin gene

McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039 · see citing works

pl5INK4B is a potentia| effector of TGF-β-induced cell cycle arrest

Hannon, G. J., & Beach, D. (1994) · Nature · doi:10.1038/371257a0 · Cited by 1,950 · see citing works

p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest.Preprint

Polyak, K., Kato, J., Solomon, M., Sherr, C., Massagué, J., Roberts, J., & Koff, A. (1994) · Genes & Development · doi:10.1101/gad.8.1.9 · Cited by 1,949 · see citing works

Transforming growth factor beta

Roberts, A. B., & Sporn, M. B. (2011) · SpringerReference · doi:10.1007/springerreference_39918 · Cited by 1,945 · see citing works

IL-21 initiates an alternative pathway to induce proinflammatory TH17 cells

Korn, T., Bettelli, E., Gao, W., Awasthi, A., Jäger, A., Strom, T. B., Oukka, M., & Kuchroo, V. K. (2007) · Nature · doi:10.1038/nature05970 · Cited by 1,841 · see citing works

Direct signaling between platelets and cancer cells induces an epithelial–mesenchymal-like transition and promotes metastasis

Labelle, M., Begum, S., & Hynes, R. O. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.009 · Cited by 1,833 · see citing works

Evidence that fibroblasts derive from epithelium during tissue fibrosis

Iwano, M., Plieth, D., Danoff, T. M., Xue, C., Okada, H., & Neilson, E. G. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15518 · Cited by 1,809 · 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

A syndrome of altered cardiovascular, craniofacial, neurocognitive and skeletal development caused by mutations in TGFBR1 or TGFBR2

Loeys, B., Chen, J., Neptune, E., Judge, D. P., Podowski, M., Holm, T. M., Meyers, J. L., Leitch, C. C., Katsanis, N., Sharifi, N., et al. (2005) · Nature Genetics · doi:10.1038/ng1511 · Cited by 1,786 · see citing works

Human transforming growth factor-β complementary DNA sequence and expression in normal and transformed cells

Derynck, R., Jarrett, J. A., Chen, E. Y., Eaton, D. H., BELL, J. R., Assoian, R. K., Roberts, A. B., Sporn, M. B., & Goeddel, D. V. (1985) · Nature · doi:10.1038/316701a0 · Cited by 1,667 · see citing works

Aneurysm Syndromes Caused by Mutations in the TGF-β Receptor

Loeys, B., Schwarze, U., Holm, T. M., Callewaert, B. L., Thomas, G. H., Pannu, H., Backer, J. F. A. D., Oswald, G. L., Symoens, S., Manouvrier‐Hanu, S., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa055695 · Cited by 1,650 · see citing works

Regulation of myostatin activity and muscle growth

Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616 · see citing works

Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer

Siegel, P. M., & Massagué, J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1208 · Cited by 1,600 · see citing works

Transforming growth factor-beta in human platelets. Identification of a major storage site, purification, and characterization.

Assoian, R. K., Komoriya, A., Meyers, C. A., Miller, D. M., & Sporn, M. B. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32345-7 · Cited by 1,597 · see citing works

Production of transforming growth factor beta by human T lymphocytes and its potential role in the regulation of T cell growth.

Kehrl, J. H., Wakefield, L. M., Roberts, A. B., Jakowlew, S. B., Álvarez‐Mon, M., Derynck, R., Sporn, M. B., & Fauci, A. S. (1986) · The Journal of Experimental Medicine · doi:10.1084/jem.163.5.1037 · Cited by 1,581 · see citing works

A deletion in the bovine myostatin gene causes the double–muscled phenotype in cattle

Grobet, L., Royo Martin, L. J., Poncelet, D., Pirottin, D., Brouwers, B., Riquet, J., Schoeberlein, A., Dunner, S., Ménissier, F., Massabanda, J., et al. (1997) · Nature Genetics · doi:10.1038/ng0997-71 · Cited by 1,556 · see citing works

TGFβ2 knockout mice have multiple developmental defects that are non-overlapping with other TGFβ knockout phenotypes

Sanford, L. P., Ormsby, I., Groot, A. C. G.-D., Sariola, H., Friedman, R., Boivin, G. P., Cardell, E. L., & Doetschman, T. (1997) · Development · doi:10.1242/dev.124.13.2659 · Cited by 1,447 · see citing works

Lessons from the Cancer Genome

Garraway, L. A., & Lander, E. S. (2013) · Cell · doi:10.1016/j.cell.2013.03.002 · Cited by 1,322 · see citing works

Dysregulation of TGF-β activation contributes to pathogenesis in Marfan syndrome

Neptune, E., Frischmeyer, P., Arking, D., Myers, L., Bunton, T., Gayraud, B., Ramirez, F., Sakai, L., & Dietz, H. (2003) · Nature Genetics · doi:10.1038/ng1116 · Cited by 1,301 · see citing works

Transforming growth factor type beta induces monocyte chemotaxis and growth factor production.

Wahl, S. M., Hunt, D. A., Wakefield, L. M., McCartney-Francis, N. L., Wahl, L. M., Roberts, A. B., & Sporn, M. B. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.16.5788 · Cited by 1,273 · see citing works

TGFβ: the molecular Jekyll and Hyde of cancer

Bierie, B., & Moses, H. L. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1926 · Cited by 1,262 · see citing works

Alveolar epithelial cell mesenchymal transition develops <i>in vivo</i> during pulmonary fibrosis and is regulated by the extracellular matrix

Kim, K. K., Kugler, M. C., Wolters, P. J., Robillard, L., Galvez, M. G., Brumwell, A. N., Sheppard, D., & Chapman, H. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605669103 · Cited by 1,257 · see citing works

SMAD proteins control DROSHA-mediated microRNA maturation

Davis‐Dusenbery, B. N., Hilyard, A. C., Lagna, G., & Hata, A. (2008) · Nature · doi:10.1038/nature07086 · Cited by 1,243 · see citing works

Transforming growth factor beta modulates the expression of collagenase and metalloproteinase inhibitor.

Edwards, D. R., Murphy, G., Reynolds, J. J., Whitham, S. E., Docherty, A. J., Angel, P., & Heath, J. K. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02449.x · Cited by 1,221 · see citing works

Mutations in <i>myostatin</i> ( <i>GDF8</i> ) in Double-Muscled Belgian Blue and Piedmontese Cattle

Kambadur, R., Sharma, M., Smith, T. P. L., & Bass, J. J. (1997) · Genome Research · doi:10.1101/gr.7.9.910 · Cited by 1,204 · see citing works

Expression cloning of noggin, a new dorsalizing factor localized to the Spemann organizer in Xenopus embryos

Smith, W. C., & Harland, R. M. (1992) · Cell · doi:10.1016/0092-8674(92)90316-5 · Cited by 1,184 · see citing works

TGFβ signalling: a complex web in cancer progression

Ikushima, H., & Miyazono, K. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2853 · Cited by 1,170 · see citing works

Neutralisation of TGF-β1 and TGF-β2 or exogenous addition of TGF-β3 to cutaneous rat wounds reduces scarring

Shah, M., Foreman, D. M., & Ferguson, M. W. J. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.3.985 · Cited by 1,168 · see citing works

TGF-β1–induced migration of bone mesenchymal stem cells couples bone resorption with formation

Tang, Y., Wu, X., Lei, W., Pang, L., Wan, C., Shi, Z., Zhao, L., Nagy, T. R., Peng, X., Hu, J., et al. (2009) · Nature Medicine · doi:10.1038/nm.1979 · Cited by 1,165 · see citing works

Balancing the activation state of the endothelium via two distinct TGF‐β type I receptors

Goumans, M., Valdimarsdóttir, G., Itoh, S., Rosendahl, A., Sideras, P., & ten Dijke, P. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1743 · Cited by 1,127 · see citing works

Type beta transforming growth factor: a bifunctional regulator of cellular growth.

Roberts, A. B., Anzano, M. A., Wakefield, L. M., Roche, N. S., Stern, D. F., & Sporn, M. B. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.1.119 · Cited by 1,093 · see citing works

Adenovector-mediated gene transfer of active transforming growth factor-beta1 induces prolonged severe fibrosis in rat lung.

Sime, P. J., Xing, Z., Graham, F. L., Csaky, K. G., & Gauldie, J. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119590 · Cited by 1,050 · see citing works

Derivation of novel human ground state naive pluripotent stem cells

Gafni, O., Weinberger, L., Mansour, A. A., Manor, Y. S., Chomsky, E., Ben‐Yosef, D., Kalma, Y., Viukov, S. V., Maza, I., Zviran, A., et al. (2013) · Nature · doi:10.1038/nature12745 · Cited by 1,047 · see citing works

Abnormal lung development and cleft palate in mice lacking TGF–β3 indicates defects of epithelial–mesenchymal interaction

Kaartinen, V., Voncken, J. W., Shuler, C. F., Warburton, D., Bu, D., Heisterkamp, N., & Groffen, J. (1995) · Nature Genetics · doi:10.1038/ng1295-415 · Cited by 1,031 · see citing works

Latent TGF-β structure and activation

Shi, M., Zhu, J., Wang, R., Chen, X., Mi, L., Walz, T., & Springer, T. A. (2011) · Nature · doi:10.1038/nature10152 · Cited by 1,013 · see citing works

Suppression of experimental glomerulonephritis by antiserum against transforming growth factor β1

Border, W. A., Okuda, S., Languino, L. R., Sporn, M. B., & Ruoslahti, E. I. (1990) · Nature · doi:10.1038/346371a0 · Cited by 984 · see citing works

Activin/Nodal and FGF pathways cooperate to maintain pluripotency of human embryonic stem cells

Vallier, L., Alexander, M., & Pedersen, R. A. (2005) · Journal of Cell Science · doi:10.1242/jcs.02553 · Cited by 948 · see citing works

Growth Differentiation Factor 11 Is a Circulating Factor that Reverses Age-Related Cardiac Hypertrophy

Loffredo, F. S., Steinhauser, M. L., Jay, S. M., Gannon, J., Pancoast, J. R., Yalamanchi, P., Sinha, M., Dall’Osso, C., Khong, D., Shadrach, J. L., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.015 · Cited by 948 · see citing works

Transforming growth factor beta induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism.

Datto, M., Li, Y., Panus, J. F., Howe, D. J., Xiong, Y., & Wang, X. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5545 · Cited by 945 · see citing works

Reversal of Cancer Cachexia and Muscle Wasting by ActRIIB Antagonism Leads to Prolonged Survival

Zhou, X., Wang, J. L., Lu, J., Song, Y., Kwak, K. S., Jiao, Q., Rosenfeld, R., Chen, Q., Boone, T. C., Simonet, W. S., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.011 · Cited by 941 · see citing works

The polarization of immune cells in the tumour environment by TGFβ

Flavell, R. A., Sanjabi, S., Wrzesinski, S. H., & Licona-Limón, P. (2010) · Nature Reviews Immunology · doi:10.1038/nri2808 · Cited by 940 · see citing works

Accelerated Healing of Incisional Wounds in Rats Induced by Transforming Growth Factor-β

Mustoe, T. A., Pierce, G. F., Thomason, A., Gramates, P. H., Sporn, M. B., & Deuel, T. F. (1987) · Science · doi:10.1126/science.2442813 · Cited by 930 · see citing works

New class of transforming growth factors potentiated by epidermal growth factor: isolation from non-neoplastic tissues.

Roberts, A. B., Anzano, M. A., Lamb, L. C., Smith, J. M., & Sporn, M. B. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.9.5339 · Cited by 919 · see citing works

The roles of TGFβ in the tumour microenvironment

Pickup, M. W., Novitskiy, S. V., & Moses, H. L. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3603 · Cited by 915 · see citing works

Mice lacking Smad3 show accelerated wound healing and an impaired local inflammatory response

Ashcroft, G. S., Yang, X., Glick, A. B., Weinstein, M., Letterio, J. J., Mizel, D. E., Anzano, M., Greenwell-Wild, T., Wahl, S. M., Deng, C., et al. (1999) · Nature Cell Biology · doi:10.1038/12971 · Cited by 911 · see citing works

Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways

Lagna, G., Hata, A., Hemmati‐Brivanlou, A., & Massagué, J. (1996) · Nature · doi:10.1038/383832a0 · Cited by 905 · see citing works

TGFβ/activin/nodal signaling is necessary for the maintenance of pluripotency in human embryonic stem cells

James, D., Levine, A. J., Besser, D., & Hemmati‐Brivanlou, A. (2005) · Development · doi:10.1242/dev.01706 · Cited by 896 · see citing works

Systematic Identification of Culture Conditions for Induction and Maintenance of Naive Human Pluripotency

Theunissen, T. W., Powell, B. E., Wang, H., Mitalipova, M., Faddah, D. A., Reddy, J., Fan, Z. P., Maetzel, D., Ganz, K., Shi, L., et al. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.07.002 · Cited by 888 · see citing works

TGF-β: A Master of All T Cell Trades

Li, M. O., & Flavell, R. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.025 · Cited by 888 · see citing works

Receptor-associated Mad homologues synergize as effectors of the TGF-β response

Zhang, Y. E., Feng, X., Wu, R.-Y., & Derynck, R. (1996) · Nature · doi:10.1038/383168a0 · Cited by 873 · see citing works

Synergistic induction of mesoderm by FGF and TGF-β and the identification of an mRNA coding for FGF in the early xenopus embryo

Kimelman, D., & Kirschner, M. W. (1987) · Cell · doi:10.1016/0092-8674(87)90110-3 · Cited by 872 · see citing works

Targeted disruption of TGF-β1/Smad3 signaling protects against renal tubulointerstitial fibrosis induced by unilateral ureteral obstruction

Sato, M., Muragaki, Y., Saika, S., Roberts, A. B., & Ooshima, A. (2003) · Journal of Clinical Investigation · doi:10.1172/jci19270 · Cited by 831 · see citing works

Restoring systemic GDF11 levels reverses age-related dysfunction in mouse skeletal muscle

Sinha, M., Jang, Y. C., Oh, J., Khong, D., Wu, E. Y., Manohar, R., Miller, C., Regalado, S. G., Loffredo, F. S., Pancoast, J. R., et al. (2014) · Science · doi:10.1126/science.1251152 · Cited by 824 · see citing works

TGF-β signaling and epithelial–mesenchymal transition in cancer progression

Katsuno, Y., Lamouille, S., & Derynck, R. (2012) · Current Opinion in Oncology · doi:10.1097/cco.0b013e32835b6371 · Cited by 785 · see citing works

Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta.

Postlethwaite, A. E., Keski-Oja, J., Moses, H. L., & Kang, A. H. (1987) · The Journal of experimental medicine · doi:10.1084/jem.165.1.251 · Cited by 777 · see citing works

BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism

Andriopoulos Jr, B., Corradini, E., Xia, Y., Faasse, S. A., Chen, S., Grgurevic, L., Knutson, M. D., Pietrangelo, A., Vukicevic, S., Lin, H. Y., et al. (2009) · Nature Genetics · doi:10.1038/ng.335 · Cited by 769 · see citing works

Growth Inhibitor from BSC-1 Cells Closely Related to Platelet Type β Transforming Growth Factor

Tucker, R. F., Shipley, G. D., Moses, H. L., & Holley, R. W. (1984) · Science · doi:10.1126/science.6093254 · Cited by 768 · see citing works

Follistatin, an antagonist of activin, is expressed in the Spemann organizer and displays direct neuralizing activity

Hemmati‐Brivanlou, A., Kelly, O., & Melton, D. A. (1994) · Cell · doi:10.1016/0092-8674(94)90320-4 · Cited by 761 · see citing works

Expression cloning of an activin receptor, a predicted transmembrane serine kinase

Mathews, L. S., & Vale, W. (1991) · Cell · doi:10.1016/0092-8674(91)90549-e · Cited by 753 · see citing works

Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells

David, L., Mallet, C., Mazerbourg, S., Feige, J., & Bailly, S. (2006) · Blood · doi:10.1182/blood-2006-07-034124 · Cited by 708 · see citing works

Müllerian-inhibiting substance function during mammalian sexual development.

Behringer, R., Finegold, M., & Cate, R. (1994) · Cell · doi:10.1016/0092-8674(94)90251-8 · Cited by 706 · see citing works

Mutations in SMAD3 cause a syndromic form of aortic aneurysms and dissections with early-onset osteoarthritis

van de Laar, I. M. B. H., Oldenburg, R. A., Pals, G., Roos‐Hesselink, J. W., de Graaf, B. M., Verhagen, J. M. A., Hoedemaekers, Y. M., Willemsen, R., Severijnen, L.-A. W. F. M., Venselaar, H., et al. (2011) · Nature Genetics · doi:10.1038/ng.744 · Cited by 691 · see citing works

Targeted disruption of TGF-β1/Smad3 signaling protects against renal tubulointerstitial fibrosis induced by unilateral ureteral obstruction

Sato, M., Muragaki, Y., Saika, S., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319270 · Cited by 686 · see citing works

Genetic characterization and cloning of mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster.

Sekelsky, J. J., Newfeld, S. J., Raftery, L. A., Chartoff, E. H., & Gelbart, W. M. (1995) · Genetics · doi:10.1093/genetics/139.3.1347 · Cited by 659 · see citing works

Heterozygous TGFBR2 mutations in Marfan syndrome

Mizuguchi, T., Collod‐Béroud, G., Akiyama, T., Abifadel, M., Harada, N., Morisaki, T., Allard, D., Varret, M., Claustres, M., Morisaki, H., et al. (2004) · Nature Genetics · doi:10.1038/ng1392 · Cited by 627 · see citing works

A vitamin D receptor/SMAD genomic circuit gates hepatic fibrotic response

Ding, N., Yu, R. T., Subramaniam, N., Sherman, M. H., Wilson, C., Rao, R., Leblanc, M., Coulter, S., He, M., Scott, C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.03.028 · Cited by 622 · see citing works

Transforming Growth Factor-β Function Blocking Prevents Myocardial Fibrosis and Diastolic Dysfunction in Pressure-Overloaded Rats

Kuwahara, F., Kai, H., Tokuda, K., Kai, M., Takeshita, A., Egashira, K., & Imaizumi, T. (2002) · Circulation · doi:10.1161/01.cir.0000020689.12472.e0 · Cited by 608 · see citing works

TGF-β1 inhibition of c-myc transcription and growth in keratinocytes is abrogated by viral transforming proteins with pRB binding domains

Pietenpol, J. A., Stein, R. W., Morán, E., Yaciuk, P., Schlegel, R., Lyons, R. M., Pittelkow, M. R., Münger, K., Howley, P. M., & Moses, H. L. (1990) · Cell · doi:10.1016/0092-8674(90)90188-k · Cited by 596 · see citing works

Lack of the bone morphogenetic protein BMP6 induces massive iron overload

Meynard, D., Kautz, L., Darnaud, V., Canonne-Hergaux, F., Coppin, H., & Roth, M.-P. (2009) · Nature Genetics · doi:10.1038/ng.320 · Cited by 587 · see citing works

TGF-β–FOXO signalling maintains leukaemia-initiating cells in chronic myeloid leukaemia

Naka, K., Hoshii, T., Muraguchi, T., Tadokoro, Y., Ooshio, T., Kondo, Y., Nakao, S., Motoyama, N., & Hirao, A. (2010) · Nature · doi:10.1038/nature08734 · Cited by 583 · see citing works

PDGF, TGF-β, and FGF signaling is important for differentiation and growth of mesenchymal stem cells (MSCs): transcriptional profiling can identify markers and signaling pathways important in differentiation of MSCs into adipogenic, chondrogenic, and osteogenic lineages

Ng, F., Boucher, S., Koh, S., Sastry, K. S. R., Chase, L., Lakshmipathy, U., Choong, C., Yang, Z., Vemuri, M. C., Rao, M. S., et al. (2008) · Blood · doi:10.1182/blood-2007-07-103697 · Cited by 580 · see citing works

TGF-β Receptor Inhibitors Target the CD44high/Id1high Glioma-Initiating Cell Population in Human Glioblastoma

Anido, J., Sáez‐Borderías, A., Gonzàlez-Juncà, A., Rodón, L., Folch, G., Carmona, M. A., Prieto-Sánchez, R. M., Barba, I., Martínez-Sáez, E. A., Prudkin, L., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.023 · Cited by 571 · see citing works

Master Transcription Factors Determine Cell-Type-Specific Responses to TGF-β Signaling

Mullen, A. C., Orlando, D. A., Newman, J. J., Lovén, J., Kumar, R., Bilodeau, S., Reddy, J., Guenther, M. G., DeKoter, R. P., & Young, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.08.050 · Cited by 563 · see citing works

Reversible inhibition of normal human prokeratinocyte proliferation by type beta transforming growth factor-growth inhibitor in serum-free medium.

Shipley, G. D., Pittelkow, M. R., Wille, J. J., Scott, R. E., & Moses, H. L. (1986) · PubMed · Cited by 553 · see citing works

Type beta transforming growth factor is an inhibitor of myogenic differentiation.

Massagué, J., Cheifetz, S., Endo, T., & Nadal‐Ginard, B. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8206 · Cited by 550 · see citing works

Latent Transforming Growth Factor β-binding Protein 1 Interacts with Fibrillin and Is a Microfibril-associated Protein

Isogai, Z., Ono, R. N., Ushiro, S., Keene, D. R., Chen, Y., Mazzieri, R., Charbonneau, N. L., Reinhardt, D. P., Rifkin, D. B., & Sakai, L. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209256200 · Cited by 548 · see citing works

A Self-Enabling TGFβ Response Coupled to Stress Signaling

Kang, Y., Chen, C.-R., & Massagué, J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00109-6 · Cited by 548 · see citing works

A critical function for TGF-β signaling in the development of natural CD4+CD25+Foxp3+ regulatory T cells

Liu, Y., Zhang, P., Li, J., Kulkarni, A. B., Perruche, S., & Chen, W. (2008) · Nature Immunology · doi:10.1038/ni.1607 · Cited by 545 · see citing works

Autocrine TGF-β Signaling Maintains Tumorigenicity of Glioma-Initiating Cells through Sry-Related HMG-Box Factors

Ikushima, H., Todo, T., Ino, Y., Takahashi, M., Miyazawa, K., & Miyazono, K. (2009) · Cell stem cell · doi:10.1016/j.stem.2009.08.018 · Cited by 540 · see citing works

Induction of c-sis mRNA and activity similar to platelet-derived growth factor by transforming growth factor beta: a proposed model for indirect mitogenesis involving autocrine activity.

Leof, E. B., Proper, J. A., Goustin, A. S., Shipley, G. D., DiCorleto, P. E., & Moses, H. L. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.8.2453 · Cited by 529 · see citing works

GDF11 increases with age and inhibits skeletal muscle regeneration

Egerman, M. A., Cadena, S. M., Gilbert, J. A., Meyer, A., Nelson, H. N., Swalley, S. E., Mallozzi, C., Jacobi, C., Jennings, L. L., Clay, I., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.010 · Cited by 527 · see citing works

TGF-β Increases Glioma-Initiating Cell Self-Renewal through the Induction of LIF in Human Glioblastoma

Peñuelas, S., Anido, J., Prieto-Sánchez, R. M., Folch, G., Barba, I., Cuartas, I., David Garcia-dorado, A., Poca, M. A., Sahuquillo, J., Baselga, J. M., et al. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.02.011 · Cited by 527 · see citing works

Caenorhabditis elegans genes sma-2, sma-3, and sma-4 define a conserved family of transforming growth factor beta pathway components.

Savage‐Dunn, C., Das, P. K., Finelli, A., Townsend, S. R., Sun, C. Y., Baird, S. E., & Padgett, R. W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.2.790 · Cited by 522 · see citing works

Activin A Maintains Pluripotency of Human Embryonic Stem Cells in the Absence of Feeder Layers

Beattie, G. M., Lopez, A. D., Bucay, N., Hinton, A. C., Firpo, M. T., King, C. C., & Hayek, A. (2005) · Stem Cells · doi:10.1634/stemcells.2004-0279 · Cited by 503 · see citing works

Integrin αVβ6-mediated activation of latent TGF-β requires the latent TGF-β binding protein-1

Annes, J. P., Chen, Y., Munger, J. S., & Rifkin, D. B. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200312172 · Cited by 500 · see citing works

Purification and characterization of two cartilage-inducing factors from bovine demineralized bone.

Seyedin, S. M., Thomas, T. C., Thompson, A. Y., Rosen, D. M., & Piez, K. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.8.2267 · Cited by 498 · see citing works

The basics of epithelial-mesenchymal transition

Kalluri, R. K., & Weinberg, R. A. (2010) · Journal of Clinical Investigation · doi:10.1172/jci39104c1 · Cited by 483 · see citing works

Loss-of-function mutations in TGFB2 cause a syndromic presentation of thoracic aortic aneurysm

Lindsay, M. E., Schepers, D., Bolar, N. A., Doyle, J. J., Gallo, E. M., Fert‐Bober, J., Kempers, M. J. E., Fishman, E. K., Chen, Y., Myers, L. A., et al. (2012) · Nature Genetics · doi:10.1038/ng.2349 · Cited by 482 · see citing works

Evidence for a critical contribution of haploinsufficiency in the complex pathogenesis of Marfan syndrome

Judge, D. P., Biery, N. J., Keene, D. R., Geubtner, J., Myers, L. A., Huso, D. L., Sakai, L. Y., & Dietz, H. C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20641 · Cited by 476 · see citing works

High TGFβ-Smad Activity Confers Poor Prognosis in Glioma Patients and Promotes Cell Proliferation Depending on the Methylation of the PDGF-B Gene

Bruna, A., Darken, R. S., Rojo, F., Ocaña, A., Peñuelas, S., Arias, A., Parı́s, R., Tortosa, A., Mora, J., Baselga, J. M., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.11.023 · Cited by 472 · see citing works

Lessons on the pathogenesis of aneurysm from heritable conditions

Lindsay, M. E., & Dietz, H. C. (2011) · Nature · doi:10.1038/nature10145 · Cited by 471 · see citing works

BMP signaling controls muscle mass

Sartori, R., Schirwis, E., Blaauw, B., Bortolanza, S., Zhao, J., Enzo, E., Stantzou, A., Mouisel, E., Toniolo, L., Ferry, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2772 · Cited by 467 · see citing works

Activation of latent myostatin by the BMP-1/tolloid family of metalloproteinases

Wolfman, N. M., McPherron, A. C., Pappano, W. N., Davies, M. V., Song, K., Tomkinson, K. N., Wright, J. F., Zhao, L., Sebald, S. M., Greenspan, D. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2534946100 · Cited by 454 · see citing works

Mesoderm Induction in Amphibians: the Role of TGF-β2-Like Factors

Rosa, F., Roberts, A. B., Danielpour, D., Dart, L. L., Sporn, M. B., & Dawid, I. B. (1988) · Science · doi:10.1126/science.3422517 · Cited by 449 · see citing works

Transforming growth factors: isolation of polypeptides from virally and chemically transformed cells by acid/ethanol extraction.

Roberts, A. B., Lamb, L. C., Newton, D., Sporn, M. B., Larco, J. E. D., & Todaro, G. J. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.6.3494 · Cited by 448 · see citing works

Latent transforming growth factor-beta 1 associates to fibroblast extracellular matrix via latent TGF-beta binding protein

Taipale, J., Miyazono, K., Ch, H., & Keski‐Oja, J. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.1.171 · Cited by 445 · see citing works

Polypeptide Transforming Growth Factors Isolated from Bovine Sources and Used for Wound Healing in Vivo

Sporn, M. B., Roberts, A. B., Shull, J. H., Smith, J. M., Ward, J. M., & Sodek, J. (1983) · Science · doi:10.1126/science.6572416 · Cited by 442 · see citing works

Synexpression groups in eukaryotes

Niehrs, C., & Pollet, N. (1999) · Nature · doi:10.1038/990025 · Cited by 440 · see citing works

Crystal Structure of Transforming Growth Factor-β2: an Unusual Fold for the Superfamily

Daopin, S., Piez, K. A., Ogawa, Y., & Davies, D. R. (1992) · Science · doi:10.1126/science.1631557 · Cited by 440 · see citing works

Functional Analysis of the Transforming Growth Factor βResponsive Elements in the WAF1/Cip1/p21 Promoter

Datto, M., Yu, Y., & Wang, X. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.48.28623 · Cited by 429 · see citing works

Type beta transforming growth factor reversibly inhibits the early proliferative response to partial hepatectomy in the rat.

Russell, W. E., Coffey, R. J., Ouellette, A. J., & Moses, H. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.14.5126 · Cited by 427 · see citing works

Smad3 deficiency attenuates bleomycin-induced pulmonary fibrosis in mice

Zhao, J., Shi, W., Wang, Y., Chen, H., Bringas, P., Datto, M., Frederick, J. P., Wang, X., & Warburton, D. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00151.2001 · Cited by 411 · see citing works

Nodal/Activin Signaling Drives Self-Renewal and Tumorigenicity of Pancreatic Cancer Stem Cells and Provides a Target for Combined Drug Therapy

Lonardo, E., Hermann, P. C., Mueller, M.-T., Huber, S. L., Balic, A., Miranda‐Lorenzo, I., Zagorac, S., Alcalá, S., Rodríguez-Arabaolaza, I., Ramírez, J. C., et al. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.10.001 · Cited by 407 · see citing works

Transient gene transfer and expression of Smad7 prevents bleomycin-induced lung fibrosis in mice

Nakao, A., Fujii, M., Matsumura, R., Kumano, K., Saitō, Y., Miyazono, K., & Iwamoto, I. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6094 · Cited by 405 · see citing works

Purification and characterization of Erythroid Differentiation Factor(EDF) isolated from human leukemia cell line THP-1

Eto, Y., Tsuji, T., Takezawa, M., Takano, S., Yokogawa, Y., & Shibai, H. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)91528-2 · Cited by 405 · see citing works

Signaling by members of the TGF-β family in vascular morphogenesis and disease

Pardali, E., Goumans, M., & ten Dijke, P. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.06.006 · Cited by 402 · see citing works

Requirement of Bmpr1a for Müllerian duct regression during male sexual development

Jamin, S. P., Arango, N. A., Mishina, Y. M., Hanks, M. C., & Behringer, R. R. (2002) · Nature Genetics · doi:10.1038/ng1003 · Cited by 399 · see citing works

A new type of transforming growth factor‐beta, TGF‐beta 3.

Derynck, R., Lindquist, P. B., Lee, A. L., Wen, D., Tamm, J. A., Graycar, J. L., Rhee, L. M., Mason, A. J., Miller, D. A., & Coffey, R. J. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03257.x · Cited by 395 · see citing works

Reversible Inhibition of Mammary Gland Growth by Transforming Growth Factor-β

Silberstein, G. B., & Daniel, C. W. (1987) · Science · doi:10.1126/science.3474783 · Cited by 393 · see citing works

Two forms of transforming growth factor-β distinguished by multipotential haematopoietic progenitor cells

Ohta, M., Greenberger, J. S., Anklesaria, P. N., Bassols, A., & Massagué, J. (1987) · Nature · doi:10.1038/329539a0 · Cited by 392 · see citing works

TGF-β switches from tumor suppressor to prometastatic factor in a model of breast cancer progression

Tang, B., Vu, M. A., Booker, T., Santner, S. J., Miller, F. R., Anver, M. R., & Wakefield, L. M. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18899 · Cited by 391 · see citing works

Complementary DNA for human glioblastoma‐derived T cell suppressor factor, a novel member of the transforming growth factor‐beta gene family.

de Martin, R., Haendler, B., Hofer-Warbinek, R., Gaugitsch, H. W., Wrann, M., Schlüsener, H., SEIFERT, J. ‐., Bodmer, S., Fontana, A., & Hofer, E. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02700.x · Cited by 384 · see citing works

TGFB2 mutations cause familial thoracic aortic aneurysms and dissections associated with mild systemic features of Marfan syndrome

National Heart, L., Boileau, C., Guo, D.-C., Hanna, N., Regalado, E. S., Detaint, D., Gong, L., Varret, M., Prakash, S. K., Li, A. H., et al. (2012) · Nature Genetics · doi:10.1038/ng.2348 · Cited by 382 · see citing works

Repression of the CDK activator Cdc25A and cell-cycle arrest by cytokine TGF-β in cells lacking the CDK inhibitor p15

lavarone, A., & Massagué, J. (1997) · Nature · doi:10.1038/387417a0 · Cited by 375 · see citing works

Type beta transforming growth factor controls the adipogenic differentiation of 3T3 fibroblasts.

Ignotz, R. A., & Massagué, J. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.24.8530 · Cited by 363 · see citing works

Mesodermal induction in early amphibian embryos by activin A (erythroid differentiation factor)

Asashima, M., Nakano, H., Shimada, K., Kinoshita, K., Ishii, K., Shibai, H., & Ueno, N. (1990) · Development Genes and Evolution · doi:10.1007/bf00383771 · Cited by 358 · see citing works

Purification and properties of a type .beta. transforming growth factor from bovine kidney

Roberts, A. B., Anzano, M. A., Meyers, C. A., Wideman, J., Blacher, R. W., Pan, Y., Stein, S., Lehrman, S., & Smith, J. M. (1983) · Biochemistry · doi:10.1021/bi00294a002 · Cited by 352 · see citing works

Orphan nuclear receptor NR4A1 regulates transforming growth factor-β signaling and fibrosis

Palumbo‐Zerr, K., Zerr, P., Distler, A., Fliehr, J., Mancuso, R., Huang, J., Mielenz, D., Tomčík, M., Fürnrohr, B. G., Scholtysek, C., et al. (2015) · Nature Medicine · doi:10.1038/nm.3777 · Cited by 344 · see citing works

Endogenous TGF‐β signaling suppresses maturation of osteoblastic mesenchymal cells

Maeda, S., Hayashi, M., Komiya, S., Imamura, T., & Miyazono, K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600067 · Cited by 339 · see citing works

An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth fact or-β2

Schlunegger, M. P., & Grütter, M. G. (1992) · Nature · doi:10.1038/358430a0 · Cited by 336 · see citing works

Heterodimeric Bone Morphogenetic Proteins Show Enhanced ActivityIn VitroandIn Vivo

Israel, D. I., Nove, J., Kerns, K. M., Kaufman, R. J., Rosen, V., Cox, K. A., & Wozney, J. M. (1996) · Growth Factors · doi:10.3109/08977199609003229 · Cited by 335 · see citing works

TGF-β switches from tumor suppressor to prometastatic factor in a model of breast cancer progression

Tang, B., Vu, M. A., Booker, T., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318899 · Cited by 329 · see citing works

Molecular Basis of Bone Morphogenetic Protein-15 Signaling in Granulosa Cells

Moore, R. K., Otsuka, F., & Shimasaki, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207362200 · Cited by 326 · see citing works

Growth differentiation factor 9:bone morphogenetic protein 15 heterodimers are potent regulators of ovarian functions

Peng, J., Li, Q., Wigglesworth, K., Rangarajan, A., Kattamuri, C., Peterson, R. T., Eppig, J. J., Thompson, T. B., & Matzuk, M. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218020110 · Cited by 321 · see citing works

Absence of integrin-mediated TGFβ1 activation in vivo recapitulates the phenotype of TGFβ1-null mice

Yang, Z., Mu, Z., Dabovic, B., Jurukovski, V., Yu, D., Sung, J. J., Xiong, X., & Munger, J. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611044 · Cited by 321 · see citing works

Selective Inhibition of Growth-Related Gene Expression in Murine Keratinocytes by Transforming Growth Factor β

Coffey, R. J., Bascom, C. C., Sipes, N. J., Graves‐Deal, R., Weissman, B. E., & Moses, H. L. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.8.3088 · Cited by 320 · see citing works

In vivo inhibition of rat stellate cell activation by soluble transforming growth factor β type II receptor: A potential new therapy for hepatic fibrosis

George, J., Roulot, D. M., Koteliansky, V., & Bissell, D. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12719 · Cited by 320 · see citing works

Absence of TGF-β Receptors and Growth Inhibitory Responses in Retinoblastoma Cells

Kimchi, A., Wang, X., Weinberg, R. A., Cheifetz, S., & Massagué, J. (1988) · Science · doi:10.1126/science.2895499 · Cited by 319 · see citing works

Mutations in a TGF-β Ligand, TGFB3, Cause Syndromic Aortic Aneurysms and Dissections

Bertoli‐Avella, A. M., Gillis, E., Morisaki, H., Verhagen, J. M. A., de Graaf, B. M., van de Beek, G., Gallo, E. M., Kruithof, B. P. T., Venselaar, H., Myers, L. A., et al. (2015) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2015.01.040 · Cited by 305 · see citing works

Genetic screens to identify elements of the decapentaplegic signaling pathway in Drosophila.

Raftery, L. A., Twombly, V. J., Wharton, K. A., & Gelbart, W. M. (1995) · Genetics · doi:10.1093/genetics/139.1.241 · Cited by 303 · see citing works

Lineage Regulators Direct BMP and Wnt Pathways to Cell-Specific Programs during Differentiation and Regeneration

Trompouki, E., Bowman, T. V., Lawton, L. N., Fan, Z. P., Wu, D.-C., DiBiase, A., Martin, C., Cech, J. N., Sessa, A. K., LeBlanc, J., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.044 · Cited by 303 · see citing works

Smad3-dependent nuclear translocation of β-catenin is required for TGF-β1-induced proliferation of bone marrow-derived adult human mesenchymal stem cellsPreprint

Jian, H., Shen, X., Liu, I. M., Semënov, M. V., He, X., & Wang, X. (2006) · Genes & Development · doi:10.1101/gad.1388806 · Cited by 300 · see citing works

Crystal Structure of BMP-9 and Functional Interactions with Pro-region and Receptors

Brown, M. A., Zhao, Q., Baker, K. A., Naik, C., Chen, C., Pukac, L., Singh, M., Tsareva, T., Parice, Y., Mahoney, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503328200 · Cited by 300 · see citing works

Activin is a nerve cell survival molecule

Schubert, D. A., Kimura, H., LaCorbiere, M., et al. (1990) · Nature · doi:10.1038/344868a0 · Cited by 295 · see citing works

Prophylactic administration of avotermin for improvement of skin scarring: three double-blind, placebo-controlled, phase I/II studies

Ferguson, M. W. J., Duncan, J. A. L., Bond, J. S., Bush, J., Durani, P., So, K., Taylor, L., Chantrey, J., Mason, T., James, G., et al. (2009) · The Lancet · doi:10.1016/s0140-6736(09)60322-6 · Cited by 290 · see citing works

Smad proteins exist as monomers in vivo and undergo homo‐ and hetero‐oligomerization upon activation by serine/threonine kinase receptors

Kawabata, M., Inoue, H., Hanyu, A., Imamura, T., & Miyazono, K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.14.4056 · Cited by 289 · see citing works

Mice Lacking Smad3 Are Protected Against Cutaneous Injury Induced by Ionizing Radiation

Flanders, K. C., Sullivan, C. D., Fujii, M., Sowers, A. L., Anzano, M. A., Arabshahi, A., Major, C. D., Deng, C., Russo, A., Mitchell, J. B., et al. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64926-7 · Cited by 283 · see citing works

Emerging role of bone morphogenetic proteins in angiogenesis

David, L., Feige, J., & Bailly, S. (2009) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2009.05.001 · Cited by 281 · see citing works

TGF-β signaling in the control of hematopoietic stem cells

Blank, U., & Karlsson, S. (2015) · Blood · doi:10.1182/blood-2014-12-618090 · Cited by 277 · see citing works

Importance of FSH-releasing protein and inhibin in erythrodifferentiation

Yu, J. C. L., Shao, L., Lemas, V. M., et al. (1987) · Nature · doi:10.1038/330765a0 · Cited by 274 · see citing works

A Role for BMP Heterodimers in Roof Plate-Mediated Repulsion of Commissural Axons

Butler, S. J., & Dodd, J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00254-x · Cited by 274 · see citing works

C/EBPβ at the core of the TGFβ cytostatic response and its evasion in metastatic breast cancer cells

Gomis, R. R., Alarcón, C. R., Nadal, C., Poznak, C. H. V., & Massagué, J. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.07.019 · Cited by 270 · see citing works

Mutations in the TGF-β repressor SKI cause Shprintzen-Goldberg syndrome with aortic aneurysm

Doyle, A. J., Doyle, J. J., Bessling, S. L., Maragh, S., Lindsay, M. E., Schepers, D., Gillis, E., Mortier, G. R., Homfray, T., Sauls, K., et al. (2012) · Nature Genetics · doi:10.1038/ng.2421 · Cited by 265 · see citing works

Dual role for the latent transforming growth factor-beta binding protein in storage of latent TGF-beta in the extracellular matrix and as a structural matrix protein.

Dallas, S. L., Miyazono, K., Skerry, T. M., Mundy, G. R., & Bonewald, L. F. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.2.539 · Cited by 263 · see citing works

Potent Ectopic Bone-Inducing Activity of Bone Morphogenetic Protein-4/7 Heterodimer

Aono, A., Hazama, M., Notoya, K., Taketomi, S., Yamasaki, H., Tsukuda, R., Sasaki, S., & Fujisawa, Y. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1712 · Cited by 258 · see citing works

Growth Differentiation Factor-9 Signaling Is Mediated by the Type I Receptor, Activin Receptor-Like Kinase 5

Mazerbourg, S., Klein, C., Roh, J., et al. (2003) · Molecular Endocrinology · doi:10.1210/me.2003-0393 · Cited by 258 · see citing works

The hotei mutation of medaka in the anti-Müllerian hormone receptor causes the dysregulation of germ cell and sexual development

Morinaga, C., Saito, D., Nakamura, S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611379104 · Cited by 257 · see citing works

Matrix control of transforming growth factor- function

Horiguchi, M., Ota, M., & Rifkin, D. B. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs089 · Cited by 256 · see citing works

Domain-specific mutations in TGFB1 result in Camurati-Engelmann disease

Kinoshita, A., Saito, T., Tomita, H., Makita, Y., Yoshida, K., Ghadami, M., Yamada, K., Kondo, S., Ikegawa, S., Nishimura, G., et al. (2000) · Nature Genetics · doi:10.1038/79128 · Cited by 249 · see citing works

Transforming growth factor-beta. A very potent inhibitor of myoblast differentiation, identical to the differentiation inhibitor secreted by Buffalo rat liver cells.

Florini, J. R., Roberts, A. B., Ewton, D. Z., et al. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66595-0 · Cited by 248 · see citing works

Bone morphogenetic protein heterodimers assemble heteromeric type I receptor complexes to pattern the dorsoventral axis

Little, S. C., & Mullins, M. C. (2009) · Nature Cell Biology · doi:10.1038/ncb1870 · Cited by 247 · see citing works

Targeting of Bone Morphogenetic Protein Growth Factor Complexes to Fibrillin

Sengle, G., Charbonneau, N. L., Ono, R. N., Sasaki, T., Alvarez, J., Keene, D. R., Bächinger, H. P., & Sakai, L. Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707820200 · Cited by 245 · see citing works

A FoxO–Smad synexpression group in human keratinocytes

Gomis, R. R., Alarcón, C. R., He, W., Wang, Q., Seoane, J., Lash, A., & Massagué, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605333103 · Cited by 245 · see citing works

Transforming growth factor‐beta is a strong and fast acting positive regulator of the level of type‐1 plasminogen activator inhibitor mRNA in WI‐38 human lung fibroblasts.

Lund, L. R., Riccio, A., Andreasen, P. A., Nielsen, L. S., Kristensen, P., Laiho, M., Saksela, O., Blasi, F., & Danø, K. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02365.x · Cited by 243 · see citing works

Dysregulation of microRNA biogenesis and gene silencing in cancer

Hata, A., & Lieberman, J. (2015) · Science Signaling · doi:10.1126/scisignal.2005825 · Cited by 235 · see citing works

Rosiglitazone Abrogates Bleomycin-Induced Scleroderma and Blocks Profibrotic Responses Through Peroxisome Proliferator-Activated Receptor-γ

Wu, M., Melichian, D. S., Chang, E., Warner-Blankenship, M., Ghosh, A. K., & Varga, J. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080574 · Cited by 233 · see citing works

Direct evidence for spatial and temporal regulation of transforming growth factor β1 expression during cutaneous wound healing

Kane, C. J. M., Hebda, P. A., Mansbridge, J. N., & Hanawalt, P. C. (1991) · Journal of Cellular Physiology · doi:10.1002/jcp.1041480119 · Cited by 226 · see citing works

Insensitivity to anti–Müllerian hormone due to a mutation in the human anti–Müllerian hormone receptor

Imbeaud, S., Faure, E., Lamarre, I., Mattéi, M., di Clemente, N., Tizard, R., Carre, D. S., Belville, C., Tragethon, L., Tonkin, C., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-382 · Cited by 226 · see citing works

TGF‐β regulates isoform switching of FGF receptors and epithelial–mesenchymal transition

Shirakihara, T., Horiguchi, K., Miyazawa, K., Ehata, S., Shibata, T., Morita, I., Miyazono, K., & Saitoh, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.351 · Cited by 225 · see citing works

ChIP-seq reveals cell type-specific binding patterns of BMP-specific Smads and a novel binding motif

Morikawa, M., Koinuma, D., Tsutsumi, S., Vasilaki, E., Kanki, Y., Heldin, C., Aburatani, H., & Miyazono, K. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr572 · Cited by 219 · see citing works

Crosstalk between TGF-β signaling and the microRNA machinery

Butz, H., Rácz, K., Hunyady, L., & Patócs, A. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.04.003 · Cited by 215 · see citing works

Mutations in the gene encoding the latency-associated peptide of TGF-β1 cause Camurati-Engelmann disease

Janssens, K., Gershoni‐Baruch, R., Guañabens, N., Migone, N., Ralston, S. H., Bonduelle, M., Lissens, W., Maldergem, L. V., Vanhoenacker, F. M. H. M., Verbruggen, L., et al. (2000) · Nature Genetics · doi:10.1038/81563 · Cited by 210 · see citing works

GDF3, a BMP inhibitor, regulates cell fate in stem cells and early embryos

Levine, A. J., & Brivanlou, A. H. (2005) · Development · doi:10.1242/dev.02192 · Cited by 203 · see citing works

Chromatin Immunoprecipitation on Microarray Analysis of Smad2/3 Binding Sites Reveals Roles of ETS1 and TFAP2A in Transforming Growth Factor β Signaling

Koinuma, D., Tsutsumi, S., Kamimura, N., Taniguchi, H., Miyazawa, K., Sunamura, M., Imamura, T., Miyazono, K., & Aburatani, H. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01038-08 · Cited by 198 · see citing works

Two Modes by which Lefty Proteins Inhibit Nodal Signaling

Chen, C., & Shen, M. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.02.042 · Cited by 197 · see citing works

Activin type IIA and IIB receptors mediate Gdf11 signaling in axial vertebral patterningPreprint

Oh, S. P., Yeo, C., Lee, Y. J., Schrewe, H., Whitman, M., & Li, E. (2002) · Genes & Development · doi:10.1101/gad.1021802 · Cited by 196 · see citing works

Evidence that fibroblasts derive from epithelium during tissue fibrosis

Iwano, M., Plieth, D., Danoff, T. M., Xue, C., Okada, H., & Neilson, E. G. (2002) · Journal of Clinical Investigation · doi:10.1172/jci200215518 · Cited by 196 · see citing works

The Harmonies Played by TGF-β in Stem Cell Biology

Oshimori, N., & Fuchs, E. V. (2012) · Cell stem cell · doi:10.1016/j.stem.2012.11.001 · Cited by 189 · see citing works

TGF-beta 1 is an autocrine-negative growth regulator of human colon carcinoma FET cells in vivo as revealed by transfection of an antisense expression vector.

Wu, S. P., Theodorescu, D., Kerbel, R. S., Willson, J. K. V., Mulder, K. M., Humphrey, L. E., & Brattain, M. G. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.116.1.187 · Cited by 180 · see citing works

Activin-Nodal signaling is involved in propagation of mouse embryonic stem cells

Ogawa, K., Saito, A., Matsui, H., Suzuki, H. I., Ohtsuka, S., Shimosato, D., Morishita, Y., Watabe, T., Niwa, H., & Miyazono, K. (2006) · Journal of Cell Science · doi:10.1242/jcs.03296 · Cited by 174 · see citing works

TGF-β family signaling in stem cells

Sakaki‐Yumoto, M., Katsuno, Y., & Derynck, R. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.08.008 · Cited by 158 · see citing works

GDF11 Forms a Bone Morphogenetic Protein 1-Activated Latent Complex That Can Modulate Nerve Growth Factor-Induced Differentiation of PC12 Cells

Ge, G., Hopkins, D. R., Ho, W., & Greenspan, D. S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.5846-5858.2005 · Cited by 158 · see citing works

Mesoderm Induction by BMP-4 and -7 Heterodimers

Suzuki, A., Kaneko, E., Maeda, J., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6219 · Cited by 156 · see citing works

The Vg1 - related protein Gdf3 acts in a Nodal signaling pathway in the pre-gastrulation mouse embryo

Chen, C., Ware, S. M., Sato, A., Houston-Hawkins, D. E., Habas, R., Matzuk, M. M., Shen, M. M., & Brown, C. (2005) · Development · doi:10.1242/dev.02210 · Cited by 149 · see citing works

TGF-β signaling to chromatin: How Smads regulate transcription during self-renewal and differentiation

Gaarenstroom, T., & Hill, C. S. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.01.009 · Cited by 146 · see citing works

SB-431542 and Gleevec inhibit transforming growth factor-beta-induced proliferation of human osteosarcoma cells.

Matsuyama, S., Iwadate, M., Kondo, M., Saitoh, M., Hanyu, A., Shimizu, K., Aburatani, H., Mishima, H. K., Imamura, T., Miyazono, K., et al. (2003) · PubMed · Cited by 142 · see citing works

More than being protective: functional roles for TGF-β/activin signaling pathways at central synapses

KRIEGLSTEIN, K. G., Zheng, F., Unsicker, K., & Alzheimer, C. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.06.002 · Cited by 136 · see citing works

Genome-wide mechanisms of Smad binding

Morikawa, M., Koinuma, D., Miyazono, K., & Ch, H. (2012) · Oncogene · doi:10.1038/onc.2012.191 · Cited by 131 · see citing works

Resistance of keratinocytes to TGFβ-mediated growth restriction and apoptosis induction accelerates re-epithelialization in skin wounds

Amendt, C., Mann, A., Schirmacher, P., & Blessing, M. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.10.2189 · Cited by 128 · see citing works

TGFβ attenuates tumour response to PD-L1 blockade by contributing to exclusion of T cells

Mariathasan, S., Turley, S. J., Nickles, D., Castiglioni, A., Yuen, K., Wang, Y., Kadel III, E. E., Koeppen, H., Astarita, J. L., Cubas, R., et al. (2018) · Nature · doi:10.1038/nature25501 · Cited by 5,400 · see citing works

Specificity, versatility, and control of TGF-β family signaling

Derynck, R., & Budi, E. H. (2019) · Science Signaling · doi:10.1126/scisignal.aav5183 · Cited by 785 · see citing works

Zinc in Wound Healing Modulation

Lin, P.-H., Sermersheim, M., Li, H., Lee, P. H. U., Steinberg, S. M., & Ma, J. (2017) · Nutrients · doi:10.3390/nu10010016 · Cited by 643 · see citing works

TGF-β Signaling in Cellular Senescence and Aging-Related Pathology

Tominaga, K., & Suzuki, H. I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205002 · Cited by 393 · see citing works

TGF-β Signaling in Control of Cardiovascular Function

Goumans, M.-J., & ten Dijke, P. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022210 · Cited by 360 · see citing works

The Role of Myofibroblasts in Physiological and Pathological Tissue Repair

Schuster, R., Younesi, F., Ezzo, M., & Hinz, B. (2023) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041231 · Cited by 232 · see citing works

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 · see citing works

TGF-&amp;beta; family co-receptor function and signaling

Nickel, J., Ten Dijke, P., & Mueller, T. D. (2018) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmx126 · Cited by 198 · see citing works

Glutaminolysis Promotes Collagen Translation and Stability via α-Ketoglutarate–mediated mTOR Activation and Proline Hydroxylation

Ge, J., Cui, H., Xie, N., Banerjee, S., Guo, S., Dubey, S., Barnes, S., & Liu, G. (2018) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2017-0238oc · Cited by 166 · see citing works

The perivascular origin of pathological fibroblasts

Di Carlo, S. E., & Peduto, L. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93558 · Cited by 164 · see citing works

Integrin-Mediated TGFβ Activation Modulates the Tumour Microenvironment

Brown, N. F., & Marshall, J. F. (2019) · Cancers · doi:10.3390/cancers11091221 · Cited by 116 · see citing works

Molecular Profiles of Pyramidal Neurons in the Superior Temporal Cortex in Schizophrenia

Pietersen, C. Y., Mauney, S. A., Kim, S. S., Lim, M. P., Rooney, R. J., Goldstein, J. M., Petryshen, T. L., Seidman, L. J., Shenton, M. E., McCarley, R. W., et al. (2014) · Journal of Neurogenetics · doi:10.3109/01677063.2014.882918 · Cited by 87 · see citing works

Screening for YAP inhibitors identifies statins as modulators of fibrosis

Santos, D. M., Pantano, L., Pronzati, G., Grasberger, P., Probst, C. K., Black, K. E., Spinney, J. J., Hariri, L. P., Nichols, R., Lin, Y., et al. (2020) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2019-0296oc · Cited by 72 · see citing works

Mutated CEACAMs Disrupt Transforming Growth Factor Beta Signaling and Alter the Intestinal Microbiome to Promote Colorectal Carcinogenesis

Gu, S., Zaidi, S., Hassan, M. I., Mohammad, T., Malta, T. M., Noushmehr, H., Nguyen, B., Crandall, K. A., Srivastav, J., Obias, V., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2019.09.023 · Cited by 63 · see citing works

The Roles of Cardiac Fibroblasts and Endothelial Cells in Myocarditis

Xuan, Y., Chen, C., Wen, Z., & Wang, D. W. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.882027 · Cited by 35 · see citing works

Distinct transcriptional changes distinguish efficient and poor remyelination in multiple sclerosis

Chen, J. Q. A., McNamara, N. B., Engelenburg, H. J., Jongejan, A., Wever, D. D., Hopman, K., van Rixel, E., Nijhuis, P. J. H., de Winter, F., Moerland, P. D., et al. (2025) · Brain · doi:10.1093/brain/awae414 · Cited by 17 · see citing works

Research advances in Peyronie's disease: a comprehensive review on genomics, pathways, phenotypic manifestation, and therapeutic targets.

Chi, J., Bi, W., Lou, K., Ma, J., Wu, J., & Cui, Y. (2024) · Sexual Medicine Reviews · doi:10.1093/sxmrev/qeae006 · Cited by 14 · see citing works

Picroside II as a Potential Anti-Inflammatory Agent

Ren, Y., Liu, Z., Wei, L., Wang, Y., Wang, Y., Guo, Y., & Ma, Z. (2026) · Pharmaceutics · doi:10.3390/pharmaceutics18040499 · Cited by 2 · see citing works

ИСПОЛЬЗОВAНИЕ ПОТЕНЦИAЛA СОЦИAЛЬНЫХ ПAРТНЕРОВ В ПОДГОТОВКЕ БУДУЩИХ ПЕДAГОГОВ

Атабекова, Б. Б. (2024) · Habaršy. Pedagogika ġylymdary seriâsy · doi:10.51889/2959-5762.2023.80.4.019

Cloning and Characterization of Rat BAT3 cDNA

Ozaki, T., Hanaoka, E., Naka, M., et al. (1999) · DNA and Cell Biology · doi:10.1089/104454999315222 · Cited by 22 · see citing works

EFFECT OF THE NEMATODE PHASMARHABDITIS HERMAPHRODITA ON YOUNG STAGES OF THE PEST SLUG ARION LUSITANICUS

Grimm, B. (2002) · Journal of Molluscan Studies · doi:10.1093/mollus/68.1.25 · Cited by 41 · see citing works

HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53Preprint

Sasaki, T., Gan, E. C., Wakeham, A. C., Kornbluth, S. A., Mak, T. W., & Okada, H. (2007) · Genes & Development · doi:10.1101/gad.1534107 · Cited by 127 · see citing works

Anthoxanthum Mosaic Virus

Catherall, P. L. (1970) · Plant Pathology · doi:10.1111/j.1365-3059.1970.tb00999.x · Cited by 6 · see citing works