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

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216

The phosphatidylinositol 3-Kinase–AKT pathway in human cancer

Vivanco, I., & Sawyers, C. L. (2002) · Nature reviews. Cancer · doi:10.1038/nrc839 · Cited by 6,155

A System for Stable Expression of Short Interfering RNAs in Mammalian Cells

Brummelkamp, T. R., Bernards, R., & Agami, R. (2002) · Science · doi:10.1126/science.1068999 · Cited by 4,295

Cellular survival: a play in three Akts

Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

Maehama, T., & Dixon, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13375 · Cited by 3,104

Mechanism of activation of protein kinase B by insulin and IGF‐1.

Alessi, D. R., Andjelković, M., Caudwell, B., Cron, P. D., MORRICE, N. A., Cohen, P., & Hemmings, B. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01045.x · Cited by 3,014

Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα

Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., & Cohen, P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00122-9 · Cited by 2,874

Exploiting the PI3K/AKT Pathway for Cancer Drug Discovery

Hennessy, B. T., Smith, D. L., Ram, P. T., Lu, Y., & Mills, G. B. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1902 · Cited by 2,214

Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,927

The protein kinase B/Akt signalling pathway in human malignancy

Nicholson, K. M., & Anderson, N. G. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00271-6 · Cited by 1,665

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

PTEN/AKT signaling pathway related to hTERT downregulation and telomere shortening induced in Toxoplasma GRA16-expressing colorectal cancer cells

Seo, S., Shin, J., Ham, D.-W., & Shin, E. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113366 · Cited by 19

PP2A regulates metastasis and vasculogenic mimicry formation via PI3K/AKT/ZEB1 axis in non-small cell lung cancers

Zhang, Y., Wang, X. T., Li, A., Guan, Y., Shen, P., Ni, Y., & Han, X. (2022) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2022.07.001 · Cited by 19

Stable SET knockdown in breast cell carcinoma inhibits cell migration and invasion

Li, J., Yang, X., Ren, X., Meng, X.-J., Huang, H., Zhao, Q.-H., Yuan, J., Hong, W., Xia, B., Huang, X., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.09.013 · Cited by 19

Ifenprodil Attenuates Methamphetamine-Induced Behavioral Sensitization Through the GluN2B-PP2A-AKT Cascade in the Dorsal Striatum of Mice

Chen, G., Li, T., Xiao, J., Wang, J., Shang, Q., Qian, H., Qiao, C., Zhang, P., Chen, T., & Liu, X. (2020) · Neurochemical Research · doi:10.1007/s11064-020-02966-8 · Cited by 19

Cancer‐derived IgG involved in cisplatin resistance through PTP‐BAS/Src/PDK1/AKT signaling pathway

Wang, L., & Gan, Y. (2020) · Oral Diseases · doi:10.1111/odi.13583 · Cited by 19

Autophagy signals orchestrate chemoresistance of gynecological cancers

Tam, C., Rao, S., Waye, M. M. Y., Ng, T. B., & Wang, C. C. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188525 · Cited by 19

Myosin 1b Regulates Nuclear AKT Activation by Preventing Localization of PTEN in the Nucleus

Yu, Y., Xiong, Y., Ladeiras, D., Yang, Z., & Ming, X. (2019) · iScience · doi:10.1016/j.isci.2019.07.010 · Cited by 18

Protein phosphatase 2A in the healthy and failing heart: New insights and therapeutic opportunities

Sergienko, N. M., Donner, D. G., Delbridge, L. M. D., McMullen, J. R., & Weeks, K. L. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110213 · Cited by 19

Regulation of Metabolism by Mitochondrial MUL1 E3 Ubiquitin Ligase

Cilenti, L., Mahar, R., Gregorio, J. D., Ambivero, C. T., Merritt, M. E., & Zervos, A. S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.904728 · Cited by 18

The microRNA Let-7 and its exosomal form: Epigenetic regulators of gynecological cancers

Wang, F., Zhou, C., Zhu, Y., & Keshavarzi, M. (2024) · Cell Biology and Toxicology · doi:10.1007/s10565-024-09884-3 · Cited by 21

MiR-17-92 represses PTPROt and PP2A phosphatases and amplifies tonic BCR signaling in DLBCL cells

Jabłońska, E., Górniak, P., Szydłowski, M., Sewastianik, T., Białopiotrowicz, E., Polak, A., Warzocha, K., & Juszczyński, P. (2016) · Experimental Hematology · doi:10.1016/j.exphem.2016.09.011 · Cited by 18

Ibrutinib therapy downregulates AID enzyme and proliferative fractions in chronic lymphocytic leukemia

Morande, P. E., Sivina, M., Uriepero, A., Seija, N., Berca, C., Fresia, P., Landoni, A. I., Noia, J. M. D., Burger, J. A., & Oppezzo, P. (2019) · Blood · doi:10.1182/blood-2018-09-876292 · Cited by 19

Depression, Estrogens, and Neuroinflammation: A Preclinical Review of Ketamine Treatment for Mood Disorders in Women

Gagne, C., Piot, A., & Brake, W. G. (2022) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2021.797577 · Cited by 18

The Nuclear Zinc Finger Protein Zfat Maintains FoxO1 Protein Levels in Peripheral T Cells by Regulating the Activities of Autophagy and the Akt Signaling Pathway

Ishikura, S., Iwaihara, Y., Tanaka, Y., Luo, H. L., Nishi, K., Doi, K., Koyanagi, M., Okamura, T., Tsunoda, T., & Shirasawa, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.723734 · Cited by 18

Dysregulation of PP2A-Akt interaction contributes to Sucrose non-fermenting related kinase (SNRK) deficiency induced insulin resistance in adipose tissue

Li, J., An, R., Lai, S., Li, L., Liu, S., & Xu, H. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.07.009 · Cited by 19

Loss of LCMT1 and biased protein phosphatase 2A heterotrimerization drive prostate cancer progression and therapy resistance

Rasool, R. U., O’Connor, C. M., Das, C. K., Alhusayan, M., Verma, B. K., Islam, S., Frohner, I. E., Deng, Q., Mitchell-Velasquez, E., Sangodkar, J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40760-6 · Cited by 17

Functional Genetic Polymorphisms in PP2A Subunit Genes Confer Increased Risks of Lung Cancer in Southern and Eastern Chinese

Yang, R., Yang, L., Qiu, F., Zhang, L., Wang, H., Yang, X., Deng, J., Fang, W., Zhou, Y., & Lü, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077285 · Cited by 17

SET protein overexpression contributes to paclitaxel resistance in MCF-7/S cells through PI3K/Akt pathway

Zhang, W., Zheng, X., Meng, T., You, H., Dong, Y., Xing, J., & Chen, S. (2016) · Journal of drug targeting · doi:10.1080/1061186x.2016.1245307 · Cited by 17

Identification of key genes in non‑alcoholic fatty liver disease progression based on bioinformatics analysis

Li, L., Liu, H., Hu, X., Huang, Y., Wang, Y., He, Y., & Lei, Q. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.8852 · Cited by 18

Dynamic Phosphoproteomics Uncovers Signaling Pathways Modulated by Anti-oncogenic Sphingolipid Analogs

Kubiniok, P., Finicle, B. T., Piffaretti, F., McCracken, A. N., Perryman, M. S., Hanessian, S., Edinger, A. L., & Thibault, P. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.001053 · Cited by 17

Loss of IGF2R indicates a poor prognosis and promotes cell proliferation and tumorigenesis in bladder cancer via AKT signaling pathway

Liu, S., Zhou, L., Wang, H. F., Li, G., Xie, Q., & Hu, B. (2019) · Neoplasma · doi:10.4149/neo_2019_190206n108 · Cited by 17

SPAG6 promotes cell proliferation and inhibits apoptosis through the PTEN/PI3K/AKT pathway in Burkitt lymphoma

Zhang, R., Zhu, H., Yuan, Y., Wang, Y., & Tian, Z. (2020) · Oncology Reports · doi:10.3892/or.2020.7776 · Cited by 16

Protein Phosphatase 2A: Role in T Cells and Diseases

Roy, S., & Batra, L. (2023) · Journal of Immunology Research · doi:10.1155/2023/4522053 · Cited by 19

Selenate induces epithelial–mesenchymal transition in a colorectal carcinoma cell line by AKT activation

Tsukamoto, T., Hama, S., Kogure, K., & Tsuchiya, H. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.05.031 · Cited by 16

Redox control of cytosolic Akt phosphorylation in PTEN null cells

Luo, L., Kumar, J. K., & Clement, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.566 · Cited by 16

eIF4E is a critical regulator of human papillomavirus (HPV)-immortalized cervical epithelial (H8) cell growth induced by nicotine

Chen, L., & Wang, H. (2019) · Toxicology · doi:10.1016/j.tox.2019.02.017 · Cited by 16

Visualization of Subunit Interactions and Ternary Complexes of Protein Phosphatase 2A in Mammalian Cells

Mo, S.-T., Chiang, S.-J., Lai, T.-Y., Cheng, Y.-L., Chung, C.-E., Kuo, S. C. H., Reece, K. M., Chen, Y.-C., Chang, N., Wadzinski, B. E., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0116074 · Cited by 17

Mechanistic target of rapamycin inhibition with rapamycin induces autophagy and correlative regulation in white shrimp (Litopenaeus vannamei)

Liu, X., Wang, M., Sun, G.-Q., Wang, B., Jiang, K., Shao, J., Qi, C., Zhao, W., Han, S.-Y., Liu, M., et al. (2018) · Aquaculture Nutrition · doi:10.1111/anu.12688 · Cited by 16

Turn motif phosphorylation negatively regulates activation loop phosphorylation in Akt

Hiraoka, D., Okumura, E., & Kishimoto, T. (2011) · Oncogene · doi:10.1038/onc.2011.155 · Cited by 17

The PP2A-B56 phosphatase opposes cyclin E autocatalytic degradation via site-specific dephosphorylation

Davis, R. J., Swanger, J., Hughes, B. T., & Clurman, B. E. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00657-16 · Cited by 15

Pro-Apoptotic Potential of Pseudevernia furfuracea (L.) Zopf Extract and Isolated Physodic Acid in Acute Lymphoblastic Leukemia Model In Vitro

Kello, M., Kuruc, T., Petrová, K., Goga, M., Michalová, Z., Čoma, M., Ručová, D., & Mojžíš, J. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13122173 · Cited by 17

The association between Salt-inducible kinase 2 (SIK2) and gamma isoform of the regulatory subunit B55 of PP2A (B55gamma) contributes to the survival of glioma cells under glucose depletion through inhibiting the phosphorylation of S6K

Li, Y., Cao, Y., Wu, X. L., Han, G., Wang, L., Zhang, Y., Chen, X., Hao, B., Yue, Z., & Liu, J. (2015) · Cancer Cell International · doi:10.1186/s12935-015-0164-6 · Cited by 15

Regional health and function in the hippocampus: Evolutionary compromises for a critical brain region

Jackson, T. C., & Foster, T. C. (2009) · Bioscience hypotheses · doi:10.1016/j.bihy.2009.02.013 · Cited by 14

RHOB expression controls the activity of serine/threonine protein phosphatase PP2A to modulate mesenchymal phenotype and invasion in non-small cell lung cancers

Calvayrac, O., Pradines, A., & Favre, G. (2016) · Small GTPases · doi:10.1080/21541248.2016.1234429 · Cited by 15

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

Toll-like receptor 2 signaling pathway activation contributes to a highly efficient inflammatory response in Japanese encephalitis virus-infected mouse microglial cells by proteomics

Zhao, G., Gao, Y., Zhang, J., Zhang, H., Xie, C., Nan, F., Feng, S., Ha, Z., Li, C., Zhu, X., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.989183 · Cited by 14

T11TS immunotherapy repairs PI3K‐AKT signaling in T‐cells: Clues toward enhanced T‐cell survival in rat glioma model

Chaudhuri, S., Singh, M. K., Bhattacharya, D., Datta, A., Hazra, I., Mondal, S., Sk, O. F., Ronsard, L., Ghosh, T. K., & Chaudhuri, S. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26047 · Cited by 14

Fine-Tuning of mTORC1-ULK1-PP2A Regulatory Triangle Is Crucial for Robust Autophagic Response upon Cellular Stress

Hajdú, B., Holczer, M., Horváth, G., Szederkényi, G., & Kapuy, O. (2022) · Biomolecules · doi:10.3390/biom12111587 · Cited by 13

Targeting protein methylation in pancreatic cancer cells results in KRAS signaling imbalance and inhibition of autophagy

Montenegro, M. F., Martí-Díaz, R., Navarro, A., Tolivia, J., Sánchez‐del‐Campo, L., Cabezas‐Herrera, J., & Rodríguez‐López, J. N. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06288-9 · Cited by 13

HSPD1 Supports Osteosarcoma Progression through Stabilizing ATP5A1 and thus Activation of AKT/mTOR Signaling

Zhang, Y., Pan, R., Li, K., Cheang, L. H., Zhao, J., Zhong, Z., Li, S., Wang, J., Zhang, X., Cheng, Y., et al. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.100015 · Cited by 13

Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58)

Yang, C.-P., Chiang, C.-W., Chen, C.-H., Lee, Y., Wu, M.-H., Tsou, Y.-H., Yang, Y.-S., Chang, W., & Lin, D.-Y. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0136-0 · Cited by 13

In search for biomarkers and potential drug targets for uterine serous endometrial cancer

Dinoi, G., Mariani, A., Martinelli, E., Ciucci, A., Zannoni, G. F., Weaver, A. L., Keeney, G. L., Vasmatzis, G., Anastasiadis, P. Z., Fanfani, F., et al. (2021) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-021-03566-x · Cited by 13

Okadaic acid induces Akt hyperphosphorylation and an oxidative stress-mediated cell death in serum starved SK-N-SH human neuroblastoma cells that are augmented by rapamycin

Edelstein, J., & Rockwell, P. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.10.052 · Cited by 13

Regulation of PP2AC Carboxylmethylation and Cellular Localisation by Inhibitory Class G-Protein Coupled Receptors in Cardiomyocytes

Longman, M. R., Ranieri, A., Avkiran, M., & Snabaitis, A. K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086234 · Cited by 13

PKCη is a negative regulator of AKT inhibiting the IGF-I induced proliferation

Shahaf, G., Rotem‐Dai, N., Koifman, G., Raveh-Amit, H., Frost, S. A., & Livneh, E. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.01.018 · Cited by 13

The B56γ3 regulatory subunit-containing protein phosphatase 2A outcompetes Akt to regulate p27KIP1 subcellular localization by selectively dephosphorylating phospho-Thr157 of p27KIP1

Lai, T.-Y., Yen, C.-J., Tsai, H.-W., Yang, Y.-S., Hong, W.-F., & Chiang, C.-W. (2015) · Oncotarget · doi:10.18632/oncotarget.6609 · Cited by 13

Anti-tumor effects of perphenazine on canine lymphoma

Tsuji, S., Yabe, R., Usui, T., Mizuno, T., Ohama, T., & Sato, K. (2016) · Journal of Veterinary Medical Science · doi:10.1292/jvms.15-0707 · Cited by 13

Antitumor effects of metformin via indirect inhibition of protein phosphatase 2A in patients with endometrial cancer

Hanawa, S., Mitsuhashi, A., & Shozu, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192759 · Cited by 12

Regulation of XPO5 phosphorylation by PP2A in hepatocellular carcinoma

Li, J., Zhou, J., Mu, X., Shen, S. Y., Xu, X., Luo, Y., Luo, Y., Ming, Y., Wu, Y., & Peng, Y. (2022) · MedComm · doi:10.1002/mco2.125 · Cited by 12

Postmitotic G1 phase survivin drives mitogen-independent cell division of B lymphocytes

Singh, A., Spitzer, M. H., Joy, J. P., Kaileh, M., Qiu, X., Nolan, G. P., & Sen, R. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2115567119 · Cited by 12

PHLPP phosphatases as a therapeutic target in insulin resistance-related diseases

Hribal, M. L., Mancuso, E., Spiga, R., Mannino, G. C., Fiorentino, T. V., Andreozzi, F., & Sesti, G. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1130822 · Cited by 12

PPP2R2D, a regulatory subunit of protein phosphatase�2A, promotes gastric cancer growth and metastasis via mechanistic target of rapamycin activation

Yu, S., Li, L., Wu, Q., Dou, N., Li, Y., & Gao, Y. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4329 · Cited by 11

Hydrogen peroxide formation by Nox4 limits malignant transformationPreprint

Helfinger, V., von Gall, F. F., Henke, N., Kunze, M. M., Schmid, T., Heidler, J., Wittig, I., Radeke, H. H., Marschall, V., Anderson, K. E., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/177055 · Cited by 12

FAM122A ensures cell cycle interphase progression and checkpoint control by inhibiting B55α/PP2A through helical motifs

Wasserman, J. S., Faezov, B., Patel, K. R., Kurimchak, A., Palacio, S. M., Glass, D. J., Fowle, H. A., McEwan, B. C., Xu, Q., Zhao, Z., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50015-7 · Cited by 11

PHLPP2 is a pseudophosphatase that lost activity in the metazoan ancestor

Husremović, T., Meier, V., Piëch, L., Siess, K. M., Antonioli, S., Grishkovskaya, I., Kircheva, N., Angelova, S., Wenzl, K., Brandstätter, A., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2417218122 · Cited by 13

Interplay between glycogen synthase kinase‐3β and tau in the cerebellum of Hsp27 transgenic mouse

Wang, S., Toth, M. E., Bereczki, E., Sántha, M., Guan, Z., Winblad, B. G., & Pei, J.-J. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22660 · Cited by 11

CD28 Blockade Ex Vivo Induces Alloantigen-Specific Immune Tolerance but Preserves T-Cell Pathogen Reactivity

Dillinger, B., Ahmadi-Erber, S. M., Soukup, K., Halfmann, A., Schrom, S., Vanhove, B., Steinberger, P., Geyeregger, R., Ladisch, S., & Dohnal, A. M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01152 · Cited by 11

Proteomic and Phosphoproteomic Reprogramming in Epithelial Ovarian Cancer Metastasis

Frederick, M. I., Hovey, O. F. J., Kakadia, J. H., Shepherd, T. G., Li, S. S. ‐., & Heinemann, I. U. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100660 · Cited by 11

Transient PP2A inhibition alleviates normal tissue stem cell susceptibility to cell death during radiotherapy

Fabbrizi, M. R., Meyer, B., Misri, S., Raj, S., Zobel, C. L., Hallahan, D. E., & Sharma, G. G. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0559-0 · Cited by 11

Small molecule H89 renders the phosphorylation of S6K1 and AKT resistant to mTOR inhibitors

Melick, C. H., & Jewell, J. L. (2020) · Biochemical Journal · doi:10.1042/bcj20190958 · Cited by 13

Perphenazine exerts antitumor effects on HUT78 cells through Akt dephosphorylation by protein phosphatase 2A

Tsuji, S., Kohyanagi, N., Mizuno, T., Ohama, T., & Sato, K. (2020) · Oncology Letters · doi:10.3892/ol.2020.12374 · Cited by 10

The role of miR-222-2p in exosomes secreted by hexavalent chromium-induced premature senescent hepatocytes as a SASP component

Ma, Y., Li, S., Ye, S., Luo, S., Wei, L. J., Su, Y., Zeng, Y., Shi, Y., Bian, H., & Xiao, F. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.123535 · Cited by 12

Depletion of CLK2 sensitizes glioma stem-like cells to PI3K/mTOR and FGFR inhibitors.

Park, S. Y., Mittal, S., Dong, J., Jeong, K., Martínez-Ledesma, E., Piao, Y., Khan, S., Henry, V. K., Verhaak, R. G. W., Majd, N., et al. (2020) · PubMed Central · Cited by 10

PME ‐1 is regulated by USP 36 in ERK and Akt signaling pathways

Kim, S., Choi, J., Lee, D., Park, J., Hwang, Y., & Baek, K. (2018) · FEBS Letters · doi:10.1002/1873-3468.13039 · Cited by 10

The B56γ3-containing protein phosphatase 2A attenuates p70S6K-mediated negative feedback loop to enhance AKT-facilitated epithelial-mesenchymal transition in colorectal cancer

Hsiao, K.-C., Ruan, S.-Y., Chen, S.-M., Lai, T.-Y., Chan, R., Zhang, Y., Chu, C., Cheng, H., Tsai, H., Tu, Y., et al. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01182-5 · Cited by 9

Microcystin-LR activates serine/threonine kinases and alters the phosphoproteome in human HepaRG cells

Ikumawoyi, V. O., Lynch, K. D., Iverson, D. T., Call, M. R., Yue, G. E., Prasad, B., & Clarke, J. (2024) · Toxicon · doi:10.1016/j.toxicon.2024.108072 · Cited by 11

Downregulation of Caveolin-1 Enhances Fusion of Human BeWo Choriocarcinoma Cells

Collett, G. P., Linton, E. A., Redman, C., & Sargent, I. L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010529 · Cited by 9

Akt kinase C-terminal modifications control activation loop dephosphorylation and enhance insulin response

Chan, T. O., Zhang, J., Tiegs, B. C., Blumhof, B., Yan, L. H., Keny, N., Penny, M. K., Li, X., Pascal, J. M., Armen, R. S., et al. (2015) · Biochemical Journal · doi:10.1042/bj20150325 · Cited by 10

A cell competition–based small molecule screen identifies a novel compound that induces dual c-Myc depletion and p53 activation

Tadele, D. S., Robertson, J. M., Crispin, R., Herrera, M. C., Chlubnová, M., Piechaczyk, L., Durán, P. A., Singh, S. K., Gedde‐Dahl, T., Fløisand, Y., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015285 · Cited by 9

Novel involvement of RhebL1 in sphingosylphosphorylcholine-induced keratin phosphorylation and reorganization: Binding to and activation of AKT1

Kim, H. J., Byun, H. J., Park, M. K., Kim, E. J., Kang, G.-J., & Lee, C. H. (2017) · Oncotarget · doi:10.18632/oncotarget.15364 · Cited by 9

MACE-Seq-based coding RNA and TrueQuant-based small RNA profile in breast cancer: tumor-suppressive miRNA-1275 identified as a novel marker

Majed, S. O., & Mustafa, S. A. (2021) · BMC Cancer · doi:10.1186/s12885-021-08218-4 · Cited by 9

PIK3IP1: structure, aberration, function, and regulation in diseases

Jia, Y., He, P., Ma, X., Lv, K., Liu, Y., & Xu, Y. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176753 · Cited by 8

Identification of a novel conserved signaling motif in CD200 receptor required for its inhibitory function

Timmerman, L. M., de Graaf, J. F., Satravelas, N., Keşmir, C., Meyaard, L., & van der Vlist, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0244770 · Cited by 8

Transcriptional feedback in the insulin signalling pathway modulates ageing in both Caenorhabditis elegans and Drosophila melanogaster

Ivanov, D. K., Papatheodorou, I., Ziehm, M., & Thornton, J. M. (2013) · Molecular BioSystems · doi:10.1039/c3mb25485b · Cited by 8

Regulation of mTOR and p70 S6 kinase by the muscarinic M4 receptor in PC12 cells

Chan, G. P. W., Wu, E. H. T., & Wong, Y. H. (2008) · Cell Biology International · doi:10.1016/j.cellbi.2008.11.010 · Cited by 8

Small-molecule modulators of B56-PP2A restore 4E-BP function to suppress eIF4E-dependent translation in cancer cells

Lum, M. A., Jonas, K. A., Parmar, S., Black, A. R., O’Connor, C. M., Dobersch, S., Yamamoto, N., Robertson, T. M., Schutter, A., Giambi, M., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci176093 · Cited by 7

Phosphatase inhibition by sodium orthovanadate displays anti-inflammatory action by suppressing AKT-IKKβ signaling in RAW264.7 cells

Kim, H. G., Jeong, S.-G., Kim, J. H., & Cho, J. Y. (2022) · Toxicology Reports · doi:10.1016/j.toxrep.2022.09.012 · Cited by 7

PI3K Signaling at the Crossroads of Lipid Metabolism and Cancer

Yilmaz, S., & Cizmecioglu, O. (2024) · Advances in experimental medicine and biology · doi:10.1007/5584_2024_832 · Cited by 7

Insights into PI3K / AKT signaling in B cell development and chronic lymphocytic leukemia

Buchner, M. (2024) · FEBS Letters · doi:10.1002/1873-3468.15079 · Cited by 11

An ultrasensitive fiveplex activity assay for cellular kinases

Smolko, C. M., & Janes, K. A. (2019) · Scientific Reports · doi:10.1038/s41598-019-55998-8 · Cited by 7

Galpha16 interacts with Class IA phosphatidylinositol 3-kinases and inhibits Akt signaling.

Yeung, W. W. S., & Wong, Y. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.05.008 · Cited by 9

Estradiol suppresses phosphorylation of ERα serine 167 through upregulation of PP2A in breast cancer cells

Hayashi, T., Hikichi, M., Yukitake, J., Harada, N., & Utsumi, T. (2017) · Oncology Letters · doi:10.3892/ol.2017.7216 · Cited by 7

AKT: A Central Node in Complex Signaling Cascades

Minegishi, K., Dobashi, Y., Kimura, E., & Goto, A. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl26414 · Cited by 7

par-1, Atypicalpkc, and PP2A/B55sur-6Are Implicated in the Regulation of Exocyst-Mediated Membrane Trafficking inCaenorhabditis elegans

Jiu, Y., Hasygar, K., Tang, L., Liu, Y., Holmberg, C. I., Bürglin, T. R., Hietakangas, V., & Jäntti, J. (2013) · G3 Genes Genomes Genetics · doi:10.1534/g3.113.006718 · Cited by 6

Lipid Emulsion Containing High Amounts of n3 Fatty Acids (Omegaven) as Opposed to n6 Fatty Acids (Intralipid) Preserves Insulin Signaling and Glucose Uptake in Perfused Rat Hearts

Lou, P., Lucchinetti, E., Hersberger, M., Clanachan, A. S., & Zaugg, M. (2019) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000004295 · Cited by 6

GRB10 sustains AR activity by interacting with PP2A in prostate cancer cells

Hao, J., Ci, X., Wang, Y., Choi, S. Y. C., Sullivan, S. E., Xue, H., Wu, R., Dong, X., Haegert, A. M., Collins, C. C., et al. (2020) · International Journal of Cancer · doi:10.1002/ijc.33335 · Cited by 6

Cancer stem cell phosphatases

Momeny, M., Arsiola, T., & Westermarck, J. K. (2021) · Biochemical Journal · doi:10.1042/bcj20210254 · Cited by 6

Cellular Protein Phosphatase 2A Regulates Cell Survival Mechanisms in Influenza A Virus Infection

Gerlt, V., Mayr, J., Sarto, J. D., Ludwig, S., & Boergeling, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011164 · Cited by 7

The Bα and Bδ regulatory subunits of PP2A are necessary for assembly of the CaMKIV·PP2A signaling complex

Reece, K. M., Mazalouskas, M. D., & Wadzinski, B. E. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.062 · Cited by 6

FTY720 inhibits germ cell apoptosis in testicular torsion/detorsion

Shih, H., Yen, J., Chiu, A. W., Chow, Y.-C., Pan, W. H. T., & Huang, C. (2015) · Journal of Surgical Research · doi:10.1016/j.jss.2015.12.035 · Cited by 6

The effects of short‐term treatment of microcystin‐LR on the insulin pathway in both the HL7702 cell line and livers of mice

Huang, P., Chen, K., Ma, T., Cao, N., Weng, D., Xu, C., & Xu, L. (2020) · Environmental Toxicology · doi:10.1002/tox.22907 · Cited by 6

Higher content of microcystin‐leucine‐arginine promotes the survival of intrahepatic cholangiocarcinoma cells via regulating SET resulting in the poorer prognosis of patients

Gu, S., He, W., Yan, M., He, J., Zhou, Q., Yan, X., Fu, X., Chen, J., Han, X., & Qiu, Y. (2020) · Cell Proliferation · doi:10.1111/cpr.12961 · Cited by 6

AKT and DUBs: a bidirectional relationship

Serratore, V., Lucibello, M., Malanga, D., Viglietto, G., & Marco, C. D. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00753-3 · Cited by 6

Network pharmacology and molecular docking reveal mechanisms of amiodarone-induced pulmonary fibrosis

Li, H., Di, R., & Kong, D. (2026) · Scientific Reports · doi:10.1038/s41598-025-34150-9 · Cited by 5

Dysregulation of post-translational modifications in glioma: advances in pathological mechanisms and clinical targeting strategies

Wu, J., Liu, H., Li, X., Huang, H., Zhu, H., Wang, J., Yue, H., Li, R., Shu, K., & You, C. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07743-9 · Cited by 5

A Novel Mouse Model of Combined Hepatocellular-Cholangiocarcinoma Induced by Diethylnitrosamine and Loss of Ppp2r5d

Omella, J. D., Cortesi, E. E., Verbinnen, I., Remmerie, M., Wu, H., Cubero, F. J., Roskams, T., & Janssens, V. (2023) · Cancers · doi:10.3390/cancers15164193 · Cited by 6

Stimulation of ectopically expressed muscarinic receptors induces IFN-γ but suppresses IL-2 production by inhibiting activation of pAKT pathways in primary T cells

Nguyen, T. T. T., Lu, W., Zhu, W. S., Ansel, K. M., Liang, H.-E., & Weiss, A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2300987120 · Cited by 5

Redox-Mediated Rewiring of Signalling Pathways: The Role of a Cellular Clock in Brain Health and Disease

Vujovic, F., Shepherd, C. E., Witting, P. K., Hunter, N., & Farahani, R. H. (2023) · Antioxidants · doi:10.3390/antiox12101873 · Cited by 5

Dipalmitoleoylphosphoethanolamine as a PP2A Enhancer Obstructs Insulin Signaling by Promoting Ser/Thr Dephosphorylation of Akt

Tsuchiya, A., Kanno, T., & Nishizaki, T. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000363027 · Cited by 5

NFluc-FHA2-Aktpep-CFluc

Zhang, H. (2008) · Europe PMC (PubMed Central)

Distinct Protein Phosphatase 2A Heterotrimers Modulate Growth Factor Signaling to Extracellular Signal-regulated Kinases and Akt

Kanegan, M. J. V., Adams, D. G., Wadzinski, B. E., & Strack, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506986200 · Cited by 133

Clk2 and B56β mediate insulin-regulated assembly of the PP2A phosphatase holoenzyme complex on Akt

Rodgers, J. T., Vogel, R. O., & Puigserver, P. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.007 · Cited by 99

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

Untitled work

(2010) · PubMed Central