Cited by 464TGF-β signaling in diseasesReceptor Mechanisms and SignalingLiver physiology and pathology

The DOI matches its Crossref record; 162 of the 162 references it cites were found in a registry or an index.

The transforming growth factor-β superfamily of receptors

de Caestecker, Mark·2004·Cytokine & Growth Factor Reviews

DOI 10.1016/j.cytogfr.2003.10.004

Open this paper in CoChat — free account

Abstract

The transforming growth factor-beta (TGF-beta) superfamily of receptors comprises two groups of transmembrane serine-threonine kinase receptors, so called type I, and type II receptors, that are activated following engagement by members of the TGF-beta superfamily of ligands. These events specify diverse downstream responses that are differentially regulated by controlling access and activation of the ligands, their receptors and downstream substrates in different cell types. The purpose of this review is to describe the biochemical properties of these receptors, focusing specifically on the mechanisms regulating receptor/ligand interactions and activation in mammalian cells.

Integrity signals

Registry

Crossref · 10.1016/j.cytogfr.2003.10.004

Cites

162 of 162 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

1 retracted

RETRACTED: Nuclear Translocation of LIM Kinase Mediates Rho-Rho Kinase Regulation of Cyclin D1 Expression
Roovers, K., Klein, E. A., Castagnino, P. A., & Assoian, R. K. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00206-5 · Cited by 56
Retracted
TGFβ Signaling in Growth Control, Cancer, and Heritable Disorders
Massagué, J., Blain, S. W., & Lo, R. S. (2000) · Cell · doi:10.1016/s0092-8674(00)00121-5 · Cited by 2,391
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
Transcriptional control by the TGF‐β/Smad signaling system
Massagué, J., & Wotton, D. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1745 · Cited by 1,990
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
SB-431542 Is a Potent and Specific Inhibitor of Transforming Growth Factor-β Superfamily Type I Activin Receptor-Like Kinase (ALK) Receptors ALK4, ALK5, and ALK7
Inman, G. J., Nicolás, F. J., Callahan, J. F., Harling, J. D., Gaster, L. M., Reith, A. D., Laping, N. J., & Hill, C. S. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.1.65 · Cited by 1,636
Regulation of myostatin activity and muscle growth
Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616
TGFβ signals through a heteromeric protein kinase receptor complex
Wrana, J. L., Attisano, L., Cárcamo, J. M., Zentella‐Dehesa, A., Doody, J. F., Laiho, M., Wang, X.-F., & Massagué, J. (1992) · Cell · doi:10.1016/0092-8674(92)90395-s · Cited by 1,528
Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
Arber, S., Barbayannis, F. A., Hanser, H., Schneider, C., Stanyon, C. A., Bernard, O., & Caroni, P. (1998) · Nature · doi:10.1038/31729 · Cited by 1,426
Active and Inactive Protein Kinases: Structural Basis for Regulation
Johnson, L. N., Noble, M. E. M., & Owen, D. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81092-2 · Cited by 1,396

Show all 161 references

Sorted by citations

Items 301–400 of 463

Subsynovial connective tissue is sensitive to surgical interventions in a rabbit model of carpal tunnel syndrome
Sun, Y., Moriya, T., Zhao, C., Kirk, R. L., Chikenji, T., Passe, S. M., An, K., & Amadio, P. C. (2011) · Journal of Orthopaedic Research® · doi:10.1002/jor.21565 · Cited by 11
Current Approaches in the Development of Molecular and Pharmacological Therapies in Craniosynostosis Utilizing Animal Models
Rachwalski, M., Khonsari, R. H., & Paternoster, G. (2018) · Molecular Syndromology · doi:10.1159/000493535 · Cited by 11
Transforming growth factor-β-regulated expression of genes in macrophages implicated in the control of cholesterol homoeostasis
Ramji, D. P., Singh, N. N., Foka, P., Irvine, S. A., & Arnaoutakis, K. (2006) · Biochemical Society Transactions · doi:10.1042/bst0341141 · Cited by 11
Activin A induces a non-fibrotic phenotype in smooth muscle cells in contrast to TGF-β
Groenendijk, B. C. W., Benus, G. F. J. D., Klous, A. M., Pacheco, Y. M., Volger, O. L., Fledderus, J. O., Ferreira, V., Engelse, M. A., Pannekoek, H., ten Dijke, P., et al. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.10.007 · Cited by 11
Mitochondrial impairment induced by postnatal ActRIIB blockade does not alter function and energy status in exercising mouse glycolytic muscle in vivo
Béchir, N., Pecchi, É., Relizani, K., Vilmen, C., Fur, Y. L., Bernard, M., Amthor, H., Bendahan, D., & Giannesini, B. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00370.2015 · Cited by 11
A Potential Negative Regulatory Function of Myostatin in the Growth of the Pacific Abalone, Haliotis discus hannai
Huang, J., Zhou, M., Chen, J., & Ke, C. (2022) · Biology · doi:10.3390/biology12010014 · Cited by 10
The Role of TGF-β, Activin and Follistatin in Inflammatory Bowel Disease
Esfahani, N. H., & Day, A. S. (2023) · Gastrointestinal Disorders · doi:10.3390/gidisord5020015 · Cited by 11
Rare heterozygous GDF6 variants in patients with renal anomalies
Martens, H., Hennies, I., Getwan, M., Christians, A., Weiss, A., Brand, F. J., Gjerstad, A. C., Christians, A., Gucev, Z. S., Geffers, R., et al. (2020) · European Journal of Human Genetics · doi:10.1038/s41431-020-0678-9 · Cited by 10
A Selection Fit Mechanism in BMP Receptor IA as a Possible Source for BMP Ligand-Receptor Promiscuity
Harth, S., Kotzsch, A., Hu, J., Sebald, W., & Mueller, T. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013049 · Cited by 11
Increased angiogenesis in primary myelofibrosis: latent transforming growth factor-β as a possible angiogenic factor
Ponce, C. C., Chauffaille, M. D. L. L. F., Ihara, S. S. M., & Silva, M. R. R. (2014) · Revista Brasileira de Hematologia e Hemoterapia · doi:10.1016/j.bjhh.2014.07.010 · Cited by 10
In vivo imaging of TGFβ signalling components using positron emission tomography
Rotteveel, L., Poot, A. J., Bogaard, H. J., ten Dijke, P., Lammertsma, A. A., & Windhorst, A. D. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2019.08.011 · Cited by 11
A Synthetic Peptide, CK2.3, Inhibits RANKL-Induced Osteoclastogenesis through BMPRIa and ERK Signaling Pathway
Nguyen, J., Kelly, S., Wood, R., Heubel, B. P., & Nohe, A. (2020) · Journal of Developmental Biology · doi:10.3390/jdb8030012 · Cited by 10
Mechanisms and factors in embryonic stem cell self-renewal
Chambers, I. (2005) · RENDICONTI LINCEI · doi:10.1007/bf02904758 · Cited by 10
Expression of Endoglin in Primary Endometrial Cancer
Zakrzewski, P. K., Cygankiewicz, A. I., Mokrosiński, J., Nowacka‐Zawisza, M., Semczuk, A., Rechberger, T., & Krajewska, W. M. (2011) · Oncology · doi:10.1159/000334240 · Cited by 10
El factor de crecimiento transformante beta como blanco terapéutico
Gálvez-Gastélum, F. J., Sandoval-Rodriguez, A. S., & Armendáriz‐Borunda, J. (2004) · Salud Pública de México · doi:10.1590/s0036-36342004000400009 · Cited by 10
Biomineralization and Bone Regeneration
Hu, J., Liu, X., & Ma, P. X. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-381422-7.10040-9 · Cited by 10
Dysregulation of Betaglycan Expression in Primary Human Endometrial Carcinomas
Zakrzewski, P. K., Mokrosiński, J., Cygankiewicz, A. I., Semczuk, A., Rechberger, T., Skomra, D. G., & Krajewska, W. M. (2011) · Cancer Investigation · doi:10.3109/07357907.2010.543213 · Cited by 10
AT1 antagonist modulates activin-like kinase 5 and TGF-β receptor II in the developing kidney
Yim, H. E., Kim, M. K., Bae, I. S., Kim, J. H., Choi, B. M., Yoo, K. H., Hong, Y. S., & Lee, J. W. (2006) · Pediatric Nephrology · doi:10.1007/s00467-006-0197-0 · Cited by 10
Exploring the Role of GDF-15 in Inflammatory Bowel Disease: A Case-Controlled Study Comparing Crohn’s Disease and Ulcerative Colitis with Non-Inflammatory Controls
Kučerka, O., Blahutová, M., Kosek, V., Mináriková, P., Horáček, J. M., Urbánek, P., & Malý, M. (2024) · Metabolites · doi:10.3390/metabo14040185 · Cited by 9
Activin A impairs ActRIIA+ neutrophil recruitment into infected skin of mice
Qi, Y., Jiang, L., Wu, C., Li, J., Wang, H., Wang, S., Chen, X., Cui, X., & Liu, Z. (2021) · iScience · doi:10.1016/j.isci.2021.102080 · Cited by 9
Adult-Specific Systemic Over-Expression Reveals Novel In Vivo Effects of the Soluble Forms of ActRIIA, ActRIIB and BMPRII
Yamawaki, K., Ueda, S., Okada, T., Oshima, T., Kakitani, M., Kato, T., & Tomizuka, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078076 · Cited by 9
Crosstalk between Erythropoiesis and Iron Metabolism
Rivella, S., Nemeth, E., & Miller, J. L. (2010) · Advances in Hematology · doi:10.1155/2010/317095 · Cited by 9
Halofuginone attenuates articular cartilage degeneration by inhibition of elevated TGF-β1 signaling in articular cartilage in a rodent osteoarthritis model
Mu, W., Xu, B., Ma, H., Ji, B., Zhang, Z., Li, J., Amat, A., & Cao, L. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7549 · Cited by 9
Modulation of the Transforming Growth Factor β1 by Vitamin E in Early Nephropathy
Cojocel, C., Al‐Maghrebi, M., Thomson, M., Rawoot, P., & Raghupathy, R. (2005) · Medical Principles and Practice · doi:10.1159/000088116 · Cited by 9
Pathomechanisms in the Kidneys in Selected Protozoan Parasitic Infections
Kot, K., Łanocha-Arendarczyk, N., Ptak, M., Łanocha, A. A., Kalisińska, E., & Kosik-Bogacka, D. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084209 · Cited by 8
Structural basis of BMP‐2 and BMP‐7 interactions with antagonists Gremlin‐1 and Noggin in Glioblastoma tumors
Choudhuri, K. S. R., & Mishra, S. (2020) · Journal of Computational Chemistry · doi:10.1002/jcc.26407 · Cited by 8
Endoglin Wild Type and Variants Associated With Hereditary Hemorrhagic Telangiectasia Type 1 Undergo Distinct Cellular Degradation Pathways
Gariballa, N., Kizhakkedath, P., Akawi, N. A., John, A., & Ali, B. R. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.828199 · Cited by 8
Changes in transcriptomic and behavioural traits in activity and ventilation rates associated with divergent individual feed efficiency in gilthead sea bream (Sparus aurata)
Calduch-Giner, J. À., Rosell-Moll, E., Besson, M., Vergnet, A., Bruant, J.-S., Clota, F., Holhorea, P. G., Allal, F., Vandeputte, M., & Pérez‐Sánchez, J. (2023) · Aquaculture Reports · doi:10.1016/j.aqrep.2023.101476 · Cited by 8
Influence of thrombophlebitis on TGF-Î˛1 and its signaling pathway in the vein wall.
Kowalewski, R., Małkowski, A., Gacko, M., & Sobolewski, K. (2011) · Folia Histochemica et Cytobiologica · doi:10.2478/v10042-010-0041-z · Cited by 9
Inactivation of Bmp4 from the Tbx1 Expression Domain Causes Abnormal Pharyngeal Arch Artery and Cardiac Outflow Tract Remodeling
Nie, X., Brown, C. B., Wang, Q., & Jiao, K. (2010) · Cells Tissues Organs · doi:10.1159/000321170 · Cited by 8
Structural and functional characterizations of activin type 2B receptor (acvr2b) ortholog from the marine fish, gilthead sea bream, Sparus aurata: evidence for gene duplication of acvr2b in fish
Funkenstein, B., Krol, E., Esterin, E., & Kim, Y.-S. (2012) · Journal of Molecular Endocrinology · doi:10.1530/jme-12-0075 · Cited by 9
Stimulation of primordial follicle assembly by estradiol-17β requires the action of bone morphogenetic protein-2 (BMP2)
Chakraborty, P. B., & Roy, S. K. (2017) · Scientific Reports · doi:10.1038/s41598-017-15833-4 · Cited by 8
Growth Factors in the Gastrointestinal Tract
Kuemmerle, J. F., Barnard, J. A., & McHugh, K. M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382026-6.00008-7 · Cited by 8
Molecular Biology of Colon Cancer
Grady, W. M. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-215-1_1 · Cited by 8
Novel Pharmacological Targets for Pulmonary Arterial Hypertension
Klinger, J. R. (2021) · Comprehensive physiology · doi:10.1002/cphy.c200015 · Cited by 10
Modulation of TGF‑β activity by latent TGF‑β‑binding protein 1 in human osteoarthritis fibroblast‑like synoviocytes
Wang, X., Dong, C., Li, N., Ma, Q., Yun, Z., Cai, C., An, M., & Ma, B. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.8086 · Cited by 7
Association of TGFBR2 rs6785358 Polymorphism with Increased Risk of Congenital Ventricular Septal Defect in a Chinese Population
Li, X., Shen, C., Zhang, R., Shi, J.-K., Li, Z., Liu, H., Sun, B., Wang, K., & Yan, L. (2015) · Pediatric Cardiology · doi:10.1007/s00246-015-1189-2 · Cited by 7
Targeting fibroblast growth factor receptors causes severe craniofacial malformations in zebrafish larvae
Gebuijs, L., Wagener, F. A. D. T. G., Zethof, J., Carels, C. E. L., den Hoff, J. W. V., & Metz, J. R. (2022) · PeerJ · doi:10.7717/peerj.14338 · Cited by 8
Toward a better understanding of the interaction between TGF-β family members and their ALK receptors
Romano, V. C., Raimondo, D., Calvanese, L., D’Auria, G., Tramontano, A. L., & Falcigno, L. (2012) · Journal of Molecular Modeling · doi:10.1007/s00894-012-1370-y · Cited by 7
Targeting Smad-Mediated TGFß Pathway in Coronary Artery Bypass Graft
Ungogo, M. A. (2020) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248420951037 · Cited by 10
Bone Morphogenetic Protein Signaling Agonist SB4 (BMPSB4) Inhibits Corticotroph Pituitary Neuroendocrine Tumors by Activation of Autophagy via a BMP4/SMADs-Dependent Pathway
Xu, L., Ning, R., Du, X., Zhang, Y., Gu, C., Wang, B., Bian, L., Sun, Q., Sun, Y., & Ren, J. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00021 · Cited by 6
Transmission analysis of TGFB1 gene polymorphisms in non-syndromic cleft lip with or without cleft palate
Raju, G. T., Bhaskar, L. V., Murthy, J., Munirajan, A., & Paul, S. F. D. (2017) · International Journal of Pediatric Otorhinolaryngology · doi:10.1016/j.ijporl.2017.06.015 · Cited by 6
Growth Factors in the Gastrointestinal Tract
Barnard, J. A., & McHugh, K. M. (2006) · Elsevier eBooks · doi:10.1016/b978-012088394-3/50010-6 · Cited by 6
Impact of the Transforming Growth Factor β (TGF-β) on Brain Aneurysm Formation and Development: A Literature Review
Sutkowska, K., Koper‐Lenkiewicz, O. M., Matowicka-Karna, J., & Kamińska, J. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01572-y · Cited by 5
Testicular expression of the TGF-β1 system and the control of Leydig cell proliferation
González, C. R., Saul, C. R., & González-Calvar, S. I. (2013) · Advances in Bioscience and Biotechnology · doi:10.4236/abb.2013.410a4001 · Cited by 5
Membrane Receptor‐Mediated Disruption of Cellular Homeostasis: Changes in Intracellular Signaling Pathways Increase the Toxicity of Ochratoxin A
Aydemir, M. C., Yaman, İ., & Kilic, M. A. (2024) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202300777 · Cited by 5
A Proliferation-Inducing Ligand Regulation in Polymorphonuclear Neutrophils by Panax ginseng
Ratajczak–Wrona, W., Wawrusiewicz‐Kurylonek, N., Garley, M., Kretowski, A. J., & Jabłońska, E. (2020) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-020-00597-z · Cited by 5
Literature-Based Automated Reconstruction, Expansion, and Refinement of the TGF-β Superfamily Ligand-Receptor Network
Mei, Q., & Saiz, L. (2014) · The Journal of Membrane Biology · doi:10.1007/s00232-014-9643-2 · Cited by 5
Transforming Growth Factor-βs in the Brain
KRIEGLSTEIN, K. G. (2006) · Springer eBooks · doi:10.1007/0-387-30395-2_6 · Cited by 5
Contribution of the TGFβ signaling pathway to pigmentation in sea cucumber (Apostichopus japonicus)
Yao, L., Zhao, B., Wang, Q., Jiang, X., Sha, H., Hu, W., & Li, C.-L. F. (2023) · Frontiers in Marine Science · doi:10.3389/fmars.2023.1101725 · Cited by 5
Serum miR-503 is a Candidate Biomarker for Differentiating Metabolic Healthy Obesity from Metabolic Unhealthy Obesity
Yue, H.-Q., Zhou, Y., Yue, G., Tang, C.-Y., Wang, F., & Zhou, H. (2020) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s262888 · Cited by 5
Development of an in vitro potency bioassay for therapeutic IL-13 antagonists: The A-549 cell bioassay
Miller, R., Sadhukhan, R., & Wu, C. (2008) · Journal of Immunological Methods · doi:10.1016/j.jim.2008.02.009 · Cited by 5
TGF-Β Family Inhibitors Blunt Adipogenesis Via Non-Canonical Regulation Of SMAD PathwaysPreprint
Aykul, S., Maust, J., Floer, M., & Martı́nez-Hackert, E. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.12.988568 · Cited by 5
TGF-β signaling in organoids: The mechanisms and applications in 3D
Zhu, S., Liu, J., Qiu, X., Cai, G., & Gao, M. (2025) · Cell organoid (Print) · doi:10.26599/co.2025.9410015 · Cited by 4
Contribution of the TGFβ signaling pathway to growth of Pacific oyster (Crassostrea gigas)
Yao, L., Liu, Y., Li, L., & Jiang, X. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.740983 · Cited by 4
Advances in Regenerative Medicine for Orthopedic Injuries: A Comprehensive Review
Das, S., Thakur, A., Datta, A., Sahoo, A., Bandyopadhyay, S., & Sah, A. K. (2025) · Cureus · doi:10.7759/cureus.79860 · Cited by 5
A Review of the Prevention and Treatment of Hypertrophic Scars: Part II. Experimental Studies
Karagöz, H., Bayram, Y., Sever, C., Şahi̇n, C., Külahçı, Y., & Ülkür, E. (2012) · Archives of Clinical and Experimental Surgery (ACES) · doi:10.5455/aces.20120218125115 · Cited by 4
The Genetics of Colorectal Cancer
Kaz, A. M., & Grady, W. M. (2010) · Cancer metastasis · doi:10.1007/978-90-481-8833-8_3 · Cited by 4
Activin A and Acvr2b mRNA from Umbilical Cord Blood Are Not Reliable Markers of Mild or Moderate Neonatal Hypoxic–Ischemic Encephalopathy
O’Sullivan, M. P., Denihan, N. M., Sikora, K. M., Finder, M., Ahearne, C. E., Clarke, G. A., Hallberg, B., Boylan, G. B., & Murray, D. M. (2021) · Neuropediatrics · doi:10.1055/s-0041-1725012 · Cited by 4
Generation and Identification of Genetically Modified Mice for BMP Receptors
Yang, J., & Mishina, Y. M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8904-1_12 · Cited by 4
Transforming growth factor (TGF) – is it a key protein in mammalian reproductive biology?
Rybska, M., Knap, S., Stefańska, K., Jankowski, M., Chamier-Gliszczyńska, A., Popis, M., Ješeta, M., Bukowska, D., Antosik, P., Kempisty, B., et al. (2018) · Medical Journal of Cell Biology · doi:10.2478/acb-2018-0020 · Cited by 4
KGF and BMP‐6 intervene in cellular reprogramming and in mesenchymal‐epithelial transition (MET) of 3T3L1 mouse adipose cells
Reza, A. M. M. T., Lee, S., Shiwani, S., & Singh, N. K. (2014) · Cell Biology International · doi:10.1002/cbin.10407 · Cited by 4
Amniotic Epithelial Stem Cells in Regenerative Medicine
Marongiu, F., Gramignoli, R., Miki, T., Ranade, A. R., Ellis, E. C. S., Dorko, K., Strom, S. C., & Davila, J. C. (2009) · doi:10.1002/9780470480151.ch10 · Cited by 4
A secreted Echinococcus multilocularis activin A homologue promotes regulatory T cell expansionPreprint
Nono, J. K., Lutz, M. B., & Brehm, K. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/618140 · Cited by 4
Increased of Langerhans Cells in Smokeless Tobacco-Associated Oral Mucosal Lesions
vila, R., de Molon, R. S., Silva, M. M. L., Consolaro, R. B., & Consolaro, A. G. (2012) · Archives of Clinical and Experimental Surgery (ACES) · doi:10.5455/aces.20120229052919 · Cited by 3
An Update of Bone Morphogenetic Proteins as Biomarker and Therapy for Cancer
Rahman, C. C. M. M. M. (2015) · Journal of Carcinogenesis & Mutagenesis · doi:10.4172/2157-2518.1000e114 · Cited by 3
Generation of optimized preparations of bone morphogenetic proteins for bone regeneration
Malysheva, K. V., Spasyuk, I. M., Pavlenko, O. K., Stoika, R. S., & Korchynskyi, O. (2016) · The Ukrainian Biochemical Journal · doi:10.15407/ubj88.06.087 · Cited by 3
The Role of TGF-β in Gastrointestinal Cancers
Wang, H., Gong, X., Xu, J., & Xie, R. (2018) · Journal of Cancer Science & Therapy · doi:10.4172/1948-5956.1000566 · Cited by 3
Role of transforming growth factor-β in airway remodelling in bronchiolitis obliterans
Wang, Z. (2023) · Growth Factors · doi:10.1080/08977194.2023.2239356 · Cited by 3
The Role of TGF-β in Bleomycin Induced Pulmonary Fibrosis
Khalil, N., & O'Connor, R. N. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-292-2_36 · Cited by 3
Activin Signaling Disruption in the Cochlea Does Not Influence Hearing in Adult Mice
Horvath, L., Bodmer, D., Radojevic, V., & Naldi, A. M. (2014) · Audiology and Neurotology · doi:10.1159/000366152 · Cited by 3
Assessment of goat activin receptor type IIB knockdown by short hairpin RNAsin vitro
Patel, A. K., Tripathi, A. K., Shah, R. K., Patel, U. A., & Joshi, C. G. (2014) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2014.922574 · Cited by 3
Mice with Disrupted TGFβ Signaling Have Normal Cerebella Development, but Exhibit Facial Dysmorphogenesis and Strain-Dependent Deficits in Their Body Wall
Asano, Y., Koishi, K., Frugier, T., & McLennan, I. S. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9354-x · Cited by 3
The potential role of transforming growth factor beta family ligand interactions in prostate cancer
Croxford, K. P., Reader, K. L., & Nicholson, H. D. (2017) · AIMS molecular science · doi:10.3934/molsci.2017.1.41 · Cited by 3
The TGFβ and Androgen Receptor Signaling Pathways Converge to Support Anoikis Resistance in Triple Negative Breast Cancer
Rosas, E., & Richer, J. K. (2021) · Springer eBooks · doi:10.1007/978-3-030-73856-3_9 · Cited by 3
Elevated Expression of TGFB1 in PBMCs Is Associated with Intracranial Aneurysm Formation, but TGFB3 Expression Implicated Rupture
Sutkowska, K., Koper‐Lenkiewicz, O. M., Żebrowska-Nawrocka, M., Jakoniuk, M., Łysoń, T., Tylicka, M., Balcerczak, E. I., Matowicka-Karna, J., & Kamińska, J. (2025) · Biomedicines · doi:10.3390/biomedicines13061273 · Cited by 2
Mitigating loss of lean muscle in GLP-1 and dual GLP-1/GIP agonists: Pipeline opportunities and limitations
Hierholzer, J. D., Benson, H., Ewida, H. A., & Ahmed, M. S. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168172 · Cited by 2
Relationship Between Iron and Erythropoiesis
Sposi, N. M. (2012) · Contact-less Assessment of In-vivo Body Signals Using Microwave Doppler Radar (InTech) · doi:10.5772/33246 · Cited by 2
Pluripotent Stem Cell Studies Elucidate the Underlying Mechanisms of Early Embryonic Development
Li, L., & Jing, N. (2011) · Genes · doi:10.3390/genes2020298 · Cited by 2
Human-induced pluripotent stem cells (iPSC) as a source of insulin-producing cells
Pellegrini, S., & Sordi, V. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814831-0.00028-2 · Cited by 2
Exogenous FSH/LH modulates TGF beta signaling genes in granulosa cells of Simmental heifers without affecting IVP results
Scarlet, D., Şerbetçi, İ., Lautner, M., Kowalewski, M. P., & Bollwein, H. (2024) · Theriogenology · doi:10.1016/j.theriogenology.2024.07.010 · Cited by 2
Phenotypic Analyses of Genetically Modified Mice for BMP Receptors
Yang, J., & Mishina, Y. M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8904-1_13 · Cited by 2
Investigating the Conformational Preferences of Transforming Growth Factor-β Isoforms using Targeted Molecular Dynamics Simulations
Warner, D. J., Paterson, I. C., & Sessions, R. B. (2009) · Journal of Chemical Theory and Computation · doi:10.1021/ct800483q · Cited by 2
Interaction of TGFβ3 ligand with its receptors type II (TβRII) and type I (TβRI): A unique mechanism of protein-protein association
Dawn, A., Khatri, K. S., Karmakar, S., & Deep, S. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140485 · Cited by 2
Regulation of Calvarial Bone Growth by Molecules Involved in the Craniosynostoses
Benson, M. D., & Opperman, L. A. (2011) · Monographs in human genetics · doi:10.1159/000320668 · Cited by 2
Transforming growth factor β signaling in colorectal cancer
Grady, W. M. (2007) · Current Colorectal Cancer Reports · doi:10.1007/s11888-007-0002-x · Cited by 2
Definitive Endoderm from Embryonic Stem Cells
Semb, H. (2006) · Regenerative Medicine · doi:10.2217/17460751.1.4.489 · Cited by 2
Structural and Functional Characteristics of a Soluble Form of Endoglin in the Context of Preeclampsia
Gregory, A. (2011) · TSpace (University of Toronto) · Cited by 2
The role of novel transmembrane serine proteases : implications for arthritis
Patel, A. (2011) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 2
GROWTH DIFFERENTIATION FACTOR 9 SIGNALLING IN THE OVARY
Kaivo-Oja, N. (2007) · Työväentutkimus Vuosikirja · Cited by 2
Pathobiology of Pulmonary Arterial Hypertension
Lewis, M. I., Voelkel, N. F., & Kadri, F. (2024) · Current Respiratory Medicine Reviews · doi:10.2174/011573398x266579240226064718 · Cited by 1
Circulating Muscle Markers for Sarcopenia in Peritoneal Dialysis
Xu, L., Ng, J. K., Fung, W. W., Chan, G. C., Chow, K., & Szeto, C. (2025) · International Journal of Nephrology · doi:10.1155/ijne/8817404 · Cited by 2
Isolation and Identification of Transforming Growth Factor β from In Vitro Matured Cumulus Oocyte Complexes
Widjiati, W., Boediono, A., Sumitro, S. B., Hinting, A., Aulanni’am, A., & Susilowati, T. (2012) · HAYATI Journal of Biosciences · doi:10.4308/hjb.19.1.6 · Cited by 1
Cell Population Model to Track Stochastic Cellular Decision-Making During Differentiation
Task, K., & Banerjee, I. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9224-9_3 · Cited by 1
Transforming growth factor-β and skeletal homeostasis
Xu, X., & Cao, X. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814841-9.00047-6 · Cited by 1
TGFβ Pathway
Robert, J. (2014) · Springer eBooks · doi:10.1007/978-3-319-14340-8_5 · Cited by 1
Transforming Growth Factor-β1 and Tumor Development
Dahl, L. (2023) · Science Insights · doi:10.15354/si.23.re298 · Cited by 1
Hypoxia and collagen deposition in the kidneys infected with Acanthamoeba sp.
Kot, K., Grabowska, M., Tarnowski, M., Kupnicka, P., Tomasiak, P., Kosik-Bogacka, D. I., & Łanocha-Arendarczyk, N. (2024) · Scientific Reports · doi:10.1038/s41598-024-79848-4 · Cited by 1
TGF-β Signaling Pathway and Its Therapeutic Role in Cancer
James, A. W., Bhat, H. M., Yousuf, S., Jan, M., Rehman, M. U., & Rashid, S. M. (2025) · Springer eBooks · doi:10.1007/978-981-96-2763-9_11 · Cited by 1
Activin type IIB receptor blockade does not limit adenosine triphosphate supply in mouse skeletal muscle in Vivo
Béchir, N., Pecchi, É., Vilmen, C., Bernard, M., Bendahan, D., & Giannesini, B. (2018) · Muscle & Nerve · doi:10.1002/mus.26306 · Cited by 1

Authors: de Caestecker, M.
Venue: Cytokine & Growth Factor Reviews
Publisher: Elsevier BV
Published: 2004-02
Volume: 15
Issue: 1
Pages: 1-11
ISSN: 1359-6101 (ISSN-L)
DOI: 10.1016/j.cytogfr.2003.10.004
OpenAlex: W2084954119
Cited by: 464
References: 161
Citations by year: 2026: 5 · 2025: 13 · 2024: 11 · 2023: 13 · 2022: 14 · 2021: 16 · 2020: 19 · 2019: 20 · 2018: 23 · 2017: 17 · 2016: 14 · 2015: 11 · 2014: 21 · 2013: 23 · 2012: 25
FWCI: 1.74
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cytokine & Growth Factor Reviews (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 › Receptor Mechanisms and Signaling
Health Sciences › Medicine › Hepatology › Liver physiology and pathology
Keywords: TGF-beta superfamily, TGF-beta receptor, type I receptor, type II receptor, serine/threonine kinase receptors, receptor activation, ligand-receptor interactions, mammalian cells
MeSH terms: Animals, Gene Expression Regulation, Multigene Family, Humans, Ligands, Models, Biological, Protein Binding, Endosomes, Signal Transduction, Receptors, Transforming Growth Factor beta, Activins

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

The transforming growth factor-β superfamily of receptors

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks