Cited by 7,556

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

TGF-β SIGNAL TRANSDUCTION

Massagué, J.·1998·Annual Review of Biochemistry

Open this paper in CoChat — free account

Abstract

The transforming growth factor β (TGF-β) family of growth factors control the development and homeostasis of most tissues in metazoan organisms. Work over the past few years has led to the elucidation of a TGF-β signal transduction network. This network involves receptor serine/threonine kinases at the cell surface and their substrates, the SMAD proteins, which move into the nucleus, where they activate target gene transcription in association with DNA-binding partners. Distinct repertoires of receptors, SMAD proteins, and DNA-binding partners seemingly underlie, in a cell-specific manner, the multifunctional nature of TGF-β and related factors. Mutations in these pathways are the cause of various forms of human cancer and developmental disorders.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1146/annurev.biochem.67.1.753

Cites

7 of 7 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
DPC4 , A Candidate Tumor Suppressor Gene at Human Chromosome 18q21.1
Hahn, S. A., Schutte, M., Shamsul Hoque, A. T. M., Moskaluk, C. A., da Costa, L. T., Rozenblum, E., Weinstein, C. L., Fischer, A., Yeo, C. J., Hruban, R. H., et al. (1996) · Science · doi:10.1126/science.271.5247.350 · Cited by 2,337
Transforming growth factor beta 1 null mutation in mice causes excessive inflammatory response and early death.
Kulkarni, A. B., Huh, C. G., Becker, D., Geiser, A., Lyght, M., Flanders, K. C., Roberts, A. B., Sporn, M. B., Ward, J. M., & Karlsson, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.2.770 · Cited by 1,967
pl5INK4B is a potentia| effector of TGF-β-induced cell cycle arrest
Hannon, G. J., & Beach, D. (1994) · Nature · doi:10.1038/371257a0 · Cited by 1,950
Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
Schreiber, S. L. (1991) · Science · doi:10.1126/science.1702904 · Cited by 1,494
Activation of Signalling by the Activin Receptor Complex
Attisano, L., Wrana, J. L., Montalvo, E., & Massagué, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.3.1066 · Cited by 316
Self-citation
Dorsal-ventral patterning of the Drosophila embryo depends on a putative negative growth factor encoded by the short gastrulation gene.
Francois, V, Solloway, M., O'Neill, J. W., Emery, J., & Bier, E. (1994) · Genes & Development · doi:10.1101/gad.8.21.2602 · Cited by 308

Show all 7 references

Items 101–180 of 180

Internalization-Dependent and -Independent Requirements for Transforming Growth Factor β Receptor Signaling via the Smad Pathway
Penheiter, S. G., Mitchell, H., Garamszegi, N., Edens, M., Doré, J. J. E., & Leof, E. B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4750-4759.2002 · Cited by 167
The Kindler syndrome protein is regulated by transforming growth factor-β and involved in integrin-mediated adhesion
Kloeker, S., Major, M. B., Calderwood, D. A., Ginsberg, M. H., Jones, D. A., & Beckerle, M. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307978200 · Cited by 163
Loss of Oncogenic H-ras-Induced Cell Cycle Arrest and p38 Mitogen-Activated Protein Kinase Activation by Disruption of Gadd45a
Bulavin, D. V., Kovalsky, O., Hollander, M. C., & Fornace, A. J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.11.3859-3871.2003 · Cited by 161
A molecular signature for anastasis, recovery from the brink of apoptotic cell death
Sun, G., Guzman, E., Balasanyan, V., Conner, C. M., Wong, K., Zhou, H. R., Kosik, K. S., & Montell, D. J. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201706134 · Cited by 151
Signaling pathways weigh in on decisions to make or break skeletal muscle
Guttridge, D. C. (2004) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/01.mco.0000134364.61406.26 · Cited by 149
Cell Proliferation, Reactive Oxygen and Cellular Glutathione
Day, R. M., & Suzuki, Y. J. (2005) · Dose-Response · doi:10.2203/dose-response.003.03.010 · Cited by 149
Kallmann syndrome: 14 novel mutations in KAL1 and FGFR1(KAL2): MUTATIONS IN BRIEF
Albuisson, J., Pêcheux, C., Carel, J.-C., Lacombe, D., Leheup, B., Lapuzina, P., Bouchard, P., Legius, E., Matthijs, G., Wasniewska, M., et al. (2005) · Human Mutation · doi:10.1002/humu.9298 · Cited by 146
Differential neuroendocrine responses to chronic variable stress in adult Long Evans rats exposed to handling-maternal separation as neonates
Ladd, C. O., Thrivikraman, K. V., Huot, R. L., & Plotsky, P. M. (2005) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2004.12.004 · Cited by 145
Transforming Growth Factor-β Family Ligands Can Function as Antagonists by Competing for Type II Receptor Binding
Aykul, S., & Martinez-Hackert, E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.713487 · Cited by 143
Targeting Endogenous Transforming Growth Factor β Receptor Signaling in SMAD4-Deficient Human Pancreatic Carcinoma Cells Inhibits Their Invasive Phenotype
Subramanian, G., Schwarz, R. E., Higgins, L., McEnroe, G., Chakravarty, S., Dugar, S., & Reiss, M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0018 · Cited by 138
The G protein-coupled receptor heterodimer network (GPCR-HetNet) and its hub components
Borroto-Escuela, D., Brito, I., Romero-Fernandez, W., Di Palma, M., Oflijan, J., Skieterska, K., Duchou, J., Van Craenenbroeck, K., Suárez-Boomgaard, D., Rivera, A., et al. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15058570 · Cited by 134
Developmental Signaling in Hydra: What Does It Take to Build a “Simple” Animal?
Steele, R. E. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0744 · Cited by 129
Sarcopenia: Molecular Pathways and Potential Targets for Intervention
Pascual-Fernández, J., Fernández-Montero, A., Córdova-Martínez, A., Pastor, D., Martínez-Rodríguez, A., & Roche, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228844 · Cited by 125
Neural melanocortin receptors in obesity and related metabolic disorders
Girardet, C., & Butler, A. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.05.004 · Cited by 128
The Evolution of the MAP Kinase Pathways: Coduplication of Interacting Proteins Leads to New Signaling Cascades
Caffrey, D. R., O'Neill, L. A. J., & Shields, D. C. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006578 · Cited by 124
The role of innate immunity activation in house dust mite allergy
Jacquet, A. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.05.014 · Cited by 126
Untitled work
Kang (2001) · doi:10.1016/s0749-0690(05)70091-4 · Cited by 125
Turning it up a Notch: cross-talk between TGFβ and Notch signaling: What the papers say
Klüppel, M., & Wrana, J. L. (2005) · BioEssays · doi:10.1002/bies.20187 · Cited by 121
Influence of BMPs on the formation of osteoblastic lesions in metastatic prostate cancer
Feeley, B. T., Gamradt, S. C., Hsu, W. K., Liu, N., Krenek, L., Robbins, P., Huard, J., & Lieberman, J. R. (2005) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.050802 · Cited by 120
Toll-like receptor 4: innate immune regulator of neuroimmune and neuroendocrine interactions in stress and major depressive disorder
Liu, J., Buisman-Pijlman, F., & Hutchinson, M. R. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00309 · Cited by 119
Extensive extracellular matrix depositions in active multiple sclerosis lesions.
van Horssen, J., Bö, L., Dijkstra, C. D., & de Vries, H. E. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.08.005 · Cited by 119
Sorting Nexin 6, a Novel SNX, Interacts with the Transforming Growth Factor-β Family of Receptor Serine-Threonine Kinases
Parks, W. T., Frank, D. B., Huff, C., Renfrew Haft, C., Martin, J., Meng, X., de Caestecker, M. P., McNally, J. G., Reddi, A., Taylor, S. I., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100606200 · Cited by 113
Depression and impulse control disorders in Parkinson׳s disease: two sides of the same coin?
Vriend, C., Pattij, T., van der Werf, Y. D., Voorn, P., Booij, J., Rutten, S., Berendse, H. W., & van den Heuvel, O. A. (2014) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2013.11.001 · Cited by 106
The tale of transforming growth factor‐beta (TGFβ) signaling: A soigné enigma
Chaudhury, A., & Howe, P. H. (2009) · IUBMB Life · doi:10.1002/iub.239 · Cited by 105
“239 IUBMB Life, 61(10): 929–939, October 2009”
BackgroundInfluential
Estrogen dependent signaling in reproductive tissues—A role for estrogen receptors and estrogen related receptors
Gibson, D. A., & Saunders, P. T. K. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.09.026 · Cited by 107
IL1 receptor accessory protein like, a protein involved in X-linked mental retardation, interacts with Neuronal Calcium Sensor-1 and regulates exocytosis
Bahi, N. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg147 · Cited by 105
Distinct Pathways for the Trafficking of Angiotensin II and Adrenergic Receptors from the Endoplasmic Reticulum to the Cell Surface
Wu, G., Zhao, G., & He, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305707200 · Cited by 103
TGFβ receptor signaling is essential for inflammation-induced but not β-cell workload-induced β-cell proliferation
Xiao, X., Wiersch, J., El-Gohary, Y., Guo, P., Prasadan, K., Paredes, J., Welsh, C., Shiota, C., & Gittes, G. K. (2013) · Diabetes · doi:10.2337/db12-1428 · Cited by 102
Structural Basis for the Versatile Interactions of Smad7 with Regulator WW Domains in TGF-β Pathways
Aragón, E., Goerner, N., Xi, Q., Gomes, T., Gao, S., Massagué, J., & Macias, M. J. (2012) · Structure · doi:10.1016/j.str.2012.07.014 · Cited by 99
Self-citation
Molecular Cargo Delivery Using Multicellular Magnetic Microswimmers
Yan, X., Xu, J., Zhou, Q., Jin, D., Vong, C. I., Feng, Q., Ng, D. H. L., Bian, L., & Zhang, L. (2019) · Applied Materials Today · doi:10.1016/j.apmt.2019.02.006 · Cited by 94
Evolution of the TGF-β Signaling Pathway and Its Potential Role in the Ctenophore, Mnemiopsis leidyi
Pang, K., Ryan, J. F., Baxevanis, A. D., & Martindale, M. Q. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024152 · Cited by 93
Remyelination is altered by bone morphogenic protein signaling in demyelinated lesions
Sabo, J. K., Aumann, T. D., Merlo, D., Kilpatrick, T. J., & Cate, H. S. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5859-10.2011 · Cited by 93
Derepression by Depolymerization
Qiao, F., Song, H., Kim, C. A., Sawaya, M. R., Hunter, J. B., Gingery, M., Rebay, I., Courey, A. J., & Bowie, J. U. (2004) · Cell · doi:10.1016/j.cell.2004.07.010 · Cited by 92
Therapeutic applications of iminosugars: Current perspectives and future opportunities
Horne, G., & Wilson, F. X. (2011) · Progress in medicinal chemistry · doi:10.1016/b978-0-12-381290-2.00004-5 · Cited by 87
Diversity in Fibroblast Growth Factor Receptor 1 Regulation: Learning from the Investigation of Kallmann Syndrome
Kim, S. ‐., Hu, Y., Cadman, S., & Bouloux, P. (2008) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2007.01627.x · Cited by 87
Calcium mobilizing second messengers derived from NAD
Guse, A. H. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.12.015 · Cited by 82
Pervasive positive selection on duplicated and nonduplicated vertebrate protein coding genes
Studer, R. A., Penel, S., Duret, L., & Robinson-Rechavi, M. (2008) · Genome Research · doi:10.1101/gr.076992.108 · Cited by 84
TGF-β receptor I/II trafficking and signaling at primary cilia are inhibited by ceramide to attenuate cell migration and tumor metastasis
Gencer, S., Oleinik, N., Kim, J., Panneer Selvam, S., De Palma, R., Dany, M., Nganga, R., Thomas, R. J., Senkal, C. E., Howe, P. H., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aam7464 · Cited by 83
Fucoidan inhibits UVB-induced MMP-1 promoter expression and down regulation of type I procollagen synthesis in human skin fibroblasts
Moon, H. J., Lee, S. H., Ku, M. J., Yu, B. C., Jeon, M. J., Jeong, S. H., Stonik, V. A., Zvyagintseva, T. N., Ermakova, S. P., & Lee, Y. H. (2009) · European Journal of Dermatology · doi:10.1684/ejd.2008.0611 · Cited by 81
On the role of volume transmission and receptor-receptor interactions in social behaviour: focus on central catecholamine and oxytocin neurons
Fuxe, K., Borroto-Escuela, D. O., Romero-Fernandez, W., Ciruela, F., Manger, P., Leo, G., Díaz-Cabiale, Z., & Agnati, L. F. (2012) · Brain Research · doi:10.1016/j.brainres.2012.01.062 · Cited by 81
Bone morphogenetic proteins 4, 6, and 7 are up-regulated in mouse spinal cord during experimental autoimmune encephalomyelitis
Ara, J., See, J., Mamontov, P., Hahn, A., Bannerman, P., Pleasure, D., & Grinspan, J. B. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21462 · Cited by 79
Long-term physical exercise induces changes in sirtuin 1 pathway and oxidative parameters in adult rat tissues
Bayod, S., del Valle, J., Lalanza, J. F., Sanchez-Roige, S., de Luxán-Delgado, B., Coto-Montes, A., Canudas, A. M., Camins, A., Escorihuela, R. M., & Pallàs, M. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.08.004 · Cited by 77
Regulation of Notch signaling genes during BMP2-induced differentiation of osteoblast precursor cells
de Jong, D. S., Steegenga, W. T., Hendriks, J. M. A., van Zoelen, E. J. J., Olijve, W., & Dechering, K. J. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.150 · Cited by 74
The ER and ageing II: Calcium homeostasis
Puzianowska-Kuznicka, M., & Kuznicki, J. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.05.002 · Cited by 73
Increased IL-1β in cortex of aged rats is accompanied by downregulation of ERK and PI-3 kinase
Maher, F. O., Martin, D. S. D., & Lynch, M. A. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.08.007 · Cited by 73
Endofin, a FYVE Domain Protein, Interacts with Smad4 and Facilitates Transforming Growth Factor-β Signaling
Chen, Y.-G., Wang, Z., Ma, J., Zhang, L., & Lu, Z. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611704200 · Cited by 73
Mammalian Glycerophosphodiester Phosphodiesterases
YANAKA, N. (2007) · Bioscience, Biotechnology, and Biochemistry · doi:10.1271/bbb.70062 · Cited by 71
Aging-related changes in the iron status of skeletal muscle
DeRuisseau, K. C., Park, Y.-M., DeRuisseau, L. R., Cowley, P. M., Fazen, C. H., & Doyle, R. P. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.08.011 · Cited by 69
Novel action of activin and bone morphogenetic protein in regulating aldosterone production by human adrenocortical cells
Suzuki, J., Otsuka, F., Inagaki, K., Takeda, M., Ogura, T., & Makino, H. (2004) · Endocrinology · doi:10.1210/en.2003-0968 · Cited by 66
Functional Significance of Smad2 in Regulating Basal Keratinocyte Migration During Wound Healing
Hosokawa, R., Urata, M. M., Ito, Y., Bringas, P., & Chai, Y. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2005.23963.x · Cited by 63
Small-Molecule Inhibitors of Signal Transducer and Activator of Transcription 3 Protect Against Angiotensin II–Induced Vascular Dysfunction and Hypertension
Johnson, A. W., Kinzenbaw, D. A., Modrick, M. L., & Faraci, F. M. (2013) · Hypertension · doi:10.1161/hypertensionaha.111.00299 · Cited by 63
Foxc1 controls the growth of the murine frontal bone rudiment by direct regulation of a Bmp response threshold of Msx2
Sun, J., Ishii, M., Ting, M.-C., & Maxson, R. (2013) · Development · doi:10.1242/dev.085225 · Cited by 57
BAMBI Elimination Enhances Alternative TGF-β Signaling and Glomerular Dysfunction in Diabetic Mice
Fan, Y., Li, X., Xiao, W., Fu, J., Harris, R. C., Lindenmeyer, M., Cohen, C. D., Guillot, N., Baron, M. H., Wang, N., et al. (2015) · Diabetes · doi:10.2337/db14-1397 · Cited by 57
The TGFβ pathway stimulates ovarian cancer cell proliferation by increasing IGF1R levels
Alsina‐Sanchis, E., Figueras, A., Lahiguera, Á., Vidal, A., Casanovas, O., Graupera, M., Villanueva, A., & Viñals, F. (2016) · International Journal of Cancer · doi:10.1002/ijc.30233 · Cited by 57
Type II Transforming Growth Factor-β Receptor Recycling Is Dependent upon the Clathrin Adaptor Protein Dab2
Penheiter, S. G., Deep Singh, R., Repellin, C. E., Wilkes, M. C., Edens, M., Howe, P. H., Pagano, R. E., & Leof, E. B. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-12-1019 · Cited by 57
A new mechanism for the regulation of Gab1 recruitment to the plasma membrane
Eulenfeld, R., & Schaper, F. (2009) · Journal of Cell Science · doi:10.1242/jcs.037226 · Cited by 57
Targeting G protein coupled receptor-related pathways as emerging molecular therapies
Ghanemi, A. (2015) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2013.07.007 · Cited by 53
Attenuation of TGF-β signaling supports tumor progression of a mesenchymal-like mammary tumor cell line in a syngeneic murine model
Biswas, T., Gu, X., Yang, J., Ellies, L. G., & Sun, L.-Z. (2014) · Cancer Letters · doi:10.1016/j.canlet.2013.12.018 · Cited by 52
“TGF-b signaling and its functions in normal epithelial tissues have been extensively reviewed [7–10].”
Setting Up a Bioluminescence Resonance Energy Transfer High throughput Screening Assay to Search for Protein/Protein Interaction Inhibitors in Mammalian Cells
Couturier, C., & Deprez, B. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00100 · Cited by 52
Transforming growth factor-β1 acts via TβR-I on microglia to protect against MPP+-induced dopaminergic neuronal loss
Liu, Z., Chen, H.-Q., Huang, Y., Qiu, Y.-H., & Peng, Y.-P. (2016) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2015.08.006 · Cited by 51
Pivotal role of RanBP9 in integrin‐dependent focal adhesion signaling and assembly
Woo, J. A., Roh, S., Lakshmana, M. K., & Kang, D. E. (2012) · The FASEB Journal · doi:10.1096/fj.11-194423 · Cited by 45
Estradiol enhances light-induced expression of transcription factors in the SCN
Abizaid, A., Mezei, G., & Horvath, T. L. (2004) · Brain Research · doi:10.1016/j.brainres.2004.01.089 · Cited by 44
An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling
Kim, S. K., Barron, L., Hinck, C. S., Petrunak, E. M., Cano, K. E., Thangirala, A., Iskra, B., Brothers, M., Vonberg, M., Leal, B., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768754 · Cited by 43
A phase I dose-escalation study to a predefined dose of a transforming growth factor-β1 monoclonal antibody (TβM1) in patients with metastatic cancer
COHN, A., LAHN, M. M., WILLIAMS, K. E., CLEVERLY, A. L., PITOU, C., KADAM, S. K., FARMEN, M. W., DESAIAH, D., RAJU, R., CONKLING, P., et al. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2679 · Cited by 43
Development and characterization of human monoclonal antibodies that neutralize multiple TGFβ isoforms
Bedinger, D., Lao, L., Khan, S., Lee, S., Takeuchi, T., & Mirza, A. M. (2016) · mAbs · doi:10.1080/19420862.2015.1115166 · Cited by 42
Brassinosteroids Plant counterparts to animal steroid hormones?
Clouse, S. D. (2002) · Vitamins & Hormones · doi:10.1016/s0083-6729(02)65065-4 · Cited by 40
Transcriptional network analysis in muscle reveals AP-1 as a partner of PGC-1α in the regulation of the hypoxic gene program
Baresic, M., Salatino, S., Kupr, B., van Nimwegen, E., & Handschin, C. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01710-13 · Cited by 40
MdmX inhibits Smad transactivation
Kadakia, M., Brown, T. L., McGorry, M. M., & Berberich, S. J. (2002) · Oncogene · doi:10.1038/sj.onc.1205993 · Cited by 39
Polymer Gard: Computer Simulation of Covalent Bond Formation in Reproducing Molecular Assemblies
Shenhav, B., Bar-Even, A., Kafri, R., & Lancet, D. (2005) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-005-5578-z · Cited by 33
Reciprocal regulation of miR-23a and lysophosphatidic acid receptor signaling in cardiomyocyte hypertrophy
Yang, J., Nie, Y., Wang, F., Hou, J., Cong, X., Hu, S., & Chen, X. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.05.005 · Cited by 30
MicroRNA-455–3P as a peripheral biomarker and therapeutic target for mild cognitive impairment and Alzheimer’s disease
Islam, M. A., Sultana, O. F., Bandari, M., Kshirsagar, S., Manna, P. R., & Reddy, P. H. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102459 · Cited by 28
Canonical TGF-β Signaling Regulates the Relationship between Prenatal Maternal Depression and Amygdala Development in Early Life
Qiu, A., Zhang, H., Wang, C., Chong, Y.-S., Shek, L. P., Gluckman, P. D., Meaney, M. J., Fortier, M. V., & Wu, Y. (2021) · Translational Psychiatry · doi:10.1038/s41398-021-01292-z · Cited by 23
Effects of direct QRFP-26 administration into the medial hypothalamic area on food intake in rats
Zagorácz, O., Kovács, A., László, K., Ollmann, T., Péczely, L., & Lénárd, L. (2015) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2015.09.004 · Cited by 20
Elongation Factor 3, EF3, Associates with the Calcium Channel Cch1 and Targets Cch1 to the Plasma Membrane in Cryptococcus neoformans
Liu, M., & Gelli, A. (2008) · Eukaryotic Cell · doi:10.1128/ec.00116-08 · Cited by 15
Simulations suggest pharmacological methods for rescuing long-term potentiation
Smolen, P., Baxter, D. A., & Byrne, J. H. (2014) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2014.07.006 · Cited by 13
Is hydrogen ion (H+) the real second messenger in calcium signalling?
Molinari, G. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.03.023 · Cited by 13
Drugs of the future for Peyronie’s disease
Gur, S., Kadowitz, P. J., & Hellstrom, W. J. G. (2012) · Medical Hypotheses · doi:10.1016/j.mehy.2011.11.008 · Cited by 10
A ubiquitin‐binding CUE domain in presenilin‐1 enables interaction with K63‐linked polyubiquitin chains
Duggan, S. P., Yan, R., & McCarthy, J. V. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.03.008 · Cited by 10
TGF-β ligand cross-subfamily interactions in the response of Caenorhabditis elegans to a bacterial pathogen
Ciccarelli, E. J., Wing, Z., Bendelstein, M., Johal, R. K., Singh, G., Monas, A., & Savage-Dunn, C. (2024) · PLOS Genetics · doi:10.1371/journal.pgen.1011324 · Cited by 7
Untitled work
(2000) · PubMed

Authors: Massagué, J.
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 1998-06
Volume: 67
Issue: 1
Pages: 753-791
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev.biochem.67.1.753
OpenAlex: W2103031848
Cited by: 7,556
References: 7
FWCI: 24.72
Type: journal article
Language: en
Open access: closed

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

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.

TGF-β SIGNAL TRANSDUCTION

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources