Signaling Receptors for TGF-β Family Members

The protein kinase complement of the human genome

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Mutational landscape and significance across 12 major cancer types

Kandoth, C., McLellan, M. D., Vandin, F., Ye, K., Niu, B., Lu, C., Xie, M., Zhang, Q., McMichael, J. F., Wyczalkowski, M. A., et al. (2013) · Nature · doi:10.1038/nature12634 · Cited by 4,419 · 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

Smad transcription factorsPreprint

Massagué, J., Seoane, J., & Wotton, D. (2005) · Genes & Development · doi:10.1101/gad.1350705 · Cited by 2,432 · see citing works

Mechanism of activation of the TGF-β receptor

Wrana, J. L., Attisano, L., Wieser, R., Ventura, F., & Massagué, J. (1994) · Nature · doi:10.1038/370341a0 · Cited by 2,340 · see citing works

SPECIFICITY AND VERSATILITY IN TGF-β SIGNALING THROUGH SMADS

Feng, X.-H., & Derynck, R. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.022404.142018 · Cited by 1,869 · 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

Losartan, an AT1 Antagonist, Prevents Aortic Aneurysm in a Mouse Model of Marfan Syndrome

Habashi, J. P., Judge, D. P., Holm, T. M., Cohn, R. D., Loeys, B. L., Cooper, T. K., Myers, L., Klein, E. C., Liu, G., Calvi, C., et al. (2006) · Science · doi:10.1126/science.1124287 · Cited by 1,794 · 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

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

Endoglin, a TGF-β binding protein of endothelial cells, is the gene for hereditary haemorrhagic telangiectasia type 1

McAllister, K. A., Grogg, K. M., Johnson, D. W., Gallione, C. J., Baldwin, M. A., Jackson, C. E., Helmbold, E. A., Markel, D. S., McKinnon, W. C., Murrel, J., et al. (1994) · Nature Genetics · doi:10.1038/ng1294-345 · Cited by 1,475 · see citing works

Targeting the TGFβ signalling pathway in disease

Akhurst, R. J., & Hata, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3810 · Cited by 1,466 · see citing works

Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation.

Kavsak, P., Rasmussen, R. K., Causing, C. G., Bonni, S., Zhu, H.-Q., Thomsen, G. H., & Wrana, J. (2000) · Molecules and Cells · doi:10.1016/s1097-2765(00)00134-9 · Cited by 1,449 · 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

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

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

Distinct endocytic pathways regulate TGF-β receptor signalling and turnover

Guglielmo, G. M. D., Roy, C. L., Goodfellow, A. F., & Wrana, J. L. (2003) · Nature Cell Biology · doi:10.1038/ncb975 · Cited by 1,152 · see citing works

Mutations in the activin receptor–like kinase 1 gene in hereditary haemorrhagic telangiectasia type 2

Johnson, D. W., Berg, J. N., Baldwin, M. A., Gallione, C. J., Marondel, I., Yoon, S.-H., Stenzel, T. T., Speer, M. C., Pericak‐Vance, M. A., Diamond, A. G., et al. (1996) · Nature Genetics · doi:10.1038/ng0696-189 · Cited by 1,113 · see citing works

Non-Smad TGF-β signals

Moustakas, A., & Heldin, C. (2005) · Journal of Cell Science · doi:10.1242/jcs.02554 · Cited by 1,069 · see citing works

BMP signaling inhibits intestinal stem cell self-renewal through suppression of Wnt–β-catenin signaling

He, X., Zhang, J., Tong, W.-G., Tawfik, O. W., Ross, J., Scoville, D. H., Tian, Q., Zeng, X., He, X., Wiedemann, L. M., et al. (2004) · Nature Genetics · doi:10.1038/ng1430 · Cited by 1,065 · see citing works

Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression

Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026 · 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

SARA, a FYVE Domain Protein that Recruits Smad2 to the TGFβ Receptor

Tsukazaki, T., Chiang, T., Davison, A. F., Attisano, L., & Wrana, J. L. (1998) · Cell · doi:10.1016/s0092-8674(00)81701-8 · Cited by 963 · see citing works

Betaglycan presents ligand to the TGFβ signaling receptor

López‐Casillas, F., Wrana, J. L., & Massagué, J. (1993) · Cell · doi:10.1016/0092-8674(93)90368-z · Cited by 901 · see citing works

Regulation of the Polarity Protein Par6 by TGFß Receptors Controls Epithelial Cell Plasticity

Ozdamar, B., Bose, R., Barrios-Rodiles, M., Wang, H.-R., Zhang, Y., & Wrana, J. L. (2005) · Science · doi:10.1126/science.1105718 · Cited by 881 · see citing works

Smurf1 Interacts with Transforming Growth Factor-β Type I Receptor through Smad7 and Induces Receptor Degradation

Ebisawa, T., Fukuchi, M., Murakami, G., Chiba, T., Tanaka, K., Imamura, T., & Miyazono, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100008200 · Cited by 845 · 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

Extracellular control of TGFβ signalling in vascular development and disease

ten Dijke, P., & Arthur, H. M. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2262 · Cited by 777 · see citing works

Regulation of Cytokine Receptors by Golgi N-Glycan Processing and Endocytosis

Partridge, E. A., Le Roy, C., Di Guglielmo, G. M., Pawling, J., Cheung, P., Granovsky, M., Nabi, I. R., Wrana, J. L., & Dennis, J. W. (2004) · Science · doi:10.1126/science.1102109 · Cited by 735 · see citing works

Silencing of TGF-β signalling by the pseudoreceptor BAMBI

Onichtchouk, D., Chen, Y., Dosch, R., Gawantka, V., Delius, H., Massagué, J., & Niehrs, C. (1999) · Nature · doi:10.1038/46794 · Cited by 727 · see citing works

High-Throughput Mapping of a Dynamic Signaling Network in Mammalian Cells

Barrios‐Rodiles, M., Brown, K. R., Ozdamar, B., Bose, R., Liu, Z., Donovan, R. S., Shinjo, F., Liu, Y., Dembowy, J., Taylor, I. W., et al. (2005) · Science · doi:10.1126/science.1105776 · Cited by 726 · 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

Activin Receptor-like Kinase (ALK)1 Is an Antagonistic Mediator of Lateral TGFβ/ALK5 Signaling

Goumans, M.-J., Valdimarsdottir, G., Itoh, S., Lebrin, F., Larsson, J., Mummery, C., Karlsson, S., & ten Dijke, P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00386-1 · Cited by 689 · see citing works

Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-β receptor system

López‐Casillas, F., Cheifetz, S., Doody, J. F., Andres, J., Lane, W. S., & Massagué, J. (1991) · Cell · doi:10.1016/0092-8674(91)90073-8 · Cited by 676 · see citing works

Endoglin promotes endothelial cell proliferation and TGF‐β/ALK1 signal transduction

Lebrin, F., Goumans, M., Jonker, L., Carvalho, R. L. C., Valdimarsdóttir, G., Thorikay, M., Mummery, C. L., Arthur, H. M., & ten Dijke, P. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600386 · Cited by 653 · see citing works

Genomic analysis of diffuse intrinsic pontine gliomas identifies three molecular subgroups and recurrent activating ACVR1 mutations

Buczkowicz, P., Hoeman, C. M., Rakopoulos, P., Pajovic, S., Létourneau, L., Dzamba, M., Morrison, A., Lewis, P. W., Bouffet, É., Bartels, U. K., et al. (2014) · Nature Genetics · doi:10.1038/ng.2936 · Cited by 649 · see citing works

Caveolin-1 Regulates Transforming Growth Factor (TGF)-β/SMAD Signaling through an Interaction with the TGF-β Type I Receptor

Razani, B., Zhang, X. L., Bitzer, M., von Gersdorff, G., Böttinger, E. P., & Lisanti, M. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008340200 · Cited by 640 · see citing works

Germline mutations of the gene encoding bone morphogenetic protein receptor 1A in juvenile polyposis

Howe, J. R., Bair, J. L., Sayed, M. G., Anderson, M. E., Mitros, F. A., Petersen, G. M., Velculescu, V. E., Traverso, G., & Vogelstein, B. (2001) · Nature Genetics · doi:10.1038/88919 · Cited by 630 · 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

Multiple targets of miR-302 and miR-372 promote reprogramming of human fibroblasts to induced pluripotent stem cells

Subramanyam, D., Lamouille, S., Judson, R. L., Liu, J. Y., Bucay, N., Derynck, R., & Blelloch, R. H. (2011) · Nature Biotechnology · doi:10.1038/nbt.1862 · Cited by 594 · see citing works

Betaglycan binds inhibin and can mediate functional antagonism of activin signalling

Lewis, K. A., Gray, P. C., Blount, A. L., MacConell, L., Wiater, E., Bilezikjian, L. M., & Vale, W. (2000) · Nature · doi:10.1038/35006129 · Cited by 585 · see citing works

TGF‐β activates Erk MAP kinase signalling through direct phosphorylation of ShcA

Lee, M. K., Pardoux, C., Hall, M. C., Lee, P. S., Warburton, D., Qing, J., Smith, S. M., & Derynck, R. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601818 · Cited by 580 · see citing works

The Mode of Bone Morphogenetic Protein (BMP) Receptor Oligomerization Determines Different BMP-2 Signaling Pathways

Nohe, A., Haßel, S., Ehrlich, M., Neubauer, F. B., Sebald, W., Henis, Y. I., & Knaus, P. I. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m102750200 · Cited by 566 · see citing works

Endoglin Is an Accessory Protein That Interacts with the Signaling Receptor Complex of Multiple Members of the Transforming Growth Factor-β Superfamily

Pece-Barbara, N., Wrana, J. L., & Letarte, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.584 · Cited by 564 · see citing works

TRAF6 Mediates Smad-Independent Activation of JNK and p38 by TGF-β

Yamashita, M., Fátyol, K., Jin, C., Wang, X., Liu, Z.-G., & Zhang, Y. E. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.09.002 · Cited by 559 · see citing works

The type I TGF-β receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner

Sorrentino, A., Thakur, N., Grimsby, S., Marcusson, A., von Bülow, V., Schuster, N., Zhang, S., Heldin, C., & Landström, M. (2008) · Nature Cell Biology · doi:10.1038/ncb1780 · Cited by 553 · see citing works

Development of TGF-β signalling inhibitors for cancer therapy

Yingling, J. M., Blanchard, K. L., & Sawyer, J. S. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1580 · Cited by 550 · see citing works

BMPR2 Haploinsufficiency as the Inherited Molecular Mechanism for Primary Pulmonary Hypertension

Machado, R. D., Pauciulo, M. W., Thomson, J. R., Lane, K. B., Morgan, N. V., Wheeler, L. A., Phillips, J. A., III, Newman, J. H., Williams, D., Galiè, N., et al. (2001) · The American Journal of Human Genetics · doi:10.1086/316947 · Cited by 535 · see citing works

Recurrent activating ACVR1 mutations in diffuse intrinsic pontine glioma

Taylor, K. R., Mackay, A. G., Truffaux, N., Butterfield, Y. S. N., Morozova, O., Philippe, C., Castel, D., Grasso, C. S., Vinci, M., Carvalho, D. M., et al. (2014) · Nature Genetics · doi:10.1038/ng.2925 · Cited by 522 · see citing works

TβRI Phosphorylation of Smad2 on Ser465 and Ser467 Is Required for Smad2-Smad4 Complex Formation and Signaling

Abdollah, S., Macías‐Silva, M., Tsukazaki, T., Hayashi, H., Attisano, L., & Wrana, J. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.27678 · Cited by 481 · see citing works

FK506 activates BMPR2, rescues endothelial dysfunction, and reverses pulmonary hypertension

Spiekerkoetter, E. F., Tian, X., Cai, J., Hopper, R. K., Sudheendra, D., Li, C. G., El‐Bizri, N., Sawada, H., Haghighat, R., Chan, R., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci65592 · Cited by 449 · see citing works

Crystal Structure of the Cytoplasmic Domain of the Type I TGF β Receptor in Complex with FKBP12

Huse, M., Chen, Y., Massagué, J., & Kuriyan, J. (1999) · Cell · doi:10.1016/s0092-8674(00)80555-3 · Cited by 446 · see citing works

<i>ACVR1</i> ^<i>R206H</i> receptor mutation causes fibrodysplasia ossificans progressiva by imparting responsiveness to activin A

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

Universal GFP reporter for the study of vascular development

Motoike, T., Loughna, S., Perens, E. A., Roman, B. L., Liao, W., Chau, T. C., Richardson, C. D., Kawate, T., Kuno, J., Weinstein, B. M., et al. (2000) · genesis · doi:10.1002/1526-968x(200010)28:2 · Cited by 446 · see citing works

Endoglin, an Ancillary TGFβ Receptor, Is Required for Extraembryonic Angiogenesis and Plays a Key Role in Heart Development

Arthur, H. M., Ure, J. M., Smith, A. J. H., Renforth, G. L., Wilson, D. I., Torsney, E., Charlton, R., Parums, D. V., Jowett, T., Marchuk, D. A., et al. (2000) · Developmental Biology · doi:10.1006/dbio.1999.9534 · Cited by 436 · see citing works

Classic and atypical fibrodysplasia ossificans progressiva (FOP) phenotypes are caused by mutations in the bone morphogenetic protein (BMP) type I receptor ACVR1

Kaplan, F. S., Xu, M., Seemann, P., Connor, J. M., Glaser, D. L., Carroll, L., Delai, P. L. R., Fastnacht-Urban, E., Forman, S. J., Gillessen‐Kaesbach, G., et al. (2008) · Human Mutation · doi:10.1002/humu.20868 · Cited by 436 · see citing works

MED12 Controls the Response to Multiple Cancer Drugs through Regulation of TGF-β Receptor Signaling

Huang, S., Hölzel, M., Knijnenburg, T., Schlicker, A., Roepman, P., McDermott, U., Garnett, M., Grernrum, W., Sun, C., Prahallad, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.035 · Cited by 430 · see citing works

Interleukin-6 Modulates the Expression of the Bone Morphogenic Protein Receptor Type II Through a Novel STAT3–microRNA Cluster 17/92 Pathway

Brock, M., Trenkmann, M., Gay, R., Michel, B., Gay, S., Fischler, M., Ulrich, S., Speich, R., & Huber, L. (2009) · Circulation Research · doi:10.1161/circresaha.109.197491 · Cited by 422 · see citing works

SD-208, a Novel Transforming Growth Factor β Receptor I Kinase Inhibitor, Inhibits Growth and Invasiveness and Enhances Immunogenicity of Murine and Human Glioma CellsIn vitroandIn vivo

Uhl, M., Aulwurm, S., Wischhusen, J., Weiler, M., Jing, Y., Almirez, R. G., Mangadu, R., Liu, Y.-W., Platten, M., Herrlinger, U., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1013 · Cited by 414 · see citing works

USP15 stabilizes TGF-β receptor I and promotes oncogenesis through the activation of TGF-β signaling in glioblastoma

Eichhorn, P. J. A., Rodón, L., Gonzàlez-Juncà, A., Dirac, A., Gili, M., Martínez-Sáez, E., Aura, C., Barba, I., Peg, V., Prat, A., et al. (2012) · Nature Medicine · doi:10.1038/nm.2619 · Cited by 409 · see citing works

Fibrodysplasia ossificans progressiva

Kaplan, F. S., Merrer, M. F. L., Glaser, D. L., Pignolo, R. J., Goldsby, R. E., Kitterman, J. A., Groppe, J. C., & Shore, E. M. (2008) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2007.11.007 · Cited by 394 · see citing works

Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites

López‐Casillas, F., Payne, H., Andres, J., & Massagué, J. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.4.557 · Cited by 393 · see citing works

The Immunophilin FKBP12 Functions as a Common Inhibitor of the TGFβ Family Type I Receptors

Wang, T., Li, B.-Y., Danielson, P. D., Shah, P. C., Rockwell, S., Lechleider, R. J., Martin, J. M., Manganaro, T. F., & Donahoe, P. K. (1996) · Cell · doi:10.1016/s0092-8674(00)80116-6 · Cited by 388 · see citing works

Phosphorylation of Ser465 and Ser467 in the C Terminus of Smad2 Mediates Interaction with Smad4 and Is Required for Transforming Growth Factor-β Signaling

Souchelnytskyi, S., Tamaki, K., Engström, U., Wernstedt, C., ten Dijke, P., & Heldin, C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.28107 · Cited by 382 · see citing works

The TGFβ Receptor Activation Process

Huse, M., Muir, T. W., Xu, L., Chen, Y., Kuriyan, J., & Massagué, J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00332-x · Cited by 381 · 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

Mutations in Transforming Growth Factor-β Receptor Type II Cause Familial Thoracic Aortic Aneurysms and Dissections

Pannu, H., Tran‐Fadulu, V., Chang, J., Lafont, A. L., Hasham, S. N., Sparks, E. A., Giampietro, P. F., Zaleski, C. A., Estrera, A. L., Safi, H. J., et al. (2005) · Circulation · doi:10.1161/circulationaha.105.537340 · Cited by 368 · 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

Mechanism of TGFβ receptor inhibition by FKBP12

Chen, Y., Liu, F., & Massagué, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3866 · Cited by 363 · see citing works

Id2 and Id3 Define the Potency of Cell Proliferation and Differentiation Responses to Transforming Growth Factor β and Bone Morphogenetic Protein

Kowanetz, M., Valcourt, U., Bergström, R., Heldin, C., & Moustakas, A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4241-4254.2004 · Cited by 346 · 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

TGF-β blockade improves the distribution and efficacy of therapeutics in breast carcinoma by normalizing the tumor stroma

Liu, J., Liao, S., Diop-Frimpong, B., Chen, W., Goel, S., Naxerova, K., Ancukiewicz, M., Boucher, Y., Jain, R. K., & Xu, L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117610109 · Cited by 332 · see citing works

Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta.

Yamashita, H., ten Dijke, P., Franzèn, P., Miyazono, K., & Heldin, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32142-7 · Cited by 326 · see citing works

Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1

Foletta, V. C., Lim, M. A., Soosairajah, J., Kelly, A. P., Stanley, E. G., Shannon, M., He, W., Das, S., Massagué, J., & Bernard, O. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212060 · Cited by 325 · see citing works

Crystal structure of the BMP-2–BRIA ectodomain complex

Kirsch, T., Sebald, W., & Dreyer, M. (2000) · Nature Structural Biology · doi:10.1038/75903 · Cited by 323 · see citing works

USP4 is regulated by AKT phosphorylation and directly deubiquitylates TGF-β type I receptor

Zhang, L., Zhou, F., Drabsch, Y., Gao, R., Snaar-Jagalska, E. B., Mickanin, C., Huang, H., Sheppard, K.-A., Porter, J. A., Lu, C., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2522 · Cited by 322 · see citing works

The miR-17-92 MicroRNA Cluster Regulates Multiple Components of the TGF-β Pathway in Neuroblastoma

Mestdagh, P., Boström, A.-K., Impens, F., Fredlund, E., Van Peer, G., De Antonellis, P., von Stedingk, K., Ghesquière, B., Schulte, S., Dews, M., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.038 · Cited by 314 · see citing works

Cytoplasmic PML function in TGF-β signalling

Lin, H., Bergmann, S., & Pandolfi, P. P. (2004) · Nature · doi:10.1038/nature02783 · Cited by 312 · see citing works

TGFβ receptor internalization into EEA1-enriched early endosomes

Hayes, S., Chawla, A., & Corvera, S. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200204088 · Cited by 301 · see citing works

Cooperative Assembly of TGF-β Superfamily Signaling Complexes Is Mediated by Two Disparate Mechanisms and Distinct Modes of Receptor Binding

Groppe, J. C., Hinck, C. S., Samavarchi‐Tehrani, P., Zubieta, C., Schuermann, J. P., Taylor, A. B., Schwarz, P. M., Wrana, J. L., & Hinck, A. P. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.11.039 · Cited by 284 · see citing works

Smad6 Is a Smad1/5-induced Smad Inhibitor

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