Protein phosphatase 2A regulatory subunits and cancer

Mdm2 promotes the rapid degradation of p53

Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506 · see citing works

Creation of human tumour cells with defined genetic elements

Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W., & Weinberg, R. A. (1999) · Nature · doi:10.1038/22780 · Cited by 2,345 · see citing works

A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells

Yeh, E., Cunningham, M., Arnold, H., Chasse, D., Monteith, T., Ivaldi, G., Hahn, W. C., Stukenberg, P. T., Shenolikar, S., Uchida, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1110 · Cited by 791 · see citing works

CIP2A inhibits PP2A in human malignancies

Junttila, M. R., Puustinen, P., Niemelä, M., Ahola, R., Arnold, H., Böttzauw, T., Ala-aho, R., Nielsen, C., Ivaska, J., Taya, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.044 · Cited by 677 · see citing works

Structure of the Protein Phosphatase 2A Holoenzyme

Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.11.033 · Cited by 450 · see citing works

Regulation of Phosphorylation of Thr-308 of Akt, Cell Proliferation, and Survival by the B55α Regulatory Subunit Targeting of the Protein Phosphatase 2A Holoenzyme to Akt

Kuo, Y.-C., Huang, K.-Y., Yang, C.-H., Yang, Y.-S., Lee, W.-Y., & Chiang, C.-W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709585200 · Cited by 367 · see citing works

Identification of specific PP2A complexes involved in human cell transformation

Chen, W., Possemato, R., Campbell, K. T., Plattner, C. A., Pallas, D. C., & Hahn, W. C. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00026-1 · Cited by 325 · see citing works

Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites

Ory, S., Zhou, M., Conrads, T. P., Veenstra, T. D., & Morrison, D. K. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00535-9 · Cited by 296 · see citing works

Protein phosphatase 2A regulatory subunit B56α associates with c-myc and negatively regulates c-myc accumulation

Arnold, H. K., & Sears, R. C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2832-2844.2006 · Cited by 251 · see citing works

FMRP Phosphorylation Reveals an Immediate-Early Signaling Pathway Triggered by Group I mGluR and Mediated by PP2A

Narayanan, U., Nalavadi, V., Nakamoto, M., Pallas, D. C., Ceman, S., Bassell, G. J., & Warren, S. T. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.2969-07.2007 · Cited by 228 · see citing works

WD40 Repeat Proteins Striatin and S/G2 Nuclear Autoantigen Are Members of a Novel Family of Calmodulin-binding Proteins That Associate with Protein Phosphatase 2A

Moreno, C. S., Park, S., Nelson, K., Ashby, D., Hubalek, F., Lane, W. S., & Pallas, D. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5257 · Cited by 194 · see citing works

A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A

Ogris, E., Du, X., Nelson, K. C., Mak, E. K., Yu, X. X., Lane, W. S., & Pallas, D. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14382 · Cited by 191 · see citing works

Selection of protein phosphatase 2A regulatory subunits is mediated by the C terminus of the catalytic Subunit

Longin, S., Zwaenepoel, K., Louis, J. V., Dilworth, S., Goris, J., & Janssens, V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704059200 · Cited by 184 · see citing works

A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation

Ito, A., Kataoka, T. R., Watanabe, M., Nishiyama, K., Mazaki, Y., Sabe, H., Kitamura, Y., & Nojima, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.562 · Cited by 159 · see citing works

Positive regulation of Raf1-MEK1/2-ERK1/2 signaling by protein serine/threonine phosphatase 2A holoenzymes

Adams, D. G., Coffee, R. L., Zhang, H., Pelech, S., Strack, S., & Wadzinski, B. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502464200 · Cited by 133 · see citing works

Protein phosphatase 2A interacts with and directly dephosphorylates RelA

Yang, J., Fan, G.-H., Wadzinski, B. E., Sakurai, H., & Richmond, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106103200 · Cited by 130 · see citing works

PP2A Regulates HDAC4 Nuclear Import

Paroni, G., Cernotta, N., Dello Russo, C., Gallinari, P., Pallaoro, M., Foti, C., Talamo, F., Orsatti, L., Steinkühler, C., & Brancolini, C. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-06-0623 · Cited by 126 · see citing works

Tissue‐specific expression of mRNAs encoding α‐ and β‐catalytic subunits of protein phosphatase 2A

Khew-Goodall, Y., & Hemmings, B. A. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80493-9 · Cited by 102 · see citing works

Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: Differences in expression, subunit interaction, and evolution

ZHOU, J., PHAM, H. T., RUEDIGER, R., & WALTER, G. (2003) · Biochemical Journal · doi:10.1042/bj20021244 · Cited by 95 · see citing works

Human T-lymphotropic virus type I tax activates I-κB kinase by inhibiting I-κB kinase-associated serine/threonine protein phosphatase 2A

Fu, D.-X., Kuo, Y.-L., Liu, B.-Y., Jeang, K.-T., & Giam, C.-Z. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210631200 · Cited by 95 · see citing works

Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells

Lee, J. A., & Pallas, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704861200 · Cited by 69 · see citing works

Protein phosphatase 2A subunit PR70 interacts with pRb and mediates its dephosphorylation

Magenta, A., Fasanaro, P., Romani, S., Di Stefano, V., Capogrossi, M. C., & Martelli, F. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00480-07 · Cited by 58 · see citing works

Ligand Binding to the Androgen Receptor Induces Conformational Changes That Regulate Phosphatase Interactions

Yang, C.-S., Xin, H.-W., Kelley, J. B., Spencer, A., Brautigan, D. L., & Paschal, B. M. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02411-06 · Cited by 55 · see citing works

Regulation of CaMKII by α4/PP2Ac contributes to learning and memory

Yamashita, T., Inui, S., Maeda, K., Hua, D. R., Takagi, K., Fukunaga, K., & Sakaguchi, N. (2006) · Brain Research · doi:10.1016/j.brainres.2006.01.101 · Cited by 41 · see citing works

Response and resistance to BET bromodomain inhibitors in triple-negative breast cancer

Shu, S., Lin, C. Y., He, H. H., Witwicki, R. M., Tabassum, D. P., Roberts, J. M., Janiszewska, M., Jin Huh, S., Liang, Y., Ryan, J., et al. (2016) · Nature · doi:10.1038/nature16508 · Cited by 632 · see citing works

MYC degradation

Farrell, A. S., & Sears, R. C. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014365 · Cited by 468 · see citing works

Protein phosphatase 2A: a target for anticancer therapy

Perrotti, D., & Neviani, P. (2013) · The Lancet Oncology · doi:10.1016/s1470-2045(12)70558-2 · Cited by 400 · see citing works

All roads lead to <scp>PP</scp>2A: exploiting the therapeutic potential of this phosphatase

Sangodkar, J., Farrington, C. C., McClinch, K., Galsky, M. D., Kastrinsky, D. B., & Narla, G. (2016) · The FEBS Journal · doi:10.1111/febs.13573 · Cited by 312 · see citing works

Regulation of autophagy by coordinated action of mTORC1 and protein phosphatase 2A

Wong, P.-M., Feng, Y., Wang, J., Shi, R., & Jiang, X. (2015) · Nature Communications · doi:10.1038/ncomms9048 · Cited by 239 · see citing works

The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity

Sents, W., Ivanova, E., Lambrecht, C., Haesen, D., & Janssens, V. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08579.x · Cited by 204 · see citing works

Identification of PP2A Complexes and Pathways Involved in Cell Transformation

Sablina, A. A., Hector, M., Colpaert, N., & Hahn, W. C. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2855 · Cited by 193 · see citing works

Activation of tumor suppressor protein PP2A inhibits KRAS-driven tumor growth

Sangodkar, J., Perl, A., Tohme, R., Kiselar, J., Kastrinsky, D. B., Zaware, N., Izadmehr, S., Mazhar, S., Wiredja, D. D., O’Connor, C. M., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci89548 · Cited by 196 · see citing works

Targeting SET/I2PP2A oncoprotein functions as a multi-pathway strategy for cancer therapy

Switzer, C. H., Cheng, R. Y. S., Vitek, T. M., Christensen, D. J., Wink, D. A., & Vitek, M. P. (2011) · Oncogene · doi:10.1038/onc.2010.622 · Cited by 171 · see citing works

α4 Is an Essential Regulator of PP2A Phosphatase Activity

Kong, M., Ditsworth, D., Lindsten, T., & Thompson, C. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.025 · Cited by 162 · see citing works

Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

Lambrecht, C., Haesen, D., Sents, W., Ivanova, E., & Janssens, V. (2013) · Methods in Molecular Biology · doi:10.1007/978-1-62703-562-0_17 · Cited by 140 · see citing works

S-nitrosylation of EGFR and Src activates an oncogenic signaling network in human basal-like breast cancer

Switzer, C. H., Glynn, S. A., Cheng, R. Y.-S., Ridnour, L. A., Green, J. E., Ambs, S., & Wink, D. A. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0124 · Cited by 141 · see citing works

The Dependence Receptor UNC5H2/B Triggers Apoptosis via PP2A-Mediated Dephosphorylation of DAP Kinase

Guenebeaud, C., Goldschneider, D., Castets, M., Guix, C., Chazot, G., Delloye-Bourgeois, C., Eisenberg-Lerner, A., Shohat, G., Zhang, M., Laudet, V., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.021 · Cited by 137 · see citing works

Non-genomic mechanisms of protein phosphatase 2A (PP2A) regulation in cancer

Kauko, O., & Westermarck, J. (2018) · The International Journal of Biochemistry &amp; Cell Biology · doi:10.1016/j.biocel.2018.01.005 · Cited by 111 · see citing works

Defects in a liver-bone axis contribute to hepatic osteodystrophy disease progression

Lu, K., Shi, T.-S., Shen, S.-Y., Shi, Y., Gao, H.-L., Wu, J., Lu, X., Gao, X., Ju, H.-X., Wang, W., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.02.006 · Cited by 126 · see citing works

Mechanisms of site‐specific dephosphorylation and kinase opposition imposed by PP2A regulatory subunits

Kruse, T., Gnosa, S. P., Nasa, I., Garvanska, D. H., Hein, J. B., Nguyen, H., Samsøe‐Petersen, J., Lopez‐Mendez, B., Hertz, E. P. T., Schwarz, J., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103695 · Cited by 97 · see citing works

Targeting Inhibitors of the Tumor Suppressor PP2A for the Treatment of Pancreatic Cancer

Farrell, A. S., Allen-Petersen, B., Daniel, C. J., Wang, X., Wang, Z., Rodriguez, S., Impey, S., Oddo, J., Vitek, M. P., Lopez, C., et al. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0542 · Cited by 114 · see citing works

Mice lacking phosphatase PP2A subunit PR61/B’δ ( <i>Ppp2r5d</i> ) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3β

Louis, J. V., Martens, E., Borghgraef, P., Lambrecht, C., Sents, W., Longin, S., Zwaenepoel, K., Pijnenborg, R., Landrieu, I., Lippens, G., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018777108 · Cited by 112 · see citing works

Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56

Wang, J., Okkeri, J., Pavic, K., Wang, Z., Kauko, O., Halonen, T., Sarek, G., Ojala, P. M., Rao, Z., Xu, W., et al. (2017) · The EMBO Reports · doi:10.15252/embr.201642788 · Cited by 95 · see citing works

Human cancer-associated mutations in the Aα subunit of protein phosphatase 2A increase lung cancer incidence in Aα knock-in and knockout mice

Ruediger, R., Ruiz, J., & Walter, G. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05744-11 · Cited by 98 · see citing works

The Angiotensin AT2 Receptor: From a Binding Site to a Novel Therapeutic Target

Steckelings, U. M., Widdop, R. E., Sturrock, E. D., Lubbe, L., Hussain, T., Kaschina, E., Unger, T., Hallberg, A., Carey, R. M., & Sumners, C. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000281 · Cited by 97 · see citing works

Tumor suppressive protein phosphatases in human cancer: Emerging targets for therapeutic intervention and tumor stratification

Meeusen, B., & Janssens, V. (2018) · The International Journal of Biochemistry &amp; Cell Biology · doi:10.1016/j.biocel.2017.10.002 · Cited by 96 · see citing works

PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer

(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93 · see citing works

Inhibition of AMP kinase by the protein phosphatase 2a heterotrimer, PP2APpp2r2d

Joseph, B. K., Liu, H.-Y., Francisco, J., Pandya, D., Donigan, M., Gallo-Ebert, C., Giordano, C., Bata, A., & Nickels, J. T. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.626259 · Cited by 91 · see citing works

CIP2A signature reveals the MYC dependency of CIP2A-regulated phenotypes and its clinical association with breast cancer subtypes

Niemelä, M., Kauko, O., Sihto, H., Mpindi, J.-P., Nicorici, D., Pernilä, P., Kallioniemi, O.-P., Joensuu, H., Hautaniemi, S., & Westermarck, J. (2012) · Oncogene · doi:10.1038/onc.2011.599 · Cited by 79 · see citing works

Deregulation of the PP2A inhibitor SET shows promising therapeutic implications and determines poor clinical outcome in patients with metastatic colorectal cancer

Cristóbal, I., Rincón, R., Manso, R., Caramés, C., Zazo, S., Madoz-Gúrpide, J., Rojo, F., & García-Foncillas, J. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-0724 · Cited by 78 · see citing works

Nitric oxide and protein phosphatase 2A provide novel therapeutic opportunities in ER-negative breast cancer

Switzer, C. H., Glynn, S. A., Ridnour, L. A., Cheng, R. Y.-S., Vitek, M. P., Ambs, S., & Wink, D. A. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.07.001 · Cited by 74 · see citing works

The basic biology of PP2A in hematologic cells and malignancies

Haesen, D., Sents, W., Lemaire, K., Hoorne, Y., & Janssens, V. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00347 · Cited by 73 · see citing works

PR55α subunit of protein phosphatase 2A supports the tumorigenic and metastatic potential of pancreatic cancer cells by sustaining hyperactive oncogenic signaling

Hein, A. L., Seshacharyulu, P., Rachagani, S., Sheinin, Y. M., Ouellette, M. M., Ponnusamy, M. P., Mumby, M. C., Batra, S. K., & Yan, Y. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2119 · Cited by 66 · see citing works

DNAJB6 chaperones PP2A mediated dephosphorylation of GSK3β to downregulate β-catenin transcription target, osteopontin

Mitra, A., Menezes, M. E., Pannell, L. K., Mulekar, M. S., Honkanen, R. E., Shevde, L. A., & Samant, R. S. (2012) · Oncogene · doi:10.1038/onc.2011.623 · Cited by 64 · see citing works

Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling

Kauko, O., Laajala, T. D., Jumppanen, M., Hintsanen, P., Suni, V., Haapaniemi, P., Corthals, G., Aittokallio, T., Westermarck, J., & Imanishi, S. Y. (2015) · Scientific Reports · doi:10.1038/srep13099 · Cited by 61 · see citing works

CIP2A promotes proliferation of spermatogonial progenitor cells and spermatogenesis in mice

Ventelä, S., Côme, C., Mäkelä, J.-A., Hobbs, R. M., Mannermaa, L., Kallajoki, M., Chan, E. K., Pandolfi, P. P., Toppari, J., & Westermarck, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033209 · Cited by 58 · see citing works

A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment

Wang, X., Garvanska, D. H., Nasa, I., Ueki, Y., Zhang, G., Kettenbach, A. N., Peti, W., Nilsson, J., & Page, R. (2020) · eLife · doi:10.7554/elife.55966 · Cited by 53 · see citing works

PP2A inhibition sensitizes cancer stem cells to ABL tyrosine kinase inhibitors in BCR-ABL ⁺ human leukemia

Lai, D., Chen, M., Su, J., Liu, X., Rothe, K., Hu, K., Forrest, D. L., Eaves, C. J., Morin, G. B., & Jiang, X. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan8735 · Cited by 47 · see citing works

PP2A Inactivation Mediated by <i>PPP2R4</i> Haploinsufficiency Promotes Cancer Development

Sents, W., Meeusen, B., Kalev, P., Radaelli, E., Sagaert, X., Miermans, E., Haesen, D., Lambrecht, C., Dewerchin, M., Carmeliet, P., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2911 · Cited by 42 · see citing works

B′-protein phosphatase 2A is a functional binding partner of delta-retroviral integrase

Maertens, G. N. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1347 · Cited by 38 · see citing works

Enhanced Insulin Sensitivity Associated with Provision of Mono and Polyunsaturated Fatty Acids in Skeletal Muscle Cells Involves Counter Modulation of PP2A

Nardi, F., Lipina, C., Magill, D., Hage Hassan, R., Hajduch, E., Gray, A., & Hundal, H. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092255 · Cited by 36 · see citing works

Cornel Iridoid Glycoside Inhibits Tau Hyperphosphorylation via Regulating Cross-Talk Between GSK-3β and PP2A Signaling

Yang, C., Li, X., Gao, W., Wang, Q., Zhang, L., Li, Y., Li, L., & Zhang, L. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00682 · Cited by 36 · see citing works

CIP2A increases self-renewal and is linked to Myc in neural progenitor cells

Kerosuo, L., Fox, H., Perälä, N., Ahlqvist, K., Suomalainen, A., Westermarck, J., Sariola, H., & Wartiovaara, K. (2010) · Differentiation · doi:10.1016/j.diff.2010.04.003 · Cited by 35 · see citing works

<i>Ppp2ca</i> knockout in mice spermatogenesis

Pan, X., Chen, X., Tong, X., Tang, C., & Li, J. (2015) · Reproduction · doi:10.1530/rep-14-0231 · Cited by 32 · see citing works

The protein phosphatase 2A regulatory subunit PR70 is a gonosomal melanoma tumor suppressor gene

van Kempen, L. C. L., Redpath, M., Elchebly, M., Klein, K. O., Papadakis, A. I., Wilmott, J. S., Scolyer, R. A., Edqvist, P.-H., Pontén, F., Schadendorf, D., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aai9188 · Cited by 29 · see citing works

PPP2R5A: A multirole protein phosphatase subunit in regulating cancer development

Mao, Z., Liu, C., Lin, X., Sun, B., & Su, C. (2018) · Cancer Letters · doi:10.1016/j.canlet.2017.11.024 · Cited by 30 · see citing works

The tumor suppressor phosphatase PP2A-B56α regulates stemness and promotes the initiation of malignancies in a novel murine model

Janghorban, M., Langer, E. M., Wang, X., Zachman, D., Daniel, C. J., Hooper, J., Fleming, W. H., Agarwal, A., & Sears, R. C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0188910 · Cited by 19 · see citing works

Cip2a promotes cell cycle progression in triple-negative breast cancer cells by regulating the expression and nuclear export of p27Kip1

Liu, H., Qiu, H., Song, Y., Liu, Y., Wang, H., Lu, M., Deng, M., Gu, Y., Yin, J., Luo, K., et al. (2017) · Oncogene · doi:10.1038/onc.2016.355 · Cited by 19 · see citing works

Patterning and gastrulation defects caused by the<i>tw18</i>lethal are due to loss of<i>Ppp2r1a</i>

Lange, L., Marks, M., Liu, J., Wittler, L., Bauer, H., Piehl, S., Bläß, G., Timmermann, B., & Herrmann, B. G. (2017) · Biology Open · doi:10.1242/bio.023200 · Cited by 19 · see citing works

Circumventing embryonic lethality with Lcmt1 deficiency: generation of hypomorphic Lcmt1 mice with reduced protein phosphatase 2A methyltransferase expression and defects in insulin signaling

MacKay, K. B., Tu, Y., Young, S. G., & Clarke, S. G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065967 · Cited by 14 · see citing works

Virus–Host Interactions in Retrovirus Integration

Engelman, A. N., & Maertens, G. N. (2018) · Retrovirus-Cell Interactions · doi:10.1016/b978-0-12-811185-7.00004-2 · Cited by 12 · see citing works

Reduction of protein phosphatase 2A Cα promotes in vivo bone formation and adipocyte differentiation

Yoshida, K., Teramachi, J., Uchibe, K., Ikegame, M., Qiu, L., Yang, D., & Okamura, H. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.11.005 · Cited by 7 · see citing works