Specificity, versatility, and control of TGF-β family signaling
Open accessAbstract
Molecular function and pathway cross-talk in TGF-β signaling reveal its complexity and open questions.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Neutralizing TGF-β antibodies need to effectively interfere with the very high binding affinity (10−11 M range) of TGF-β to cell surface receptor complexes.
“they need to effectively interfere with the very high binding affinity (10−11 M range) of TGF-β to cell surface receptor complexes65.”
From TGFβ biology in cancer progression and immunotherapy (2021) · cites this paper as [65]
By design, TβRII ligand trap-based chimeras should sequester TGF-β1 and TGF-β3 only, similarly to dimerized TβRII receptor.
“By design, these chimeras, based on the TβRII ligand trap, should sequester TGF-β1 and -β3 only, similarly to dimerized TβRII receptor65.”
From TGFβ biology in cancer progression and immunotherapy (2021) · cites this paper as [65]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145 · cited 1× · see citing works
“On the basis of sequence characteristics, the type I and type II receptors are predicted dual-specificity kinases, able to phosphorylate on serine and threonine, as well as tyrosine, and are phylogenetically clustered proximal to other dual-specificity kinases such asMEK kinases (65, 66).”
BackgroundMolecular mechanisms of epithelial–mesenchymal transition
Lamouille, S., Xu, J., & Derynck, R. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3758 · Cited by 8,091 · see citing works
Self-citationmTOR Signaling in Growth, Metabolism, and Disease
Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.02.004 · Cited by 7,555 · see citing works
Massagué, J. (2008) · Cell · doi:10.1016/j.cell.2008.07.001 · Cited by 3,907 · see citing works
mTOR Signaling in Growth, Metabolism, and Disease.
Saxton, R., & Sabatini, D. (2017) · Cell · doi:10.1016/j.cell.2017.03.035 · Cited by 3,889 · cited 1× · see citing works
“12, eaav5183 (2019) 26 February 2019 rylates and thus activates mTOR, which, among other responses, promotes protein synthesis and cell metabolism, is required for cell migration, and phosphorylates AKT in a positive feedback loop (311, 312).”
BackgroundMassagué, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3434 · Cited by 3,130 · see citing works
The PI3K Pathway in Human Disease
Fruman, D. A., Chiu, H., Hopkins, B. D., Bagrodia, S., Cantley, L. C., & Abraham, R. T. (2017) · Cell · doi:10.1016/j.cell.2017.07.029 · Cited by 2,749 · 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
Swatek, K. N., & Komander, D. (2016) · Cell Research · doi:10.1038/cr.2016.39 · Cited by 2,066 · 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
Self-citationThe GDNF family: Signalling, biological functions and therapeutic value
Airaksinen, M. S., & Saarma, M. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn812 · Cited by 1,832 · see citing works
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
Self-citationRegulation 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 · cited 1× · see citing works
“When expressed in transfected cells, myostatin (also known as GDF8) and GDF11 are also secreted as latent complexes, in which the propolypepide association prevents mature ligand from binding and activating the receptors (19, 41).”
BackgroundAssoian, 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
Yuan, J., Yang, F., Wang, F., Ma, J., Guo, Y., Tao, Q.-F., Liu, F., Pan, W. X., Wang, T.-T., Zhou, C., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.03.010 · Cited by 1,515 · see citing works
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
Identification of a Member of the MAPKKK Family as a Potential Mediator of TGF-β Signal Transduction
Yamaguchi, T., Shirakabe, K., Shibuyà, H., Irie, K., Oishi, I., Ueno, N., Taniguchi, T., Nishida, E., & Matsumoto, K. (1995) · Science · doi:10.1126/science.270.5244.2008 · Cited by 1,344 · see citing works
TGF-β and the TGF-β family: context-dependent roles in cell and tissue physiology
Morikawa, M., Derynck, R., & Miyazono, K. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021873 · Cited by 1,321 · see citing works
Self-citationSMAD 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
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
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
Akt, FoxO and regulation of apoptosis
Zhang, X., Tang, N., Hadden, T. J., & Rishi, A. K. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.03.010 · Cited by 1,112 · see citing works
Bhowmick, N., Ghiassi, M., Bakin, A. V., Aakre, M., Lundquist, C., Engel, M., Arteaga, C., & Moses, H. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.1.27 · Cited by 1,087 · see citing works
Pituitary FSH is released by a heterodimer of the β-subunits from the two forms of inhibin
LING, N. C., Ying, S., Ueno, N., Shimasaki, S., Esch, F. S., Hotta, M., & Guillemin, R. (1986) · Nature · doi:10.1038/321779a0 · Cited by 1,082 · see citing works
Seoane, J., Le, H.-V., Shen, L., Anderson, S. A., & Massagué, J. (2004) · Cell · doi:10.1016/s0092-8674(04)00298-3 · Cited by 1,029 · 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
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
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
Human Smad3 and Smad4 Are Sequence-Specific Transcription Activators
Zawel, L. S., Dai, J. L., Buckhaults, P., Zhou, S., Kinzler, K. W., Vogelstein, B., & Kern, S. E. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80061-1 · Cited by 940 · see citing works
TGF-β Signaling from Receptors to SmadsPreprint
Hata, A., & Chen, Y. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022061 · Cited by 897 · 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
50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond
Verdin, E. M., & Ott, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3931 · Cited by 876 · see citing works
Synergistic Signaling in Fetal Brain by STAT3-Smad1 Complex Bridged by p300
Nakashima, K., Yanagisawa, M., Arakawa, H., Kimura, N., Hisatsune, T., Kawabata, M., Miyazono, K., & Taga, T. (1999) · Science · doi:10.1126/science.284.5413.479 · Cited by 867 · see citing works
Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
Roy, C. L., & Wrana, J. L. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1571 · Cited by 862 · see citing works
A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
Zhu, H., Kavsak, P. A., Abdollah, S., Wrana, J. L., & Thomsen, G. H. (1999) · Nature · doi:10.1038/23293 · Cited by 847 · see citing works
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
Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-β-induced transcription
Zhang, Y., Feng, X.-H., & Derynck, R. (1998) · Nature · doi:10.1038/29814 · Cited by 809 · see citing works
Self-citationTGF-β1 Signaling and Tissue Fibrosis
Kim, K. K., Sheppard, D., & Chapman, H. A. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022293 · Cited by 800 · see citing works
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 798 · see citing works
GFRAL is the receptor for GDF15 and the ligand promotes weight loss in mice and nonhuman primates
Mullican, S. E., Lin-Schmidt, X., Chin, C.-N., Chavez, J. A., Furman, J. L., Armstrong, A. A., Beck, S. C., South, V. J., Dinh, T. Q., Cash-Mason, T. D., et al. (2017) · Nature Medicine · doi:10.1038/nm.4392 · Cited by 774 · see citing works
Integration of TGF‐β/Smad and Jagged1/Notch signalling in epithelial‐to‐mesenchymal transition
Zavadil, J., C̆ermák, L., Soto-Nieves, N., & Böttinger, E. P. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600069 · Cited by 747 · 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
Crystal Structure of a Smad MH1 Domain Bound to DNA
Shi, Y., Wang, Y., Jayaraman, L., Yang, H., Massagué, J., & Pavletich, N. P. (1998) · Cell · doi:10.1016/s0092-8674(00)81600-1 · Cited by 726 · see citing works
Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressorPreprint
Hata, A., Lagna, G., Massagué, J., & Hemmati‐Brivanlou, A. (1998) · Genes & Development · doi:10.1101/gad.12.2.186 · Cited by 726 · 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
TGF‐β receptor‐activated p38 MAP kinase mediates Smad‐independent TGF‐β responses
Yu, L., DeRouen, M. C., & Zhang, Y. E. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf366 · Cited by 721 · see citing works
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 · see citing works
Mason, A. J., Hayflick, J. S., LING, N. C., Esch, F. S., Ueno, N., Ying, S., Guillemin, R., Niall, H. D., & Seeburg, P. H. (1985) · Nature · doi:10.1038/318659a0 · Cited by 713 · see citing works
Signaling Receptors for TGF-β Family Members
Heldin, C.-H., & Moustakas, A. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022053 · Cited by 711 · see citing works
The transforming growth factor-β system, a complex pattern of cross-reactive ligands and receptors
Cheifetz, S., Weatherbee, J. A., Tsang, M., Anderson, J. K., Mole, J. E., Lucas, R., & Massagué, J. (1987) · Cell · doi:10.1016/0092-8674(87)90192-9 · Cited by 701 · see citing works
Non-Smad Signaling Pathways of the TGF-β FamilyPreprint
Zhang, Y. E. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022129 · Cited by 701 · see citing works
Wieser, R., Wrana, J. L., & Massagué, J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07214.x · Cited by 689 · see citing works
Hocevar, B. A., Brown, T. L., & Howe, P. H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1345 · Cited by 671 · see citing works
The E3 Ligase TRAF6 Regulates Akt Ubiquitination and Activation
Yang, W., Wang, J., Chan, C., Lee, S.-W., Campos, A. D., Lamothe, B., Hur, L., Grabiner, B. C., Lin, X., Darnay, B. G., et al. (2009) · Science · doi:10.1126/science.1175065 · Cited by 669 · see citing works
The myogenic regulatory factors, determinants of muscle development, cell identity and regeneration
Hernández‐Hernández, J. M., García-González, E. G., Brun, C. E., & Rudnicki, M. A. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.11.010 · Cited by 669 · cited 1× · see citing works
“For example, cooperation of TGF-b–activated Smad3-Smad4 complexes with Snail1 confers coordinate regulation of genes during EMT (279), whereas Smad associations with myogenic bHLH transcription factors coordinately repress myogenic differentiation genes (191, 205, 282).”
BackgroundGFRAL is the receptor for GDF15 and is required for the anti-obesity effects of the ligand
Yang, L., Chang, C.-C., Sun, Z., Madsen, D., Zhu, H., Padkjær, S. B., Wu, X., Huang, T., Hultman, K., Paulsen, S. J., et al. (2017) · Nature Medicine · doi:10.1038/nm.4394 · Cited by 668 · see citing works
Vincent, C. T., Neve, E. P. A., Johnson, J. R., Kukalev, A., Rojo, F., Albanell, J., Pietras, K., Virtanen, I., Philipson, L., Leopold, P. L., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1905 · Cited by 651 · see citing works
Signaling Cross Talk between TGF-β/Smad and Other Signaling PathwaysPreprint
Luo, K. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022137 · Cited by 642 · see citing works
TGF-β Family Signaling in the Control of Cell Proliferation and Survival
Zhang, Y., Alexander, P. B., & Wang, X.-F. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022145 · Cited by 626 · see citing works
Integrating signals from RTKs to ERK/MAPK
Mckay, M., & Morrison, D. K. (2007) · Oncogene · doi:10.1038/sj.onc.1210394 · Cited by 616 · see citing works
Morphogen Gradients: From Generation to Interpretation
Rogers, K. W., & Schier, A. F. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154148 · Cited by 610 · 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
Self-citationDaniels, C. E., Wilkes, M. C., Edens, M., Kottom, T. J., Murphy, S. J., LIMPER, A. H., & Leof, E. B. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19603 · Cited by 576 · see citing works
Lamouille, S., & Derynck, R. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611146 · Cited by 573 · see citing works
Self-citationMaster 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
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
A Smad Transcriptional Corepressor
Wotton, D., Lo, R. S., Lee, S., & Massagué, J. (1999) · Cell · doi:10.1016/s0092-8674(00)80712-6 · Cited by 554 · 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
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
The HECT Family of E3 Ubiquitin Ligases: Multiple Players in Cancer Development
Bernassola, F., Karin, M., Ciechanover, A., & Melino, G. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.06.001 · Cited by 541 · see citing works
Interdependent SMAD and JNK Signaling in Transforming Growth Factor-β-mediated Transcription
Engel, M. E., McDonnell, M. A., Law, B. K., & Moses, H. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37413 · Cited by 531 · see citing works
Alliston, T., Choy, L., Ducy, P., Karsenty, G., & Derynck, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.9.2254 · Cited by 526 · see citing works
Self-citationFeng, X., Zhang, Y. E., Wu, R.-Y., & Derynck, R. (1998) · Genes & Development · doi:10.1101/gad.12.14.2153 · Cited by 525 · see citing works
Self-citationRegulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
Zhang, Y. E., Chang, C., Gehling, D. J., Hemmati‐Brivanlou, A., & Derynck, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.974 · Cited by 523 · see citing works
Self-citationTGF-β Family Signaling in Tumor Suppression and Cancer ProgressionPreprint
Seoane, J., & Gomis, R. R. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022277 · Cited by 512 · see citing works
FAM/USP9x, a Deubiquitinating Enzyme Essential for TGFβ Signaling, Controls Smad4 Monoubiquitination
Dupont, S., Mamidi, A., Cordenonsi, M., Montagner, M., Zacchigna, L., Adorno, M., Martello, G., Stinchfield, M. J., Soligo, S., Morsut, L., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.051 · Cited by 494 · see citing works
Daniels, C. E., Wilkes, M. C., Edens, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200419603 · Cited by 493 · see citing works
PPM1A Functions as a Smad Phosphatase to Terminate TGFβ Signaling
Lin, X., Duan, X., Liang, Y.-Y., Su, Y., Wrighton, K. H., Long, J., Hu, M., Davis, C. M., Wang, J., Brunicardi, F. C., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.044 · Cited by 486 · see citing works
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 · cited 1× · see citing works
“Various transmembraneproteins and receptors are functionally regulated by acetylation on Lys (147, 148) ormethylation on Lys orArg (149); however, these modes of posttranslational regulation are less studied than the control of protein function by phosphorylation.”
BackgroundTran, D. Q., Andersson, J., Wang, R., Ramsey, H. E., Unutmaz, D., & Shevach, E. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901944106 · Cited by 473 · 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
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
Hanafusa, H., Ninomiya‐Tsuji, J., Masuyama, N., Nishita, M., Fujisawa, J., Shibuyà, H., Matsumoto, K., & Nishida, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.27161 · Cited by 442 · 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
Regulation of TGF-β Family Signaling by Inhibitory Smads
Miyazawa, K., & Miyazono, K. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022095 · Cited by 439 · see citing works
Balancing BMP Signaling through Integrated Inputs into the Smad1 Linker
Sapkota, G. P., Alarcón, C. R., Spagnoli, F. M., Brivanlou, A. H., & Massagué, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.006 · Cited by 419 · see citing works
Edlund, S., Landström, M., Heldin, C., & Aspenström, P. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-08-0398 · Cited by 418 · see citing works
TAK1 is Critical for IκB Kinase-mediated Activation of the NF-κB Pathway
Takaesu, G., Surabhi, R. M., Park, K.-J., Ninomiya‐Tsuji, J., Matsumoto, K., & Gaynor, R. B. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01404-3 · Cited by 404 · see citing works
Regulation of the Bioavailability of TGF-β and TGF-β-Related Proteins
Robertson, I. B., & Rifkin, D. B. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021907 · Cited by 403 · see citing works
Persson, U., Izumi, H., Souchelnytskyi, S., Itoh, S., Grimsby, S., Engström, U., Heldin, C., Funa, K., & ten Dijke, P. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00954-5 · Cited by 400 · see citing works
Liu, D., Black, B. L., & Derynck, R. (2001) · Genes & Development · doi:10.1101/gad.925901 · Cited by 399 · see citing works
Self-citationAkt interacts directly with Smad3 to regulate the sensitivity to TGF-β-induced apoptosis
Conery, A. R., Cao, Y., Thompson, E. A., Townsend, C. M., Ko, T. C., & Luo, K. (2004) · Nature Cell Biology · doi:10.1038/ncb1117 · Cited by 398 · see citing works
Smad2, Smad3 and Smad4 cooperate with Sp1 to induce p15Ink4B transcription in response to TGF‐β
Feng, X., Lin, X., & Derynck, R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.19.5178 · Cited by 397 · see citing works
Self-citationBlokzijl, A., Dahlqvist, C., Reissmann, E., Falk, A., Moliner, A., Lendahl, U., & Ibáñez, C. F. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200305112 · Cited by 396 · see citing works
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
Smad Proteins Bind a Conserved RNA Sequence to Promote MicroRNA Maturation by Drosha
Davis‐Dusenbery, B. N., Hilyard, A. C., Nguyen, P. H., Lagna, G., & Hata, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.011 · Cited by 384 · see citing works
Control of Smad7 Stability by Competition between Acetylation and Ubiquitination
Gronroos, E. C., Hellman, U., Heldin, C., & Ericsson, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00639-1 · Cited by 383 · see citing works
The SMAD2/3 interactome reveals that TGFβ controls m6A mRNA methylation in pluripotency
Bertero, A., Brown, S. E., Madrigal, P., Osnato, A., Ortmann, D., Yiangou, L., Kadiwala, J., Hubner, N. C., Mozos, I. R. D. L., Sadée, C., et al. (2018) · Nature · doi:10.1038/nature25784 · 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
Jiang, Z. Y., Zhou, Q. L., Coleman, K. A., Chouinard, M., Boese, Q., & Czech, M. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1332633100 · Cited by 378 · see citing works
Targeting of TAK1 in inflammatory disorders and cancer
Sakurai, H. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.06.007 · Cited by 377 · cited 16× · see citing works
“H. Sakurai, Targeting of TAK1 in inflammatory disorders and cancer.”
BackgroundInfluentialNodal Signals to Smads through Cripto-Dependent and Cripto-Independent Mechanisms
Yeo, C., & Whitman, M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00249-0 · Cited by 376 · cited 1× · see citing works
“Cripto enables Nodal binding to the activin receptor complex, thus activating Nodal signaling, whereas its absence promotes activin signaling and prevents Nodal signaling (75, 89, 90).”
BackgroundSignaling pathway cooperation in TGF-β-induced epithelial–mesenchymal transition
Derynck, R., Muthusamy, B.-P., & Saeteurn, K. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.09.001 · Cited by 373 · see citing works
Self-citationCross Talk among TGF- Signaling Pathways, Integrins, and the Extracellular Matrix
Munger, J. S., & Sheppard, D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005017 · Cited by 372 · see citing works
PKB/Akt modulates TGF-β signalling through a direct interaction with Smad3
Remy, I., Montmarquette, A., & Michnick, S. W. (2004) · Nature Cell Biology · doi:10.1038/ncb1113 · Cited by 371 · see citing works
Thuault, S., Tan, E., Peinado, H., Cano, A., Heldin, C., & Moustakas, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802016200 · Cited by 365 · see citing works
Structural Biology and Evolution of the TGF-β FamilyPreprint
Hinck, A. P., Mueller, T. D., & Springer, T. A. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022103 · Cited by 364 · 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
Determinants of specificity in TGF-β signal transductionPreprint
Chen, Y., Hata, A., Lo, R. S., Wotton, D., Shi, Y., Pavletich, N. P., & Massagué, J. (1998) · Genes & Development · doi:10.1101/gad.12.14.2144 · Cited by 361 · see citing works
Transcriptional Control by the SMADs
Hill, C. S. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022079 · Cited by 351 · see citing works
Repression of Runx2 function by TGF‐β through recruitment of class II histone deacetylases by Smad3
Kang, J. S., Alliston, T. N., Delston, R. B., & Derynck, R. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600729 · Cited by 344 · see citing works
Self-citationLévy, L., & Hill, C. S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.18.8108-8125.2005 · Cited by 343 · see citing works
FBN1: The disease-causing gene for Marfan syndrome and other genetic disorders
Sakai, L. Y., Keene, D. R., Renard, M., & Backer, J. F. A. D. (2016) · Gene · doi:10.1016/j.gene.2016.07.033 · Cited by 343 · see citing works
Schlunegger, M. P., & Grütter, M. G. (1992) · Nature · doi:10.1038/358430a0 · Cited by 336 · 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
Pradella, D., Naro, C., Sette, C., & Ghigna, C. (2017) · Molecular Cancer · doi:10.1186/s12943-016-0579-2 · Cited by 325 · 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
Lamouille, S., Connolly, E. C., Smyth, J. W., Akhurst, R. J., & Derynck, R. (2012) · Journal of Cell Science · doi:10.1242/jcs.095299 · Cited by 310 · see citing works
Self-citationEndocytic regulation of TGF-β signaling
Chen, Y. (2008) · Cell Research · doi:10.1038/cr.2008.315 · Cited by 309 · see citing works
BMP signalling: agony and antagony in the family
Brazil, D. P., Church, R. H., Surae, S., Godson, C., & Martin, F. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.004 · Cited by 306 · see citing works
Signaling by dual specificity kinases
Dhanasekaran, N., & Reddy, E. P. (1998) · Oncogene · doi:10.1038/sj.onc.1202251 · Cited by 304 · cited 1× · see citing works
“Similar to other dual-specificity kinases (69), TGF-b family receptors have a lower ability to phosphorylate on tyrosine than on serine and threonine (61, 67, 68).”
BackgroundCrystal Structure of a Phosphorylated Smad2
Wu, J.-W., Hu, M., Chai, J., Seoane, J., Huse, M., Li, C., Rigotti, D. J., Kyin, S., Muir, T. W., Fairman, R., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00421-x · Cited by 300 · see citing works
TRAF6, a molecular bridge spanning adaptive immunity, innate immunity and osteoimmunology
Wu, H., & Arron, J. R. (2003) · BioEssays · doi:10.1002/bies.10352 · Cited by 299 · see citing works
Structural Basis of Smad2 Recognition by the Smad Anchor for Receptor Activation
Wu, G., Chen, Y., Ozdamar, B., Gyuricza, C. A., Chong, P. A., Wrana, J. L., Massagué, J., & Shi, Y. (2000) · Science · doi:10.1126/science.287.5450.92 · Cited by 298 · see citing works
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 · see citing works
Kawabata, M., Inoue, H., Hanyu, A., Imamura, T., & Miyazono, K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.14.4056 · Cited by 289 · cited 2× · see citing works
“The association of R-Smadswith the receptor complexes then enables the type I receptor kinases to phosphorylate R-Smads at two C-terminal serines, thus promoting the dissociation of the two activated R-Smads from the receptors and their association with Smad4 in trimeric complexes (63, 151, 160, 161).”
BackgroundA Poised Chromatin Platform for TGF-β Access to Master Regulators
Xi, Q., Wang, Z., Zaromytidou, A.-I., Zhang, X. H.-F., Chow-Tsang, L.-F., Liu, J. X., Kim, H., Barlas, A., Manova-Todorova, K. O., Kaartinen, V., et al. (2011) · Cell · doi:10.1016/j.cell.2011.11.032 · Cited by 287 · see citing works
Transforming Growth Factor-β Receptors and Smads: Regulatory Complexity and Functional Versatility
Budi, E. H., Duan, D., & Derynck, R. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.04.005 · Cited by 287 · see citing works
Self-citationInsulin action on glucose transporters through molecular switches, tracks and tethers
Zaid, H., Antonescu, C. N., Randhawa, V. K., & Klip, A. (2008) · Biochemical Journal · doi:10.1042/bj20080723 · Cited by 286 · see citing works
Daly, A. C., Randall, R. A., & Hill, C. S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01192-08 · Cited by 280 · see citing works
Tang, L.-Y., Heller, M., Meng, Z., Yu, L., Tang, Y., Zhou, M., & Zhang, Y. E. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.773085 · Cited by 278 · see citing works
Germain, S., Howell, M. T., Esslemont, G., & Hill, C. S. (2000) · Genes & Development · doi:10.1101/gad.14.4.435 · Cited by 277 · see citing works
Neogenin mediates the action of repulsive guidance molecule
Rajagopalan, S., Deitinghoff, L., Davis, D., Conrad, S., Skutella, T., Chédotal, A., Mueller, B. K., & Strittmatter, S. M. (2004) · Nature Cell Biology · doi:10.1038/ncb1156 · Cited by 276 · see citing works
Force interacts with macromolecular structure in activation of TGF-β
Dong, X., Zhao, B., Iacob, R. E., Zhu, J., Koksal, A. C., Lu, C., Engen, J. R., & Springer, T. A. (2017) · Nature · doi:10.1038/nature21035 · Cited by 273 · see citing works
TGF-β Family Signaling in Mesenchymal DifferentiationPreprint
Grafe, I., Alexander, S., Peterson, J. R., Snider, T. N., Lévi, B., Lee, B., & Mishina, Y. M. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022202 · Cited by 272 · see citing works
Requirement for Activin a and Transforming Growth Factor--β1 Pro-Regions in Homodimer Assembly
Gray, A., & Mason, A. J. (1990) · Science · doi:10.1126/science.2315700 · Cited by 271 · see citing works
Matrix Metalloproteinase-14 (MT1-MMP)–Mediated Endoglin Shedding Inhibits Tumor Angiogenesis
Hawinkels, L. J. A. C., Kuiper, P., Wiercinska, E., Verspaget, H. W., Liu, Z., Pardali, E., Sier, C. F. M., & ten Dijke, P. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4466 · Cited by 270 · cited 1× · see citing works
“Like betaglycan, the ectodomain of endoglin can be proteolytically released and may thus serve as a soluble scavenger (84).”
BackgroundGADD34–PP1c recruited by Smad7 dephosphorylates TGFβ type I receptor
Shi, W., Sun, C., He, B., Xiong, W., Shi, X., Yao, D., & Cao, X. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307151 · Cited by 267 · see citing works
Lo, R. S., Chen, Y., Shi, Y., Pavletich, N. P., & Massagué, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.4.996 · Cited by 266 · see citing works
Ski and SnoN, potent negative regulators of TGF-β signaling
Deheuninck, J., & Luo, K. (2008) · Cell Research · doi:10.1038/cr.2008.324 · Cited by 257 · see citing works
Zhang, S., Fei, T., Zhang, L., Zhang, R., Chen, F., Ning, Y., Han, Y., Feng, X., Meng, A., & Chen, Y. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-06 · Cited by 257 · see citing works
Membrane protein GARP is a receptor for latent TGF‐β on the surface of activated human Treg
Stockis, J., Colau, D., Coulie, P. G., & Lucas, S. (2009) · European Journal of Immunology · doi:10.1002/eji.200939684 · Cited by 252 · see citing works
Galliher, A. J., & Schiemann, W. P. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3851 · Cited by 249 · see citing works
A Smad action turnover switch operated by WW domain readers of a phosphoserine codePreprint
Aragón, E., Goerner, N., Zaromytidou, A.-I., Xi, Q., Escobedo, A., Massagué, J., & Macías, M. J. (2011) · Genes & Development · doi:10.1101/gad.2060811 · Cited by 249 · see citing works
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 248 · see citing works
Little, S. C., & Mullins, M. C. (2009) · Nature Cell Biology · doi:10.1038/ncb1870 · Cited by 247 · cited 2× · see citing works
“Increasing evidence, however, much of it from developmental genetics, indicates or suggests that TGF-b family proteins often act as heterodimers with activities that are stronger or distinct from the homodimers, as illustrated with the heterodimers of BMP-2 and BMP7 (28) and Vg1 and Nodal (29, 30) (Fig.”
BackgroundAxin and GSK3-β control Smad3 protein stability and modulate TGF-β signalingPreprint
Guo, X., Ramirez, A., Waddell, D. S., Li, Z., Liu, X., & Wang, X. (2008) · Genes & Development · doi:10.1101/gad.1590908 · Cited by 247 · see citing works
The type III TGF-β receptor suppresses breast cancer progression
Dong, M., How, T., Kirkbride, K. C., Gordon, K. J., Lee, J. D., Hempel, N., Kelly, P., Moeller, B. J., Marks, J. R., & Blobe, G. C. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29293 · Cited by 246 · see citing works
Specificity of Drosophila Cytonemes for Distinct Signaling Pathways
Roy, S., Hsiung, F., & Kornberg, T. B. (2011) · Science · doi:10.1126/science.1198949 · Cited by 241 · see citing works
Kimura, N., Matsuo, R., Shibuyà, H., Nakashima, K., & Taga, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m908622199 · Cited by 240 · cited 1× · see citing works
“For example, Smad6 and Smad7 can inhibit BMP-induced p38MAPK activation (306), and Smad6 was reported to inhibit TGF-b–induced TAK1, JNK, and p38 MAPK activation (307).”
BackgroundTransforming Growth Factor β1 Induces Nuclear Export of Inhibitory Smad7
Itoh, S., Landström, M., Hermansson, A., Itoh, F., Heldin, C., Heldin, N., & ten Dijke, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.29195 · Cited by 239 · see citing works
Lai, C.-F., & Cheng, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200794200 · Cited by 238 · see citing works
Wang, Y.-K., Yu, X., Cohen, D. M., Wozniak, M. A., Yang, M. T., Gao, L., Eyckmans, J., & Chen, C. S. (2011) · Stem Cells and Development · doi:10.1089/scd.2011.0293 · Cited by 237 · see citing works
Nucleocytoplasmic shuttling of Smad proteins
Hill, C. S. (2008) · Cell Research · doi:10.1038/cr.2008.325 · Cited by 235 · see citing works
Alternatively Spliced Variant of Smad2 Lacking Exon 3
Yagi, K., Goto, D., Hamamoto, T., Takenoshita, S., Kato, M., & Miyazono, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.703 · Cited by 234 · see citing works
Kume, S., Haneda, M., Kanasaki, K., Sugimoto, T., Araki, S., Isshiki, K., Isono, M., Uzu, T., Guarente, L., Kashiwagi, A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605904200 · Cited by 231 · see citing works
The N domain of Smad7 is essential for specific inhibition of transforming growth factor-β signaling
Hanyu, A., Ishidou, Y., Ebisawa, T., Shimanuki, T., Imamura, T., & Miyazono, K. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200106023 · Cited by 229 · see citing works
Type I Transforming Growth Factor β Receptor Binds to and Activates Phosphatidylinositol 3-Kinase
Yi, J. Y., Shin, I., & Arteaga, C. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413223200 · Cited by 228 · see citing works
The corepressor CtBP interacts with Evi-1 to repress transforming growth factor β signaling
Izutsu, K., Kurokawa, M., Imai, Y., Maki, K., Mitani, K., & Hirai, H. (2001) · Blood · doi:10.1182/blood.v97.9.2815 · Cited by 227 · see citing works
Edlund, S., Bu, S., Schuster, N., Aspenström, P., Heuchel, R. L., Heldin, N., ten Dijke, P., Heldin, C., & Landström, M. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.02-03-0037 · Cited by 227 · see citing works
Ligand-dependent Degradation of Smad3 by a Ubiquitin Ligase Complex of ROC1 and Associated Proteins
Fukuchi, M., Imamura, T., Chiba, T., Ebisawa, T., Kawabata, M., Tanaka, K., & Miyazono, K. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.5.1431 · Cited by 226 · see citing works
Activation of p21ras by transforming growth factor beta in epithelial cells.
Mulder, K. M., & Morris, S. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42722-6 · Cited by 224 · see citing works
Bourguignon, L., Singleton, P. A., Zhu, H., & Zhou, B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204320200 · Cited by 224 · see citing works
TRAF4 Promotes TGF-β Receptor Signaling and Drives Breast Cancer Metastasis
Zhang, L., Zhou, F., de Vinuesa, A. G., de Kruijf, E. M., Mesker, W. E., Li, H., Drabsch, Y., Li, Y., Bauer, A., Rousseau, A., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.07.014 · Cited by 224 · see citing works
Hamidi, A., Song, J., Thakur, N., Itoh, S., Marcusson, A., Bergh, A. R. J., Heldin, C., & Landström, M. (2017) · Science Signaling · doi:10.1126/scisignal.aal4186 · Cited by 224 · see citing works
Castonguay, R., Werner, E. D., Matthews, R. G., Presman, E., Mulivor, A. W., Solban, N., Sako, D., Pearsall, R. S., Underwood, K. W., Seehra, J. S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.260133 · Cited by 221 · see citing works
Activation of LIMK1 by binding to the BMP receptor, BMPRII, regulates BMP‐dependent dendritogenesis
Lee-Hoeflich, S. T., Causing, C. G., Podkowa, M., Zhao, X., Wrana, J. L., & Attisano, L. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600418 · Cited by 220 · 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
Kuratomi, G., Komuro, A., Goto, K., Shinozaki, M., Miyazawa, K., Miyazono, K., & Imamura, T. (2005) · Biochemical Journal · doi:10.1042/bj20040738 · Cited by 217 · see citing works
Mitchell, H., Choudhury, A., Pagano, R. E., & Leof, E. B. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-03-0245 · Cited by 215 · see citing works
Crystal structure of the human TβR2 ectodomain–TGF-β3 complex
Hart, P. J., Deep, S., Taylor, A. B., Shu, Z., Hinck, C. S., & Hinck, A. P. (2002) · Nature Structural Biology · doi:10.1038/nsb766 · Cited by 214 · see citing works
Feng, X., & Derynck, R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3912 · Cited by 211 · see citing works
Self-citationTGF-β drives epithelial-mesenchymal transition through δEF1-mediated downregulation of ESRP
Horiguchi, K., Sakamoto, K., Koinuma, D., Semba, K., Inoue, A., Inoue, S., Fujii, H., Yamaguchi, A., Miyazawa, K., Miyazono, K., et al. (2011) · Oncogene · doi:10.1038/onc.2011.493 · Cited by 210 · see citing works
Dual Roles of Cripto as a Ligand and Coreceptor in the Nodal Signaling Pathway
Yan, Y., Liu, J.-J., Luo, Y., Chaosu, E., Haltiwanger, R. S., Abate-Shen, C. T., & Shen, M. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4439-4449.2002 · Cited by 209 · cited 1× · see citing works
“Cripto enables Nodal binding to the activin receptor complex, thus activating Nodal signaling, whereas its absence promotes activin signaling and prevents Nodal signaling (75, 89, 90).”
BackgroundStructural Basis of Heteromeric Smad Protein Assembly in TGF-β Signaling
Chacko, B. M., Qin, B. Y., Tiwari, A., Shi, G., Lam, S. S., Hayward, L. J., deCaestecker, M. P., & Lin, K. F. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.07.016 · Cited by 208 · see citing works
Komuro, A., Imamura, T., Saitoh, M., Yoshida, Y., Yamori, T., Miyazono, K., & Miyazawa, K. (2004) · Oncogene · doi:10.1038/sj.onc.1207885 · Cited by 205 · see citing works
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
Twisted gastrulation can function as a BMP antagonist
Chang, C., Holtzman, D. A., Chau, S., Chickering, T. W., Woolf, E. A., Holmgren, L. M., Bodorova, J., Gearing, D. P., Holmes, W. E., & Brivanlou, A. H. (2001) · Nature · doi:10.1038/35068583 · Cited by 202 · see citing works
Integration of TGF-ß and Ras/MAPK Signaling Through p53 Phosphorylation
Cordenonsi, M., Montagner, M., Adorno, M., Zacchigna, L., Martello, G., Mamidi, A., Soligo, S., Dupont, S., & Piccolo, S. (2007) · Science · doi:10.1126/science.1135961 · Cited by 202 · see citing works
Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads
Itoh, F., Asao, H., Sugamura, K., Heldin, C., ten Dijke, P., & Itoh, S. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4132 · Cited by 202 · see citing works
TGF-β 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
Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling
Scott, I., Blitz, I. L., Pappano, W., Maas, S. A., Cho, K. W. Y., & Greenspan, D. (2001) · Nature · doi:10.1038/35068572 · Cited by 195 · see citing works
USP15 is a deubiquitylating enzyme for receptor-activated SMADs
Inui, M., Manfrin, A., Mamidi, A., Martello, G., Morsut, L., Soligo, S., Enzo, E., Moro, S., Polo, S., Dupont, S., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2346 · Cited by 193 · see citing works
The Discovery and Early Days of TGF-β: A Historical PerspectivePreprint
Moses, H. L., Roberts, A. B., & Derynck, R. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021865 · Cited by 189 · see citing works
Self-citationThe Balance between Acetylation and Deacetylation Controls Smad7 Stability
Simonsson, M., Heldin, C., Ericsson, J., & Gronroos, E. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503134200 · Cited by 184 · see citing works
Emergence, development and diversification of the TGF-β signalling pathway within the animal kingdom
Huminiecki, Ł., Goldovsky, L., Freilich, S., Moustakas, A., Ouzounis, C. A., & Heldin, C. (2009) · BMC Evolutionary Biology · doi:10.1186/1471-2148-9-28 · Cited by 183 · see citing works
Regulating the stability of TGFβ receptors and Smads
Lönn, P., Morén, A., Raja, E., Dahl, M., & Moustakas, A. (2008) · Cell Research · doi:10.1038/cr.2008.308 · Cited by 183 · see citing works
TRAF6 ubiquitinates TGFβ type I receptor to promote its cleavage and nuclear translocation in cancer
Mu, Y., Sundar, R., Thakur, N., Ekman, M., Gudey, S. K., Yakymovych, M., Hermansson, A., Dimitriou, H., Bengoechea-Alonso, M. T., Ericsson, J., et al. (2011) · Nature Communications · doi:10.1038/ncomms1332 · Cited by 182 · see citing works
Hgs (Hrs), a FYVE Domain Protein, Is Involved in Smad Signaling through Cooperation with SARA
Miura, S., Takeshita, T., Asao, H., Kimura, Y., Murata, K., Sasaki, Y., Hanai, J., Beppu, H., Tsukazaki, T., Wrana, J. L., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9346-9355.2000 · Cited by 182 · see citing works
Liu, Y., Liu, H., Meyer, C., Li, J., Nadalin, S., Königsrainer, A., Weng, H., Dooley, S., & ten Dijke, P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.478685 · Cited by 181 · see citing works
Advances in kinase targeting: current clinical use and clinical trials
Rask‐Andersen, M., Zhang, J., Fabbro, D., & Schiöth, H. B. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.09.007 · Cited by 181 · see citing works
A Milieu Molecule for TGF-β Required for Microglia Function in the Nervous System
Qin, Y., Garrison, B. S., Ma, W., Wang, R., Jiang, A., Li, J., Mistry, M., Bronson, R. T., Santoro, D., Franco, C., et al. (2018) · Cell · doi:10.1016/j.cell.2018.05.027 · Cited by 180 · see citing works
Kurisaki, A., Kose, S., Yoneda, Y., Heldin, C., & Moustakas, A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.4.1079 · Cited by 176 · see citing works
Essential Role of TGF-β Signaling in Glucose-Induced Cell Hypertrophy
Wu, L., & Derynck, R. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.05.010 · Cited by 167 · see citing works
Self-citationStructural basis for the inhibition of activin signalling by follistatin
Harrington, A. E., Morris-Triggs, S. A., Ruotolo, B. T., Robinson, C. V., Ohnuma, S., & Hyvönen, M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601000 · Cited by 166 · see citing works
Sapkota, G. P., Knockaert, M., Alarcón, C. R., Montalvo, E., Brivanlou, A. H., & Massagué, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610172200 · Cited by 164 · see citing works
Smads orchestrate specific histone modifications and chromatin remodeling to activate transcription
Ross, S., Cheung, E. C. W., Petrakis, T. G., Howell, M. T., Kraus, W. L., & Hill, C. S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601332 · Cited by 163 · see citing works
Binding of two growth factor families to separate domains of the proteoglycan betaglycan.
Andres, J., DeFalcis, D., Noda, M., & Massagué, J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42643-9 · Cited by 160 · see citing works
Agricola, E., Randall, R. A., Gaarenstroom, T., Dupont, S., & Hill, C. S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.020 · Cited by 158 · see citing works
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 · cited 1× · see citing works
“Rather, the release of myostatin and GDF11 from latency depends on cleavage of the prodomain by BMP1 and mTolloid metalloproteases (50, 51).”
Background
Flagged first, then by citations
1 of the 347 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- [1]Derynck R, Miyazono K, The Biology of the TGF-β Family. (Cold Spring Harbor Laboratory Press, New York, ed. Derynck Rik, Miyazono Kohei 2016), pp. 1164.
Cited by
Sorted by citations
Inference and analysis of cell-cell communication using CellChat
Jin, S., Guerrero-Juarez, C. F., Zhang, L., Chang, I., Ramos, R., Kuan, C.-H., Myung, P., Plikus, M. V., & Nie, Q. (2021) · Nature Communications · doi:10.1038/s41467-021-21246-9 · Cited by 8,409 · see citing works
Liver Fibrosis: Mechanistic Concepts and Therapeutic Perspectives
Roehlen, N., Crouchet, E., & Baumert, T. F. (2020) · Cells · doi:10.3390/cells9040875 · Cited by 1,237 · see citing works
“Both the canonical and the non-canonical pathways contribute to HSCs activation but also to macrophages activation and polarization [136].”
BackgroundTGF-β-Mediated Epithelial-Mesenchymal Transition and Cancer Metastasis
Hao, Y., Baker, D. A., & ten Dijke, P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112767 · Cited by 1,155 · see citing works
TGFβ biology in cancer progression and immunotherapy
Derynck, R., Turley, S. J., & Akhurst, R. J. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0403-1 · Cited by 944 · see citing works
Self-citationExtracellular matrix and its therapeutic potential for cancer treatment
Huang, J., Zhang, L., Wan, D., Zhou, L., Zheng, S., Lin, S., & Qiao, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00544-0 · Cited by 962 · see citing works
Tzavlaki, K., & Moustakas, A. (2020) · Biomolecules · doi:10.3390/biom10030487 · Cited by 816 · see citing works
“Authoritative accounts for many such proteins can be found in relatively recent articles, and we direct the reader to these articles for deeper or more comprehensive reading on this important topic [10,11].”
BackgroundInfluentialTGF-β in Hepatic Stellate Cell Activation and Liver Fibrogenesis—Updated 2019
Dewidar, B., Meyer, C., Dooley, S., & Meindl-Beinker, A. N. (2019) · Cells · doi:10.3390/cells8111419 · Cited by 837 · see citing works
Fibroblast and myofibroblast activation in normal tissue repair and fibrosis
Younesi, F. S., Miller, A. E., Barker, T. H., Rossi, F. M. V., & Hinz, B. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00716-0 · Cited by 711 · see citing works
Cellular mechanotransduction in health and diseases: from molecular mechanism to therapeutic targets
Di, X., Gao, X., Peng, L., Ai, J., Jin, X., Qi, S., Li, H., Wang, K., & Luo, D. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01501-9 · Cited by 659 · see citing works
“The Smad family proteins, which are the central transducers of the TGFβ signaling pathway, are classified as R-Smad, inhibitory Smad (I-Smad), and universal Smad (co-Smad, Smad4).(347) In R-Smad, Smad2/3 are considered the main mediators of the TGFβ signaling pathway, and Smad1/5/8 mediate the BMP signaling pathway.”
Targeting cytokine and chemokine signaling pathways for cancer therapy
Yi, M., Li, T., Niu, M., Zhang, H., Wu, Y., Wu, K., & Dai, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01868-3 · Cited by 491 · see citing works
TGF-β1 – A truly transforming growth factor in fibrosis and immunity
Lodyga, M., & Hinz, B. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.12.010 · Cited by 462 · see citing works
Wu, M., Wu, S., Chen, W., & Li, Y.-P. (2024) · Cell Research · doi:10.1038/s41422-023-00918-9 · Cited by 445 · see citing works
Targeting TGFβ signal transduction for cancer therapy
Liu, S., Ren, J., & ten Dijke, P. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00436-9 · Cited by 413 · 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
“Characteristic combinations of seven type I receptors (activin receptor-like kinase 1-7, ALK1-7) and five type II receptors (TβRII, ActRIIA, ActRIIB, BMPRII, and AMHRII) correspond to signal transduction by individual members of the TGF-β family [18,19].”
BackgroundOvercoming TGFβ-mediated immune evasion in cancer
Tauriello, D. V. F., Sancho, E., & Batlle, E. (2022) · Nature Reviews Cancer · doi:10.1038/s41568-021-00413-6 · Cited by 377 · see citing works
Intricacies of TGF-β signaling in Treg and Th17 cell biology
Wang, J., Zhao, X., & Wan, Y. Y. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01036-7 · Cited by 377 · see citing works
Wang, L., & He, C.-Q. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.967193 · Cited by 352 · see citing works
“Under the effects of MMPs and/or serine proteases (for example, cathepsins), TGF-b proteins are released from the complex of ECM (86).”
BackgroundInfluentialPakshir, P., Noskovicova, N., Lodyga, M., Son, D. O., Schuster, R., Goodwin, A., Karvonen, H., & Hinz, B. (2020) · Journal of Cell Science · doi:10.1242/jcs.227900 · Cited by 293 · see citing works
TGF ‐β as a driver of fibrosis: physiological roles and therapeutic opportunities
Budi, E. H., Schaub, J. R., Decaris, M. L., Turner, S., & Derynck, R. (2021) · The Journal of Pathology · doi:10.1002/path.5680 · Cited by 300 · see citing works
“While Smad signaling uniquely de fi nes ‘ canonical ’ signaling for the TGF-β family proteins, TGF-β also activates non-Smad signaling pathways, including the PI3K – Akt – mTOR pathway, Erk MAPK and p38 MAPK signaling, and Src and Rho GTPases [48,74] (Figure 3).”
BackgroundInfluentialSelf-citationTranscription factors: Bridge between cell signaling and gene regulation
Weidemüller, P., Kholmatov, M. M., Petsalaki, E., & Zaugg, J. B. (2021) · PROTEOMICS · doi:10.1002/pmic.202000034 · Cited by 282 · see citing works
Signaling pathways in cancer‐associated fibroblasts: recent advances and future perspectives
Fang, Z., Meng, Q., Xu, J., Wang, W., Zhang, B., Liu, J., Liang, C., Hua, J., Zhao, Y., Yu, X., et al. (2022) · 癌症:英文版 · doi:10.1002/cac2.12392 · Cited by 292 · see citing works
“The secretion and deposition of TGF-β from the latent complex is triggered by an activation mechanism that locally releases activated TGF-β [95].”
BackgroundThe role of hepatokines in NAFLD
Stefan, N., Schick, F., Birkenfeld, A. L., Häring, H., & White, M. F. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.01.006 · Cited by 282 · see citing works
Pre-metastatic niche: formation, characteristics and therapeutic implication
Wang, Y., Jia, J., Wang, F., Fang, Y., Yang, Y., Zhou, Q., Yuan, W., Gu, X., Hu, J., & Yang, S. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01937-7 · Cited by 275 · see citing works
TGF-β-Induced Endothelial to Mesenchymal Transition in Disease and Tissue Engineering
Ma, J., Sánchez‐Duffhues, G., Goumans, M., & ten Dijke, P. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00260 · Cited by 247 · see citing works
“These complexes can translocate into the nucleus, where they regulate specific gene transcriptional responses (Shi and Massagué, 2003; Derynck and Budi, 2019).”
BackgroundTransforming growth factor–β1 in regulatory T cell biology
Moreau, J. M., Velegraki, M., Bolyard, C. M., Rosenblum, M. D., & Li, Z. (2022) · Science Immunology · doi:10.1126/sciimmunol.abi4613 · Cited by 247 · see citing works
“Therefore, TGF-1–induced Foxp3 expression in tTregs may occur through a noncanonical pathway, which does not require direct Smad binding to the Foxp3 locus and may occur independently of Smad signaling altogether (36, 52).”
BackgroundTGFβ-induced metabolic reprogramming during epithelial-to-mesenchymal transition in cancer
Hua, W., ten Dijke, P., Kostidis, S., Giera, M. A., & Hornsveld, M. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03398-6 · Cited by 237 · see citing works
“TGFβ induces the formation of heteromeric complexes in which the TGFβR2 kinase phosphorylates TGFβR1 [10].”
BackgroundInfluentialPathobiology of the Klotho Antiaging Protein and Therapeutic Considerations
Prud’homme, G. J., Kurt, M., & Wang, Q. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.931331 · Cited by 225 · see citing works
“TGF-β signaling and its regulation are complex (Mullen and Wrana, 2017; Derynck and Budi, 2019; Aashaq et al., 2022), and only a brief outline is provided here.”
BackgroundKatsuno, Y., Meyer, D. S., Zhang, Z., Shokat, K. M., Akhurst, R. J., Miyazono, K., & Derynck, R. (2019) · Science Signaling · doi:10.1126/scisignal.aau8544 · Cited by 219 · see citing works
“The activated Smad proteins form complexes with Smad4 and regulate target gene expression through association with high-affinity DNA binding transcription factors at regulatory sequences (11, 12).”
Self-citationTGF‐β signaling: A recap of SMAD‐independent and SMAD‐dependent pathways
Aashaq, S., Batool, A., Mir, S. A., Beigh, M. A., Andrabi, K. I., & Shah, Z. A. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30529 · Cited by 215 · see citing works
“Dysregulation of TGF‐β signaling results in the development of various diseases like cancer and fibrotic diseases and also leads to various developmental defects (Rik Derynck & Budi, 2019).”
BackgroundEpithelial plasticity, epithelial-mesenchymal transition, and the TGF-β family
Katsuno, Y., & Derynck, R. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.028 · Cited by 187 · see citing works
Self-citationCorneal stromal wound healing: Major regulators and therapeutic targets
Kamil, S., & Mohan, R. R. (2020) · The Ocular Surface · doi:10.1016/j.jtos.2020.10.006 · Cited by 192 · see citing works
Implant Fibrosis and the Underappreciated Role of Myofibroblasts in the Foreign Body Reaction
Noskovicova, N., Hinz, B., & Pakshir, P. (2021) · Cells · doi:10.3390/cells10071794 · Cited by 184 · see citing works
Extracellular Matrix Remodeling in Chronic Liver Disease
Ortiz, C., Schierwagen, R., Schaefer, L., Klein, S., Trepat, X., & Trebicka, J. (2021) · Current Tissue Microenvironment Reports · doi:10.1007/s43152-021-00030-3 · Cited by 183 · see citing works
CellPhoneDB v5: inferring cell–cell communication from single-cell multiomics data
Troulé, K., Petryszak, R., Çakır, B., Cranley, J. J., Harasty, A., Prete, M., Tuong, Z. K., Teichmann, S. A., García‐Alonso, L., & Vento-Tormo, R. (2025) · Nature Protocols · doi:10.1038/s41596-024-01137-1 · Cited by 199 · see citing works
“…complexes, as (1) some proteins only function when all subunits are present (that is, expressed), and (2) different subunit combinations can alter binding specificity, enabling complexes to bind distinct ligands and activate unique downstream signals or transcription factors (TFs) 20,21 .”
TGF-beta signal transduction: biology, function and therapy for diseases
Tie, Y., Tang, F., Peng, D., Zhang, Y., & Shi, H. (2022) · Molecular Biomedicine · doi:10.1186/s43556-022-00109-9 · Cited by 178 · see citing works
“The adaptor protein 1 complexes are activated by the ERK, JNK, and MAPK pathways [4, 118, 119].”
BackgroundInfluentialA Perspective on the Development of TGF-β Inhibitors for Cancer Treatment
Huynh, L., Hipolito, C. J., & ten Dijke, P. (2019) · Biomolecules · doi:10.3390/biom9110743 · Cited by 172 · see citing works
“It plays an important role in embryogenesis and in maintaining tissue homeostasis in multicellular organisms [1,2].”
BackgroundEpithelial-Mesenchymal Transition (EMT) as a Therapeutic Target
Jonckheere, S., Adams, J., Groote, D. D., Campbell, K., Berx, G., & Goossens, S. (2021) · Cells Tissues Organs · doi:10.1159/000512218 · Cited by 173 · see citing works
“The best-known inducer of EMT is TGF-β [Thiery et al., 2009; Fabregat et al., 2014; Lamouille et al., 2014; Zarzynska, 2014], a multifunctional cytokine belonging to a larger family of structurally and functionally related proteins including activins/inhibins and the BMPs [Derynck and Budi, 2019].”
BackgroundThe role of TGF-beta3 in cartilage development and osteoarthritis
Du, X., Cai, L., Xie, J., & Zhou, X. (2023) · Bone Research · doi:10.1038/s41413-022-00239-4 · Cited by 165 · see citing works
“ALK4/5/7 proteins phosphorylate Smad2/3, and Smad2/3/4 complexes, which bind to the GTCTAGAC sequence.(53) I-Smad proteins inhibit TGF-β3-triggered R-Smad signaling pathways by directly binding to R-Smads and blocking their modification, including phosphorylation and threonylation.”
BackgroundCellular rejuvenation: molecular mechanisms and potential therapeutic interventions for diseases
Ji, S., Xiong, M., Chen, H., Liu, Y., Zhou, L., Hong, Y., Wang, M., Wang, C., Fu, X., & Sun, X. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01343-5 · Cited by 166 · see citing works
“More importantly, dysregulation of the TGF-β/SMAD pathway is reported as an essential causative agent in tissue fibrosis, like hepatic, pulmonary, and cardiac fibrosis.(157) TGF-β modulates several intracellular signaling cascades to deliver profibrotic effects, and the numerous ways of TGF-β interacting with other pr…”
BackgroundContreras, O., Rossi, F. M. V., & Théret, M. (2021) · Skeletal Muscle · doi:10.1186/s13395-021-00265-6 · Cited by 156 · see citing works
“TGF-β enhances the proliferation and differentiation of several cell types, including stromal cells (for review, see [123, 124].”
BackgroundTransforming growth factor-β signaling: From tissue fibrosis to therapeutic opportunities
Ren, L., Li, X., Duan, T., Li, Z.-H., Yang, J., Zhang, Y., Zou, L., Miao, H., & Zhao, Y. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110289 · Cited by 155 · see citing works
TGF-β signaling in intervertebral disc health and disease
Chen, S., Liu, S., Ma, K., Zhao, L., Lin, H., & Shao, Z. (2019) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2019.05.005 · Cited by 147 · see citing works
Aortic aneurysms: current pathogenesis and therapeutic targets
Cho, M. J., Lee, M.-R., & Park, J. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01130-w · Cited by 142 · see citing works
Keloid disorder: Fibroblast differentiation and gene expression profile in fibrotic skin diseases
Macarak, E. J., Wermuth, P. J., Rosenbloom, J., & Uitto, J. (2020) · Experimental Dermatology · doi:10.1111/exd.14243 · Cited by 142 · see citing works
An overview of signaling pathways regulating YAP/TAZ activity
Heng, B. C., Zhang, X., Aubel, D., Bai, Y., Li, X., Yan, W., Fussenegger, M., & Deng, X. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03579-8 · Cited by 140 · see citing works
TGFβ control of immune responses in cancer: a holistic immuno-oncology perspective
Nixon, B. G., Gao, S., Wang, X., & Li, M. O. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00796-z · Cited by 138 · see citing works
TGFβ2 and TGFβ3 isoforms drive fibrotic disease pathogenesis
Sun, T., Huang, Z., Liang, W.-C., Yin, J., Lin, W. Y., Wu, J., Vernes, J.-M., Lutman, J., Caplazi, P., Jeet, S., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe0407 · Cited by 134 · see citing works
Targeting immunosuppression by TGF-β1 for cancer immunotherapy
de Streel, G., & Lucas, S. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114697 · Cited by 129 · see citing works
Wu, B., Zhang, S., Guo, Z., Bi, Y., Zhou, M., Li, P., Seyedsadr, M., Xu, X., Li, J., Markovic‐Plese, S., et al. (2021) · Immunity · doi:10.1016/j.immuni.2020.12.010 · Cited by 122 · see citing works
“Both ActivinA and TGF-β1 induce the phosphorylation of Smad2 and Smad3 and the degradation of SKI protein (Derynck and Budi, 2019; Zhang et al., 2017).”
BackgroundDinnon, K. H., Leist, S. R., Okuda, K., Dang, H., Fritch, E. J., Gully, K. L., la Cruz, G. D., Evangelista, M. D., Asakura, T., Gilmore, R. C., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abo5070 · Cited by 133 · see citing works
“6I), suggesting posttranslational rather than transcriptional regulation of TGF- signaling (52).”
Roles of TGF-β signaling pathway in tumor microenvirionment and cancer therapy
Zhao, H., Wei, J., & Sun, J. M. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.107101 · Cited by 117 · see citing works
The role of endothelial cell–pericyte interactions in vascularization and diseases
Li, G., Gao, J., Ding, P., & Gao, Y. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.01.016 · Cited by 115 · see citing works
Distinct inflammatory and wound healing responses to complex caudal fin injuries of larval zebrafish
Miskolci, V., Squirrell, J. M., Rindy, J., Vincent, W. J. B., Sauer, J., Gibson, A. L. F., Eliceiri, K. W., & Anna Huttenlocher, A. (2019) · eLife · doi:10.7554/elife.45976 · Cited by 114 · see citing works
Signaling Pathways That Regulate the Crustacean Molting Gland
Mykles, D. L. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.674711 · Cited by 111 · see citing works
Xia, Y., Inoue, K., Du, Y., Baker, S. J., Reddy, E. P., Greenblatt, M. B., & Zhao, B. (2022) · Nature Communications · doi:10.1038/s41467-022-31475-1 · Cited by 110 · see citing works
Si, D., Ageeva, E. S., & Żukow, W. (2022) · Journal of Education Health and Sport · doi:10.12775/jehs.2022.12.08.074 · Cited by 105 · see citing works
Fibrosis in Chronic Kidney Disease: Pathophysiology and Therapeutic Targets
Reiss, A. B., Jacob, B., Zubair, A. S., Srivastava, A., Johnson, M., & Leon, J. D. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13071881 · Cited by 105 · see citing works
“Smad2 and Smad3 then form a complex with Smad4 that translocates to the nucleus [111,112].”
BackgroundReparative and Maladaptive Inflammation in Tendon Healing
Arvind, V., & Huang, A. H. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.719047 · Cited by 104 · see citing works
Colchicine acts selectively in the liver to induce hepatokines that inhibit myeloid cell activation
Weng, J., Koch, P. D., Luan, H. H., Tu, H.-C., Shimada, K., Ngan, I., Ventura, R., Jiang, R., & Mitchison, T. J. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00366-y · Cited by 103 · see citing works
Tao, R., Han, X., Bai, X., Yu, J., Ma, Y.-W., Chen, W., Zhang, D., & Li, Z. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1354825 · Cited by 105 · see citing works
Current perspectives on inhibitory SMAD7 in health and disease
van Capelle, C. D. C., Spit, M., & ten Dijke, P. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828260 · Cited by 100 · see citing works
Sex‐specific aging in animals: Perspective and future directions
Bronikowski, A., Meisel, R., Biga, P. R., Walters, J., Mank, J., Larschan, E. N., Wilkinson, G., Valenzuela, N., Conard, A., de Magalhães, J. D., et al. (2022) · Aging Cell · doi:10.1111/acel.13542 · Cited by 78 · see citing works
Sundqvist, A., Vasilaki, E., Voytyuk, O., Bai, Y., Morikawa, M., Moustakas, A., Miyazono, K., Heldin, C., ten Dijke, P., & van Dam, H. (2020) · Oncogene · doi:10.1038/s41388-020-1299-z · Cited by 98 · see citing works
TGF-β Promotes Metabolic Reprogramming in Lung Fibroblasts via mTORC1-dependent ATF4 Activation
O’Leary, E. M., Tian, Y., Niğdelioğlu, R., Witt, L. J., Çetin-Atalay, R., Meliton, A. Y., Woods, P. S., Kimmig, L. M., Sun, K. A., Gökalp, G. A., et al. (2020) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2020-0143oc · Cited by 97 · see citing works
Dual inhibition of αvβ6 and αvβ1 reduces fibrogenesis in lung tissue explants from patients with IPF
Decaris, M. L., Schaub, J. R., Chen, C., Cha, J., Lee, G. G., Rexhepaj, M., Ho, S. S., Rao, V., Marlow, M. M., Kotak, P., et al. (2021) · Respiratory Research · doi:10.1186/s12931-021-01863-0 · Cited by 94 · see citing works
Self-citationGonzález-Loyola, A., Bovay, E., Kim, J., Lozano, T. W., Sabine, A., Renevey, F., Arroz-Madeira, S., Rapin, A., Wypych, T. P., Rota, G., et al. (2021) · Science Advances · doi:10.1126/sciadv.abf4335 · Cited by 94 · see citing works
The Interplay Between TGF-β Signaling and Cell Metabolism
Liu, H., & Chen, Y. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.846723 · Cited by 98 · see citing works
TGF-β: A novel predictor and target for anti-PD-1/PD-L1 therapy
Yi, M., Li, T., Niu, M., Wu, Y., Zhao, Z., & Wu, K. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1061394 · Cited by 94 · see citing works
“Following the recruitment and phosphorylation of TGF-b type I receptors (TGFbRI) by TGFbRII , SMAD2 and SMAD3 are phosphorylated and further assembled into trimeric complexes with SMAD4 (6).”
BackgroundThe TGF-β Pathway: A Pharmacological Target in Hepatocellular Carcinoma?
Gonzalez‐Sanchez, E., Vaquero, J., Fernández‐Barrena, M. G., Lasarte, J. J., Avila, M. A., Sarobe, P., Reig, M., Calvo, M., & Fabregat, I. (2021) · Cancers · doi:10.3390/cancers13133248 · Cited by 95 · see citing works
“In addition to the SMAD pathway, TGF-β can also initiate multiple non-SMAD or noncanonical signaling pathways (Figure 1A) [10,11].”
BackgroundInfluentialTGFβ-Directed Therapeutics: 2020
Teicher, B. A. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107666 · Cited by 92 · see citing works
“The TGFβ2 crystal structure elucidated two monomers, each with two antiparallel pairs of β-strands that form a flat surface and a separate α–helix (10, 11).”
BackgroundReceptor binding competition: A paradigm for regulating TGF-β family action
Martı́nez-Hackert, E., Sundan, A., & Holien, T. (2020) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2020.09.003 · Cited by 91 · see citing works
TGFβ family signaling and development
Jia, S., & Meng, A. (2021) · Development · doi:10.1242/dev.188490 · Cited by 91 · see citing works
Metabolic requirements of pulmonary fibrosis: role of fibroblast metabolism
Hamanaka, R. B., & Mutlu, G. M. (2021) · FEBS Journal · doi:10.1111/febs.15693 · Cited by 90 · see citing works
Hormonal control of the crustacean molting gland: Insights from transcriptomics and proteomics
Mykles, D. L., & Chang, E. S. (2020) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2020.113493 · Cited by 88 · see citing works
Signaling pathways and targeted therapeutic strategies for polycystic ovary syndrome
Wang, K., & Lǐ, Y. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1191759 · Cited by 99 · see citing works
Emerging Roles of Macrophage Polarization in Osteoarthritis: Mechanisms and Therapeutic Strategies
Yuan, Z. L., Jiang, D., Yang, M., Tao, J., Hu, X., Yang, X., & Zeng, Y. (2024) · Orthopaedic Surgery · doi:10.1111/os.13993 · Cited by 87 · see citing works
The Pathogenesis of Hydrocephalus Following Aneurysmal Subarachnoid Hemorrhage
Kuo, L., & Huang, A. P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22095050 · Cited by 85 · see citing works
“Decorin also impedes activation of TGF-β receptors and inhibits downstream signaling pathways by competitive inhibition [64,65].”
BackgroundLi, Y., Fan, W., Link, F., Wang, S., & Dooley, S. (2021) · JHEP Reports · doi:10.1016/j.jhepr.2021.100397 · Cited by 88 · see citing works
“Activated receptor complexes are usually internalised for signalling and subsequently undergo either proteasomal degradation or recycling to the cell surface.(16,17) These processes have a”
BackgroundPreininger, M. K., & Kaufer, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116217 · Cited by 84 · see citing works
TGFβ signaling pathways in human health and disease
Chen, P., Qin, L., & Simons, M. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1113061 · Cited by 84 · see citing works
“During development, all three TGFβ ligands are produced by a number of different cell types (Pelton et al., 1991; Derynck and Budi, 2019).”
BackgroundThe Synergistic Cooperation between TGF-β and Hypoxia in Cancer and Fibrosis
Mallikarjuna, P., Zhou, Y., & Landström, M. (2022) · Biomolecules · doi:10.3390/biom12050635 · Cited by 82 · see citing works
“The intracellular Smad2/3 are next activated by phosphorylation, initiated by TGFβRI; pSmad2/3 form a complex with Smad4 and, together with certain transcriptio factors (TF), activ te specific targets genes that contain Smad-binding elements (SBEs), implicated in growth inhibition, apoptosis, ECM synthesis, and immune…”
BackgroundInfluentialvan den Bosch, M. H. J., Blom, A. B., & van der Kraan, P. M. (2023) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2023.12.005 · Cited by 86 · see citing works
Ashrafizadeh, M., Zarrabi, A., Hushmandi, K., Zarrin, V., Moghadam, E. R., Hashemi, F., Makvandi, P., Samarghandian, S., Khan, H. Z., Hashemi, F., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.585413 · Cited by 79 · see citing works
“Next, proteolytic cleavage of disulfide bonds by furin family proteins result in generation of two characteristic proteins including N-terminal long dimeric and disulfide-linked propeptide, known as latencyassociated peptide (LAP) and C-terminal short dimeric disulfidelinked polypeptide, known as mature TGF-β (Ten Dij…”
BackgroundTGFβ-induced fibroblast activation requires persistent and targeted HDAC-mediated gene repression
Jones, D. L., Haak, A. J., Caporarello, N., Choi, K. M., Ye, Z., Yan, H., Varelas, X., Ordog, T., Ligresti, G., & Tschumperlin, D. J. (2019) · Journal of Cell Science · doi:10.1242/jcs.233486 · Cited by 77 · see citing works
“…The transcriptional effects of TGFβ are known to be mediated by a complex network of canonical and non-canonical pathways and transcriptional complexes including SMAD (or non-canonical) transcriptional effectors that may link to HDACs to mediate repressive functions (Derynck and Budi, 2019).”
BackgroundTherapeutic targeting of TGF-β in cancer: hacking a master switch of immune suppression
van den Bulk, J., de Miranda, N. F. C. C., & ten Dijke, P. (2021) · Clinical Science · doi:10.1042/cs20201236 · Cited by 75 · see citing works
Transforming growth factor-beta (TGF-β) in prostate cancer: A dual function mediator?
Mirzaei, S., Paskeh, M. D. A., Saghari, Y., Zarrabi, A., Hamblin, M. R., Entezari, M., Hashemi, M., Aref, A. R., Hushmandi, K., Kumar, A. P., et al. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.02.094 · Cited by 74 · see citing works
Khan, I., Rahman, S. U., Tang, E., Engel, K. W., Hall, B., Kulkarni, A. B., & Arany, P. R. (2021) · Scientific Reports · doi:10.1038/s41598-021-92650-w · Cited by 76 · see citing works
Bu, M. T., Chandrasekhar, P., Ding, L., & Hugo, W. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108211 · Cited by 72 · see citing works
“There are multiple excellent reviews covering the details of the TGF-β family proteins and their related signaling pathways (Derynck & Budi, 2019; Derynck & Zhang, 2003; Glasgow & Mishra, 2008; Haque & Morris, 2017; Massagué, Blain, & Lo, 2000; Morikawa et al., 2016; Shi & Massagué, 2003; Smith,…”
BackgroundTGF-β1 dominates stromal fibroblast-mediated EMT via the FAP/VCAN axis in bladder cancer cells
Ping, Q., Wang, C., Cheng, X., Zhong, Y., Yan, R., Yang, M., Shi, Y., Li, X., Li, X., Huang, W., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04303-3 · Cited by 73 · see citing works
Understanding the mechanism of radiation induced fibrosis and therapy options
Ejaz, A., Greenberger, J. S., & Rubin, P. J. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107399 · Cited by 73 · see citing works
Valle-Tenney, R., Rebolledo, D. L., Lipson, K. E., & Brandan, E. (2019) · Matrix Biology · doi:10.1016/j.matbio.2019.09.003 · Cited by 71 · see citing works
Yang, D., Dai, F., Yuan, M., Zheng, Y., Liu, S., Deng, Z., Tan, W., Chen, L., Zhang, Q., Zhao, X., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.689181 · Cited by 78 · see citing works
Correlation between Oxidative Stress and Transforming Growth Factor-Beta in Cancers
Chung, J., Huda, M. N., Shin, Y., Han, S., Akter, S., Kang, I., Ha, J., Choe, W., Choi, T. G., & Kim, S. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413181 · Cited by 69 · see citing works
“effector molecules in the TGF-β signaling pathway [55].”
BackgroundContextual Regulation of TGF-β Signaling in Liver Cancer
Tu, S., Huang, W., Huang, C., Luo, Z., & Yan, X. (2019) · Cells · doi:10.3390/cells8101235 · Cited by 70 · see citing works
“TGF-β is a prototype of the TGF-β family cytokines, which is composed of 33 members in mammals according to their genomes [25].”
BackgroundInfluentialEpithelial–Mesenchymal Transition Mechanisms in Chronic Airway Diseases: A Common Process to Target?
Mottais, A., Riberi, L., Falco, A., Soccal, S., Gohy, S. T., & Rose, V. D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512412 · Cited by 72 · see citing works
“TGF-β1 is the first isoform to have been identified [25], and it has been found to play a crucial role in fibrotic lung diseases [26,32–37], particularly in airway remodelling [38,39].”
BackgroundBathish, B., Robertson, H., Dillon, J. F., Dinkova‐Kostova, A. T., & Hayes, J. D. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.06.226 · Cited by 68 · see citing works
Anti-Inflammatory Role of the Klotho Protein and Relevance to Aging
Prud’homme, G. J., & Wang, Q. (2024) · Cells · doi:10.3390/cells13171413 · Cited by 69 · see citing works
Merčnik, M. H., Schliefsteiner, C., Sánchez‐Duffhues, G., & Wadsack, C. (2024) · Human Reproduction Update · doi:10.1093/humupd/dmae007 · Cited by 72 · see citing works
“Of note, on certain occasions, TGF b s, activins, and GDFs can activate both Smad1/5/8 and Smad2/3 signalling.”
BackgroundInfluentialChen, Y., Fan, Y., Guo, D.-Y., Xu, B., Shi, X.-Y., Li, J.-T., & Duan, L.-F. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110413 · Cited by 63 · see citing works
TGF-β Pathway in Salivary Gland Fibrosis
Zhang, X., Yun, J. S., Han, D., Yook, J. I., Kim, H. S., & Cho, E. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239138 · Cited by 63 · see citing works
- Authors
- Derynck, R., & Budi, E. H.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Derynck, Rik
- Venue
- Science Signaling
- Published
- 2019-02-26
- Volume
- 12
- Issue
- 570
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- PMC
- PMC6800142
- OpenAlex
- W2917714624
- Cited by
- 785
- References
- 347
- Citations by year
- 2026: 83 · 2025: 85 · 2024: 129 · 2023: 118 · 2022: 102 · 2021: 152 · 2020: 77 · 2019: 35 · 2018: 1
- FWCI
- 8.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute (RO1-CA63101, RO1-CA136690)
- JDRF (3-APF-2017-392-A-N)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- Smad proteins, TGF-beta receptor, dual-specificity kinase, signaling crosstalk, non-Smad signaling, cancer, fibrosis, developmental anomalies
- MeSH terms
- Animals, Cell Differentiation, Gene Expression Regulation, Humans, Ligands, Neoplasms, Protein Binding, Signal Transduction, Transforming Growth Factor beta, Receptors, Transforming Growth Factor beta
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 ›
Are you an author, or do you see a problem with this page? Request a review