A P53-Phosphoinositide Signalosome Regulates Nuclear AKT Activation

Correlation Coefficients: Appropriate Use and Interpretation

Schober, P., Boer, C., & Schwarte, L. A. (2018) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000002864 · Cited by 10,986 · see citing works

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 · see citing works

AKT/PKB Signaling: Navigating the Network

Manning, B. D., & Toker, A. (2017) · Cell · doi:10.1016/j.cell.2017.04.001 · Cited by 3,772 · see citing works

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

Alessi, D., James, S., Downes, C., Holmes, A. B., Gaffney, P., Reese, C., & Cohen, P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00122-9 · Cited by 3,047 · see citing works

The PI3K Pathway in Human Disease

Fruman, D. A., Chiu, H., Hopkins, B. D., Bagrodia, S., Cantley, L. C., & Abraham, R. T. (2017) · Cell · doi:10.1016/j.cell.2017.07.029 · Cited by 2,749 · see citing works

Alpelisib for <i>PIK3CA</i> -Mutated, Hormone Receptor–Positive Advanced Breast Cancer

André, F., Ciruelos, E., Rubovszky, G., Campone, M., Loibl, S., Rugo, H. S., Iwata, H., Conte, P., Mayer, I. A., Kaufman, B., et al. (2019) · New England Journal of Medicine · doi:10.1056/nejmoa1813904 · Cited by 2,622 · see citing works

The PI3K–AKT network at the interface of oncogenic signalling and cancer metabolism

Hoxhaj, G., & Manning, B. D. (2020) · Nature Reviews Cancer · doi:10.1038/s41568-019-0216-7 · Cited by 2,137 · see citing works

Putting p53 in context

Kastenhuber, E. R., & Lowe, S. W. (2017) · Cell · doi:10.1016/j.cell.2017.08.028 · Cited by 1,906 · see citing works

p53 mutations in cancer

Muller, P. A. J., & Vousden, K. H. (2013) · Nature Cell Biology · doi:10.1038/ncb2641 · Cited by 1,647 · see citing works

Mutant p53 in Cancer: New Functions and Therapeutic Opportunities

Muller, P. A. J., & Vousden, K. H. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.01.021 · Cited by 1,545 · see citing works

Automatic and Quantitative Measurement of Protein-Protein Colocalization in Live Cells

Costes, S. V., Daelemans, D., Cho, E. H., Dobbin, Z. C., Pavlakis, G. N., & Lockett, S. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.038422 · Cited by 1,431 · see citing works

Mutant p53 gain of function in two mouse models of Li-Fraumeni syndrome

Olive, K. P., Tuveson, D. A., Ruhe, Z. C., Yin, B., Willis, N. A., Bronson, R. T., Crowley, D., & Jacks, T. (2004) · Cell · doi:10.1016/j.cell.2004.11.004 · Cited by 1,308 · see citing works

Dual Role of Phosphatidylinositol-3,4,5-trisphosphate in the Activation of Protein Kinase B

Stokoe, D., Stephens, L. R., Copeland, T., Gaffney, P. R. J., Reese, C. B., Painter, G. F., Holmes, A. B., McCormick, F. P., & Hawkins, P. T. (1997) · Science · doi:10.1126/science.277.5325.567 · Cited by 1,202 · see citing works

Akt, FoxO and regulation of apoptosis

Zhang, X., Tang, N., Hadden, T. J., & Rishi, A. K. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.03.010 · Cited by 1,112 · see citing works

Role of Translocation in the Activation and Function of Protein Kinase B

Andjelkovic, M., Alessi, D. R., Meier, R., Fernandez, A., Lamb, N. J. C., Frech, M., Cron, P., Cohen, P., Lucocq, J. M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31515 · Cited by 1,051 · see citing works

Increased expression of mutant forms of p53 oncogene in primary lung cancer

Iggo, R. D., Bártek, J., Lane, D. P., Gatter, K. C., Harris, A. L., & Bártek, J. (1990) · The Lancet · doi:10.1016/0140-6736(90)90801-b · Cited by 1,030 · see citing works

The PI3K/AKT Pathway as a Target for Cancer Treatment

Mayer, I. A., & Arteaga, C. L. (2015) · Annual Review of Medicine · doi:10.1146/annurev-med-062913-051343 · Cited by 826 · see citing works

Mutant p53 drives invasion by promoting integrin recycling

Muller, P. A. J., Caswell, P. T., Doyle, B., Iwanicki, M. P., Tan, E. H., Karim, S., Lukashchuk, N., Gillespie, D. A., Ludwig, R. L., Gosselin, P., et al. (2009) · Cell · doi:10.1016/j.cell.2009.11.026 · Cited by 796 · see citing works

FoxO transcription factors; Regulation by AKT and 14-3-3 proteins

Tzivion, G., Dobson, M., & Ramakrishnan, G. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.002 · Cited by 728 · see citing works

Histone H2AX phosphorylation: a marker for DNA damage.

Sharma, A., Singh, K., & Almasan, A. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-998-3_40 · Cited by 679 · see citing works

FOXO transcription factors: key regulators of cellular quality control

Webb, A. E., & Brunet, A. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.003 · Cited by 620 · see citing works

Immunohistochemical staining patterns of p53 can serve as a surrogate marker for TP53 mutations in ovarian carcinoma: an immunohistochemical and nucleotide sequencing analysis

Yemelyanova, A. V., VANG, R. S., Kshirsagar, M. P., Lü, D., Marks, M. A., Shih, I., & Kurman, R. J. (2011) · Modern Pathology · doi:10.1038/modpathol.2011.85 · Cited by 515 · see citing works

PTEN tumor suppressor regulates p53 protein levels and activity through phosphatase-dependent and -independent mechanisms

Freeman, D. J., Li, A. G., Wei, G., Li, H.-H., Kertesz, N. L., Lesche, R., Whale, A. D., Martinez-Diaz, H., Rozengurt, N., Cardiff, R. D., et al. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00021-7 · Cited by 512 · see citing works

PKBα/Akt1 Acts Downstream of DNA-PK in the DNA Double-Strand Break Response and Promotes Survival

Bozulic, L., Sürücü, B., Hynx, D., & Hemmings, B. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.024 · Cited by 386 · see citing works

PtdIns(3,4,5) P 3-Dependent Activation of the mTORC2 Kinase Complex

Liu, P., Gan, W., Chin, Y. R., Ogura, K., Guo, J., Zhang, J., Wang, B., Blenis, J., Cantley, L. C., Toker, A., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0460 · Cited by 385 · see citing works

Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1

Currie, R. A., Walker, K. S., Alex, G. R. A. Y., Deák, M., Casamayor, A., Downes, C. P., Cohen, P., Alessi, D. R., & Lucocq, J. M. (1999) · Biochemical Journal · doi:10.1042/bj3370575 · Cited by 379 · see citing works

Mitogenic Activation, Phosphorylation, and Nuclear Translocation of Protein Kinase Bβ

Meier, R., Alessi, D. R., Cron, P., Andjelković, M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30491 · Cited by 378 · see citing works

Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo

Casamayor, A., MORRICE, N. A., & Alessi, D. R. (1999) · Biochemical Journal · doi:10.1042/bj3420287 · Cited by 343 · see citing works

Phosphoinositide Signaling Pathways in Nuclei Are Associated with Nuclear Speckles Containing Pre-mRNA Processing Factors

Boronenkov, I. V., Loijens, J. C., Umeda, M., & Anderson, R. A. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.12.3547 · Cited by 337 · see citing works

Synthesis of polyphosphoinositides in nuclei of Friend cells. Evidence for polyphosphoinositide metabolism inside the nucleus which changes with cell differentiation

Cocco, L., Gilmour, R. S., Ognibene, A., Letcher, A., Manzoli, F. A., & Irvine, R. F. (1987) · Biochemical Journal · doi:10.1042/bj2480765 · Cited by 321 · see citing works

Akt: A Double-Edged Sword in Cell Proliferation and Genome Stability

Xu, N., Lao, Y., Zhang, Y., & Gillespie, D. A. (2012) · Journal of Oncology · doi:10.1155/2012/951724 · Cited by 308 · see citing works

Intramolecular and Intermolecular Interactions of Protein Kinase B Define Its Activation In Vivo

Calleja, V., Alcor, D., Laguerre, M. S., Park, J., Vojnovic, B., Hemmings, B. A., Downward, J., Parker, P. J., & Larijani, B. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050095 · Cited by 303 · see citing works

Two hot spot mutant p53 mouse models display differential gain of function in tumorigenesis

Hanel, W. G., Marchenko, N. D., Xu, S., Yu, S., Weng, W., & Moll, U. M. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.17 · Cited by 278 · see citing works

Akt Phosphorylation of p300 at Ser-1834 Is Essential for Its Histone Acetyltransferase and Transcriptional Activity

Huang, W., & Chen, C. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.15.6592-6602.2005 · Cited by 276 · see citing works

A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs

Mellman, D. L., Gonzales, M. L., Song, C., Barlow, C. A., Wang, P., Kendziorski, C. M., & Anderson, R. A. (2008) · Nature · doi:10.1038/nature06666 · Cited by 249 · see citing works

Therapeutic Ablation of Gain-of-Function Mutant p53 in Colorectal Cancer Inhibits Stat3-Mediated Tumor Growth and Invasion

Schulz‐Heddergott, R., Stark, N., Edmunds, S. J., Li, J., Conradi, L., Bohnenberger, H., Ceteci, F., Greten, F. R., Dobbelstein, M., & Moll, U. M. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.07.004 · Cited by 239 · see citing works

Regulation of FOXO protein stability via ubiquitination and proteasome degradation

Huang, H., & Tindall, D. J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.01.007 · Cited by 227 · see citing works

PI(3,4,5)P 3 Engagement Restricts Akt Activity to Cellular Membranes

Ebner, M., Lučić, I., Leonard, T. A., & Yudushkin, I. A. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.028 · Cited by 220 · see citing works

Regulation of mTORC2 Signaling

Fu, W., & Hall, M. N. (2020) · Genes · doi:10.3390/genes11091045 · Cited by 213 · see citing works

Nuclear Targeting of Akt Enhances Kinase Activity and Survival of Cardiomyocytes

Shiraishi, I., Melendez, J., Ahn, Y., Skavdahl, M., Murphy, E., Welch, S., Schaefer, E., Walsh, K., Rosenzweig, A., Torella, D., et al. (2004) · Circulation Research · doi:10.1161/01.res.0000124394.01180.be · Cited by 212 · see citing works

MDM2 Acts Downstream of p53 as an E3 Ligase to Promote FOXO Ubiquitination and Degradation

Fu, W., Ma, Q., Chen, L., Li, P., Zhang, M., Ramamoorthy, S., Nawaz, Z., Shimojima, T., Wang, H., Yang, Y., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901758200 · Cited by 202 · see citing works

The emerging multiple roles of nuclear Akt

Martelli, A. M., Tabellini, G., Bressanin, D., Ognibene, A., Goto, K., Cocco, L., & Evangelisti, C. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.08.017 · Cited by 198 · see citing works

Akt Promotes Post-Irradiation Survival of Human Tumor Cells through Initiation, Progression, and Termination of DNA-PKcs–Dependent DNA Double-Strand Break Repair

Toulany, M., Lee, K. J., Fattah, K. R., Lin, Y., Fehrenbacher, B., Schaller, M., Chen, B. P., Chen, D. J., & Rodemann, H. P. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0592 · Cited by 183 · see citing works

p53 stabilization in response to DNA damage requires Akt/PKB and DNA-PK

Boehme, K. A., Kulikov, R., & Blattner, C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703423105 · Cited by 151 · see citing works

Quantitative Lipid Imaging Reveals a New Signaling Function of Phosphatidylinositol-3,4-Bisphophate: Isoform- and Site-Specific Activation of Akt

Liu, S.-L., Wang, Z.-G., Hu, Y., Xin, Y., Singaram, I., Gorai, S., Zhou, X., Shim, Y., Min, J.-H., Gong, L.-W., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.035 · Cited by 141 · see citing works

Role of AKT signaling in DNA repair and clinical response to cancer therapy

Liu, Q., Turner, K. M., Yung, W. K. A., Chen, K., & Zhang, W. (2014) · Neuro-Oncology · doi:10.1093/neuonc/nou058 · Cited by 140 · see citing works

Nuclear phosphoinositides: a signaling enigma wrapped in a compartmental conundrum

Barlow, C. A., Laishram, R. S., & Anderson, R. A. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.09.009 · Cited by 140 · see citing works

AKT1 Inhibits Homologous Recombination by Inducing Cytoplasmic Retention of BRCA1 and RAD51

Plo, I., Laulier, C., Gauthier, L., Lebrun, F., Calvo, F. M., & López, B. S. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0861 · Cited by 132 · see citing works

Agonist-stimulated phosphatidylinositol-3,4,5-trisphosphate generation by scaffolded phosphoinositide kinases

Choi, S., Hedman, A. C., Sayedyahossein, S., Thapa, N., Sacks, D. B., & Anderson, R. A. (2016) · Nature Cell Biology · doi:10.1038/ncb3441 · Cited by 130 · see citing works

Nuclear PI3K signaling in cell growth and tumorigenesis

Davis, W. J., Lehmann, P. Z., & Li, W. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00024 · Cited by 127 · see citing works

Thermophoresis for characterizing biomolecular interaction

Asmari, M., Ratih, R., Alhazmi, H. A., & Deeb, S. E. (2018) · Methods · doi:10.1016/j.ymeth.2018.02.003 · Cited by 123 · see citing works

Biochemical and Structural Characterization of an Intramolecular Interaction in FOXO3a and Its Binding with p53

Wang, F., Marshall, C. B., Yamamoto, K., Li, G., Plevin, M. J., You, H., Mak, T. W., & Ikura, M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.025 · Cited by 117 · see citing works

The role of PI3K/AKT-related PIP5K1α and the discovery of its selective inhibitor for treatment of advanced prostate cancer

Semenas, J., Hedblom, A., Рифкатовна, М. Р., Sarwar, M., Larsson, R., Shcherbina, L., Johansson, M., Härkönen, P. L., Sterner, O., & Persson, J. L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405801111 · Cited by 117 · see citing works

Direct Modification and Activation of a Nuclear Receptor–PIP ₂ Complex by the Inositol Lipid Kinase IPMK

Blind, R. D., Suzawa, M., & Ingraham, H. A. (2012) · Science Signaling · doi:10.1126/scisignal.2003111 · Cited by 117 · see citing works

A Nuclear Phosphoinositide Kinase Complex Regulates P53

Choi, S., Chen, M., Cryns, V. L., & Anderson, R. A. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0297-2 · Cited by 106 · see citing works

Phosphatidylinositol 3-kinase signalling is spatially organized at endosomal compartments by microtubule-associated protein 4

Thapa, N., Chen, M., Horn, H. T., Choi, S., Wen, T., & Anderson, R. A. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-00596-4 · Cited by 102 · see citing works

FOXO3 signalling links ATM to the p53 apoptotic pathway following DNA damage

Chung, Y. M., Park, S., Tsai, W.-B., Wang, S., Ikeda, M.-A., Berek, J. S., Chen, D. J., & Hu, M. C. ‐. (2012) · Nature Communications · doi:10.1038/ncomms2008 · Cited by 100 · see citing works

The signaling phospholipid PIP 3 creates a new interaction surface on the nuclear receptor SF-1

Blind, R. D., Sablin, E. P., Kuchenbecker, K. M., Chiu, H., Deacon, A. M., Das, D., Fletterick, R. J., & Ingraham, H. A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416740111 · Cited by 96 · see citing works

DNA Damage Causes Rapid Accumulation of Phosphoinositides for ATR Signaling

Wang, Y.-H., Hariharan, A., Bastianello, G., Toyama, Y., Shivashankar, G. V., Foiani, M., & Sheetz, M. P. (2017) · Nature Communications · doi:10.1038/s41467-017-01805-9 · Cited by 94 · see citing works

Akt-Mediated Phosphorylation of XLF Impairs Non-Homologous End-Joining DNA Repair

Liu, P., Gan, W., Guo, C., Xie, A., Gao, D., Guo, J., Zhang, J., Willis, N. A., Su, A., Asara, J. M., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.005 · Cited by 77 · see citing works

AKT can be activated in the nucleus

Wang, R., & Brattain, M. G. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.01.020 · Cited by 76 · see citing works

Threonine 308 phosphorylated form of akt translocates to the nucleus of PC12 cells under nerve growth factor stimulation and associates with the nuclear matrix protein nucleolin

Borgatti, P., Martelli, A. M., Tabellini, G., Bellacosa, A., Capitani, S., & Neri, L. M. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10279 · Cited by 70 · see citing works

Inositol Polyphosphate Multikinase Is a Coactivator of P53-Mediated Transcription and Cell Death

Xu, R., Sen, N., Paul, B. D., Snowman, A. M., Rao, F., Vandiver, M. S., Xu, J., & Snyder, S. H. (2013) · Science Signaling · doi:10.1126/scisignal.2003405 · Cited by 52 · see citing works

Enhanced Metastasis Suppression by Targeting TRAIL Receptor 2 in a Murine Model of Triple-Negative Breast Cancer

Malin, D., Chen, F., Schiller, C. L., Koblinski, J. E., & Cryns, V. L. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-0099 · Cited by 48 · see citing works

The Specificity of EGF-Stimulated IQGAP1 Scaffold Towards the PI3K-Akt Pathway is Defined by the IQ3 motif

Chen, M., Choi, S., Jung, O., Wen, T., Baum, C., Thapa, N., Lambert, P. F., Rapraeger, A. C., & Anderson, R. A. (2019) · Scientific Reports · doi:10.1038/s41598-019-45671-5 · Cited by 42 · see citing works

Global tumor protein p53/p63 interactome

Huang, Y., Jeong, J. S., Okamura, J., Sook-Kim, M., Zhu, H., Guerrero-Preston, R. E., & Ratovitski, E. A. (2012) · Cell Cycle · doi:10.4161/cc.20863 · Cited by 41 · see citing works

The nuclear phosphoinositide response to stress

Chen, M., Wen, T., Horn, H. T., Chandrahas, V. K., Thapa, N., Choi, S., Cryns, V. L., & Anderson, R. A. (2020) · Cell Cycle · doi:10.1080/15384101.2019.1711316 · Cited by 38 · see citing works

P53 negatively regulates the transcriptional activity of FOXO3a under oxidative stress

Miyaguchi, Y., Tsuchiya, K., & Sakamoto, K. (2009) · Cell Biology International · doi:10.1016/j.cellbi.2009.04.017 · Cited by 37 · see citing works

DNA-PK promotes activation of the survival kinase AKT in response to DNA damage through an mTORC2-ECT2 pathway

Liu, L., Dai, X., Yin, S., Liu, P., Hill, E. G., Wei, W., & Gan, W. (2022) · Science Signaling · doi:10.1126/scisignal.abh2290 · Cited by 31 · see citing works

Proliferative and Antiapoptotic Signaling Stimulated by Nuclear-Localized PDK1 Results in Oncogenesis

Kikani, C. K., Verona, E. V., Ryu, J., Shen, Y., Ye, Q., Li, Z., Qian, Z., Sakaue, H., Nakamura, K., Du, J., et al. (2012) · Science Signaling · doi:10.1126/scisignal.2003065 · Cited by 29 · see citing works

Phosphoinositide spatially free AKT/PKB activation to all membrane compartments

Thapa, N., Horn, H. T., & Anderson, R. A. (2019) · Advances in Biological Regulation · doi:10.1016/j.jbior.2019.04.002 · Cited by 22 · see citing works

Assessing In Situ Phosphoinositide–Protein Interactions Through Fluorescence Proximity Ligation Assay in Cultured Cells

Chen, M., Horn, H. T., Wen, T., Cryns, V. L., & Anderson, R. A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1142-5_9 · Cited by 20 · see citing works

Serine 396 of PDK1 is required for maximal PKB activation

Moon, Z., Wang, Y., Aryan, N., Mousseau, D. D., & Scheid, M. P. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.07.015 · Cited by 8 · see citing works

Energy metabolism in health and diseases

Liu, H., Wang, S., Wang, J., Guo, X., Song, Y., Fu, K., Gao, Z., Liu, D., He, W., & Yang, L. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02141-x · Cited by 438 · see citing works

The mTORC2 signaling network: targets and cross-talks

Ragupathi, A., Kim, C., & Jacinto, E. (2024) · Biochemical Journal · doi:10.1042/bcj20220325 · Cited by 113 · see citing works

Crosstalk between metabolism and cell death in tumorigenesis

Yang, S., Hu, C., Chen, X., Tang, Y., Li, J., Yang, H., Yang, Y., Ying, B., Xiao, X., Li, S., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-01977-1 · Cited by 71 · see citing works

Nanoparticles targeting mutant p53 overcome chemoresistance and tumor recurrence in non-small cell lung cancer

Bi, Y., Qiu, C., Yang, M., Xing, L., & Jiang, H. (2024) · Nature Communications · doi:10.1038/s41467-024-47080-3 · Cited by 67 · see citing works

Regulating obesity-induced osteoarthritis by targeting p53-FOXO3, osteoclast ferroptosis, and mesenchymal stem cell adipogenesis

Zhao, C., Kong, K.-Y., Liu, P., Chen, X.-Z., Rong, K.-W., Zhang, P., Wang, L., & Wang, X. (2025) · Nature Communications · doi:10.1038/s41467-025-59883-z · Cited by 42 · see citing works

Gut microbiota and radiation-induced injury: mechanistic insights and microbial therapies

Li, L., Yang, Z., Yi, Y., Song, Y., & Zhang, W. Y. (2025) · Gut Microbes · doi:10.1080/19490976.2025.2528429 · Cited by 36 · see citing works

Rational Design of a Hetero-multinuclear Gadolinium(III)–Copper(II) Complex: Integrating Magnetic Resonance Imaging, Photoacoustic Imaging, Mild Photothermal Therapy, Chemotherapy and Immunotherapy of Cancer

Man, X., Li, W., Zhu, M., Li, S., Xu, G., Zhang, Z., Liang, H., & Yang, F. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01273 · Cited by 34 · see citing works

Nuclear phosphoinositide signaling promotes YAP/TAZ-TEAD transcriptional activity in breast cancer

Jung, O., Baek, M.-J., Wooldrik, C., Johnson, K. R., Fisher, K. W., Lou, J., Ricks, T. J., Wen, T., Best, M. D., Cryns, V. L., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00085-6 · Cited by 32 · see citing works

Nuclear Phosphoinositides as Key Determinants of Nuclear Functions

Vidalle, M. C., Sheth, B., Fazio, A., Marvi, M. V., Leto, S., Koufi, F., Neri, I., Casalin, I., Ramazzotti, G., Follo, M. Y., et al. (2023) · Biomolecules · doi:10.3390/biom13071049 · Cited by 29 · see citing works

A sterol‐PI(4)P exchanger modulates the Tel1/ATM axis of the DNA damage response

Ovejero, S., Kumanski, S., Soulet, C., Azarli, J., Pardo, B., Santt, O., Constantinou, A., Pasero, P., & Moriel‐Carretero, M. (2023) · The EMBO Journal · doi:10.15252/embj.2022112684 · Cited by 26 · see citing works

Nuclear PTEN’s Functions in Suppressing Tumorigenesis: Implications for Rare Cancers

Langdon, C. G. (2023) · Biomolecules · doi:10.3390/biom13020259 · Cited by 26 · see citing works

Phosphoinositide signaling at the cytoskeleton in the regulation of cell dynamics

Hou, X., Chen, Y., Carrillo, N. D., Cryns, V. L., Anderson, R. A., Sun, J., Wang, S., & Chen, M. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07616-x · Cited by 25 · see citing works

When PIP2 Meets p53: Nuclear Phosphoinositide Signaling in the DNA Damage Response

Wang, Y., & Sheetz, M. P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.903994 · Cited by 24 · see citing works

Da-Chai-Hu-Tang Formula inhibits the progression and metastasis in HepG2 cells through modulation of the PI3K/AKT/STAT3-induced cell cycle arrest and apoptosis

Duan, Z.-W., Liu, Y., Zhang, P., Hu, J., Mo, Z.-X., Liu, W.-Q., Ma, X., Xiao-hui, Z., Zhou, X., Hu, X., et al. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118293 · Cited by 23 · see citing works

Phosphoinositide kinases in cancer: from molecular mechanisms to therapeutic opportunities

Lope, A. L., Arora, G. K., Murad, R., & Emerling, B. M. (2025) · Nature reviews. Cancer · doi:10.1038/s41568-025-00810-1 · Cited by 22 · see citing works

Selenium-ruthenium complex blocks H1N1 influenza virus-induced cell damage by activating GPx1/TrxR1

Li, Y., Chen, D., Su, J., Chen, M., Chen, T., Jia, W., & Zhu, B. (2023) · Theranostics · doi:10.7150/thno.83522 · Cited by 23 · see citing works

A p85 isoform switch enhances PI3K activation on endosomes by a MAP4- and PI3P-dependent mechanism

Thapa, N., Chen, M., Cryns, V. L., & Anderson, R. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114119 · Cited by 22 · see citing works

PTEN: an emerging target in rheumatoid arthritis?

Zhou, P., Meng, X., Nie, Z., Wang, H., Wang, K., Du, A., & Lei, Y. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01618-6 · Cited by 22 · see citing works

Phosphoinositide signalling in cell motility and adhesion

Hou, X., Ren, C., Jin, J., Chen, Y., Lyu, X.-Y., Bi, K., Carrillo, N. D., Cryns, V. L., Anderson, R. A., Sun, J., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01647-4 · Cited by 21 · see citing works

Tumor suppressor p53 mediates interleukin-6 expression to enable cancer cell evasion of genotoxic stress

Phan, T. T. T., Truong, N. V., Wu, W., Su, Y.-C., Hsu, T.-S., & Lin, L. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01638-0 · Cited by 20 · see citing works

Environmental pollutants and phosphoinositide signaling in autoimmunity

Ren, C., Carrillo, N. D., Cryns, V. L., Anderson, R. A., & Chen, M. (2023) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2023.133080 · Cited by 19 · see citing works

DHCR24 in Tumor Diagnosis and Treatment: A Comprehensive Review

Fu, X., & Wang, Z. (2024) · Technology in Cancer Research & Treatment · doi:10.1177/15330338241259780 · Cited by 18 · see citing works

Advances in the understanding of nuclear pore complexes in human diseases

Li, Y., Zhu, J., Zhai, F., Kong, L., Li, H., & Jin, X. (2024) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-024-05881-5 · Cited by 16 · see citing works

Blue light impairs cornea and corneal wound healing by downregulating VCAM1 partly

Chen, K., Jin, L., Wen, Y., Yang, Q., Xiang, L., Zhang, L., Wang, L., Xia, Y., Chen, Z., Xie, C., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108448 · Cited by 15 · see citing works

Mutant p53 gain-of-function stimulates canonical Wnt signaling via PI3K/AKT pathway in colon cancer

Alvarado-Ortiz, E., Ortíz-Sánchez, E., Sarabia-Sánchez, M. Á., de la Cruz-López, K. G., García-Carrancá, A. M., & Robles‐Flores, M. (2023) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-023-00793-4 · Cited by 17 · see citing works

Nuclear Phospholipids and Signaling: An Update of the Story

Casalin, I., Ceneri, E., Ratti, S., Manzoli, L., Cocco, L., & Follo, M. Y. (2024) · Cells · doi:10.3390/cells13080713 · Cited by 15 · see citing works

GRK2-mediated AKT activation controls cell cycle progression and G2 checkpoint in a p53-dependent manner

Rivas, V., González-Muñoz, T., Albitre, Á., Lafarga, V., Delgado‐Arévalo, C., Mayor, F., & Penela, P. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02143-8 · Cited by 15 · see citing works

Lipid transfer proteins and PI4KIIα initiate nuclear p53-phosphoinositide signaling

Carrillo, N. D., Chen, M., Awasthi, P., Wen, T., Yang, X., Sterling, C., Brahmbhatt, D., Cryns, V. L., & Anderson, R. A. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113123 · Cited by 14 · see citing works

Regulation of Phosphoinositide Signaling by Scaffolds at Cytoplasmic Membranes

Wen, T., Thapa, N., Cryns, V. L., & Anderson, R. A. (2023) · Biomolecules · doi:10.3390/biom13091297 · Cited by 15 · see citing works

Identification of copper metabolism and cuproptosis-related subtypes for predicting prognosis tumor microenvironment and drug candidates in hepatocellular carcinoma

Liu, X., Sun, B., Yao, Y., Lai, L., Wang, X., Xiong, J., Zhang, X., & Jiang, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.996308 · Cited by 14 · see citing works

Regulation of NRF2 by stably associated phosphoinositides and small heat shock proteins in response to stress

Chen, C., Carrillo, N. D., Chen, M., Wen, T., Awasthi, P., Anderson, R. A., & Cryns, V. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110367 · Cited by 13 · see citing works

Transcription‐independent functions of p53 in DNA repair pathway selection

Wang, Y., & Sheetz, M. P. (2022) · BioEssays · doi:10.1002/bies.202200122 · Cited by 13 · see citing works

AKTs do not translocate to the nucleus upon stimulation but AKT3 can constitutively signal from the nuclear envelope

Wainstein, E., Maik-Rachline, G., Blenis, J., & Seger, R. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111733 · Cited by 13 · see citing works

Phosphorylation of AKT by lysyl oxidase-like 2 activates the PI3K/AKT signaling pathway to promote proliferation, invasion and metastasis in esophageal squamous carcinoma

Fan, Z., Liu, Y., Liu, X., Nian, W., Huang, X., Yang, Q., Hou, S., & Chen, F. (2023) · Clinical & Translational Oncology · doi:10.1007/s12094-023-03133-5 · Cited by 13 · see citing works

CEP55 as a promising biomarker and therapeutic target on gallbladder cancer

Huang, M., Zhong, F., Chen, M., Hong, L., Chen, W., Abudukeremu, X., She, F., & Chen, Y. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1156177 · Cited by 12 · see citing works

DYRK1B phosphorylates FOXO1 to promote hepatic gluconeogenesis

Li, S., Huang, K., Chu, X., Zhang, H., Wang, X., Zhang, R., Lu, Y., Mohan, M., & Hu, C. H. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf319 · Cited by 12 · see citing works

Paeoniflorin Inhibits Atrial Fibrosis and Atrial Fibrillation in Angiotensin II-Infused Mice Through the PI3K-Akt Pathway

Ji, Y., & Ning, Z. (2024) · Dose-Response · doi:10.1177/15593258241277919 · Cited by 11 · see citing works

Nuclear patterns of phosphatidylinositol 4,5‐ and 3,4‐bisphosphate revealed by super‐resolution microscopy differ between the consecutive stages of RNA polymerase II transcription

Hoboth, P., Sztacho, M., & Hozák, P. (2024) · FEBS Journal · doi:10.1111/febs.17136 · Cited by 10 · see citing works

Navigating AKT-ivity across cellular compartments

Sun, J., & Chen, M. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.08.001 · Cited by 10 · see citing works

Smurf1 Suppression Enhances Temozolomide Chemosensitivity in Glioblastoma by Facilitating PTEN Nuclear Translocation

Dong, L., Li, Y., Liu, L., Meng, X., Li, S., Han, D., Xiao, Z., & Xia, Q. (2022) · Cells · doi:10.3390/cells11203302 · Cited by 10 · see citing works

The poly(A) polymerase Star-PAP is regulated by stably associated phosphoinositide messengers

Wen, T., Chen, M., Cryns, V. L., & Anderson, R. A. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110412 · Cited by 9 · see citing works

Phosphoinositide signaling in the nucleus: Impacts on chromatin and transcription regulation

Hifdi, N., Vaucourt, M., Hnia, K., Panasyuk, G., & Vandromme, M. (2024) · Biology of the Cell · doi:10.1111/boc.202400096 · Cited by 9 · see citing works

α-arbutin prevents UVA-induced skin photodamage via alleviating DNA damage and collagen degradation in NIH-3T3 cells

Zhao, N., Nie, X., Yan, Y., Liu, Z., Chen, X., Shu, P., & Zhong, J. (2025) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2025.113100 · Cited by 8 · see citing works

The nuclear phosphoinositide-p53 signalosome in the regulation of cell motility

Hou, X., Chen, Y., Zhou, B., Liu, F., Dai, L., Chen, C., Carrillo, N. D., Cryns, V. L., Anderson, R. A., Sun, J., et al. (2025) · Protein & Cell · doi:10.1093/procel/pwaf043 · Cited by 8 · see citing works

Immune Pathway and Gene Database (IMPAGT) Revealed the Immune Dysregulation Dynamics and Overactivation of the PI3K/Akt Pathway in Tumor Buddings of Cervical Cancer

Choi, Y., Park, J. Y., Le, T. M., Lee, E., Lee, D. H., Nguyen, H. D. T., Cho, J., Park, J. Y., Han, H. S., & Chong, G. O. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44110350 · Cited by 8 · see citing works

In silico discovery of a novel potential allosteric PI3Kα inhibitor incorporating 2-oxopropyl urea targeting head and neck squamous cell carcinoma

Jia, W., Li, G., Cheng, X., Zhang, R., & Ma, Y. (2025) · BMC Chemistry · doi:10.1186/s13065-025-01420-6 · Cited by 7 · see citing works

Apigenin Inhibits Cell Ferroptosis by Activating the PI3K/Akt Pathway and Alleviates Renal Injury Caused by Hypertension

Zhang, H., Cao, Y., Jiao, L., & Wan, J. (2025) · Dose-Response · doi:10.1177/15593258251335814 · Cited by 7 · see citing works

Agonist- and stress-driven compartmentalized phosphoinositide signaling in cells

Chen, M., Tan, J. X., Sun, Y., Thapa, N., Cryns, V. L., & Anderson, R. A. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2025.159662 · Cited by 7 · see citing works

Structural and mechanistic basis of mTORC2 activation of protein kinase AKT/PKB

Chu, N. K., Le, N. T. T., Nebie, O., & Yang, S. (2026) · Biochemical Journal · doi:10.1042/bcj20253108 · Cited by 7 · see citing works

Lysosomal PIP 3 revealed by genetically encoded lipid biosensors

Sahan, A. Z., Chen, M., Su, Q., Li, Q., Wang, D., & Zhang, J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2426929122 · Cited by 8 · see citing works

The expanding roles of PI4P and PI(4,5)P2 at the plasma membrane: Role of phosphatidylinositol transfer proteins

Cockcroft, S. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2023.159394 · Cited by 7 · see citing works

Elucidation of the mechanism of action of ailanthone in the treatment of colorectal cancer: integration of network pharmacology, bioinformatics analysis and experimental validation

Ma, S., Guo, X., Han, R., Meng, Q., Zhang, Y., Quan, W., Miao, S., Yang, Z., Shi, X., & Wang, S. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1355644 · Cited by 6 · see citing works

p53 Modulates the Gut‐Liver Axis via PI3K/AKT/Wnt Signaling Pathways in Type 2 Diabetes

Li, Q., Zhang, L., Sun, Y., Du, Z., Xu, S., Wang, X., Wei, S., Tao, Y., Li, B., Jiang, J., et al. (2025) · The FASEB Journal · doi:10.1096/fj.202500755rr · Cited by 6 · see citing works

Aspirin boosts the synergistic effect of EGFR/p53 inhibitors on lung cancer cells by regulating AKT/mTOR and p53 pathways

Liu, Z., Cui, L., Wang, J., Zhao, W., & Teng, Y. (2023) · Cell Biochemistry and Function · doi:10.1002/cbf.3902 · Cited by 6 · see citing works

The human adenovirus PI3K-Akt activator E4orf1 is targeted by the tumor suppressor p53

Göttig, L., Jummer, S., Staehler, L., Groitl, P., Karimi, M., Blanchette, P., Kosulin, K., Branton, P. E., & Schreiner, S. (2024) · Journal of Virology · doi:10.1128/jvi.01701-23 · Cited by 6 · see citing works

Li–Fraumeni Syndrome: Narrative Review Through a Case Report with Ten Years of Primary Tumor Remission Associated with Sechium H387 07 Supplementation

Amador-Gómez, A. I., Aguíñiga-Sánchez, I., Mendoza-Núñez, V. M., Cadena-Íñiguez, J., Romero-López, E., & Santiago‐Osorio, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111477 · Cited by 6 · see citing works

Unlocking the molecular mechanisms of anticancer and immunomodulatory potentials of cariprazine in triple negative breast cancer

Lazovic, A., Marković, B. S., Corovic, I. F., Markovic, T., Andjelkovic, M., Stojanović, B., Jovanović, I., & Mitrović, M. M. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.117931 · Cited by 6 · see citing works

ACKnowledging the role of the Activated-Cdc42 associated kinase (ACK) in regulating protein stability in cancer

Hodder, S. L., Fox, M., Mokhtar, A. M. A., Mott, H. R., & Owen, D. (2023) · Small GTPases · doi:10.1080/21541248.2023.2212573 · Cited by 6 · see citing works

Regulation of NRF2 by Phosphoinositides and Small Heat Shock ProteinsPreprint

Chen, C., Chen, M., Wen, T., Awasthi, P., Carrillo, N. D., Anderson, R. A., & Cryns, V. L. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.26.564194 · Cited by 6 · see citing works

Gegen Qinlian Decoction Ameliorated DSS-Induced Colitis by Attenuating Inflammation, Restoring Intestinal Mucosal Barrier and Modulating Gut Microbiota

Wang, Y., Yan, R., Ye, L.-R., Tang, C., Zhou, H., & Zhao, G. (2025) · Journal of Inflammation Research · doi:10.2147/jir.s505423 · Cited by 5 · see citing works

Nuclear phosphoinositide signaling in cell biology and disease

Sun, Y., Liu, F., Chen, C., Sun, J., & Chen, M. (2026) · Developmental Cell · doi:10.1016/j.devcel.2026.02.004 · Cited by 5 · see citing works

HMGA2 promotes resistance against paclitaxel by targeting the p53 signaling pathway in colorectal cancer cells

Jiang, H., Li, X., Zhou, F., Xi, Y., & Xu, G. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e31431 · Cited by 5 · see citing works

Tudor-SN exacerbates pathological vascular remodeling by promoting the polyubiquitination of PTEN via NEDD4-1

Wu, Y., Chen, Z., Zheng, Z., Li, X., Shu, J., Mao, R., An, J., Fan, S., Luo, R., Guo, Y., et al. (2024) · Journal of Biomedical Science · doi:10.1186/s12929-024-01076-9 · Cited by 5 · see citing works

Autocrine and paracrine LIF signals to collaborate sorafenib-resistance in hepatocellular carcinoma and effects of Kanglaite Injection

Shao, Y., Pu, W., Su, R., Wang, Y., Yin, S., Zhong, H., Han, L., & Yu, H. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.156262 · Cited by 5 · see citing works

Regulation of the MDM2-p53 nexus by a nuclear phosphoinositide and small heat shock protein complex

Lee, J. H., Chen, M., Wen, T., Anderson, R. A., & Cryns, V. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110527 · Cited by 5 · see citing works

Regulation of the poly(A) Polymerase Star-PAP by a Nuclear Phosphoinositide SignalosomePreprint

Wen, T., Chen, M., Cryns, V. L., & Anderson, R. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.01.601467 · Cited by 5 · see citing works

Pip5k1a regulates mandibular homeostasis by orchestrating osteogenesis in mice

Zhou, B. O., Feng, Y., Liang, J., Lu, Z., Zhang, S., Wang, X., Zhang, R., Shuai, S., Wang, S., & Chen, M. (2025) · Oral Science and Homeostatic Medicine · doi:10.26599/oshm.2025.9610026 · Cited by 4 · see citing works

Ovalbumin Peptide–Selenium Nanoparticles Alleviate Immune Suppression in Cyclophosphamide-Induced Mice: A Combined Transcriptomic and Proteomic Approach to Reveal the Mechanism

Zeng, Y., Yang, Q., Du, Z., Liu, X., Shang, X., Xu, M., Liu, J., Lyu, S., & Zhang, T. (2025) · Foods · doi:10.3390/foods14132295 · Cited by 4 · see citing works

Macrophage polarization as a therapeutic target in lung diseases: From pathogenesis to precision intervention

Kuang, H., Chen, Y., Yang, X., Sun, R., Chen, Y., Hu, Z., Ye, L., Deng, C., Li, X., & Wu, J. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116660 · Cited by 8 · see citing works

Silencing the long noncoding RNA MALAT1 inhibits vitreous-induced epithelial–mesenchymal transition in RPE cells by regulating the PDGFRs/AKT axis

Yang, G., Huang, Y., Li, D., Tang, J., Li, W., & Huang, X. (2024) · International Ophthalmology · doi:10.1007/s10792-024-03295-3 · Cited by 4 · see citing works

PARP12-mediated ADP-ribosylation contributes to breast cancer cell fate by regulating AKT activation and DNA-damage response

Pavithran, A., Matarese, M., Morone, B., Filograna, A., Monte, M. L., Dathan, N. A., Corda, D., & Grimaldi, G. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05586-z · Cited by 4 · see citing works

PTEN: a new dawn in Parkinson’s disease treatment

Yang, X., Liu, T., & Cheng, H. (2025) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2025.1497555 · Cited by 4 · see citing works

The Role of Nuclear Phosphoinositides in the p53-MDM2 Nexus

Lee, J. H., Salah, M. K., Chen, X., Kucherenko, N. V., Cryns, V. L., & Anderson, R. A. (2025) · Cells · doi:10.3390/cells14151126 · Cited by 4 · see citing works

The oily nucleus– role of phospholipids in genome biology: membrane-directed roles and signaling in the nucleoplasm

Umair, Z., Nawaz, Z., Hasnain, S., & Fischle, W. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05825-3 · Cited by 3 · see citing works

The Inner Nuclear Membrane Has a Unique Lipid Signature

Niu, Y., & Balla, T. (2025) · BioEssays · doi:10.1002/bies.70055 · Cited by 3 · see citing works

TRAF6-mediated ubiquitination of AKT1 in the nucleus occurs in a β-arrestin2-dependent manner upon insulin stimulation

Hu, L., Liu, H., Ma, H., Zeng, X., Cao, Y., Liu, B., Li, H., & Zhang, X. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116362 · Cited by 3 · see citing works

Interneuron migration impairment and brain region-specific DNA damage response following irradiation during early neurogenesis in mice

Berden, L., Rajan, N., Mfossa, A. C. M., Bie, I. D., Etlioglu, E., Benotmane, M. A., Verslegers, M., Aourz, N., Smolders, I. J., Rigo, J., et al. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05643-7 · Cited by 3 · see citing works

Ru(II)-Photodynamic Therapy Suppresses Nonfunctioning Pituitary Adenoma Growth by Targeting PI3K/AKT/p53 Signaling

Dong, F., Wang, Z., Yuan, X., Luo, S., Zhan, R., Hu, W., Chen, H., Wang, W., Liu, J., Wang, Z., et al. (2025) · ACS Applied Bio Materials · doi:10.1021/acsabm.5c01123 · Cited by 2 · see citing works

Pro-Apoptosis Effects of Yangzheng-Xiaoji Capsules in Hepatocellular Carcinoma: Activation of the p53-Induced Apoptotic Pathway and Inhibition of the PI3K/Akt Pathway

Zhou, T., Li, L., Guo, T., Wang, Y., Sun, D., Tan, J., Yu, C., Shen, W., & Cheng, H. (2025) · Integrative Cancer Therapies · doi:10.1177/15347354251352848 · Cited by 2 · see citing works

Spatial organization of phosphoinositide signaling

Lai, S., Huang, W., & He, K. (2025) · FEBS Letters · doi:10.1002/1873-3468.70227 · Cited by 2 · see citing works

A retrospective on phosphatidylinositol transfer proteins (PITPs) – A fifty-year journey

Cockcroft, S. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2025.159714 · Cited by 2 · see citing works

The mTORC2 component SIN1 post-transcriptionally regulates TYMS levels and modulates P53 activity in response to 5-FU chemotherapy

Sayed, A. E., Gomes, N., Zakrzewski, M., Liudkovska, V., Serwa, R. A., & Azzi, A. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-025-02640-y · Cited by 2 · see citing works

Endosomes as central hubs of interorganellar communication and cellular homeostasis

Feng, Y., Zhou, B., Lu, Z., Guo, M., Zhang, S., Wang, S., & Chen, M. (2026) · Protein & Cell · doi:10.1093/procel/pwag018 · Cited by 2 · see citing works

P53 Deficiency Accelerate Esophageal Epithelium Intestinal Metaplasia Malignancy

Qiu, Q., Guo, G., Guo, X., Hu, X., Yu, T., Liu, G., Zhang, H., Chen, Y., & She, J. (2023) · Biomedicines · doi:10.3390/biomedicines11030882 · Cited by 2 · see citing works

Sialin2 Senses Nitrate to Activate Endosomal PI3K-AKT- NOS SignalingPreprint

Li, X., Jiang, O., Cao, Z., Zhou, B., Chen, X., Feng, Y., Zhang, C., Wang, J., Zhou, J., Yan, R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.04.652107 · Cited by 2 · see citing works

From Obscurity to Prominence: IPMK’s Expanding Role in Cellular Signaling, Physiology, and Disease

Mishra, S. H., Chatterjee, S., Viera-Preval, L., & Guha, P. (2025) · Biomolecules · doi:10.3390/biom15091266 · Cited by 1 · see citing works

The Critical Role of HMGB1Cys106 in Regulating Sex-Specific p53 Signaling in Pulmonary Arterial Hypertension

Lawal, O., Niihori, M., James, J., Hinkle, A. J., Sano, T., McClain, N., Rafikov, R., & Rafikova, O. (2025) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2024-0296oc · Cited by 1 · see citing works

Nuclear trafficking of PDK1 in importin7-dependent manner is required for insulin-induced AKT ubiquitination

Wang, F., Hu, L., Zeng, X., You, W., Li, H., Liu, B., & Zhang, X. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123934 · Cited by 1 · see citing works

Phosphoinositide dynamics in virus-associated malignancies

Li, M., Zhong, W., Hirsch, E., & Yan, D. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.09.002 · Cited by 1 · see citing works

FOXO4-DRI regulates endothelial cell senescence via the P53 signaling pathway

Hu, Z., Li, F., Hu, C., Shan, Q., Tang, Z., Jiang, M., Yi, X., Chen, X., Jin, L., Wang, X., et al. (2026) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2025.1729166 · Cited by 1 · see citing works

Mutant p53 and TP53 mutations in esophageal squamous cell carcinoma: consistency and diagnostic significance

Zhuang, X., Lin, N., & Xu, Y. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2026.1680422 · Cited by 1 · see citing works

NRF2 stabilization by isoform-specific nuclear phosphoinositides in stress response

Tang, Y., Chen, Y., Carrillo, N. D., Cryns, V. L., Anderson, R. A., Sun, J., & Chen, M. (2026) · Oral Science and Homeostatic Medicine · doi:10.26599/oshm.2026.9610041 · Cited by 1 · see citing works

Potential Mechanisms of MAP Kinase JNK’s Involvement in Modulating Cancer Cell Fate in a Cisplatin Concentration-Dependent Manner

Tenkutytė, M., Kalvelytė, A. V., & Stulpinas, A. (2026) · Pharmaceuticals · doi:10.3390/ph19030509 · Cited by 1 · see citing works

Integrated genomic profiling identifies predictive biomarkers for neoadjuvant therapy response in Chinese breast cancer patients

Ying, X., Zhang, K., Jiang, S., Chen, L., Li, J.-J., Liu, G.-Y., Yu, K.-D., Wu, J., Di, G. H., Wang, Y.-Y., et al. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218503 · Cited by 1 · see citing works

Lipid transfer proteins and PI4KIIα generate a phosphoinositide-linked proteome

Carrillo, N. D., Chen, M., Awasthi, P., Wen, T., Chen, X., Vũ, G. T., Brahmbhatt, D., Herlihy, M., Minkoff, B. B., Sussman, M., et al. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113089 · Cited by 1 · see citing works

Systematic Interrogation of the Temperature Perturbation in the Insulin Signaling Pathway for Optogenetic Stimulation

Dong, Q., Endo, M., Kawamura, G., & Ozawa, T. (2022) · Cells · doi:10.3390/cells11193136 · Cited by 1 · see citing works

Comentarios a la Ley 9/2010 de 30 de julio, de Aguas para Andalucía: en especial los derechos de uso y el régimen económico-financiero

Beceiro, M. S. (2010) · Revista de derecho urbanístico y medio ambiente/Revista de derecho urbanístico y medio ambiente

Reconstructing emergent biological phenomena through comparative functional architectonicsPreprint

Pérez, V., & Lyubarsky, G. Y. (2023) · Qeios · doi:10.32388/uri5sf

Protective effect of puerarin esters against oxygen and glucose deprivation-reoxygenation- induced microglial cells damagePreprint

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