Cited by 317TGF-β signaling in diseasesProtein Kinase Regulation and GTPase SignalingDevelopmental Biology and Gene Regulation

The DOI matches its Crossref record; 62 of the 63 references it cites were found in a registry or an index, and 1 are not checked yet.

Activation of Signalling by the Activin Receptor Complex

Open access

Attisano, Liliana, Wrana, Jeffrey L., Montalvo, Ermelinda, Massagué, Joan·1996·Molecular and Cellular Biology

DOI 10.1128/mcb.16.3.1066PMC PMC231089

Open this paper in CoChat — free account

Abstract

Activin exerts its effects by simultaneously binding to two types of p rotein serine/threonine kinase receptors, each type existing in various isoforms. Using the ActR-IB and ActR-IIB receptor isoforms, we have investigated the mechanism of activin receptor activation. ActR-IIB are phosphoproteins with demonstrable affinity for each other. However, activin addition strongly promotes an interaction between these two proteins. Activin binds directly to ActR-IIB, and this complex associates with ActR-IB, which does not bind ligand on its own. In the resulting complex, ActR-IB becomes hyperphosphorylated, and this requires the kinase activity of ActR-IIB. Mutation of conserved serines and threonines in the GS domain, a region just upstream of the kinase domain in ActR-IB, abrogates both phosphorylation and signal propagation, suggesting that this domain contains phosphorylation sites required for signalling. ActR-IB activation can be mimicked by mutation of Thr-206 to aspartic acid, which yields a construct, ActR-IB(T206D), that signals in the absence of ligand. Furthermore, the signalling activity of this mutant construct is undisturbed by overexpression of a dominant negative kinase-defective ActR-IIB construct, indicating that ActR-IB(T206D) can signal independently of ActR-IIB. The evidence suggests that ActR-IIB acts as a primary activin receptor and ActR-IB acts as a downstream transducer of activin signals.

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 · 10.1128/mcb.16.3.1066

Cites

62 of 63 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.

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?

Self-check

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

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

Signal transduction by receptors with tyrosine kinase activity
Ullrich, A., & Schlessinger, J. (1990) · Cell · doi:10.1016/0092-8674(90)90801-k · Cited by 5,435
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
Self-citation
Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells
Cowley, S. A. (1994) · Cell · doi:10.1016/0092-8674(94)90133-3 · Cited by 1,959
The TGF-beta superfamily: new members, new receptors, and new genetic tests of function in different organisms.Preprint
Kingsley, D. M. (1994) · Genes & Development · doi:10.1101/gad.8.2.133 · Cited by 1,920
Dimerization of cell surface receptors in signal transduction
Heldin, C.-H. (1995) · Cell · doi:10.1016/0092-8674(95)90404-2 · Cited by 1,634
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
Self-citation
Transformation of Mammalian Cells by Constitutively Active MAP Kinase Kinase
Mansour, S. J., Matten, W. T., Hermann, A. S., Candia, J. M., Rong, S., Fukasawa, K., Woude, G. F. V., & Ahn, N. G. (1994) · Science · doi:10.1126/science.8052857 · Cited by 1,355
Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
Andersson, S., Davis, D. L., Dahlbäck, H., Jörnvall, H., & Russell, D. W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83172-6 · Cited by 1,229
The structure of an antigenic determinant in a protein
Wilson, I. A., Niman, H. L., Houghten, R. A., Cherenson, A. R., Connolly, M. L., & Lerner, R. A. (1984) · Cell · doi:10.1016/0092-8674(84)90412-4 · Cited by 829
Cloning of a TGF$beta; type I receptor that forms a heteromeric complex with the TGF$beta; type II receptor
Franzèn, P. (1993) · Cell · doi:10.1016/0092-8674(93)90489-d · Cited by 774
A transcript from a Drosophila pattern gene predicts a protein homologous to the transforming growth factor-β family
Padgett, R. W., Johnston, D. S., & Gelbart, W. M. (1987) · Nature · doi:10.1038/325081a0 · Cited by 758
Expression cloning of an activin receptor, a predicted transmembrane serine kinase
Mathews, L. S., & Vale, W. (1991) · Cell · doi:10.1016/0092-8674(91)90549-e · Cited by 731
GS domain mutations that constitutively activate T beta R‐I, the downstream signaling component in the TGF‐beta receptor complex.
Wieser, R., Wrana, J. L., & Massagué, J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07214.x · Cited by 689
Self-citation
Identification of human activin and TGFβ type I receptors that form heteromeric kinase complexes with type II receptors
Attisano, L. (1993) · Cell · doi:10.1016/0092-8674(93)90488-c · Cited by 639
Self-citation
Human Type II Receptor for Bone Morphogenic Proteins (BMPs): Extension of the Two-Kinase Receptor Model to the BMPs
Liu, F., Ventura, F., Doody, J. F., & Massagué, J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3479 · Cited by 593
Self-citation
A truncated activin receptor inhibits mesoderm induction and formation of axial structures in Xenopus embryos
Hemmati‐Brivanlou, A., & Melton, D. (1992) · Nature · doi:10.1038/359609a0 · Cited by 559
Characterization of Type I Receptors for Transforming Growth Factor-β and Activin
ten Dijke, P., Yamashita, H., Ichijo, H., Franzèn, P., Laiho, M., Miyazono, K., & Heldin, C. (1994) · Science · doi:10.1126/science.8140412 · Cited by 551
The TGF-β family and its composite receptors
Massagué, J., Attisano, L., & Wrana, J. L. (1994) · Trends in Cell Biology · doi:10.1016/0962-8924(94)90202-x · Cited by 545
Self-citation
Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects.
Yamashita, H., ten Dijke, P., Huylebroeck, D., Sampath, T. K., Andries, M., Smith, J. C., Heldin, C., & Miyazono, K. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.1.217 · Cited by 496
decapentaplegic acts as a morphogen to organize dorsal-ventral pattern in the Drosophila embryo
Ferguson, E. L., & Anderson, K. V. (1992) · Cell · doi:10.1016/0092-8674(92)90514-d · Cited by 492
Novel activin receptors: Distinct genes and alternative mRNA splicing generate a repertoire of serine/threonine kinase receptors
Attisano, L., Wrana, J. L., Cheifetz, S., & Massagué, J. (1992) · Cell · doi:10.1016/0092-8674(92)90209-u · Cited by 469
Self-citation
Purification and characterization of Erythroid Differentiation Factor(EDF) isolated from human leukemia cell line THP-1
Eto, Y., Tsuji, T., Takezawa, M., Takano, S., Yokogawa, Y., & Shibai, H. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)91528-2 · Cited by 405
Type I Receptors Specify Growth-Inhibitory and Transcriptional Responses to Transforming Growth Factor β and Activin
Cárcamo, J. M., Weis‐Garcia, F., Ventura, F., Wieser, R., Wrana, J. L., Attisano, L., & Massagué, J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.3810 · Cited by 373
Self-citation
Three protein kinase structures define a common motif
Taylor, S. S., & Radzio-Andzelm, E. (1994) · Structure · doi:10.1016/s0969-2126(00)00036-8 · Cited by 371
Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta.
Yamashita, H., ten Dijke, P., Franzèn, P., Miyazono, K., & Heldin, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32142-7 · Cited by 326
Characterization and relationship of dpp receptors encoded by the saxophone and thick veins genes in Drosophila
Brummel, T., Twombly, V. J., Marqués, G., Wrana, J. L., Newfeld, S. J., Attisano, L., Massagué, J., O’Connor, M. B., & Gelbart, W. M. (1994) · Cell · doi:10.1016/0092-8674(94)90295-x · Cited by 313
Self-citation
Concomitant loss of transforming growth factor (TGF)-beta receptor types I and II in TGF-beta-resistant cell mutants implicates both receptor types in signal transduction.
Laiho, M., Weis, M., & Massagué, J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44782-x · Cited by 311
Self-citation
An absolute requirement for both the type II and type I receptors, punt and thick veins, for Dpp signaling in vivo
Ruberte, E., Marty, T., Anthamatten, D., Affolter, M., & Basler, K. (1995) · Cell · doi:10.1016/0092-8674(95)90292-9 · Cited by 308
What do BMPs do in mammals? Clues from the mouse short-ear mutation
Kingsley, D. M. (1994) · Trends in Genetics · doi:10.1016/0168-9525(94)90014-0 · Cited by 293
An activity gradient of decapentaplegic is necessary for the specification of dorsal pattern elements in the Drosophila embryo
Wharton, K. A., Ray, R. P., & Gelbart, W. M. (1993) · Development · doi:10.1242/dev.117.2.807 · Cited by 292
TGF-β receptors and actions
Attisano, L., Wrana, J. L., López‐Casillas, F., & Massagué, J. (1994) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(94)90026-4 · Cited by 284
Self-citation
Vertebrate Embryonic Induction: Mesodermal and Neural Patterning
Kessler, D. S., & Melton, D. A. (1994) · Science · doi:10.1126/science.7939714 · Cited by 281
Drosophila Dpp signaling is mediated by the punt gene product: A dual ligand-binding type II receptor of the TGFβ receptor family
Letsou, A., Arora, K., Wrana, J. L., Simin, K. J., Twombly, V. J., Jamal, J., Staehling‐Hampton, K., Hoffmann, F. M., Gelbart, W. M., Massagué, J., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90293-7 · Cited by 275
Self-citation
Identification of two bone morphogenetic protein type I receptors in Drosophila and evidence that Brk25D is a decapentaplegic receptor
Penton, A. L., Chen, Y., Staehling‐Hampton, K., Wrana, J. L., Attisano, L., Szidonya, J., Cassill, J. A., Massagué, J., & Hoffmann, F. M. (1994) · Cell · doi:10.1016/0092-8674(94)90294-1 · Cited by 254
Self-citation
Determination of Type I Receptor Specificity by the Type II Receptors for TGF-β or Activin
Ebner, R., Chen, R., Lawler, S. E., Zioncheck, T. F., & Derynck, R. (1993) · Science · doi:10.1126/science.8235612 · Cited by 253
A Drosophila growth factor homolog, decapentaplegic, regulates homeotic gene expression within and across germ layers during midgut morphogenesis
Panganiban, G. E. F., Reuter, R., Scott, M. P., & Hoffmann, F. M. (1990) · Development · doi:10.1242/dev.110.4.1041 · Cited by 245
The Inhibin/Activin Family of Hormones and Growth Factors
Vale, W., Hsueh, A. J. W., RIVIER, C. L., & Yu, J. (1990) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-74781-6_8 · Cited by 221
Cloning of a Second Type of Activin Receptor and Functional Characterization in Xenopus Embryos
Mathews, L. S., Vale, W., & Kintner, C. R. (1992) · Science · doi:10.1126/science.1313188 · Cited by 217
Disruption of Transforming Growth Factor β Signaling by a Mutation That Prevents Transphosphorylation within the Receptor Complex
Cárcamo, J. M., Zentella‐Dehesa, A., & Massagué, J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1573 · Cited by 216
Self-citation
Activin can induce the formation of axial structures and is expressed in the hypoblast of the chick
Mitrani, E., Ziv, T., Thomsen, G. H., Shimoni, Y., Melton, D. A., & Bril, A. (1990) · Cell · doi:10.1016/0092-8674(90)90446-l · Cited by 206
Activin A: an autocrine inhibitor of initiation of DNA synthesis in rat hepatocytes.
Yasuda, H., Mine, T., Shibata, H., Eto, Y., Hasegawa, Y., Takeuchi, T., Asano, S., & Kojima, I. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116727 · Cited by 204
Cloning of a Novel Type II Serine/Threonine Kinase Receptor through Interaction with the Type I Transforming Growth Factor-β Receptor
Kawabata, M., Chytil, A., & Moses, H. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5625 · Cited by 189
Growth inhibition by transforming growth factor beta (TGF-beta) type I is restored in TGF-beta-resistant hepatoma cells after expression of TGF-beta receptor type II cDNA.
Inagaki, M., Moustakas, A., Lin, H. Y.-F., Lodish, H. F., & Carr, B. I. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5359 · Cited by 188
Inhibin and activin modulate the release of gonadotropin-releasing hormone, human chorionic gonadotropin, and progesterone from cultured human placental cells.
Petraglia, F., Vaughan, J. M., & Vale, W. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.13.5114 · Cited by 183
Receptors for Transforming Growth Factor-β
Miyazono, K., ten Dijke, P., Ichijo, H., & Heldin, C. (1993) · Advances in immunology · doi:10.1016/s0065-2776(08)60510-6 · Cited by 177
Cloning of a New Member of the TGF-β Family: A Putative New Activin βC Chain
Hötten, G., Neidhardt, H., Schneider, C., & Pohl, J. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1086 · Cited by 167
Developmental expression of four novel serine/threonine kinase receptors homologous to the activin/transforming growth factor‐β type II receptor family
He, W. W., Gustafson, M. L., Hirobe, S., & Donahoe, P. K. (1993) · Developmental Dynamics · doi:10.1002/aja.1001960207 · Cited by 166
Inhibition of vascular endothelial cell growth by activin-A.
McCarthy, S. A., & Bicknell, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49426-x · Cited by 154
Two distinct transmembrane serine/threonine kinases from Drosophila melanogaster form an activin receptor complex.
Wrana, J. L., Tran, H., Attisano, L., Arora, K., Childs, S. R., Massagué, J., & O’Connor, M. B. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.2.944 · Cited by 149
Self-citation
Multiple requirements for the receptor serine/threonine kinase thick veins reveal novel functions of TGFβ homologs during Drosophila embryogenesis
Affolter, M., Nellen, D., Nussbaumer, U., & Basler, K. (1994) · Development · doi:10.1242/dev.120.11.3105 · Cited by 141
Cloning and characterization of a transmembrane serine kinase that acts as an activin type I receptor.
Tsuchida, K., Mathews, L. S., & Vale, W. W. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11242 · Cited by 125
Constitutive mutant and putative regulatory serine phosphorylation site of mammalian MAP kinase kinase (MEK1).
Pagès, G., Brunet, A., L’Allemain, G., & Pouysségur, J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06599.x · Cited by 125
Bovine bone activin enhances bone morphogenetic protein-induced ectopic bone formation.
Ogawa, Y., Schmidt, D. K., Nathan, R. M., Armstrong, R. M., Miller, K. L., Sawamura, S. J., Ziman, J. M., Erickson, K. L., de Leon, E. R., & Rosen, D. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49702-0 · Cited by 122
Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor beta receptor kinases.
Chen, F., & Weinberg, R. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1565 · Cited by 116
Mesoderm‐inducing factors in early vertebrate development.
Smith, J. C. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06135.x · Cited by 115
Identification of a Drosophila activin receptor.
Childs, S. R., Wrana, J. L., Arora, K., Attisano, L., O’Connor, M. B., & Massagué, J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9475 · Cited by 112
Self-citation
Activin-A, Inhibin and Transforming Growth Factor-β Modulate Growth of Two Gonadal Cell Lines*
González‐Manchón, C., & Vale, W. (1989) · Endocrinology · doi:10.1210/endo-125-3-1666 · Cited by 96
A widely expressed transmembrane serine/threonine kinase that does not bind activin, inhibin, transforming growth factor beta, or bone morphogenic factor
Matsuzaki, K., Xu, J., Wang, F., McKeehan, W. L., KRUMMEN, L. A., & Kan, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31447-9 · Cited by 87
Characterization of type II activin receptors. Binding, processing, and phosphorylation.
Mathews, L. S., & Vale, W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46728-7 · Cited by 81
Reconstitution and transphosphorylation of TGF‐beta receptor complexes.
Ventura, F., Doody, J. F., Liu, F., Wrana, J. L., & Massagué, J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06895.x · Cited by 80
Self-citation
Phosphorylation-dependent Interaction of the Cytoplasmic Domains of the Type I and Type II Transforming Growth Factor-β Receptors
Chen, R., Moses, H. L., Maruoka, E. M., Derynck, R., & Kawabata, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.12235 · Cited by 79
Signaling Activity of Homologous and Heterologous Transforming Growth Factor-β Receptor Kinase Complexes
Vivien, D., Attisano, L., Wrana, J. L., & Massagué, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7134 · Cited by 78
Self-citation
Two Distinct Transmembrane Serine/Threonine Kinases from Drosophila melanogaster Form an Activin Receptor Complex
Wrana, J. L., Tran, H., Attisano, L., et al. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.2.944-950.1994 · Cited by 24
Self-citation

Research works printed but not linked: 2

Harlow E., 1988, Antibodies: a laboratory handbook
Wrana J. L., 1994, Mol. Cell. Biol., 14, 944

Sorted by citations

TGF-β SIGNAL TRANSDUCTION
Massagué, J. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.753 · Cited by 7,571
Self-citation
TGF-β signalling from cell membrane to nucleus through SMAD proteins
Heldin, C., Miyazono, K., & ten Dijke, P. (1997) · Nature · doi:10.1038/37284 · Cited by 3,697
M2 microglia and macrophages drive oligodendrocyte differentiation during CNS remyelination
Miron, V. E., Boyd, A., Zhao, J.-W., Yuen, T. J., Ruckh, J. M., Shadrach, J. L., van Wijngaarden, P., Wagers, A. J., Williams, A., Franklin, R. J. M., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3469 · Cited by 1,777
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
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
Self-citation

See all 317

Authors: Attisano, L., Wrana, J. L., Montalvo, E., & Massagué, J.
Affiliations: Memorial Sloan Kettering Cancer Center (US)
ORCID: Attisano, Liliana
Wrana, Jeffrey L.
Massagué, Joan
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1996-03-01
Volume: 16
Issue: 3
Pages: 1066-1073
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.16.3.1066
PMC: PMC231089
OpenAlex: W2103042473
Cited by: 316
References: 62
Citations by year: 2026: 1 · 2025: 7 · 2024: 2 · 2023: 6 · 2022: 4 · 2021: 9 · 2020: 6 · 2019: 9 · 2018: 9 · 2017: 2 · 2016: 12 · 2015: 4 · 2014: 3 · 2013: 4 · 2012: 5
FWCI: 9.35
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (CA34610)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords: activin signalling, receptor activation, receptor phosphorylation, receptor kinase activity, signal transduction
MeSH terms: Amino Acid Sequence, Animals, Cell Line, Ligands, Molecular Sequence Data, Mutation, Transfection, Signal Transduction, Protein Serine-Threonine Kinases, Receptors, Growth Factor, Activin Receptors

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

Activation of Signalling by the Activin Receptor Complex

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks