The DOI matches its Crossref record; 37 of the 39 references it cites were found in a registry or an index.
TGF-β inhibits p70 S6 kinase via protein phosphatase 2A to induce G1 arrest
Open accessAbstract
On TGF-beta binding, the TGF-beta receptor directly phosphorylates and activates the transcription factors Smad2/3, leading to G(1) arrest. Here, we present evidence for a second, parallel, TGF-beta-dependent pathway for cell cycle arrest, achieved via inhibition of p70(s6k). TGF-beta induces association of its receptor with protein phosphatase-2A (PP2A)-Balpha. Concomitantly, three PP2A-subunits, Balpha, Abeta, and Calpha, associate with p70(s6k), leading to its dephosphorylation and inactivation. Although either pathway is sufficient to induce G(1) arrest, abrogation of both, the inhibition of p70(s6k), and transcription through Smad proteins is required for release of epithelial cells from TGF-beta-induced G(1) arrest. TGF-beta thereby modulates the translational and posttranscriptional control of cell cycle progression.
Overview
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
Verification
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?
In the citing paper
“In the PI3K/AKT pathway, both PI3K and AKT downstream signaling factors are substrates of PP2A (Kuo et al., 2008; Petritsch et al., 2000).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Petritsch et al., 2000
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Production of high-titer helper-free retroviruses by transient transfection.
Pear, W. S., Nolan, G. P., Scott, M. L., & Baltimore, D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8392 · Cited by 2,267
Controlling TGF-beta signaling.
Massagué, J., & Chen, Y. (2000) · PubMed · Cited by 1,780
Controlling TGF-β signalingPreprint
Massagué, J., & Chen, Y. (2000) · Genes & Development · doi:10.1101/gad.14.6.627 · Cited by 1,589
Cheatham, B., Vlahos, C. J., Cheatham, L. A., Wang, L., Blenis, J., & Kahn, C. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4902-4911.1994 · Cited by 1,062
Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
Lagna, G., Hata, A., Hemmati‐Brivanlou, A., & Massagué, J. (1996) · Nature · doi:10.1038/383832a0 · Cited by 905
Yang, X. Y., Letterio, J. J., Lechleider, R. J., Chen, L., Hayman, R., Gu, H., Roberts, A. B., & Deng, C. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1280 · Cited by 889
Receptor-associated Mad homologues synergize as effectors of the TGF-β response
Zhang, Y. E., Feng, X., Wu, R.-Y., & Derynck, R. (1996) · Nature · doi:10.1038/383168a0 · Cited by 873
Eppert, K., Scherer, S. W., Özçelik, H., Pirone, R., Hoodless, P. A., Kim, H., Tsui, L.-C., Bapat, B. V., Gallinger, S., Andrulis, I. L., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)80128-2 · Cited by 845
Phosphorylation and Activation of p70 s6k by PDK1
Pullen, N., Dennis, P. B., Andjelkovic, M., Dufner, A., Kozma, S. C., Hemmings, B. A., & Thomas, G. (1998) · Science · doi:10.1126/science.279.5351.707 · Cited by 826
Regulation of protein kinase cascades by protein phosphatase 2A
Millward, T. A., Zołnierowicz, S., & Hemmings, B. A. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01375-4 · Cited by 793
Flagged first, then by citations
2 of the 39 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Mechanisms of TGF-β Signaling from Cell Membrane to the Nucleus
Shi, Y., & Massagué, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00432-x · Cited by 5,860
Smad-dependent and Smad-independent pathways in TGF-β family signalling
Derynck, R., & Zhang, Y. E. (2003) · Nature · doi:10.1038/nature02006 · Cited by 5,498
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
Self-citationNon-Smad pathways in TGF-β signaling
Zhang, Y. E. (2008) · Cell Research · doi:10.1038/cr.2008.328 · Cited by 1,834
Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer
Siegel, P. M., & Massagué, J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1208 · Cited by 1,626
TGFβ: the molecular Jekyll and Hyde of cancer
Bierie, B., & Moses, H. L. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1926 · Cited by 1,291
Moustakas, A., & Heldin, C.-H. (2005) · Journal of Cell Science · doi:10.1242/jcs.02554 · Cited by 958
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 929
TGF-β signaling: positive and negative effects on tumorigenesis
Wakefield, L. M. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(01)00259-3 · Cited by 827
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
Role of Transforming Growth Factor Beta in Human Cancer
Elliott, R. L., & Blobe, G. C. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.02.047 · Cited by 717
Mechanisms of TGF-β signaling in regulation of cell growth and differentiation
Moustakas, A., Pardali, K., Gaál, A., & Heldin, C. (2002) · Immunology Letters · doi:10.1016/s0165-2478(02)00023-8 · Cited by 541
Actions of TGF-β as tumor suppressor and pro-metastatic factor in human cancer
Pardali, K., & Moustakas, A. (2006) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2006.06.004 · Cited by 549
TGF-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 528
Oxidative stress and glutathione in TGF-β-mediated fibrogenesis
Liu, R.-M., & Pravia, K. A. G. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.09.026 · Cited by 473
TGF-β receptors: In and beyond TGF-β signaling
Ark, A. V., Cao, J., & Li, X. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.09.002 · Cited by 481
The transforming growth factor-β superfamily of receptors
de Caestecker, M. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2003.10.004 · Cited by 464
Arsham, A. M., Howell, J. J., & Simon, M. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212770200 · Cited by 463
Regulation of cell proliferation by Smad proteins
ten Dijke, P., Goumans, M., Itoh, F., & Itoh, S. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10066 · Cited by 453
Dysregulation of growth factor signaling in human hepatocellular carcinoma
Breuhahn, K., Longerich, T., & Schirmacher, P. (2006) · Oncogene · doi:10.1038/sj.onc.1209556 · Cited by 394
N-Glycans in cancer progression
Lau, K. S., & Dennis, J. W. (2008) · Glycobiology · doi:10.1093/glycob/cwn071 · Cited by 390
TGF‐β signaling: A tale of two responses
Rahimi, R. A., & Leof, E. B. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21501 · Cited by 371
Phospho-control of TGF-β superfamily signaling
Wrighton, K. H., Lin, X., & Feng, X. (2008) · Cell Research · doi:10.1038/cr.2008.327 · Cited by 366
Functions and regulation of the 70 kDa ribosomal S6 kinases
Fenton, T. R., & Gout, I. T. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.09.018 · Cited by 350
New regulatory mechanisms of TGF-β receptor function
Kang, J. S., Liu, C., & Derynck, R. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.05.008 · Cited by 335
An, W.-L., Cowburn, R. F., Li, L., Braak, H., Alafuzoff, I., Iqbal, K., Iqbal, I.-G., Winblad, B., & Pei, J.-J. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63687-5 · Cited by 312
Daly, A. C., Randall, R. A., & Hill, C. S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01192-08 · Cited by 280
Foster, D. A., Yellen, P., Xu, L., & Saqcena, M. (2010) · Genes & Cancer · doi:10.1177/1947601910392989 · Cited by 279
Saika, S. (2005) · Laboratory Investigation · doi:10.1038/labinvest.3700375 · Cited by 276
Sierra-Filardi, E., Puig-Kröger, A., Blanco, F. J., Nieto, C., Bragado, R., Palomero, M. I., Bernabéu, C., Vega, M. A., & Corbí, A. L. (2011) · Blood · doi:10.1182/blood-2010-09-306993 · Cited by 268
Micropeptide CIP2A-BP encoded by LINC00665 inhibits triple-negative breast cancer progression
Guo, B., Wu, S., Zhu, X., Zhang, L., Deng, J., Li, F., Wang, Y., Zhang, S., Wu, R., Lu, J., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019102190 · Cited by 243
The S6K protein family in health and disease
Tavares, M. R., Pavan, I. C. B., do Amaral, C. L., Meneguello, L., Luchessi, A. D., & Simabuco, F. M. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.03.001 · Cited by 252
The Stress-activated Protein Kinases p38α and JNK1 Stabilize p21Cip1 by Phosphorylation
Kim, G.-Y., Mercer, S. E., Ewton, D. Z., Yan, Z., Jin, K., & Friedman, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201299200 · Cited by 231
TGF‐β control of cell proliferation
Huang, S. S., & Huang, J. S. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20558 · Cited by 221
Elucidation of Smad Requirement in Transforming Growth Factor-β Type I Receptor-induced Responses
Itoh, S., Thorikay, M., Kowanetz, M., Moustakas, A., Itoh, F., Heldin, C., & ten Dijke, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208258200 · Cited by 211
Yu, S., Shen, G., Khor, T. O., Kim, J. H., & Kong, A. T. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2400 · Cited by 192
A Novel Mechanism for Regulating Transforming Growth Factor β (TGF-β) Signaling
Blobe, G. C., Liu, X., Fang, S. J., How, T., & Lodish, H. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106831200 · Cited by 187
Saika, S., Okada, Y., Miyamoto, T., Yamanaka, O., Ohnishi, Y., Ooshima, A., Liu, C., Weng, D. Y., & Kao, W. W. ‐. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0700 · Cited by 177
TGF-β and the Smad signal transduction pathway
Mehra, A., & Wrana, J. L. (2002) · Biochemistry and Cell Biology · doi:10.1139/o02-161 · Cited by 174
Cellular growth inhibition by IGFBP‐3 and TGF‐β 1 requires LRP‐1
Huang, S. S., Ling, T., Tseng, W.-F., Huang, Y.-H., Tang, F.-M., Leal, S. M., & Huang, J. S. (2003) · The FASEB Journal · doi:10.1096/fj.03-0256com · Cited by 161
Escaping from the TGF anti-proliferative control
Seoane, J. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl068 · Cited by 151
McKarns, S. C., Schwartz, R. H., & Kaminski, N. E. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.7.4275 · Cited by 141
Regulated Phosphorylation of 40S Ribosomal Protein S6 in Root Tips of Maize
Williams, A. J., Werner-Fraczek, J., Chang, I., & Bailey-Serres, J. N. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.022749 · Cited by 127
Lekmine, F., Shahab Uddin, M. S., Sassano, A., Parmar, S., Brachmann, S. M., Majchrzak, B., Sonenberg, N., Hay, N., Fish, E. N., & Platanias, L. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301364200 · Cited by 125
P70 S6 kinase mediates tau phosphorylation and synthesis
Pei, J.-J., An, W., Zhou, X., Nishimura, T., Norberg, J., Benedikz, E., Götz, J., & Winblad, B. G. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.059 · Cited by 121
Functions and regulation of transforming growth factor-beta (TGF-β) in the prostate
Danielpour, D. (2005) · European Journal of Cancer · doi:10.1016/j.ejca.2004.12.027 · Cited by 115
Akt Controls Vascular Smooth Muscle Cell Proliferation In Vitro and In Vivo by Delaying G1/S Exit
Stabile, E., Zhou, Y. F., Saji, M., Castagna, M. T., Shou, M., Kinnaird, T. D., Baffour, R., Ringel, M. D., Epstein, S. E., & Fuchs, S. (2003) · Circulation Research · doi:10.1161/01.res.0000105086.31909.1b · Cited by 111
TGF-β Signal Transduction in Corneal Wound Healing as a Therapeutic Target
Saika, S. (2004) · Cornea · doi:10.1097/01.ico.0000136668.41000.73 · Cited by 110
Kim, B.-C., Mamura, M., Choi, K. S., Calabretta, B., & Kim, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1369-1378.2002 · Cited by 107
TGF-beta in neural stem cells and in tumors of the central nervous system
Aigner, L., & Bogdahn, U. (2007) · Cell and Tissue Research · doi:10.1007/s00441-007-0466-7 · Cited by 103
Buck, M. B., Fritz, P., Dippon, J., Zugmaier, G., & Knabbe, C. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-0320-03 · Cited by 100
Song, K. W., Cornelius, S. C., Reiß, M., & Danielpour, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304583200 · Cited by 98
Distinct Roles of mTOR Targets S6K1 and S6K2 in Breast Cancer
Sridharan, S., & Basu, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041199 · Cited by 95
Meeusen, B., & Janssens, V. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.002 · Cited by 96
TGF-β-activated kinase-1: New insights into the mechanism of TGF-β signaling and kidney disease
Kim, S. I., & Choi, M. E. (2012) · Kidney Research and Clinical Practice · doi:10.1016/j.krcp.2012.04.322 · Cited by 96
p70 Ribosomal protein S6 kinase ( Rps6kb1 ): an update
Bahrami-B, F., Ataie-Kachoie, P., Pourgholami, M. H., & Morris, D. L. (2014) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2014-202560 · Cited by 101
Piek, E., & Roberts, A. B. (2001) · Advances in cancer research · doi:10.1016/s0065-230x(01)83001-3 · Cited by 94
PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer
(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93
Regulation of TGF-β signalling by protein phosphatases
Liu, T., & Feng, X. (2010) · Biochemical Journal · doi:10.1042/bj20100427 · Cited by 93
Beyond controlling cell size: functional analyses of S6K in tumorigenesis
Wu, X., Xie, W., Xie, W., Wei, W., & Guo, J. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05081-4 · Cited by 96
The kinase activity of the Ser/Thr kinase BUB1 promotes TGF-β signaling
Nyati, S., Schinske, K. A., Pitchiaya, S., Chekhovskiy, K., Chator, A., Chaudhry, N., Dosch, J. S., Dort, M. E. V., Varambally, S., Kumar‐Sinha, C., et al. (2015) · Science Signaling · doi:10.1126/scisignal.2005379 · Cited by 90
Guan, L., Song, K. W., Pysz, M. A., Curry, K., Hizli, A. A., Danielpour, D., Black, A. R., & Black, J. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610513200 · Cited by 80
Batut, J., Schmierer, B., Cao, J., Raftery, L. A., Hill, C. S., & Howell, M. T. (2008) · Development · doi:10.1242/dev.020842 · Cited by 84
TGF‐β signaling in human skeletal and patterning disorders
Serra, R. A., & Chang, C. (2003) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.10023 · Cited by 80
Gu, S., & Feng, X. (2018) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmy092 · Cited by 80
Björkdahl, C., Sjögren, M. J. C., Zhou, X., Concha, H., Ávila, J., Winblad, B. G., & Pei, J.-J. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21589 · Cited by 78
p70 S6 Kinase and Tau in Alzheimer's Disease
Pei, J.-J., Björkdahl, C., Zhang, H., Zhou, X., & Winblad, B. G. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14405 · Cited by 75
Qi, C., Mårtensson, A., Mattioli, M., Dalla‐Favera, R., Lobanenkov, V. V., & Morse, H. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0237127100 · Cited by 73
Jechlinger, M., Grünert, S., & Beug, H. (2002) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1023/a:1024090116451 · Cited by 78
Self-citationThe role of transforming growth factor-beta in primary brain tumors
Rich, J. N. (2003) · Frontiers in bioscience · doi:10.2741/992 · Cited by 74
Francois, A., Terro, F., Quellard, N., Fernandez, B., Chassaing, D., Janet, T., Bilan, A. R., Paccalin, M., & Page, G. (2014) · Molecular Brain · doi:10.1186/s13041-014-0056-z · Cited by 62
Valovka, T., Verdier, F., Cramer, R., Zhyvoloup, A., Fenton, T. R., Rebholz, H., Wang, M., Gzhegotsky, M. R., Lutsyk, A. D., Matsuka, G. K., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.852-863.2003 · Cited by 70
Oyanagi, J., Ogawa, T., Sato, H., Higashi, S., & Miyazaki, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0053209 · Cited by 71
Inhibition of p38MAP kinase suppresses fibrotic reaction of retinal pigment epithelial cells
Saika, S., Yamanaka, O., Ikeda, K., Kim‐Mitsuyama, S., Flanders, K. C., Yoo, J., Roberts, A. B., Ishida, I., Ohnishi, Y., Muragaki, Y., et al. (2005) · Laboratory Investigation · doi:10.1038/labinvest.3700294 · Cited by 67
TGFB1/INHBA Homodimer/Nodal-SMAD2/3 Signaling Network: A Pivotal Molecular Target in PDAC Treatment
Mouti, M. A., & Pauklin, S. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.01.002 · Cited by 70
Cao, Z., Flanders, K. C., Bertolette, D. C., Lyakh, L. A., Würthner, J., Parks, W. T., Letterio, J. J., Ruscetti, F. W., & Roberts, A. B. (2002) · Blood · doi:10.1182/blood-2002-05-1549 · Cited by 66
Peng, B., Fleming, J. B., Breslin, T. M., Grau, A. M., Fojioka, S., Abbruzzese, J. L., Evans, D. B., Ayers, D., Wathen, K., Wu, T., et al. (2002) · PubMed · Cited by 66
The Role of TGF-β Signaling Pathways in Cancer and Its Potential as a Therapeutic Target
Yang, Y., Ye, W.-L., Zhang, R., He, X., Wang, J., Liu, Y., Wang, Y., Yang, X., Zhang, Y., & Gan, W.-J. (2021) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2021/6675208 · Cited by 66
Silvestri, C., Bose, R., Attisano, L., & Wrana, J. L. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00070-x · Cited by 64
Bettoun, D. J., Buck, D. W., Lu, J., Khalifa, B., Chin, W. W., & Nagpal, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200187200 · Cited by 63
Yang, Y.-A., Tang, B., Robinson, G. W., Hennighausen, L. G., Brodie, S. G., Deng, C., & Wakefield, L. M. (2002) · PubMed · Cited by 63
Jackson, J. B., & Pallas, D. C. (2012) · Neoplasia · doi:10.1593/neo.12768 · Cited by 60
Smad inhibition by the Ste20 kinase Misshapen
Kaneko, S., Chen, X., Lu, P., Yao, X., Wright, T. G., Rajurkar, M., Kariya, K., Mao, J., Ip, Y. T., & Xu, L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104128108 · Cited by 60
TGF-β S ignal T ransduction in O ro - facial H ealth and N on - malignant D isease (P art I)
Prime, S. S., Pring, M., Davies, M., & Paterson, I. C. (2004) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/154411130401500602 · Cited by 61
LRP‐1/TβR‐V mediates TGF‐β1‐induced growth inhibition in CHO cells
Tseng, W.-F., Huang, S. S., & Huang, J. S. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00185-1 · Cited by 59
Choudhury, G. G., & Abboud, H. E. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(03)00094-9 · Cited by 58
Buck, A., Buchholz, M., Wagner, M., Adler, G., Gress, T. M., & Ellenrieder, V. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0081 · Cited by 58
Mysteries of TGF-β Paradox in Benign and Malignant Cells
Zhang, Q., Yu, N., & Lee, C. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00094 · Cited by 57
Kim, S. I., Kwak, J. H., Wang, L. Q., & Choi, M. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801263200 · Cited by 52
Cardiomyocyte SMAD4-Dependent TGF-β Signaling is Essential to Maintain Adult Heart Homeostasis
Umbarkar, P., Singh, A. P., Gupte, M., Verma, V. K., Galindo, C. L., Guo, Y., Zhang, Q., McNamara, J. W., Force, T. L., & Lal, H. (2019) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2018.10.003 · Cited by 53
Bengtsson, L., Schwappacher, R., Roth, M., Boergermann, J. H., Haßel, S., & Knaus, P. I. (2009) · Journal of Cell Science · doi:10.1242/jcs.039552 · Cited by 52
Ozaki, I., Hamajima, H., Matsuhashi, S., & Mizuta, T. (2011) · Frontiers in Physiology · doi:10.3389/fphys.2011.00078 · Cited by 52
Phosphorylation of eEF1A1 at Ser300 by TβR-I results in inhibition of mRNA translation.
Lin, K., Yakymovych, I., Jia, M., Yakymovych, M., & Souchelnytskyi, S. (2010) · Current Biology · doi:10.1016/j.cub.2010.08.017 · Cited by 59
Cho, D., Choi, Y. J., Jo, S. A., Ryou, J., Kim, J. Y., Chung, J., & Jo, I. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00491.2005 · Cited by 49
The rasGAP‐binding protein, Dok‐1, mediates activin signaling via serine/threonine kinase receptors
Yamakawa, N., Tsuchida, K., & Sugino, H. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1684 · Cited by 49
Tgfb3 collaborates with PP2A and notch signaling pathways to inhibit retina regeneration
Lee, M., Wan, J., & Goldman, D. J. (2020) · eLife · doi:10.7554/elife.55137 · Cited by 47
Pro‐metastasis function of TGFβ mediated by the smad pathway
Kang, Y. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20928 · Cited by 49
Biphasic role of TGF‐β1 in signal transduction and crosstalk
Wenner, C. E., & Yan, S. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10243 · Cited by 48
Daly, A. C., Vizán, P., & Hill, C. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.043877 · Cited by 48
Parathath, S. R., Mainwaring, L. A., Fernández-L, A., Campbell, D. O., & Kenney, A. M. (2008) · Development · doi:10.1242/dev.022871 · Cited by 48
Metadata
- Authors
- Petritsch, C., Beug, H., Balmain, A., & Oft, M.
- Affiliations
- University of California, San Francisco (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-12-15
- Volume
- 14
- Issue
- 24
- Pages
- 3093-3101
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC317138
- OpenAlex
- W1999086610
- Cited by
- 223
- References
- 39
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 3 · 2023: 6 · 2022: 2 · 2021: 5 · 2020: 4 · 2019: 5 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 6 · 2014: 8 · 2013: 7 · 2012: 9
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- TGF-beta, p70 S6 kinase, protein phosphatase 2A, G1 cell cycle arrest, Smad2/3 signaling, TGF-beta receptor, protein dephosphorylation, translational regulation, post-transcriptional regulation, cell cycle progression, epithelial cells
- MeSH terms
- Wortmannin, Receptor, Transforming Growth Factor-beta Type I, Receptor, Transforming Growth Factor-beta Type II, Androstadienes, Animals, Cells, Cultured, Chromones, DNA-Binding Proteins, Dose-Response Relationship, Drug, Enzyme Inhibitors, Epithelial Cells, Fibroblasts, Morpholines, Mutation, Phosphoprotein Phosphatases, Phosphorylation, Quinazolines, Protein Biosynthesis, Signal Transduction, Trans-Activators, G1 Phase, S Phase, Transforming Growth Factor beta, Protein Serine-Threonine Kinases, Receptors, Transforming Growth Factor beta, Ribosomal Protein S6 Kinases, Sirolimus, Activin Receptors, Type I, Smad2 Protein, Protein Phosphatase 2, ErbB Receptors
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