The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Molecular and Cell Biology of TGF-β
Abstract
The TGF-βs are a remarkable set of peptides consisting of three highly homologous isoforms, TGF-β 1, 2, and 3. Distinguished initially for their ability to inhibit the growth of most epithelial and hematopoietic cells and to regulate the production of extracellular matrix by mesenchymal cells, these peptides are now known to act via autocrine, paracrine, and endocrine modes to control a wide variety of developmental processes and to play key roles in the pathogenesis of many diseases including especially fibrotic diseases, parasitic diseases, autoimmune diseases, and carcinogenesis. The activity of these peptides is under tight control by processes including regulation of the expression of the isoforms and their receptors and of the trafficking and activation of their latent forms.
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Cites
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
Transforming Growth Factor β in Tissue Fibrosis
Epstein, F. H., Border, W. A., & Noble, N. A. (1994) · New England Journal of Medicine · doi:10.1056/nejm199411103311907 · Cited by 3,069
Kingsley, D. M. (1994) · Genes & Development · doi:10.1101/gad.8.2.133 · Cited by 1,933
The Molecular and Cellular Biology of Wound Repair
(1988) · Springer eBooks · doi:10.1007/978-1-4615-1795-5 · Cited by 1,516
McAllister, K. A., Grogg, K. M., Johnson, D. W., Gallione, C. J., Baldwin, M. A., Jackson, C. E., Helmbold, E. A., Markel, D. S., McKinnon, W. C., Murrel, J., et al. (1994) · Nature Genetics · doi:10.1038/ng1294-345 · Cited by 1,482
Kaartinen, V., Voncken, J. W., Shuler, C., Warburton, D., Bu, D., Heisterkamp, N., & Groffen, J. (1995) · Nature Genetics · doi:10.1038/ng1295-415 · Cited by 1,031
Transforming growth factor–β3 is required for secondary palate fusion
Proetzel, G., Pawlowski, S. A., Wiles, M. V., Yin, M., Boivin, G. P., Howles, P. N., Ding, J., Ferguson, M. W. J., & Doetschman, T. (1995) · Nature Genetics · doi:10.1038/ng1295-409 · Cited by 908
The Transforming Growth Factor-βs
Roberts, A. B., & Sporn, M. B. (1991) · Peptide Growth Factors and Their Receptors I · doi:10.1007/978-1-4612-3210-0_8 · Cited by 861
Self-citationPhysiological Actions and Clinical Applications of Transforming Growth Factor-β (TGF-β)
Roberts, A. B., & Sporn, M. B. (1993) · Growth Factors · doi:10.3109/08977199309029129 · Cited by 755
Self-citationA transcriptional partner for MAD proteins in TGF-β signalling
Chen, X., Rubock, M. J., & Whitman, M. (1996) · Nature · doi:10.1038/383691a0 · Cited by 684
Cited by
Regulation of Wound Healing by Growth Factors and Cytokines
WERNER, S., & GROSE, R. (2003) · Physiological Reviews · doi:10.1152/physrev.2003.83.3.835 · Cited by 3,629
Verrecchia, F., & Mauviel, A. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.01641.x · Cited by 666
Prokić, M. D., Radovanović, T. B., Gavrić, J. P., & Faggio, C. (2019) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2018.12.001 · Cited by 527
TGF-β signalling and its role in cancer progression and metastasis
Drabsch, Y., & ten Dijke, P. (2012) · Cancer and Metastasis Reviews · doi:10.1007/s10555-012-9375-7 · Cited by 428
Proteolysis of Latent Transforming Growth Factor-β (TGF-β)-binding Protein-1 by Osteoclasts
Dallas, S. L., Rosser, J. L., Mundy, G. R., & Bonewald, L. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111663200 · Cited by 414
Metadata
- Authors
- Roberts, A. B.
- Venue
- Mineral and Electrolyte Metabolism
- Publisher
- S. Karger AG
- Published
- 1998
- Volume
- 24
- Issue
- 2-3
- Pages
- 111-119
- ISSN
- 0378-0392 (ISSN-L)
- 1423-016X
- OpenAlex
- W2041172831
- Cited by
- 386
- References
- 62
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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