The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
mTORC1 amplifies the ATF4-dependent de novo serine-glycine pathway to supply glycine during TGF-β 1 –induced collagen biosynthesis
Open accessAbstract
Through mTORC1 signaling, TGF-β 1 stimulates glycine synthesis from glucose to support collagen production in lung fibroblasts.
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Citations
Cites
mTOR 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
Efficacy and Safety of Nintedanib in Idiopathic Pulmonary Fibrosis
Richeldi, L., du Bois, R. M., Raghu, G., Azuma, A., Brown, K. K., Costabel, U., Cottin, V., Flaherty, K. R., Hansell, D. M., Inoue, Y., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1402584 · Cited by 4,654 · cited 1×
“Although the approval of pirfenidone and the small molecule tyrosine kinase inhibitor, nintedanib, for the treatment of IPF represented a watershed moment for the development of anti-fibrotic therapeutics, these agents slow but do not halt disease progression (4, 5).”
BackgroundA phase 3 trial of pirfenidone in patients with idiopathic pulmonary fibrosis.
King, T. E., Bradford, W. Z., Castro-Bernardini, S., Fagan, E. A., Glaspole, I., Glassberg, M. K., Gorina, E., Hopkins, P. M., Kardatzke, D., Lancaster, L., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1402582 · Cited by 3,975 · cited 1×
“Although the approval of pirfenidone and the small molecule tyrosine kinase inhibitor, nintedanib, for the treatment of IPF represented a watershed moment for the development of anti-fibrotic therapeutics, these agents slow but do not halt disease progression (4, 5).”
BackgroundActivation of a metabolic gene regulatory network downstream of mTOR complex 1
Düvel, K., Yecies, J. L., Menon, S., Raman, P., Lipovsky, A. I., Souza, A. L., Triantafellow, E., Ma, Q., Gorski, R., Cleaver, S., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.022 · Cited by 2,020
Extracellular Matrix Assembly: A Multiscale Deconstruction
Mouw, J. K., Ou, G., & Weaver, V. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3902 · Cited by 1,534
The mTOR Signalling Pathway in Human Cancer
Pópulo, H., Lopes, J. M., & Soares, P. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13021886 · Cited by 830
mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle
Ben-Sahra, I., Hoxhaj, G., Ricoult, S. J. H., Asara, J. M., & Manning, B. D. (2016) · Science · doi:10.1126/science.aad0489 · Cited by 795
The myofibroblast matrix: implications for tissue repair and fibrosis
Klingberg, F., Hinz, B., & White, E. S. (2013) · The Journal of Pathology · doi:10.1002/path.4104 · Cited by 776
Glycolytic Reprogramming in Myofibroblast Differentiation and Lung Fibrosis
Xie, N., Tan, Z., Banerjee, S., Cui, H., Ge, J., Liu, R.-M., Bernard, K., Thannickal, V. J., & Liu, G. (2015) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201504-0780oc · Cited by 582
A PHGDH inhibitor reveals coordination of serine synthesis and one-carbon unit fate
Pacold, M. E., Brimacombe, K. R., Chan, S. H., Rohde, J. M., Lewis, C. A., Swier, L. J. Y. M., Possemato, R., Chen, W. W., Sullivan, L. B., Fiske, B. P., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2070 · Cited by 553
Cited by
Myofibroblasts and Fibrosis: Mitochondrial and Metabolic Control of Cellular Differentiation
Gibb, A. A., Lazaropoulos, M. P., & Elrod, J. W. (2020) · Circulation Research · doi:10.1161/circresaha.120.316958 · Cited by 434
Idiopathic Pulmonary Fibrosis: An Update on Pathogenesis
Mei, Q., Liu, Z., Zuo, H., Yang, Z., & Qu, J. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.797292 · Cited by 360
TGF‐β as a driver of fibrosis: physiological roles and therapeutic opportunities
Budi, E. H., Schaub, J. R., Decaris, M., Turner, S., & Derynck, R. (2021) · The Journal of Pathology · doi:10.1002/path.5680 · Cited by 292
Proline biosynthesis is a vent for TGFβ‐induced mitochondrial redox stress
Schwörer, S., Berisa, M., Violante, S., Qin, W., Zhu, J., Hendrickson, R. C., Cross, J. R., & Thompson, C. B. (2020) · The EMBO Journal · doi:10.15252/embj.2019103334 · Cited by 193
Regulatory mechanisms of one-carbon metabolism enzymes
Petrova, B., Maynard, A. G., Wang, P., & Kanarek, N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105457 · Cited by 103
Metadata
- Authors
- Selvarajah, B., Azuelos, I., Platé, M., Guillotin, D., Forty, E. J., Contento, G., Woodcock, H. V., Redding, M., Taylor, A., Brunori, G., Durrenberger, P. F., Ronzoni, R., Blanchard, A. D., Mercer, P. F., Anastasiou, D., & Chambers, R. C.
- Venue
- Science Signaling
- Published
- 2019-05-21
- Volume
- 12
- Issue
- 582
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- OpenAlex
- W2946604129
- Cited by
- 172
- References
- 14
- FWCI
- 5.59
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: mTORC1 amplifies the ATF4-dependent de novo serine-glycine pathway to supply glycine during TGF-β 1 –induced collagen biosynthesis. https://app.cochat.ai/papers/10.1126/scisignal.aav3048
- The paper
- Selvarajah, B., Azuelos, I., Platé, M., Guillotin, D., Forty, E. J., Contento, G., Woodcock, H. V., Redding, M., Taylor, A., Brunori, G., Durrenberger, P. F., Ronzoni, R., Blanchard, A. D., Mercer, P. F., Anastasiou, D., & Chambers, R. C. (2019). mTORC1 amplifies the ATF4-dependent de novo serine-glycine pathway to supply glycine during TGF-β 1 –induced collagen biosynthesis. Science Signaling. https://doi.org/10.1126/scisignal.aav3048
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
