Protein phosphatase 2A: a target for anticancer therapy

The genomic and transcriptomic architecture of 2,000 breast tumours reveals novel subgroups

METABRIC Group, Curtis, C., Shah, S. P., Chin, S.-F., Turashvili, G., Rueda, O. M., Dunning, M. J., Speed, D., Lynch, A. G., Samarajiwa, S., et al. (2012) · Nature · doi:10.1038/nature10983 · Cited by 6,097

Oncogenic Transcription Factors in the Human Acute Leukemias

Look, A. T. (1997) · Science · doi:10.1126/science.278.5340.1059 · Cited by 1,181

Principles of Tumor Suppression

Sherr, C. J. (2004) · Cell · doi:10.1016/s0092-8674(03)01075-4 · Cited by 1,028

Bcl-2 family proteins and cancer

Yip, K. W., & Reed, J. C. (2008) · Oncogene · doi:10.1038/onc.2008.307 · Cited by 913

Ubiquitination regulates PTEN nuclear import and tumor suppression

Trotman, L. C., Wang, X., Alimonti, A., Chen, Z., Teruya-Feldstein, J., Yang, H., Pavletich, N. P., Carver, B. S., Cordon-Cardo, C., Erdjument-Bromage, H., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.040 · Cited by 748

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

The biology of CML blast crisis

Calabretta, B., & Perrotti, D. (2004) · Blood · doi:10.1182/blood-2003-12-4111 · Cited by 608

Protein phosphatase 2A regulatory subunits and cancer

Eichhorn, P. J. A., Creyghton, M. P., & Bernards, R. (2009) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.05.005 · Cited by 513

The tumor suppressor PP2A is functionally inactivated in blast crisis CML through the inhibitory activity of the BCR/ABL-regulated SET protein

Neviani, P., Santhanam, R., Trotta, R., Notari, M., Blaser, B. W., Liu, S., Mao, H. C., Chang, J. S., Galietta, A., Uttam, A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.015 · Cited by 481

Involvement of vacuolar H+‐ ATP ase in killing of human melanoma cells by the sphingosine kinase analogue FTY 720

Tay, K. H., Liu, X., Chi, M., Jin, L., Jiang, C. C., Guo, S., Verrills, N. M., Tseng, H., & Zhang, X. D. (2014) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12326 · Cited by 20

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

Review of PP2A Tumor Biology and Antitumor Effects of PP2A Inhibitor LB100 in the Nervous System

Bryant, J.-P., Levy, A. S., Heiss, J. D., & Banasavadi‐Siddegowda, Y. (2021) · Cancers · doi:10.3390/cancers13123087 · Cited by 20

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

Molecular targets and mechanisms of anti-cancer effects of withanolides

Zhang, Z., Yang, Y., Xu, Y., Liu, Y., Li, H., & Chen, L. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110698 · Cited by 19

The Emerging Role of Ubiquitin-Specific Protease 36 (USP36) in Cancer and Beyond

Niu, M.-Y., Liu, Y.-J., Shi, J., Chen, R.-Y., Zhang, S., Li, C.-Y., Cao, J.-F., Yang, G., & Chen, J. (2024) · Biomolecules · doi:10.3390/biom14050572 · Cited by 20

Cellular Casein Kinase 2 and Protein Phosphatase 2A Modulate Replication Site Assembly of Bluetongue Virus

Mohl, B.-P., & Roy, P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.714766 · Cited by 19

Shwachman–Bodian–Diamond syndrome (SBDS) protein is a direct inhibitor of protein phosphatase 2A (PP2A) activity and overexpressed in acute myeloid leukaemia

Dun, M. D., Mannan, A., Rigby, C. J., Butler, S. M., Toop, H. D., Beck, D., Connerty, P., Sillar, J. R., Kahl, R. G. S., Duchatel, R. J., et al. (2020) · Leukemia · doi:10.1038/s41375-020-0814-0 · Cited by 19

Antiviral Effects of Inhibiting Host Gene Expression

Tripp, R. A., & Tompkins, M. (2014) · Current topics in microbiology and immunology · doi:10.1007/82_2014_409 · Cited by 19

Phosphatases: Their Roles in Cancer and Their Chemical Modulators

Fontanillo, M., & Köhn, M. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-32805-8_10 · Cited by 18

Atypical Chronic Myeloid Leukemia: A Rare Entity with Management Challenges

Dhakal, P., Gundabolu, K., Amador, C., Rayamajhi, S., & Bhatt, V. R. (2017) · Future Oncology · doi:10.2217/fon-2017-0334 · Cited by 19

TRIM-endous functional network of tripartite motif 29 (TRIM29) in cancer progression and beyond

Wu, Q., Nandi, D., & Sharma, D. (2024) · Cancer and Metastasis Reviews · doi:10.1007/s10555-024-10226-2 · Cited by 22

Arpp19 Promotes Myc and Cip2a Expression and Associates with Patient Relapse in Acute Myeloid Leukemia

Mäkelä, E., Löyttyniemi, E., Salmenniemi, U., Kauko, O., Varila, T., Kairisto, V., Itälä‐Remes, M., & Westermarck, J. K. (2019) · Cancers · doi:10.3390/cancers11111774 · Cited by 18

Leucine Carboxyl Methyltransferase Downregulation and Protein Phosphatase Methylesterase Upregulation Contribute Toward the Inhibition of Protein Phosphatase 2A by α-Synuclein

Tian, H. M., Lu, Y., Liu, J., Liu, W., Lu, L., Duan, C., Gao, G., & Yang, H. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00173 · 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

The Interplay between PP2A and microRNAs in Leukemia

Ruvolo, P. P. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00043 · Cited by 17

Ethnopharmacological and phytomedical knowledge of Coleus forskohlii: An approach towards its safety and therapeutic value

Shivaprasad, H. N., Pandit, S., Bhanumathy, M., Manohar, D., Jain, V. K., Thandu, S. A., & Su, X. Q. (2014) · Oriental Pharmacy and Experimental Medicine · doi:10.1007/s13596-014-0169-z · Cited by 18

Phosphorylated protein phosphatase 2A determines poor outcome in patients with metastatic colorectal cancer

Cristóbal, I., Manso, R., Rincón, R., Caramés, C., Zazo, S., del Pulgar, T. G., Cebrián, A., Madoz‐Gúrpide, J., Rojo, F., & García‐Foncillas, J. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.376 · Cited by 17

Overexpression of SET oncoprotein is associated with tumor progression and poor prognosis in human gastric cancer

Yuan, X., Zhang, T., Zheng, X. M., Zhang, Y., Feng, T., Liu, P., Sun, Z., Qin, S., Liu, X., Zhang, L., et al. (2017) · Oncology Reports · doi:10.3892/or.2017.5788 · Cited by 17

SET Overexpression is Associated with Worse Recurrence-Free Survival in Patients with Primary Breast Cancer Receiving Adjuvant Tamoxifen Treatment

Huang, Y.-H., Chu, P., Chen, J., Huang, C., Lee, C.-H., Lau, K.-Y., Wang, W., Wang, Y.-L., Lien, P., Tseng, L., et al. (2018) · Journal of Clinical Medicine · doi:10.3390/jcm7090245 · Cited by 17

Potential of phenothiazines to synergistically block calmodulin and reactivate PP2A in cancer cells

Manoharan, G. B., Okutachi, S., & Abankwa, D. (2022) · PLoS ONE · doi:10.1371/journal.pone.0268635 · Cited by 18

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

Inhibition of PP2A ameliorates intervertebral disc degeneration by reducing annulus fibrosus cells apoptosis via p38/MAPK signal pathway

Zhu, P., Wu, X., Ni, L., Chen, K., Dong, Z., Du, J., Kong, F., Mao, Y., Tao, H., Chu, M., et al. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166888 · Cited by 16

Fas Versatile Signaling and Beyond: Pivotal Role of Tyrosine Phosphorylation in Context-Dependent Signaling and Diseases

Chakrabandhu, K., & Hueber, A. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00429 · Cited by 17

STAMBPL1 knockdown has antitumour effects on gastric cancer biological activities

Yu, D., Qian, J., Jin, X., Li, J., Guo, C., & Yue, X. (2019) · Oncology Letters · doi:10.3892/ol.2019.10789 · Cited by 16

Cell Density-Dependent Increase in Tyrosine-Monophosphorylated ERK2 in MDCK Cells Expressing Active Ras or Raf

Kawabata, N., & Matsuda, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167940 · Cited by 16

High CFTR expression in philadelphia chromosome-positive acute leukemia protects and maintains continuous activation of BCR-ABL and related signaling pathways in combination with PP2A

Yang, X., Yan, T., Gong, Y., Liu, X., Sun, H., Xu, W., Wang, C., Naren, D., & Zheng, Y. (2017) · Oncotarget · doi:10.18632/oncotarget.15510 · Cited by 16

Conditional knockout in mice reveals the critical roles of Ppp2ca in epidermis development

Fang, C., Li, L., & Li, J. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050756 · Cited by 15

Role of cyanotoxins in the development and promotion of cancer

Rajput, S., Jain, S., Dash, D., Gupta, N. M., Rajpoot, R., Upadhyaya, C. P., Khan, M. L., & Koiri, R. K. (2024) · Toxicology Reports · doi:10.1016/j.toxrep.2024.101798 · Cited by 15

Theophylline Represses IL-8 Secretion from Airway Smooth Muscle Cells Independently of Phosphodiesterase Inhibition. Novel Role as a Protein Phosphatase 2A Activator

Patel, B. S., Rahman, M. M., Rumzhum, N. N., Oliver, B. G. G., Verrills, N. M., & Ammit, A. J. (2015) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2015-0308oc · Cited by 15

HDAC1 controls CIP2A transcription in human colorectal cancer cells

Balliu, M., Cellai, C., Lulli, M., Laurenzana, A., Torre, E., Vannucchi, A. M., & Paoletti, F. (2016) · Oncotarget · doi:10.18632/oncotarget.8406 · Cited by 15

The mir‐465 family is upregulated with age and attenuates growth hormone signaling in mouse liver

Elias, A. E., Kun, B., Sabula, I. M. C., Golomb‐Mello, G., Zablah, A. C., & Kreiling, J. A. (2019) · Aging Cell · doi:10.1111/acel.12892 · Cited by 15

Cooperation of imipramine blue and tyrosine kinase blockade demonstrates activity against chronic myeloid leukemia

Laidlaw, K. M. E., Berhan, S., Liu, S., Silvestri, G., Holyoake, T. L., Frank, D. A., Aggarwal, B. B., Bonner, M. Y., Perrotti, D., Jørgensen, H. G., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.10541 · Cited by 15

Knockdown of sodium–calcium exchanger 1 induces epithelial-to-mesenchymal transition in kidney epithelial cells

Balasubramaniam, S. L., Gopalakrishnapillai, A., Petrelli, N. J., & Barwe, S. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.752352 · Cited by 15

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

Protein Phosphatase 2A as a Therapeutic Target in Small Cell Lung Cancer

Mirzapoiazova, T., Xiao, G., Mambetsariev, B., Nasser, M. W., Miaou, E., Singhal, S. S., Srivastava, S., Mambetsariev, I., Nelson, M. S., Nam, A., et al. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0013 · Cited by 14

Synthesis, spectral and DNA/Protein binding evaluation of novel Cu(II) chelates of an NNO donor tridentate aroylhydrazone: Halogen bonding directed close packing

Nair, Y., Venkataraman, S. K., Joy, F., Krishna, P. M., Agarwal, A. K., Vinod, T. P., Madathil, P. K., & Kurup, M. R. P. (2020) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2020.128453 · Cited by 14

The PP2A regulatory subunits, Cdc55 and Rts1, play distinct roles in Candida albicans’ growth, morphogenesis, and virulence

Han, Q., Pan, C., Wang, Y., Wang, N., Wang, Y., & Sang, J. (2019) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2019.103240 · Cited by 15

Curcumol and FTY720 synergistically induce apoptosis and differentiation in chronic myelomonocytic leukemia via multiple signaling pathways

Zhao, M., Yang, C., Chai, S., Yuan, Y., Zhang, J., Cao, P., Wang, Y., Xiao, X., Wu, K., Yan, H., et al. (2020) · Phytotherapy Research · doi:10.1002/ptr.6968 · Cited by 14

Knockdown of Clusterin Expression Increases the In Vitro Sensitivity of Human Prostate Cancer Cells to Paclitaxel

Chun, Y. (2014) · Journal of Toxicology and Environmental Health · doi:10.1080/15287394.2014.951760 · Cited by 14

A novel anti-melanoma SRC-family kinase inhibitor

Halaban, R., Bacchiocchi, A., Straub, R., Cao, J. P., Sznol, M., Narayan, D., Allam, A., Krauthammer, M. O., & Mansour, T. S. (2019) · Oncotarget · doi:10.18632/oncotarget.26787 · Cited by 13

Combination of celecoxib and calyculin-A inhibits epithelial-mesenchymal transition in human oral cancer cells

Velmurugan, B. K., Hua, C.-H., Tsai, M.-H., Lee, C.-P., Chung, C., & Ko, Y.-C. (2020) · Biotechnic & Histochemistry · doi:10.1080/10520295.2019.1700429 · Cited by 13

PPP2R4 dysfunction promotes KRAS-mutant lung adenocarcinoma development and mediates opposite responses to MEK and mTOR inhibition

Meeusen, B., Cortesi, E. E., Omella, J. D., Sablina, A. A., Ventura, J., & Janssens, V. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.06.022 · Cited by 14

Thirty years of SET/TAF1β/I2PP2A: from the identification of the biological functions to its implications in cancer and Alzheimer’s disease

Mambro, A. D., & Esposito, M. T. (2022) · Bioscience Reports · doi:10.1042/bsr20221280 · Cited by 12

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

TLR2 ligation induces corticosteroid insensitivity in A549 lung epithelial cells: Anti-inflammatory impact of PP2A activators

Rahman, M. M., Prabhala, P., Rumzhum, N. N., Patel, B. S., Wickop, T., Hansbro, P. M., Verrills, N. M., & Ammit, A. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.030 · Cited by 13

The role of SET/I2PP2A in canine mammary tumors

Kake, S., Tsuji, S., Enjoji, S., Hanasaki, S., Hayase, H., Yabe, R., Tanaka, Y., Nakagawa, T., Liu, H., Chang, S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-04291-7 · Cited by 13

Small Cell Lung Cancer from Traditional to Innovative Therapeutics: Building a Comprehensive Network to Optimize Clinical and Translational Research

Subbiah, S. P., Nam, A., Garg, N., Behal, A., Kulkarni, P., & Salgia, R. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9082433 · Cited by 14

RACK1 stabilises the activity of PP2A to regulate the transformed phenotype in mammary epithelial cells

Bailey‐Whyte, M., Adams, D. R., Hayes, S. L., O’Connor, R., Baillie, G. S., & Kiely, P. A. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.09.001 · Cited by 12

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

Inhibiting PP2Acα Promotes the Malignant Phenotype of Gastric Cancer Cells through the ATM/METTL3 Axis

Cheng, Z., Gao, S., Liang, X., Lian, C., Chen, J., & Fang, C. (2021) · BioMed Research International · doi:10.1155/2021/1015293 · Cited by 12

PP2A Catalytic Subunit α promotes fibroblast activation and kidney fibrosis via ERK pathway

Lu, Q., Tan, M., Hou, Q., Wang, M., & Dai, C. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110187 · 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

The Pursuit of Enzyme Activation: A Snapshot of the Gold Rush

Teng, M., Young, D. W., & Tan, Z. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01291 · Cited by 12

Ethoxysanguinarine inhibits viability and induces apoptosis of colorectal cancer cells by inhibiting CIP2A

Jin, L., Si, Y., Hong, X., Liu, P., Zhu, B., Yu, H., Zhao, X., Qin, S., Xiong, M., Liu, Y., et al. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4323 · Cited by 12

Deletion of Pr72 causes cardiac developmental defects in Zebrafish

Song, G., Han, M., Li, Z., Gan, X., Chen, X., Yang, J., Dong, S., Yan, M., Wan, J., Wang, Y., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0206883 · Cited by 12

Antagonizing SET Augments the Effects of Radiation Therapy in Hepatocellular Carcinoma through Reactivation of PP2A-Mediated Akt Downregulation

Huang, C., Hung, M., Shih, C.-T., Hsieh, F., Kuo, C.-W., Tsai, M.-H., Chang, S.-S., Hsiao, Y., Chen, L., Chao, T., et al. (2018) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.118.249102 · Cited by 12

From Basic Science to Clinical Practice: The Role of Cancerous Inhibitor of Protein Phosphatase 2A (CIP2A)/p90 in Cancer

Chen, B., Hu, H., & Chen, X. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1110656 · Cited by 12

Atypical CML- the role of morphology and precision genomics

Lasho, T. L. (2019) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2019.101133 · Cited by 11

Epstein-Barr Virus Induces Lymphangiogenesis and Lympth Node Metastasis via Upregulation of VEGF-C in Nasopharyngeal Carcinoma

Li, D.-K., Chen, X.-R., Wang, L.-N., Wang, J.-H., Wen, Y.-T., Zhou, Z.-Y., Li, J.-K., Liu, J.-X., Cai, L.-B., Zhong, S.-S., et al. (2021) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-21-0164 · Cited by 11

The Pivotal Role of Protein Phosphatase 2A (PP2A) in Brain Tumors

Cucinotta, L., Filippone, A., Casili, G., Lanza, M., Bova, V., Capra, A. P., Giuffrida, R., Colarossi, C., Sciacca, D., Paterniti, I., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415717 · Cited by 11

A novel PP2A enhancer induces caspase-independent apoptosis of MKN28 gastric cancer cells with high MEK activity

Tsuchiya, A., Kanno, T., Shimizu, T., Nakao, S., Tanaka, A., Tabata, C., Nakano, T., & Nishizaki, T. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.01.034 · Cited by 11

Aberrant expression of vasculogenic mimicry, PRRX1, and CIP2A in clear cell renal cell carcinoma and its clinicopathological significance

Wang, X., Yang, R., Wang, Q., Wang, Y., Ci, H., & Wu, S. (2019) · Medicine · doi:10.1097/md.0000000000017028 · Cited by 11

Sphingosine‐1‐phosphate receptor‐independent lung endothelial cell barrier disruption induced by FTY720 regioisomers

Camp, S. M., Marciniak, A., Chiang, E. T., Garcia, A. N., Bittman, R., Polt, R. L., Perez, R. G., Dudek, S. M., & Garcia, J. G. N. (2020) · Pulmonary Circulation · doi:10.1177/2045894020905521 · Cited by 11

Co-phosphorylation networks reveal subtype-specific signaling modules in breast cancer

Ayati, M., Chance, M. R., & Koyutürk, M. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa678 · Cited by 10

Primary cilia and lipid raft dynamics

Nishimura, Y., Yamakawa, D., Uchida, K., Shiromizu, T., Watanabe, M., & Inagaki, M. (2021) · Open Biology · doi:10.1098/rsob.210130 · Cited by 12

Anticancer Effects and Molecular Action of 7-α-Hydroxyfrullanolide in G2/M-Phase Arrest and Apoptosis in Triple Negative Breast Cancer Cells

Chimplee, S., Roytrakul, S., Sukrong, S., Srisawat, T., Graidist, P., & Kanokwiroon, K. (2022) · Molecules · doi:10.3390/molecules27020407 · Cited by 11

PPP2CA Is a Novel Therapeutic Target in Neuroblastoma Cells That Can Be Activated by the SET Inhibitor OP449

Galiger, C., Dahlhaus, M., Vitek, M. P., Debatin, K., & Beltinger, C. P. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.744984 · Cited by 11

Visualization Tools for Detecting Microcystin-LR in the Biological System via Near-Infrared Fluorescent Probes

Chuan, H., Li, B., Wang, Z., Li, J., Xie, P., & Liu, Y. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c01992 · Cited by 10

SET-PP2A complex as a new therapeutic target in KMT2A (MLL) rearranged AML

Mambro, A. D., Arroyo-Berdugo, Y., Fioretti, T., Randles, M. J., Cozzuto, L., Rajeeve, V., Cevenini, A., Austin, M. J., Esposito, G., Ponomarenko, J. V., et al. (2023) · Oncogene · doi:10.1038/s41388-023-02840-1 · Cited by 9

TTC36 promotes proliferation and drug resistance in hepatocellular carcinoma cells by inhibiting c-Myc degradation

Shao, F., Wang, R., Li, X., Hu, Y., Zhang, Z., Cai, J., Yang, J.-R., Feng, X., Ren, S., Huang, Z., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07663-4 · Cited by 10

PP2Acα Deficiency in Vascular Smooth Muscle Cells Accelerates Aortic Aneurysm and Dissection by Regulating KLF4 Phosphorylation and Ubiquitination

Hu, W., Cai, Z., Li, Q. L., Zhang, T., Chu, X., Wang, C., Zhang, Q., & Qi, R. (2025) · Advanced Science · doi:10.1002/advs.202500102 · Cited by 10

Select Stabilization of a Tumor-Suppressive PP2A Heterotrimer

Shah, V. M., English, I. A., & Sears, R. C. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.06.008 · Cited by 10

SWATH-MS proteomics of PANC-1 and MIA PaCa-2 pancreatic cancer cells allows identification of drug targets alternative to MEK and PI3K inhibition

Aguilar‐Valdés, A., Noriega, L. G., Tovar, A. R., Ibarra-Sánchez, M. D. J., Sosa‐Hernández, V. A., Maravillas‐Montero, J. L., & Martínez‐Aguilar, J. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.03.018 · Cited by 10

Protein Phosphatase 2A Deficiency in Macrophages Increases Foam Cell Formation and Accelerates Atherosclerotic Lesion Development

Li, R. Q., Zhang, C., Xie, F., Zhou, X., Hu, X., Shi, J., Du, X., Lin, Z., & Dong, N. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.745009 · Cited by 10

New Interactors of the Truncated EBNA-LP Protein Identified by Mass Spectrometry in P3HR1 Burkitt’s Lymphoma Cells

Chelouah, S., Cochet, E., Couvé, S., Balkaran, S., Robert, A., May, E., Ogryzko, V. V., & Wiels, J. (2018) · Cancers · doi:10.3390/cancers10010012 · Cited by 10

Anti-tumoral Effect of a Cell Penetrating and Interfering Peptide Targeting PP2A/SET Interaction

Andrini, L. B., Marin, G. H., Inda, A. M., Bruzzoni‐Giovanelli, H., García, M. N., Errecalde, J. O., & Rebollo, A. (2020) · Folia Medica · doi:10.3897/folmed.62.e47737 · Cited by 10

Carfilzomib induces leukaemia cell apoptosis via inhibiting ELK 1/ KIAA 1524 (Elk‐1/ CIP 2A) and activating PP 2A not related to proteasome inhibition

Liu, C., Hsieh, F., Chu, P., Tsai, W., Huang, C., Yu, Y., Huang, T., Ko, P., Hung, M., Wang, W., et al. (2017) · British Journal of Haematology · doi:10.1111/bjh.14620 · Cited by 10

PP2A regulates signaling through hormonal receptors in breast cancer with important therapeutic implications

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