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Specificity, versatility, and control of TGF-β family signaling
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Molecular function and pathway cross-talk in TGF-β signaling reveal its complexity and open questions.
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“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]
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“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]
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“The activation of particular intracellular signaling pathways by the SY-LB compounds to increase cell viability and the rate of wound healing raises an enduring problem in the BMP/BMP receptor field of how the choice of down-stream pathway is regulated [9,15,19,68–70].”
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Assessment of BMP responses in an in vitro model of acute ethanol toxicity
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Sun, Y., & Li, Z. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00741-1 · Cited by 2
Abnormal GRHL2 Methylation Confers Malignant Progression to Acute Leukemia
Hua, J., Ma, C., Wang, C. H., Wang, Y., Feng, S., Xiao, T., & Zhu, C. (2022) · Applied Bionics and Biomechanics · doi:10.1155/2022/9708829 · Cited by 2
RetractedControlling Smad4 signaling with a Wip
ten Dijke, P., & Baker, D. A. (2020) · EMBO Reports · doi:10.15252/embr.202050246 · Cited by 2
Non-Smad, BMP-dependent signaling protects against the effects of acute ethanol toxicity
Habeeb, N., Najafi, S., & Perron, J. C. (2021) · Toxicology Letters · doi:10.1016/j.toxlet.2021.10.009 · Cited by 2
Contreras, O., Soliman, H., Théret, M., Rossi, F. M. V., & Brandan, E. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.05.895334 · Cited by 3
Spit, M., & ten Dijke, P. (2021) · Springer eBooks · doi:10.1007/978-3-030-57401-7_10062 · Cited by 2
The Therapeutic Effects of Long-term Photobiomodulation on Aging in MicePreprint
Ahmet, I., Syed, S. B., Chakir, K., Morrell, C. H., Arany, P. R., & Lakatta, E. G. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.05.552116 · Cited by 2
“Considering the critical role TGF‐β in cellular degeneration, fibrosis, inflammation, regenerative capacity and metabolic functions in humans and mouse alike [34, 35], it is clear that TGF-β1 signaling is part of the mechanistic pathways of PBM.”
BackgroundMonsivais, D., Liao, Z., Tang, S., Jiang, P., Geng, T., Cope, D. I., Dunn, T. N., Guner, J. Z., Radilla, L. A., & Guan, X. (2023) · Research Square · doi:10.21203/rs.3.rs-3471243/v1 · Cited by 2
An optogenetic toolkit for robust activation of FGF, BMP, & Nodal signaling in zebrafish
Iannucci, L. E., Thomas, V. S. M., Anderson, W. K., Murphy, M. R., Donahue, C. E. T., Campbell, C. E., Monaghan, M. T., Saul, A. J., & Rogers, K. W. (2026) · Developmental Biology · doi:10.1016/j.ydbio.2026.05.003 · Cited by 3
Mathematical modelling of tissue growth control by positive and negative feedbacks
Kaźmierczak, B., & Volpert, V. A. (2025) · PLoS ONE · doi:10.1371/journal.pone.0319120 · Cited by 2
Cheng, K.-C., Lee, H.-M., Shu, Y.-T., Chu, Y.-C., Hsiao, J.-T., Hsieh, M., & Hsieh, Y.-H. (2025) · Life · doi:10.3390/life15121915 · Cited by 1
“First, although gamma irradiation did not alter the concentration of TGF-β 1, its potential impact on protein conformation or bioactivity requires further verification through functional assays, such as Smad phosphorylation or downstream gene expression analysis [22,23].”
Oxidative stress and GPX2 control pancreatic vs. non-pancreatic cell fate in human endoderm
Szpotkowska, J., Szlachcic, W. J., Błaszczyk, K., Baginska, M., Socha, M., & Borowiak, M. (2026) · Nature Communications · doi:10.1038/s41467-025-68145-x · Cited by 1
Wang, X., He, J., Shen, S., Li, M., Yuan, S., Xu, W., Zhu, S., Ding, Y., & Wang, X. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112362 · Cited by 1
Mitigative effects of Otilonium Bromide on methotrexate-induced hepatic damage in rats
Arı, M., Erdogan, M. A., & Erbaş, O. (2026) · BMC Research Notes · doi:10.1186/s13104-025-07585-6 · Cited by 1
“Excessive TGF-β activation is known to contribute to fibrosis in organs such as the liver, lungs, and kidneys [29].”
Gramatikoff, K., Stoykov, M., & Milkov, M. P. (2026) · Biomedicines · doi:10.3390/biomedicines14010181 · Cited by 1
Rodrigues‐Junior, D. M., Doumani, M. A., Fu, H., van den Bor, J., Idevall‐Hagren, O., & Moustakas, A. (2026) · FEBS Journal · doi:10.1111/febs.70520 · Cited by 1
van Dinther, M., Schwartze, T. A., Zhang, J., Fan, K., van der Zon, G., Power, L., Hinck, C. S., Ciancia, C., Mukundan, A., González‐Prieto, R., et al. (2026) · Advanced Science · doi:10.1002/advs.75322 · Cited by 3
Yan, X., Zhang, J., Heldin, C., Feng, X.-H., & Chen, Y. (2026) · Cell Regeneration · doi:10.1186/s13619-026-00286-w · Cited by 2
“…factors (GDFs), and the bone morphogenetic protein (BMP) subfamily that includes eleven BMPs, four GDFs, and the anti-Muellerian hormone (AMH) (for reviews, see Derynck and Budi 2019; Hata and Chen 2016; Jia and Meng 2021; Massagué and Sheppard 2023; Morikawa et al. 2016; Yu and Feng 2019).”
Berti, C. C., Montali, I., Doselli, S., Farina, B., Schivazappa, S., Vecchi, A. L., Rossi, M., Reverberi, V., Montali, A., Sambarino, D., et al. (2026) · Journal of Hepatology · doi:10.1016/j.jhep.2026.05.020 · Cited by 1
Targeting vascular smooth muscle cells with natural compounds to combat atherosclerosis
Qin, X., Zhou, Z., Zheng, Z., Wen, X., & Yang, H. (2026) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(26)61117-x · Cited by 2
Mohammad-Rezaei, M., Shafaghat, Z., Noroozbeygi, M., Velu, P., Safaee, M., Heiranizadeh, N., & Safari, E. (2026) · Clinical & Translational Oncology · doi:10.1007/s12094-026-04450-1 · Cited by 1
Overview of biophysical approaches to study osteogenic proteins in lipidic interfaces
Hayann, L., de Melo, M. T., Cominal, J. G., Lima, I. S., Andrilli, L. H. D. S., Machado, J. P. M., de Sousa, J. D. R. S., Azevedo, P. A. B. S., Oliveira, M. F., Ramos, A. P., et al. (2026) · Biophysical Reviews · doi:10.1007/s12551-026-01455-6 · Cited by 1
Xia, F., He, C., Ni, X., Zhang, T., Li, Q., Luo, Y., Long, W., & Wu, R. J. (2022) · Clinical and Experimental Hypertension · doi:10.1080/10641963.2022.2079665 · Cited by 1
“Once activated, the interaction of the Smad2 and Smad3 transcription factors with the Smad4 transcription factor is triggered via phosphorylation, where together they translocate to the nucleus to induce gene transcription (30).”
BackgroundFactors affecting the induction of uncoupling protein 1 in C2C12 myogenic cells
Yamamoto, T., Diao, Z., Murakami, M., Shimokawa, F., Matsui, T., & Funaba, M. (2022) · Cytokine · doi:10.1016/j.cyto.2022.155936 · Cited by 1
Mohammed, S. A. D., Liu, H., Baldi, S., Chen, P., Wang, Y., Lü, F., & Liu, S. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/6924197 · Cited by 1
Musthafa, A., Ryanto, G. R. T., Suraya, R., Nagano, T., Suzuki, Y., Hara, T., Hirata, K., & Emoto, N. (2023) · PubMed Central · doi:10.24546/0100483406 · Cited by 1
“Additionally, transcriptional modulation of proteins from the same family is common [27], possibly including the endothelin peptide family.”
Background
Metadata
- 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
- 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
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