Cited by 517TGF-β signaling in diseasesDevelopmental Biology and Gene RegulationHeterotopic Ossification and Related Conditions

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Signal transduction of bone morphogenetic protein receptors

Nohe, A·2004·Cellular Signalling

DOI 10.1016/j.cellsig.2003.08.011

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Abstract

Bone morphogenetic proteins (BMPs) play a crucial role during all stages of embryonic development. Although only two major signaling pathways have been characterized (the p38 and Smad pathways), the BMP signaling is complex and includes several negative feedback mechanisms. This article reviews the current state of BMP receptor signaling and provides a summary of the crosstalk of the BMP receptor pathway with other major signaling pathways.

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TGF-β SIGNAL TRANSDUCTION
Massagué, J. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.753 · Cited by 7,571
Bone: Formation by Autoinduction
Urist, M. R. (1965) · Science · doi:10.1126/science.150.3698.893 · Cited by 5,529
Mechanism of activation of the TGF-β receptor
Wrana, J. L., Attisano, L., Wieser, R., Ventura, F., & Massagué, J. (1994) · Nature · doi:10.1038/370341a0 · Cited by 2,340
Identification of Smad7, a TGFβ-inducible antagonist of TGF-β signalling
Nakao, A., Afrakhte, M., Morn, A., Nakayama, T., Christian, J. L., Heuchel, R. L., Itoh, S., Kawabata, M., Heldin, N., Heldin, C., et al. (1997) · Nature · doi:10.1038/39369 · Cited by 1,796
Direct binding of Smad3 and Smad4 to critical TGFβ‐inducible elements in the promoter of human plasminogen activator inhibitor‐type 1 gene
Dennler, S., Itoh, S., Vivien, D., ten Dijke, P., Huet, S., & Gauthier, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.3091 · Cited by 1,793
Growth differentiation factor-9 is required during early ovarian folliculogenesis
Dong, J., Albertini, D. F., Nishimori, K., Kumar, T. R., Lu, N., & Matzuk, M. M. (1996) · Nature · doi:10.1038/383531a0 · Cited by 1,652
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
The MAD-Related Protein Smad7 Associates with the TGFβ Receptor and Functions as an Antagonist of TGFβ Signaling
Hayashi, H., Abdollah, S., Qiu, Y., Cai, J., Xu, Y., Grinnell, B. W., Richardson, M. A., Topper, J. N., Gimbrone, M. A., Wrana, J. L., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80303-7 · Cited by 1,322
TGF‐β receptor‐mediated signalling through Smad2, Smad3 and Smad4
Nakao, A., Imamura, T., Souchelnytskyi, S., Kawabata, M., Ishisaki, A., Oeda, E., Tamaki, K., Hanai, J., Heldin, C., Miyazono, K., et al. (1997) · The EMBO Journal · doi:10.1093/emboj/16.17.5353 · Cited by 1,071
Smad6 inhibits signalling by the TGF-β superfamily
Imamura, T., Takase, M., Nishihara, A., Oeda, E., Hanai, J., Kawabata, M., & Miyazono, K. (1997) · Nature · doi:10.1038/39355 · Cited by 1,023

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Authors: Nohe, A.
Affiliations: Western University (CA)
Corresponding author: Nohe, A
ORCID: Nohe, A
Venue: Cellular Signalling
Publisher: Elsevier BV
Published: 2004-03
Volume: 16
Issue: 3
Pages: 291-299
ISSN: 0898-6568 (ISSN-L)
DOI: 10.1016/j.cellsig.2003.08.011
OpenAlex: W2093271566
Cited by: 514
References: 133
Citations by year: 2026: 3 · 2025: 5 · 2024: 11 · 2023: 7 · 2022: 17 · 2021: 10 · 2020: 12 · 2019: 9 · 2018: 17 · 2017: 16 · 2016: 30 · 2015: 31 · 2014: 22 · 2013: 26 · 2012: 31
FWCI: 7.24
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cellular Signalling (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 › Developmental Biology and Gene Regulation
Health Sciences › Medicine › Rheumatology › Heterotopic Ossification and Related Conditions
Keywords: bone morphogenetic proteins, BMP receptors, signal transduction, Smad signaling, p38 MAPK pathway, negative feedback regulation, signaling crosstalk, embryonic development
MeSH terms: Animals, Carrier Proteins, DNA-Binding Proteins, Models, Biological, Signal Transduction, Trans-Activators, Receptors, Growth Factor, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System, Feedback, Physiological, p38 Mitogen-Activated Protein Kinases, Adaptor Proteins, Signal Transducing, Smad Proteins, Bone Morphogenetic Protein Receptors

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Signal transduction of bone morphogenetic protein receptors

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