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TGF-β SIGNAL TRANSDUCTION
Abstract
The transforming growth factor β (TGF-β) family of growth factors control the development and homeostasis of most tissues in metazoan organisms. Work over the past few years has led to the elucidation of a TGF-β signal transduction network. This network involves receptor serine/threonine kinases at the cell surface and their substrates, the SMAD proteins, which move into the nucleus, where they activate target gene transcription in association with DNA-binding partners. Distinct repertoires of receptors, SMAD proteins, and DNA-binding partners seemingly underlie, in a cell-specific manner, the multifunctional nature of TGF-β and related factors. Mutations in these pathways are the cause of various forms of human cancer and developmental disorders.
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Citations
Cites
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
DPC4 , 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
Kulkarni, A. B., Huh, C. G., Becker, D., Geiser, A., Lyght, M., Flanders, K. C., Roberts, A. B., Sporn, M. B., Ward, J. M., & Karlsson, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.2.770 · Cited by 1,967
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
Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
Schreiber, S. L. (1991) · Science · doi:10.1126/science.1702904 · Cited by 1,494
Activation of Signalling by the Activin Receptor Complex
Attisano, L., Wrana, J. L., Montalvo, E., & Massagué, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.3.1066 · Cited by 316
Self-citationFrancois, V, Solloway, M., O'Neill, J. W., Emery, J., & Bier, E. (1994) · Genes & Development · doi:10.1101/gad.8.21.2602 · Cited by 308
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Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
Regulation of Wound Healing by Growth Factors and Cytokines
WERNER, S., & GROSE, R. (2003) · Physiological Reviews · doi:10.1152/physrev.2003.83.3.835 · Cited by 3,629
Mechanisms of Diabetic Complications
Forbes, J. M., & Cooper, M. E. (2013) · Physiological Reviews · doi:10.1152/physrev.00045.2011 · Cited by 2,890
Dopamine in motivational control: rewarding, aversive, and alerting
Bromberg-Martin, E. S., Matsumoto, M., & Hikosaka, O. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.022 · Cited by 2,396
TGF-β signaling and the fibrotic response
Leask, A., & Abraham, D. J. (2004) · The FASEB Journal · doi:10.1096/fj.03-1273rev · Cited by 2,319
TGF-β Signaling in Tumor Suppression and Cancer Progression
Derynck, R., Akhurst, R. J., & Balmain, A. (2001) · Nature Genetics · doi:10.1038/ng1001-117 · Cited by 2,275
RAS oncogenes: the first 30 years
Malumbres, M., & Barbacid, M. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1097 · Cited by 1,902
Mechanisms of photoaging and chronological skin aging
Fisher, G. J., Kang, S., Varani, J., Bata-Csorgo, Z., Wan, Y., Datta, S., & Voorhees, J. J. (2002) · Archives of Dermatology · doi:10.1001/archderm.138.11.1462 · Cited by 1,849
Hyperactive Ras in developmental disorders and cancer
Schubbert, S., Shannon, K., & Bollag, G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2109 · Cited by 1,583
Vogl, T., Tenbrock, K., Ludwig, S., Leukert, N., Ehrhardt, C., van Zoelen, M. A. D., Nacken, W., Foell, D., van der Poll, T., Sorg, C., et al. (2007) · Nature Medicine · doi:10.1038/nm1638 · Cited by 1,418
Viruses and interferon: a fight for supremacy
Katze, M. G., He, Y., & Gale, M. (2002) · Nature Reviews Immunology · doi:10.1038/nri888 · Cited by 1,419
Transvascular delivery of small interfering RNA to the central nervous system
Kumar, P., Wu, H., McBride, J. L., Jung, K.-E., Hee Kim, M., Davidson, B. L., Kyung Lee, S., Shankar, P., & Manjunath, N. (2007) · Nature · doi:10.1038/nature05901 · Cited by 1,246
The discovery of receptor tyrosine kinases: targets for cancer therapy
Gschwind, A., Fischer, O. M., & Ullrich, A. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1360 · Cited by 1,227
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
Membrane fluidity and its roles in the perception of environmental signals
Los, D. A., & Murata, N. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.08.002 · Cited by 1,020
Lin, A. W., Barradas, M., Stone, J. C., van Aelst, L., Serrano, M., & Lowe, S. W. (1998) · Genes & Development · doi:10.1101/gad.12.19.3008 · Cited by 945
Crossing the endothelial barrier during metastasis
Reymond, N., d'Água, B. B., & Ridley, A. J. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3628 · Cited by 922
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
Valavanidis, A., Vlachogianni, T., Fiotakis, K., & Loridas, S. (2013) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph10093886 · Cited by 910
Estradiol and the Developing Brain
McCARTHY, M. M. (2008) · Physiological Reviews · doi:10.1152/physrev.00010.2007 · Cited by 885
TGF-β signaling in health and disease
Massagué, J., & Sheppard, D. (2023) · Cell · doi:10.1016/j.cell.2023.07.036 · Cited by 890
Self-citationHigh levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
Tanno, T., Bhanu, N. V., Oneal, P. A., Goh, S.-H., Staker, P., Lee, Y. T., Moroney, J. W., Reed, C. H., Luban, N. L., Wang, R.-H., et al. (2007) · Nature Medicine · doi:10.1038/nm1629 · Cited by 854
The Radical-Pair Mechanism of Magnetoreception
Hore, P. J., & Mouritsen, H. (2016) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-032116-094545 · Cited by 813
REGULATION OF MUSCLE MASS BY MYOSTATIN
Lee, S.-J. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.012103.135836 · Cited by 819
PRESTO-Tango as an open-source resource for interrogation of the druggable human GPCRome
Kroeze, W. K., Sassano, M. F., Huang, X.-P., Lansu, K., McCorvy, J. D., Giguère, P. M., Sciaky, N., & Roth, B. L. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3014 · Cited by 755
Dopaminergic modulation of synaptic transmission in cortex and striatum
Tritsch, N. X., & Sabatini, B. L. (2012) · Neuron · doi:10.1016/j.neuron.2012.09.023 · Cited by 756
Simonneaux, V., & Ribelayga, C. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.2.2 · Cited by 740
Nuclear CDKs Drive Smad Transcriptional Activation and Turnover in BMP and TGF-β Pathways
Alarcón, C., Zaromytidou, A.-I., Xi, Q., Gao, S., Yu, J., Fujisawa, S., Barlas, A., Miller, A. N., Manova-Todorova, K., Macias, M. J., et al. (2009) · Cell · doi:10.1016/j.cell.2009.09.035 · Cited by 719
Self-citationTransforming Growth Factor-β1 to the Bone
Janssens, K., ten Dijke, P., Janssens, S., & Van Hul, W. (2005) · Endocrine Reviews · doi:10.1210/er.2004-0001 · Cited by 710
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
A dynamic role of HAUSP in the p53-Mdm2 pathway
Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679
Neurogenin promotes neurogenesis and inhibits glial differentiation by independent mechanisms.
Sun, Y., Nadal-Vicens, M., Misono, S., Lin, M. Z., Zubiaga, A., Hua, X., Fan, G., & Greenberg, M. E. (2001) · Cell · doi:10.1016/s0092-8674(01)00224-0 · Cited by 681
Activity-dependent regulation of inhibitory synapse development by Npas4
Lin, Y., Bloodgood, B. L., Hauser, J. L., Lapan, A. D., Koon, A. C., Kim, T.-K., Hu, L. S., Malik, A. N., & Greenberg, M. E. (2008) · Nature · doi:10.1038/nature07319 · Cited by 639
A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
Wang, R.-H., Li, C., Xu, X., Zheng, Y., Xiao, C., Zerfas, P., Cooperman, S., Eckhaus, M., Rouault, T., Mishra, L., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.010 · Cited by 614
Cretney, E., Xin, A., Shi, W., Minnich, M., Masson, F., Miasari, M., Belz, G. T., Smyth, G. K., Busslinger, M., Nutt, S. L., et al. (2011) · Nature Immunology · doi:10.1038/ni.2006 · Cited by 605
Mitotic Misregulation and Human Aging
Ly, D. H., Lockhart, D. J., Lerner, R. A., & Schultz, P. G. (2000) · Science · doi:10.1126/science.287.5462.2486 · Cited by 599
Lito, P., Pratilas, C. A., Joseph, E. W., Tadi, M., Halilovic, E., Zubrowski, M., Huang, A., Wong, W. L., Callahan, M. K., Merghoub, T., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.10.009 · Cited by 562
Retinoids in the treatment of skin aging: an overview of clinical efficacy and safety
Mukherjee, S., Date, A., Patravale, V., Korting, H. C., Roeder, A., & Weindl, G. (2006) · Clinical Interventions in Aging · doi:10.2147/ciia.2006.1.4.327 · Cited by 580
Abnormal angiogenesis but intact hematopoietic potential in TGF‐β type I receptor‐deficient mice
Larsson, J., Goumans, M., Sjöstrand, L. J., van Rooijen, M. A., Ward, D., Levéen, P., Xu, X., ten Dijke, P., Mummery, C. L., & Karlsson, S. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1663 · Cited by 563
Relaxin family peptides and their receptors
Bathgate, R. A. D., Halls, M. L., van der Westhuizen, E. T., Callander, G. E., Kocan, M., & Summers, R. J. (2013) · Physiological Reviews · doi:10.1152/physrev.00001.2012 · Cited by 534
Alterations in components of the TGF-β superfamily signaling pathways in human cancer
LEVY, L., & HILL, C. (2006) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2005.09.009 · Cited by 539
Barcia, G., Fleming, M. R., Deligniere, A., Gazula, V.-R., Brown, M. R., Langouet, M., Chen, H., Kronengold, J., Abhyankar, A., Cilio, R., et al. (2012) · Nature Genetics · doi:10.1038/ng.2441 · Cited by 525
Alliston, T., Choy, L., Ducy, P., Karsenty, G., & Derynck, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.9.2254 · Cited by 526
Mathematical Models of Protein Kinase Signal Transduction
Heinrich, R., Neel, B. G., & Rapoport, T. A. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00528-2 · Cited by 511
Signal transduction of bone morphogenetic protein receptors
Nohe, A. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2003.08.011 · Cited by 514
The growing family of interferon regulatory factors
Nguyen, H., Hiscott, J., & Pitha, P. M. (1997) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(97)00019-1 · Cited by 480
Non-histone protein methylation as a regulator of cellular signalling and function
Biggar, K. K., & Li, S. S.-C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3915 · Cited by 479
The endoplasmic reticulum–mitochondria connection: One touch, multiple functions
Marchi, S., Patergnani, S., & Pinton, P. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.015 · Cited by 475
Wong, S. T., Trinh, K., Hacker, B., Chan, G. C. K., Lowe, G., Gaggar, A., Xia, Z., Gold, G. H., & Storm, D. R. (2000) · Neuron · doi:10.1016/s0896-6273(00)00060-x · Cited by 470
Muscarinic acetylcholine receptors: novel opportunities for drug development
Kruse, A. C., Kobilka, B. K., Gautam, D., Sexton, P. M., Christopoulos, A., & Wess, J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4295 · Cited by 437
Molecular mechanisms underlying the activation of eNOS
Fleming, I. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0767-7 · Cited by 437
Transforming growth factor‐β in stem cells and tissue homeostasis
Xu, X., Zheng, L., Yuan, Q., Zhen, G., Crane, J. L., Zhou, X., & Cao, X. (2018) · Bone Research · doi:10.1038/s41413-017-0005-4 · Cited by 414
Transient receptor potential M3 channels are ionotropic steroid receptors in pancreatic β cells
Wagner, T. F. J., Loch, S., Lambert, S., Straub, I., Mannebach, S., Mathar, I., Düfer, M., Lis, A., Flockerzi, V., Philipp, S. E., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1801 · Cited by 392
The neurobiology of pair bonding: Insights from a socially monogamous rodent
Young, K. A., Gobrogge, K. L., Liu, Y., & Wang, Z. (2011) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2010.07.006 · Cited by 389
Meno, C., Gritsman, K., Ohishi, S., Ohfuji, Y., Heckscher, E., Mochida, K., Shimono, A., Kondoh, H., Talbot, W. S., Robertson, E. J., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80331-7 · Cited by 374
Kim, Y. J., Hwang, S. J., Bae, Y. C., & Jung, J. S. (2009) · Stem Cells · doi:10.1002/stem.235 · Cited by 373
IL-13 Activates a Mechanism of Tissue Fibrosis That Is Completely TGF-β Independent
Kaviratne, M., Hesse, M., Leusink, M., Cheever, A. W., Davies, S. J., McKerrow, J. H., Wakefield, L. M., Letterio, J. J., & Wynn, T. A. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.6.4020 · Cited by 370
Sorting out the cellular functions of sorting nexins
Worby, C. A., & Dixon, J. E. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm974 · Cited by 364
Molecular Genetics of Mating Recognition in Basidiomycete Fungi
Casselton, L. A., & Olesnicky, N. S. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.55-70.1998 · Cited by 353
Regulation and organization of adenylyl cyclases and cAMP
COOPER, D. M. F. (2003) · Biochemical Journal · doi:10.1042/bj20031061 · Cited by 356
Adipocyte-derived endotrophin promotes malignant tumor progression
Park, J., & Scherer, P. E. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63930 · Cited by 350
Mechanisms of estrogen signaling and gene expression via GPR30
Prossnitz, E. R., & Maggiolini, M. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.03.026 · Cited by 346
FOXO transcription factors throughout T cell biology
Hedrick, S. M., Michelini, R. H., Doedens, A. L., Goldrath, A. W., & Stone, E. L. (2012) · Nature Reviews Immunology · doi:10.1038/nri3278 · Cited by 347
Altucci, L., Rossin, A., Raffelsberger, W., Reitmair, A., Chomienne, C., & Gronemeyer, H. (2001) · Nature Medicine · doi:10.1038/89050 · Cited by 340
Smad3 Mediates Transforming Growth Factor-β–Induced α-Smooth Muscle Actin Expression
Hu, B., Wu, Z., & Phan, S. H. (2003) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2003-0063oc · Cited by 325
Functional role of mitochondrial respiratory supercomplexes
Genova, M. L., & Lenaz, G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.11.002 · Cited by 306
Hydrogen peroxide stimulates macrophages and monocytes to actively release HMGB1
Tang, D., Shi, Y., Kang, R., Li, T., Xiao, W., Wang, H., & Xiao, X. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0806540 · Cited by 312
Robins, S. C., Stewart, I., McNay, D. E., Taylor, V., Giachino, C., Goetz, M., Ninkovic, J., Briancon, N., Maratos-Flier, E., Flier, J. S., et al. (2013) · Nature Communications · doi:10.1038/ncomms3049 · Cited by 306
de la Mora, M. P., Gallegos-Cari, A., Arizmendi-García, Y., Marcellino, D., & Fuxe, K. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2009.10.010 · Cited by 296
Activins and Inhibins: Roles in Development, Physiology, and Disease
Namwanje, M., & Brown, C. W. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021881 · Cited by 294
Halder, S. K., Beauchamp, R. D., & Datta, P. K. (2005) · Neoplasia · doi:10.1593/neo.04640 · Cited by 288
Cao, J., Papadopoulou, N., Kempuraj, D., Boucher, W. S., Sugimoto, K., Cetrulo, C. L., & Theoharides, T. C. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.12.7665 · Cited by 285
Mechanisms and treatments of photoaging
Poon, F., Kang, S., & Chien, A. L. (2015) · Photodermatology, Photoimmunology & Photomedicine · doi:10.1111/phpp.12145 · Cited by 284
Transforming growth factor-β: a therapeutic target for cancer
Haque, S., & Morris, J. C. (2017) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2017.1327107 · Cited by 276
The podocyte slit diaphragm--from a thin grey line to a complex signalling hub
Grahammer, F., Schell, C., & Huber, T. B. (2013) · Nature Reviews Nephrology · doi:10.1038/nrneph.2013.169 · Cited by 269
Hematopoietic cytokine receptor signaling
Baker, S. J., Rane, S. G., & Reddy, E. P. (2007) · Oncogene · doi:10.1038/sj.onc.1210757 · Cited by 256
Selective control of inhibitory synapse development by Slitrk3-PTPδ trans-synaptic interaction
Takahashi, H., Katayama, K.-I., Sohya, K., Miyamoto, H., Prasad, T., Matsumoto, Y., Ota, M., Yasuda, H., Tsumoto, T., Aruga, J., et al. (2012) · Nature Neuroscience · doi:10.1038/nn.3040 · Cited by 250
Relative roles of TGF‐β1 and Wnt in the systemic regulation and aging of satellite cell responses
Carlson, M. E., Conboy, M. J., Hsu, M., Barchas, L., Jeong, J., Agrawal, A., Mikels, A. J., Agrawal, S., Schaffer, D. V., & Conboy, I. M. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00517.x · Cited by 244
Resende, R., Ferreiro, E., Pereira, C., & Resende de Oliveira, C. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.06.036 · Cited by 235
Postsynaptic ProSAP/Shank scaffolds in the cross-hair of synaptopathies
Grabrucker, A. M., Schmeisser, M. J., Schoen, M., & Boeckers, T. M. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.07.003 · Cited by 233
Tobacco smoke causes premature skin aging
Morita, A. (2007) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2007.06.015 · Cited by 224
Interleukin-1β impairs brain derived neurotrophic factor-induced signal transduction
Tong, L., Balazs, R., Soiampornkul, R., Thangnipon, W., & Cotman, C. W. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.027 · Cited by 222
Dynamic Allostery: Linkers Are Not Merely Flexible
Ma, B., Tsai, C.-J., Haliloğlu, T., & Nussinov, R. (2011) · Structure · doi:10.1016/j.str.2011.06.002 · Cited by 222
Structural insights into BMP receptors: Specificity, activation and inhibition
Yadin, D., Knaus, P., & Mueller, T. D. (2016) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.11.005 · Cited by 221
Strategies to Discover Unexpected Targets for Drugs Active at G Protein–Coupled Receptors
Allen, J. A., & Roth, B. L. (2011) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100553 · Cited by 216
The adaptor molecule Disabled‐2 links the transforming growth factor β receptors to the Smad pathway
Hocevar, B. A., Smine, A., Xu, X., & Howe, P. H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2789 · Cited by 213
TGF-β2 is an exercise-induced adipokine that regulates glucose and fatty acid metabolism
Takahashi, H., Alves, C. R. R., Stanford, K. I., Middelbeek, R. J. W., Nigro, P., Ryan, R. E., Xue, R., Sakaguchi, M., Lynes, M. D., So, K., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-018-0030-7 · Cited by 204
Wound-Healing Studies in Transgenic and Knockout Mice
Grose, R., & Werner, S. (2004) · Molecular Biotechnology · doi:10.1385/mb:28:2:147 · Cited by 197
Targeted tumor therapy with the TGF-β2 antisense compound AP 12009
SCHLINGENSIEPEN, K., SCHLINGENSIEPEN, R., STEINBRECHER, A., HAU, P., BOGDAHN, U., FISCHERBLASS, B., & JACHIMCZAK, P. (2006) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2005.09.002 · Cited by 195
Freeman, S. M., Inoue, K., Smith, A. L., Goodman, M. M., & Young, L. J. (2014) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2014.03.023 · Cited by 185
Modeling formalisms in Systems Biology
Machado, D., Costa, R. S., Rocha, M., Ferreira, E. C., Tidor, B., & Rocha, I. (2011) · AMB Express · doi:10.1186/2191-0855-1-45 · Cited by 189
Effect of TGF-?/Smad signaling pathway on lung myofibroblast differentiation
GU, L., ZHU, Y.-J., YANG, X., GUO, Z.-J., XU, W.-B., & TIAN, X.-L. (2007) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2007.00468.x · Cited by 184
Targeting the mitogen-activated protein kinase pathway: physiological feedback and drug response
Pratilas, C. A., & Solit, D. B. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-3064 · Cited by 183
MicroRNA-155 Targets SMAD2 and Modulates the Response of Macrophages to Transforming Growth Factor-β
Louafi, F., Martinez-Nunez, R. T., & Sanchez-Elsner, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.146852 · Cited by 181
Bollard, C. M., Tripic, T., Cruz, C. R., Dotti, G., Gottschalk, S., Torrano, V., Dakhova, O., Carrum, G., Ramos, C. A., Liu, H., et al. (2018) · Journal of Clinical Oncology · doi:10.1200/jco.2017.74.3179 · Cited by 181
Formation of the definitive endoderm in mouse is a Smad2-dependent process
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Metadata
- Authors
- Massagué, J.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1998-06
- Volume
- 67
- Issue
- 1
- Pages
- 753-791
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2103031848
- Cited by
- 7,556
- References
- 7
- FWCI
- 24.72
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.