The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
PPM1A Functions as a Smad Phosphatase to Terminate TGFβ Signaling
Open accessOverview
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
Cites
Statistics
Verification
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.
Citations
Cites
Smad-dependent and Smad-independent pathways in TGF-β family signalling
Derynck, R., & Zhang, Y. E. (2003) · Nature · doi:10.1038/nature02006 · Cited by 5,373
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
SPECIFICITY AND VERSATILITY IN TGF-β SIGNALING THROUGH SMADS
Feng, X.-H., & Derynck, R. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.022404.142018 · Cited by 1,869
Self-citationDennler, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.3091 · Cited by 1,793
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 1,634
New insights into TGF-β–Smad signalling
Dijke, P. T., & Hill, C. S. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.03.008 · Cited by 1,180
Seoane, J., Le, H.-V., Shen, L., Anderson, S. A., & Massagué, J. (2004) · Cell · doi:10.1016/s0092-8674(04)00298-3 · Cited by 1,028
Kip/Cip and Ink4 Cdk inhibitors cooperate to induce cell cycle arrest in response to TGF-beta.
Reynisdóttir, I., Polyak, K., Iavarone, A., & Massagué, J. (1995) · Genes & Development · doi:10.1101/gad.9.15.1831 · Cited by 962
Moustakas, A., & Heldin, C.-H. (2005) · Journal of Cell Science · doi:10.1242/jcs.02554 · Cited by 958
Datto, M. B., Li, Y., Panus, J. F., Howe, D. J., Xiong, Y., & Wang, X. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5545 · Cited by 950
The two faces of transforming growth factor β in carcinogenesis
Roberts, A. B., & Wakefield, L. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1633291100 · Cited by 747
Insulin signaling in health and disease
White, M. F. (2003) · Science · doi:10.1126/science.1092952 · Cited by 733
Nodal Signaling in Vertebrate Development
Schier, A. F. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.041603.094522 · Cited by 633
Cyclin-dependent kinases regulate the antiproliferative function of Smads
Matsuura, I., Denissova, N. G., Wang, G., He, D., Long, J., & Liu, F. (2004) · Nature · doi:10.1038/nature02650 · Cited by 503
Self-citationEstablishment of vertebrate left–right asymmetry
Hamada, H., Meno, C., Watanabe, D., & Saijoh, Y. (2002) · Nature Reviews Genetics · doi:10.1038/nrg732 · Cited by 489
E2F4/5 and p107 as Smad Cofactors Linking the TGFβ Receptor to c-myc Repression
Chen, C.-R., Kang, Y., Siegel, P. M., & Massagué, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00801-2 · Cited by 487
Nucleocytoplasmic Shuttling of Smads 2, 3, and 4 Permits Sensing of TGF-β Receptor Activity
Inman, G. J., Nicolás, F. J., & Hill, C. S. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00585-3 · Cited by 417
Smad2, Smad3 and Smad4 cooperate with Sp1 to induce p15Ink4B transcription in response to TGF-β
Feng, X.-H., Lin, X., & Derynck, R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.19.5178 · Cited by 397
Self-citationPardali, K., Kurisaki, A., Morén, A., ten Dijke, P., Kardassis, D., & Moustakas, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909467199 · Cited by 392
Expression of zebrafish goosecoid and no tail gene products in wild-type and mutant no tail embryos
Schulte-Merker, S., Hammerschmidt, M., Beuchle, D., Cho, K. W., Robertis, E. M. D., & Nüsslein-Volhard, C. (1994) · Development · doi:10.1242/dev.120.4.843 · Cited by 301
Crystal Structure of a Phosphorylated Smad2
Wu, J.-W., Hu, M., Chai, J., Seoane, J., Huse, M., Li, C., Rigotti, D. J., Kyin, S., Muir, T. W., Fairman, R., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00421-x · Cited by 301
Self-citationProtein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways
Takekawa, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4744 · Cited by 286
From developmental disorder to heritable cancer: it's all in the BMP/TGF-β family
Waite, K. A., & Eng, C. (2003) · Nature Reviews Genetics · doi:10.1038/nrg1178 · Cited by 276
GADD34–PP1c recruited by Smad7 dephosphorylates TGFβ type I receptor
Shi, W., Sun, C., He, B., Xiong, W., Shi, X., Yao, D., & Cao, X. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307151 · Cited by 266
Xu, L., Kang, Y., Çöl, S., & Massagué, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00586-5 · Cited by 261
Feng, X.-H., Liang, Y.-Y., Liang, M., Zhai, W., & Lin, X. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00430-0 · Cited by 231
Self-citationFrederick, J. P., Liberati, N. T., Waddell, D. S., Shi, Y., & Wang, X.-F. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2546-2559.2004 · Cited by 221
Self-citationElucidation of Smad Requirement in Transforming Growth Factor-β Type I Receptor-induced Responses
Itoh, S., Thorikay, M., Kowanetz, M., Moustakas, A., Itoh, F., Heldin, C.-H., & ten Dijke, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208258200 · Cited by 209
Opposed Regulation of Corepressor CtBP by SUMOylation and PDZ Binding
Lin, X., Sun, B., Liang, M., Liang, Y.-Y., Gast, A., Hildebrand, J., Brunicardi, F. C., Melchior, F., & Feng, X.-H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00175-8 · Cited by 172
Self-citationDephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
Cheng, A., Ross, K. E., Kaldis, P., & Solomon, M. J. (1999) · Genes & Development · doi:10.1101/gad.13.22.2946 · Cited by 168
Protein serine/threonine phosphatases: life, death, and sleeping
Gallego, M., & Virshup, D. M. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.01.002 · Cited by 157
TGFβ signaling in health and disease
Akhurst, R. J. (2004) · Nature Genetics · doi:10.1038/ng0804-790 · Cited by 154
Datta, P. K., Blake, M. C., & Moses, H. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000508200 · Cited by 144
Identification of phosphatases for Smad in the BMP/DPP pathwayPreprint
Chen, H. B., Shen, J., Ip, Y. T., & Xu, L. (2006) · Genes & Development · doi:10.1101/gad.1384706 · Cited by 136
Zebrafish Dpr2 Inhibits Mesoderm Induction by Promoting Degradation of Nodal Receptors
Zhang, L., Zhou, H., Su, Y., Sun, Z., Zhang, H., Zhang, L., Zhang, Y., Ning, Y., Chen, Y., & Meng, A. (2004) · Science · doi:10.1126/science.1100569 · Cited by 134
Self-citationAlexandrow, M. G., Kawabata, M., Aakre, M. E., & Moses, H. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.8.3239 · Cited by 130
Griswold‐Prenner, I., Kamibayashi, C., Maruoka, E. M., Mumby, M. C., & Derynck, R. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6595 · Cited by 127
Protein Phosphatase 2Cα Dephosphorylates Axin and Activates LEF-1-dependent Transcription
Strovel, E. T., Wu, D., & Sussman, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2399 · Cited by 121
Stroschein, S. L., Wang, W., & Luo, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9431 · Cited by 121
PP1 binds Sara and negatively regulates Dpp signaling in Drosophila melanogaster
Bennett, D., & Alphey, L. (2002) · Nature Genetics · doi:10.1038/ng938 · Cited by 96
Probing the Function of Conserved Residues in the Serine/Threonine Phosphatase PP2Cα
Jackson, M. D., Fjeld, C. C., & Denu, J. M. (2003) · Biochemistry · doi:10.1021/bi034074+ · Cited by 68
Jazag, A., Ijichi, H., Kanai, F., Imamura, T., Guleng, B., Ohta, M., Imamura, J., Tanaka, Y., Tateishi, K., Ikenoue, T., et al. (2004) · Oncogene · doi:10.1038/sj.onc.1208102 · Cited by 68
Cao, Z., Flanders, K. C., Bertolette, D. C., Lyakh, L. A., Würthner, J., Parks, W. T., Letterio, J. J., Ruscetti, F. W., & Roberts, A. B. (2002) · Blood · doi:10.1182/blood-2002-05-1549 · Cited by 66
Overview of protein serine/threonine phosphatases
Cohen, P. T. W. (2003) · Topics in current genetics · doi:10.1007/978-3-540-40035-6_1 · Cited by 64
Yoshizaki, T., Maegawa, H., Egawa, K., Ugi, S., Nishio, Y., Imamura, T., Kobayashi, T., Tamura, S., Olefsky, J. M., & Kashiwagi, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313745200 · Cited by 58
Using viral species specificity to define a critical protein/RNA interaction surfacePreprint
Coburn, G. A., Wiegand, H. L., Kang, Y., Ho, D. N., Georgiadis, M. M., & Cullen, B. R. (2001) · Genes & Development · doi:10.1101/gad.888201 · Cited by 27
Cited by
Massagué, J. (2008) · Cell · doi:10.1016/j.cell.2008.07.001 · Cited by 3,907
Specificity, versatility, and control of TGF-β family signaling
Derynck, R., & Budi, E. H. (2019) · Science Signaling · doi:10.1126/scisignal.aav5183 · Cited by 785
TGF-β Superfamily Signaling in Embryonic Development and Homeostasis
Wu, M. Y., & Hill, C. S. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.02.012 · Cited by 746
Nuclear CDKs Drive Smad Transcriptional Activation and Turnover in BMP and TGF-β Pathways
Alarcón, C., Zaromytidou, A.-I., Xi, Q., Gao, S., Yu, J., Fujisawa, S., Barlas, A., Miller, A. N., Manova-Todorova, K., Macias, M. J., et al. (2009) · Cell · doi:10.1016/j.cell.2009.09.035 · Cited by 719
TGF-β Family Signaling in the Control of Cell Proliferation and Survival
Zhang, Y., Alexander, P. B., & Wang, X.-F. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022145 · Cited by 626
Metadata
- Authors
- Lin, X., Duan, X., Liang, Y.-Y., Su, Y., Wrighton, K. H., Long, J., Hu, M., Davis, C. M., Wang, J., Brunicardi, F. C., Shi, Y., Chen, Y.-G., Meng, A., & Feng, X.-H.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-06
- Volume
- 125
- Issue
- 5
- Pages
- 915-928
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2034779933
- Cited by
- 485
- References
- 46
- FWCI
- 14.73
- Type
- journal article
- Language
- en
- Open access
- bronze
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.