Regulating tumor suppressor genes: post-translational modifications

Functional Analysis of the Roles of Posttranslational Modifications at the p53 C Terminus in Regulating p53 Stability and Activity

Feng, L., Lin, T., Uranishi, H., Gu, W., & Xu, Y. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5389-5395.2005 · Cited by 236

DUBs, Hypoxia, and Cancer

Mennerich, D., Kubaichuk, K. I., & Kietzmann, T. (2019) · Trends in cancer · doi:10.1016/j.trecan.2019.08.005 · Cited by 234

New insights into PTEN

Tamgüney, T., & Stokoe, D. (2007) · Journal of Cell Science · doi:10.1242/jcs.015230 · Cited by 230

MDMX: from bench to bedside

Marine, J.-C. W., Dyer, M. A., & Jochemsen, A. G. (2007) · Journal of Cell Science · doi:10.1242/jcs.03362 · Cited by 228

Methylation of the Retinoblastoma Tumor Suppressor by SMYD2

Saddic, L., West, L. E., Aslanian, A., Yates, J. R., Rubin, S. M., Gozani, O., & Sage, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.137612 · Cited by 226

Direct identification of PTEN phosphorylation sites

Miller, S. J., Lou, D. Y., Seldin, D. C., Lane, W. S., & Neel, B. G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03274-x · Cited by 225

Assembly and Specific Recognition of K29- and K33-Linked Polyubiquitin

Michel, M. A., Elliott, P. R., Swatek, K. N., Šimíček, M., Pruneda, J. N., Wagstaff, J. L., Freund, S. M. V., & Komander, D. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.042 · Cited by 219

Therapeutic targeting of tumor suppressor genes

Morris, L. G. T., & Chan, T. A.-T. (2014) · Cancer · doi:10.1002/cncr.29140 · Cited by 209

Rak Functions as a Tumor Suppressor by Regulating PTEN Protein Stability and Function

Yim, E.-K., Peng, G., Dai, H., Hu, R., Li, K., Lu, Y., Mills, G. B., Meric‐Bernstam, F., Hennessy, B. T., Craven, R. J., et al. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.02.012 · Cited by 209

THE REGULATION OF PROTEIN PHOSPHORYLATION

Chen, S.-L. (1983) · Purdue e-Pubs (Purdue University System) · Cited by 207

Regulation of Receptors and Transporters by Ubiquitination: New Insights into Surprisingly Similar Mechanisms

Miranda, M., & Sorkin, A. D. (2007) · Molecular Interventions · doi:10.1124/mi.7.3.7 · Cited by 205

How important are post-translational modifications in p53 for selectivity in target-gene transcription and tumour suppression?

Olsson, A., Manzl, C., Strasser, A., & Villunger, A. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402196 · Cited by 204

NEMO specifically recognizes K63‐linked poly‐ubiquitin chains through a new bipartite ubiquitin‐binding domain

Laplantine, E., Fontan, E., Chiaravalli, J., Lopez, T. E., Lakisic, G., Véron, M., Agou, F., & Israël, A. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.241 · Cited by 204

Inhibition of Pluripotency Networks by the Rb Tumor Suppressor Restricts Reprogramming and Tumorigenesis

Kareta, M. S., Gorges, L. L., Hafeez, S., Benayoun, B. A., Marro, S. G., Zmoos, A., Cecchini, M. J., Spacek, D. V., Batista, L. F. Z., O’Brien, M., et al. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.10.019 · Cited by 204

Activation of p53 by MDM2 Antagonists Can Protect Proliferating Cells from Mitotic Inhibitors

Carvajal, D. M., Tovar, C., Yang, H. S., Vu, B. T., Heimbrook, D. C., & Vassilev, L. T. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3576 · Cited by 202

Targeting the RB-E2F pathway in breast cancer

Johnson, J., Thijssen, B., McDermott, U., Garnett, M. J., Wessels, L. F. A., & Bernards, R. (2016) · Oncogene · doi:10.1038/onc.2016.32 · Cited by 201

Acetylation-regulated interaction between p53 and SET reveals a widespread regulatory mode

Wang, D., Kon, N., Lasso, G., Jiang, L., Leng, W., Zhu, W., Qin, J., Honig, B. H., & Gu, W. J. (2016) · Nature · doi:10.1038/nature19759 · Cited by 198

OTUB1 Co-opts Lys48-Linked Ubiquitin Recognition to Suppress E2 Enzyme Function

Juang, Y.-C. A., Landry, M.-C., Sanches, M., Vittal, V., Leung, C. C. Y., Ceccarelli, D. F. J., Mateo, A.-R. F., Pruneda, J. N., Mao, D. Y. L., Szilard, R. K., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.011 · Cited by 198

Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1

Sun, X., Challagundla, K. B., & Dai, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.434 · Cited by 195

Mechanisms of Resistance to CDK4/6 Inhibitors: Potential Implications and Biomarkers for Clinical Practice

McCartney, A., Migliaccio, I., Bonechi, M., Biagioni, C., Romagnoli, D., Luca, F. D., Galardi, F., Risi, E., Santo, I. D., Benelli, M., et al. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00666 · Cited by 195

Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein

Kalejta, R. F., & Shenk, T. E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0538058100 · Cited by 194

Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53

Rajendra, R., Malegaonkar, D., Pungaliya, P., Marshall, H., Rasheed, Z. A., Brownell, J. E., Liu, L. F., Lutzker, S. G., Saleem, A., & Rubin, E. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400300200 · Cited by 192

Molecular Pathways: Targeting the TGF-β Pathway for Cancer Therapy

Smith, A., Robin, T. P., & Ford, H. L. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-3224 · Cited by 192

Small-molecule RETRA suppresses mutant p53-bearing cancer cells through a p73-dependent salvage pathway

Kravchenko, J. E., Ilyinskaya, G. V., Komarov, P. G., Agapova, L. S., Кочетков, Д. В., Strom, E., Frolova, E. I., Kovriga, I. E., Gudkov, A. V., Feinstein, E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802091105 · Cited by 191

Enhanced Mdm2 activity inhibits pRB function via ubiquitin‐dependent degradation

Uchida, C., Miwa, S., Kitagawa, K., Hattori, T., Isobe, T., Otani, S., Oda, T., Sugimura, H., Kamijo, T., Ookawa, K., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600486 · Cited by 191

Structure, Function, and Aggregation of the Zinc-Free Form of the p53 DNA Binding Domain

Butler, J. S., & Loh, S. N. (2003) · Biochemistry · doi:10.1021/bi026635n · Cited by 190

The C-terminal lysines fine-tune p53 stress responses in a mouse model, but are not required for stability control or transactivation

Krummel, K. A., Lee, C. J., Toledo, F., & Wahl, G. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503068102 · Cited by 187

SnapShot: p53 Posttranslational Modifications

Kruse, J.-P., & Gu, W. J. (2008) · Cell · doi:10.1016/j.cell.2008.05.020 · Cited by 183

BRCA 1, a ‘complex’ protein involved in the maintenance of genomic stability

Savage, K. I., & Harkin, D. P. (2014) · FEBS Journal · doi:10.1111/febs.13150 · Cited by 183

Combined Inhibition of mTOR and CDK4/6 Is Required for Optimal Blockade of E2F Function and Long-term Growth Inhibition in Estrogen Receptor–positive Breast Cancer

Michaloglou, C., Crafter, C., Siersbæk, R., Delpuech, O., Curwen, J., Carnevalli, L. S., Staniszewska, A. D., Polanska, U. M., Cheraghchi-Bashi, A., Lawson, M., et al. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0537 · Cited by 182

PI(3) kinase is associated with a mechanism of immunoresistance in breast and prostate cancer

Crane, C. A., Panner, A., Murray, J. C., Wilson, S. P., Xu, H., Chen, L., Simko, J. P., Waldman, F. M., Pieper, R. O., & Parsa, A. T. (2009) · Oncogene · doi:10.1038/onc.2008.384 · Cited by 181

PTEN-opathies: from biological insights to evidence-based precision medicine

Yehia, L., Ngeow, J. Y. Y., & Eng, C. (2019) · Journal of Clinical Investigation · doi:10.1172/jci121277 · Cited by 178

Cancer and Central Nervous System Tumor Surveillance in Pediatric Neurofibromatosis 1

Evans, D. G., Salvador, H., Chang, V. Y., Erez, A., Voss, S. D., Schneider, K. W., Scott, H. S., Plon, S. E., & Tabori, U. Y. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-0589 · Cited by 178

PI3K-AKT-mTOR and NFκB Pathways in Ovarian Cancer: Implications for Targeted Therapeutics

Ghoneum, A., & Said, N. A. (2019) · Cancers · doi:10.3390/cancers11070949 · Cited by 176

In utero nanoparticle delivery for site-specific genome editing

Ricciardi, A. S., Bahal, R., Farrelly, J. S., Quijano, E., Bianchi, A. H., Luks, V. L., Putman, R., López‐Giráldez, F., Coşkun, S., Song, E., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04894-2 · Cited by 176

GSK-3β-dependent phosphorylation of adenomatous polyposis coli gene product can be modulated by β-catenin and protein phosphatase 2A complexed with Axin

Ikeda, S., Kishida, M., Matsuura, Y., Usui, H., & Kikuchi, A. (2000) · Oncogene · doi:10.1038/sj.onc.1203359 · Cited by 175

Phosphorylation and acetylation modifications of FOXO3a: Independently or synergistically?

Wang, X., Hu, S., & Liu, L. (2017) · Oncology Letters · doi:10.3892/ol.2017.5851 · Cited by 175

Non-canonical functions of the RB protein in cancer

Dick, F. A., Goodrich, D. W., Sage, J., & Dyson, N. J. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0008-5 · Cited by 175

Targeting epigenetics for cancer therapy

Park, J. W., & Han, J. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01126-z · Cited by 171

An RB-EZH2 Complex Mediates Silencing of Repetitive DNA Sequences

Ishak, C. A., Marshall, A. E., Passos, D. T., White, C. R., Kim, S. J., Cecchini, M. J., Ferwati, S., MacDonald, W. A., Howlett, C. J., Welch, I. D., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.10.021 · Cited by 167

Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?

Minde, D., Anvarian, Z., Rüdiger, S., & Maurice, M. M. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-101 · Cited by 166

Reactivation of p53 gene by MDM2 inhibitors: A novel therapy for cancer treatment

Gupta, A., Shah, K., Oza, M. J., & Behl, T. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.10.155 · Cited by 166

CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53

Shi, D., Pop, M. S., Kulikov, R., Love, I. M., Kung, A. L., & Grossman, S. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904305106 · Cited by 165

K29-Selective Ubiquitin Binding Domain Reveals Structural Basis of Specificity and Heterotypic Nature of K29 Polyubiquitin

Kristariyanto, Y. A., Rehman, S. A. A., Campbell, D. G., Morrice, N. A., Johnson, C., Toth, R. L., & Kulathu, Y. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.041 · Cited by 164

Inhibition of Nuclear PTEN Tyrosine Phosphorylation Enhances Glioma Radiation Sensitivity through Attenuated DNA Repair

Ma, J., Benítez, J. A., Li, J., Miki, S., de Albuquerque, C. P., Galatro, T. F. D. A., Orellana, L., Zanca, C., Reed, R., Boyer, A. D., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.020 · Cited by 162

PTEN, DICER1, FH, and Their Associated Tumor Susceptibility Syndromes: Clinical Features, Genetics, and Surveillance Recommendations in Childhood

Schultz, K. A. P., Rednam, S. P., Kamihara, J., Doros, L. A., Achatz, M. I., Wasserman, J. D., Diller, L., Brugières, L., Druker, H. A., Schneider, K. A., et al. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-0629 · Cited by 160

Guadecitabine (SGI-110) in treatment-naive patients with acute myeloid leukaemia: phase 2 results from a multicentre, randomised, phase 1/2 trial

Kantarjian, H. M., Roboz, G. J., Kropf, P. L., Yee, K. W. L., O'Connell, C. L., Tibes, R., Walsh, K. J., Podoltsev, N. A., Griffiths, E. A., Jabbour, E. J., et al. (2017) · The Lancet Oncology · doi:10.1016/s1470-2045(17)30576-4 · Cited by 158

Ser18 and 23 phosphorylation is required for p53‐dependent apoptosis and tumor suppression

Chao, C., Herr, D., Chun, J., & Xu, Y. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601167 · Cited by 158

Fluorescence-Based Sensors to Monitor Localization and Functions of Linear and K63-Linked Ubiquitin Chains in Cells

van Wijk, S. J. L., Fiškin, E., Putyrski, M., Pampaloni, F., Hou, J., Wild, P. S., Kensche, T., Grecco, H. E., Bastiaens, P. I. H., & Đikić, I. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.017 · Cited by 157

Genomic Models of Metastatic Cancer: Functional Analysis of Death-from-Cancer Signature Genes Reveals Aneuploid, Anoikis-Resistant, Metastasis-Enabling Phenotype with Altered Cell Cycle Control and Activated PcG Protein Chromatin Silencing Pathway

Glinsky, G. V. (2006) · Cell Cycle · doi:10.4161/cc.5.11.2796 · Cited by 157

Mechanisms of p53 degradation

Chao, C. C. ‐. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.08.015 · Cited by 155

Unconventional Ways to Live and Die: Cell Death and Survival in Development, Homeostasis, and Disease

Gudipaty, S. A., Conner, C. M., Rosenblatt, J., & Montell, D. J. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100616-060748 · Cited by 150

Post-translational modifications in mitochondria: protein signaling in the powerhouse

Stram, A. R., & Payne, R. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2280-4 · Cited by 149

Regulation of PTEN binding to MAGI-2 by two putative phosphorylation sites at threonine 382 and 383.

Tolkacheva, T., Boddapati, M., Sanfiz, A., Tsuchida, K., Kimmelman, A. C., & Chan, A. M.-L. (2001) · PubMed · Cited by 149

Phosphorylation-induced Conformational Changes in the Retinoblastoma Protein Inhibit E2F Transactivation Domain Binding

Burke, J. R., Deshong, A. J., Pelton, J. G., & Rubin, S. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.108167 · Cited by 148

The amplified WWP1 gene is a potential molecular target in breast cancer

Chen, C., Zhou, Z., Ross, J. S., Zhou, W., & Dong, J. (2007) · International Journal of Cancer · doi:10.1002/ijc.22653 · Cited by 148

E2F-associated chromatin modifiers and cell cycle control

Blais, A., & Dynlacht, B. D. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.10.003 · Cited by 146

ATM Engages Autodegradation of the E3 Ubiquitin Ligase COP1 After DNA Damage

Dornan, D., Shimizu, H., Mah, A. S., Dudhela, T., Eby, M. T., O’Rourke, K. M., Seshagiri, S., & Dixit, V. M. (2006) · Science · doi:10.1126/science.1127335 · Cited by 145

Rapamycin treatment for a child with germline PTEN mutation

Marsh, D. J., Trahair, T. N., Martin, J. L., Chee, W. Y., Walker, J. L., Kirk, E. P., Baxter, R. C., & Marshall, G. M. (2008) · Nature Clinical Practice Oncology · doi:10.1038/ncponc1112 · Cited by 143

Genetics and Epigenetics of Human Retinoblastoma

Benavente, C. A., & Dyer, M. A. (2015) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040259 · Cited by 143

PRMT5 is required for lymphomagenesis triggered by multiple oncogenic drivers

Li, Y., Chitnis, N., Nakagawa, H., Kita, Y., Natsugoe, S., Yang, Y., Li, Z., Wasik, M., Klein-Szanto, A. J. P., Rustgi, A. K., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0625 · Cited by 143

Proapoptotic Function of the Retinoblastoma Tumor Suppressor Protein

Ianari, A., Natale, T., Calo, E., Ferretti, E., Alesse, E., Screpanti, I., Haigis, K. M., Gulino, A., & Lees, J. A. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.01.026 · Cited by 142

JTV1 co‐activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress

Liu, J., Chung, H., Vogt, M., Jin, Y., Malide, D., He, L., Dundr, M., & Levens, D. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.11 · Cited by 141

ROCK1 functions as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability

Vemula, S., Shi, J., Hanneman, P., Wei, L., & Kapur, R. (2009) · Blood · doi:10.1182/blood-2009-08-237222 · Cited by 138

The missing Zinc: p53 misfolding and cancer

Loh, S. N. (2010) · Metallomics · doi:10.1039/c003915b · Cited by 137

A Perturbed Ubiquitin Landscape Distinguishes Between Ubiquitin in Trafficking and in Proteolysis

Ziv, I., Matiuhin, Y., Kirkpatrick, D. S., Erpapazoglou, Z., Sébastien Léon, A., Pantazopoulou, M., Kim, W., Gygi, S. P., Haguenauer‐Tsapis, R., Reis, N., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.009753 · Cited by 137

Role of the ubiquitin–proteasome system in brain ischemia: Friend or foe?

Caldeira, M. V., Salazar, I. L., Curcio, M., Canzoniero, L. M. T., & Duarte, C. B. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.10.003 · Cited by 135

ASPPs and cancer

Trigiante, G., & Lü, X. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1818 · Cited by 135

RASSF tumor suppressor gene family: Biological functions and regulation

Volodko, N. V., Gordon, M., Salla, M., Ghazaleh, H. A., & Baksh, S. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.02.041 · Cited by 135

PARK2 Depletion Connects Energy and Oxidative Stress to PI3K/Akt Activation via PTEN S-Nitrosylation

Gupta, A., Anjomani‐Virmouni, S., Koundouros, N., Dimitriadi, M., Choo-Wing, R., Valle, A., Zheng, Y., Chiu, Y., Agnihotri, S., Zadeh, G. M., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.019 · Cited by 135

Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle controlPreprint

Burke, J. R., Hura, G. L., & Rubin, S. M. (2012) · Genes & Development · doi:10.1101/gad.189837.112 · Cited by 134

MDM2-ARF complex regulates p53 sumoylation

Chen, L., & Chen, J. (2003) · Oncogene · doi:10.1038/sj.onc.1206851 · Cited by 134

The role of genetic abnormalities of PTEN and the phosphatidylinositol 3-kinase pathway in breast and ovarian tumorigenesis, prognosis, and therapy

Mills, G. B., Lu, Y., Fang, X., Wang, H., Eder, A., Mao, M., Swaby, R., Cheng, K. W., Stokoe, D., Siminovitch, K., et al. (2001) · Seminars in Oncology · doi:10.1016/s0093-7754(01)90290-8 · Cited by 133

A HECT Domain E3 Enzyme Assembles Novel Polyubiquitin Chains

You, J., & Pickart, C. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100034200 · Cited by 130

Stress-Activated NRF2-MDM2 Cascade Controls Neoplastic Progression in Pancreas

Todoric, J., Antonucci, L., Caro, G. D., Li, N., Wu, X., Lytle, N. K., Dhar, D., Banerjee, S., Fagman, J. B., Browne, C. D., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.10.011 · Cited by 129

Human p53 Is Phosphorylated on Serines 6 and 9 in Response to DNA Damage-inducing Agents

Higashimoto, Y., Saito, S., Tong, X., Hong, A. L., Sakaguchi, K., Appella, E., & Anderson, C. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002674200 · Cited by 128

The role of ubiquitination and deubiquitination in the regulation of cell junctions

Cai, J., Culley, M. K., Zhao, Y., & Zhao, J. (2017) · Protein & Cell · doi:10.1007/s13238-017-0486-3 · Cited by 127

Inositol Pyrophosphates Mediate the DNA-PK/ATM-p53 Cell Death Pathway by Regulating CK2 Phosphorylation of Tti1/Tel2

Rao, F., Cha, J., Xu, J., Xu, R., Vandiver, M. S., Tyagi, R., Tokhunts, R. A., Koldobskiy, M. A., Fu, C., Barrow, R. K., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.020 · Cited by 126

Roles of the functional loss of p53 and other genes in astrocytoma tumorigenesis and progression

Nozaki, M., Tada, M., Kobayashi, H., Zhang, C. L., Sawamura, Y., Abe, H., Ishii, N., & Meir, E. G. V. (1999) · Neuro-Oncology · doi:10.1093/neuonc/1.2.124 · Cited by 126

Ubiquitin E3 ligase WWP1 as an oncogenic factor in human prostate cancer

Chen, C., Sun, X., Guo, P., Dong, X. Y., Sethi, P., Zhou, W., Zhou, Z., Petros, J. A., Hf, F., Rl, V., et al. (2006) · Oncogene · doi:10.1038/sj.onc.1210021 · Cited by 126

Lysine methylation regulates the pRb tumour suppressor protein

Munro, S., Khaire, N., Inche, A. G., Carr, S. M., & Thangue, N. B. L. (2010) · Oncogene · doi:10.1038/onc.2009.511 · Cited by 124

A Code of Mono-phosphorylation Modulates the Function of RB

Sanidas, I., Morris, R. T., Fella, K. A., Rumde, P. H., Boukhali, M., Tai, E. C., Ting, D. T., Lawrence, M. S., Haas, W., & Dyson, N. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.004 · Cited by 124

Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23

MacPherson, D., Kim, J., Kim, T., Rhee, B. K., van Oostrom, C. T., DiTullio, R. A., Venere, M., Halazonetis, T. D., Bronson, R., de Vries, A., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600363 · Cited by 124

Overexpression of MDM2, due to enhanced translation, results in inactivation of wild-type p53 in Burkitt's lymphoma cells

Métay, C., Paillerets, B. B., Lefrère, I., Ronsin, M., Feunteun, J., Tursz, T., & Wiels, J. (1998) · Oncogene · doi:10.1038/sj.onc.1201702 · Cited by 123

Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chainsPreprint

Tran, H., Hamada, F., Schwarz, T., & Bienz, M. (2008) · Genes & Development · doi:10.1101/gad.463208 · Cited by 122

LKB1 interacts with and phosphorylates PTEN: a functional link between two proteins involved in cancer predisposing syndromes

Mehenni, H., Lin-Marq, N., Buchet-Poyau, K., Reymond, A., Collart, M. A., Picard, D., & Antonarakis, S. E. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi225 · Cited by 122

RB localizes to DNA double-strand breaks and promotes DNA end resection and homologous recombination through the recruitment of BRG1Preprint

Vélez-Cruz, R., Manickavinayaham, S., Biswas, A., Clary, R. W., Premkumar, T., Cole, F., & Johnson, D. G. (2016) · Genes & Development · doi:10.1101/gad.288282.116 · Cited by 122

Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth

McDonald, E. R., & El‐Deiry, W. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307459101 · Cited by 121

Increased Sensitivity to UV Radiation in Mice with a p53 Point Mutation at Ser389

Bruins, W., Zwart, E., Attardi, L. D., Iwakuma, T., Hoogervorst, E. M., Beems, R. B., Miranda, B., van Oostrom, C. T. M., van den Berg, J., van den Aardweg, G. J., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8884-8894.2004 · Cited by 121

Mutant p53 targeting by the low molecular weight compound STIMA‐1

Zache, N., Lambert, J. M. R., Rökaeus, N., Shen, J., Hainaut, P. L., Bergman, J., Wiman, K. G., & Bykov, V. J. N. (2008) · Molecular Oncology · doi:10.1016/j.molonc.2008.02.004 · Cited by 120

UBE4B promotes Hdm2-mediated degradation of the tumor suppressor p53

Wu, H., Pomeroy, S. L., Ferreira, M., Teider, N., Mariani, J., Nakayama, K. I., Hatakeyama, S., Tron, V. A., Saltibus, L. F., Spyracopoulos, L., et al. (2011) · Nature Medicine · doi:10.1038/nm.2283 · Cited by 120

Ser46 Phosphorylation Regulates p53-Dependent Apoptosis and Replicative Senescence

Feng, L., Hollstein, M., & Xu, Y. (2006) · Cell Cycle · doi:10.4161/cc.5.23.3526 · Cited by 119

Protective mechanisms of p53-p21-pRb proteins against DNA damage-induced cell death

Garner, E., & Raj, K. (2008) · Cell Cycle · doi:10.4161/cc.7.3.5328 · Cited by 119

Acetylation of Mouse p53 at Lysine 317 Negatively Regulates p53 Apoptotic Activities after DNA Damage

Chao, C., Wu, Z., Mazur, S. J., Borges, H. L., Rossi, M., Lin, T., Wang, J. Y. J., Anderson, C. W., Appella, E., & Xu, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00062-06 · Cited by 119

Physiological, Pathological, and Targetable Membraneless Organelles in Neurons

Ryan, V. H., & Fawzi, N. L. (2019) · Trends in Neurosciences · doi:10.1016/j.tins.2019.08.005 · Cited by 119

CREBBP and p300 lysine acetyl transferases in the DNA damage response

Dutto, I., Scalera, C., & Prosperi, E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2717-4 · Cited by 118

Restoring p53 active conformation by zinc increases the response of mutant p53 tumor cells to anticancer drugs

Puca, R., Nardinocchi, L., Porru, M., Simon, A. J., Rechavi, G., Leonetti, C., Givol, D., & D’Orazi, G. (2011) · Cell Cycle · doi:10.4161/cc.10.10.15642 · Cited by 117

Interplay between lysine methylation and Cdk phosphorylation in growth control by the retinoblastoma protein

Carr, S. M., Munro, S., Kessler, B. M., Oppermann, U. C. T., & Thangue, N. B. L. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.311 · Cited by 115

Functional interplay between p53 and E2F through co-activator p300

Lee, C., Sørensen, T. S., Shikama, N., & Thangue, N. B. L. (1998) · Oncogene · doi:10.1038/sj.onc.1201818 · Cited by 115

Abemaciclib, a Selective CDK4/6 Inhibitor, Enhances the Radiosensitivity of Non–Small Cell Lung Cancer In Vitro and In Vivo

Naz, S., Sowers, A. L., Choudhuri, R., Wissler, M. F., Gamson, J., Mathias, A., Cook, J. A., & Mitchell, J. B. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3575 · Cited by 113

Targeting tumor suppressor genes for cancer therapy

Liu, Y., Hu, X., Han, C., Wang, L., Zhang, X., He, X., & Lu, X. (2015) · BioEssays · doi:10.1002/bies.201500093 · Cited by 112

Skp2-Dependent Ubiquitination and Activation of LKB1 Is Essential for Cancer Cell Survival under Energy Stress

Lee, S.-W., Li, C., Jin, G., Cai, Z., Han, F., Chan, C., Yang, W., Li, B., Rezaeian, A. H., Li, H., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.015 · Cited by 112

p53 stability is regulated by diverse deubiquitinating enzymes

Kwon, S., Saindane, M., & Baek, K. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.08.001 · Cited by 112

MDM2 antagonists as a novel treatment option for acute myeloid leukemia: perspectives on the therapeutic potential of idasanutlin (RG7388)

Khurana, A., & Shafer, D. A. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s172315 · Cited by 111

Tumour suppressor genes in chemotherapeutic drug response

Lai, D., Grieve, S., & Yang, X. (2012) · Bioscience Reports · doi:10.1042/bsr20110125 · Cited by 110

Modulation of the p53/MDM2 interplay by HAUSP inhibitors

Tavana, O., & Gu, W. J. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw049 · Cited by 110

To the edge of cell death and back

Gong, Y., Crawford, J. C., Heckmann, B. L., & Green, D. R. (2018) · FEBS Journal · doi:10.1111/febs.14714 · Cited by 110

Lenalidomide promotes p53 degradation by inhibiting MDM2 auto-ubiquitination in myelodysplastic syndrome with chromosome 5q deletion

Wei, S., Chen, X., McGraw, K. L., Zhang, L., Komrokji, R. S., Clark, J., Cáceres, G., Billingsley, D., Sokol, L., Lancet, J. E., et al. (2012) · Oncogene · doi:10.1038/onc.2012.139 · Cited by 109

Haplo-insufficiency? Let me count the ways: Figure 1.Preprint

Quon, K. C., & Berns, A. J. M. (2001) · Genes & Development · doi:10.1101/gad.949001 · Cited by 109

Live-cell p53 single-molecule binding is modulated by C-terminal acetylation and correlates with transcriptional activity

Loffreda, A., Jacchetti, E., Antunes, S., Rainone, P., Daniele, T., Morisaki, T., Bianchi, M. E., Tacchetti, C., & Mazza, D. (2017) · Nature Communications · doi:10.1038/s41467-017-00398-7 · Cited by 109

PP1 and PP2A phosphatases – cooperating partners in modulating retinoblastoma protein activation

KOLUPAEVA, V. G., & Janssens, V. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08511.x · Cited by 107

Synoviolin, protein folding and the maintenance of joint homeostasis

Yagishita, N., Yamasaki, S., Nishioka, K., & Nakajima, T. (2008) · Nature Clinical Practice Rheumatology · doi:10.1038/ncprheum0699 · Cited by 106

SCH529074, a Small Molecule Activator of Mutant p53, Which Binds p53 DNA Binding Domain (DBD), Restores Growth-suppressive Function to Mutant p53 and Interrupts HDM2-mediated Ubiquitination of Wild Type p53

Demma, M. J., Maxwell, E., Ramos, R., Liang, L., Li, C., Hesk, D., Rossman, R. R., Mallams, A. K., Doll, R. J., Liu, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083469 · Cited by 105

Chromatin Remodeling Factor LSH Drives Cancer Progression by Suppressing the Activity of Fumarate Hydratase

He, X., Yan, B., Liu, S., Jia, J., Lai, W., Xing, X., Tang, C., Luo, D., Tan, T., Jiang, Y., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0268 · Cited by 105

Accommodating haploinsufficient tumour suppressor genes in Knudson's model

Cook, W. D., & McCaw, B. J. (2000) · Oncogene · doi:10.1038/sj.onc.1203653 · Cited by 104

The Tumor Suppressor PALB2: Inside Out

Ducy, M., Sesma-Sanz, L., Guitton-Sert, L., Lashgari, A., Gao, Y., Brahiti, N., Rodrigue, A., Margaillan, G., Caron, M., Côté, J., et al. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.10.008 · Cited by 104

TRIM24 Is a p53-Induced E3-Ubiquitin Ligase That Undergoes ATM-Mediated Phosphorylation and Autodegradation during DNA Damage

Jain, A. K., Allton, K. L., Duncan, A. D., & Barton, M. C. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01705-12 · Cited by 103

Post-translational Modifications of Key Machinery in the Control of Mitophagy

Wang, L., Qi, H., Tang, Y., & Shen, H. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.08.002 · Cited by 102

Regulation of p53 Localization and Activity by Ubc13

Laine, A. M., Topisirović, I., Zhai, D., Reed, J. C., Borden, K. L. B., & Ronai, Z. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01156-06 · Cited by 101

The Biology of Retinoblastoma

Mendoza, P. R., & Grossniklaus, H. E. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.06.012 · Cited by 101

The Next Phase of Human Gene-Therapy Oversight

Collins, F. S., & Gottlieb, S. L. (2018) · New England Journal of Medicine · doi:10.1056/nejmp1810628 · Cited by 98

The N-Terminal Phosphorylation of RB by p38 Bypasses Its Inactivation by CDKs and Prevents Proliferation in Cancer Cells

Gubern, A., Joaquin, M., Marqués, M., Maseres, P., Garcı́a-Garcı́a, J., Amat, R., González-Nuñez, D., Oliva, B., Real, F. X., de Nadal, E., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.015 · Cited by 96

BAI1 Suppresses Medulloblastoma Formation by Protecting p53 from Mdm2-Mediated Degradation

Zhu, D., Osuka, S., Zhang, Z., Reichert, Z. R., Yang, L., Kanemura, Y., Jiang, Y., You, S., Zhang, H., Devi, N. S., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.05.006 · Cited by 96

PI3K/mTOR Pathway Inhibition: Opportunities in Oncology and Rare Genetic Diseases

Hillmann, P., & Fabbro, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225792 · Cited by 96

TP53 Mutation and Its Prognostic Significance in Waldenstrom's Macroglobulinemia

Poulain, S., Roumier, C., Bertrand, E., Renneville, A., Caillault, A., Doye, E., Geffroy, S., Sebda, S., Nibourel, O., Nudel, M., et al. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-0007 · Cited by 96

BRCA1 and BRCA2 mutations and the risk for colorectal cancer

Sopik, V., Phelan, C., Cybulski, C., & Narod, S. A. (2014) · Clinical Genetics · doi:10.1111/cge.12497 · Cited by 95

Cancer genes associated with phenotypes in monoallelic and biallelic mutation carriers: new lessons from old players

Rahman, N., & Scott, R. H. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm026 · Cited by 95

Curcumin Reactivates Silenced Tumor Suppressor Gene RARβ by Reducing DNA Methylation

Jiang, A., Wang, X., Shan, X., Li, Y., Wang, P., Jiang, P., & Feng, Q. (2015) · Phytotherapy Research · doi:10.1002/ptr.5373 · Cited by 94

Diversity within the pRb pathway: is there a code of conduct?

Munro, S., Carr, S. M., & Thangue, N. B. L. (2012) · Oncogene · doi:10.1038/onc.2011.603 · Cited by 93

In vivo analysis of p53 tumor suppressor function using genetically engineered mouse models

Brož, D. K., & Attardi, L. D. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp331 · Cited by 92

Conditional RNA interference in vivo to study mutant p53 oncogenic gain of function on tumor malignancy

Bossi, G., Marampon, F., Maor-Aloni, R., ZANI, B. M., Rotter, V., Oren, M., Strano, S., Blandino, G., & Sacchi, A. (2008) · Cell Cycle · doi:10.4161/cc.7.12.6161 · Cited by 92

Protein arginine methylation: an emerging regulator of the cell cycle

Raposo, A. E., & Piller, S. C. (2018) · Cell Division · doi:10.1186/s13008-018-0036-2 · Cited by 91

Palbociclib plus endocrine therapy in older women with HR+/HER2– advanced breast cancer: a pooled analysis of randomised PALOMA clinical studies

Rugo, H. S., Turner, N. C., Finn, R. S., Joy, A. A., Verma, S., Harbeck, N., Masuda, N., Im, S., Huang, X., Kim, S., et al. (2018) · European Journal of Cancer · doi:10.1016/j.ejca.2018.05.017 · Cited by 91

A PALB2-interacting domain in RNF168 couples homologous recombination to DNA break-induced chromatin ubiquitylation

Luijsterburg, M. S., Typas, D., Caron, M., Wiegant, W. W., van den Heuvel, D., Boonen, R. A. C. M., Couturier, A. M., Mullenders, L. H. F., Masson, J., & van Attikum, H. (2017) · eLife · doi:10.7554/elife.20922 · Cited by 91

Targeting MDM2 for novel molecular therapy: Beyond oncology

Wang, W., Qin, J., Rajaei, M., Li, X., Yu, X., Hunt, C., & Zhang, R. (2019) · Medicinal Research Reviews · doi:10.1002/med.21637 · Cited by 90

Oncogenes and tumor suppressor genes: comparative genomics and network perspectives

Zhu, K., Liu, Q., Zhou, Y., Tao, C., Zhao, Z., Sun, J., & Xu, H. (2015) · BMC Genomics · doi:10.1186/1471-2164-16-s7-s8 · Cited by 89

Plk1-mediated Phosphorylation of Topors Regulates p53 Stability

Yang, X., Li, H., Zhou, Z., Wang, W., Deng, A., ANDRISANI, O. M., & Liu, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.001560 · Cited by 89

Acetylation of the DNA Binding Domain Regulates Transcription-independent Apoptosis by p53

Sykes, S. M., Stanek, T. J., Frank, A. K., Murphy, M. E., & McMahon, S. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026096 · Cited by 88

The Methyltransferase Set7/9 (Setd7) Is Dispensable for the p53-Mediated DNA Damage Response In Vivo

Campaner, S., Spreafico, F., Burgold, T., Doni, M., Rosato, U., Amati, B. B., & Testa, G. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.007 · Cited by 88

CARPs Are Ubiquitin Ligases That Promote MDM2-independent p53 and Phospho-p53ser20 Degradation

Yang, W., Rozan, L. M., McDonald, E. R., Navaraj, A., Liu, J. J., Matthew, E. M., Wang, W., Dicker, D. T., & El‐Deiry, W. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610793200 · Cited by 88

Stabilization of LKB1 and Akt by neddylation regulates energy metabolism in liver cancer

Barbier‐Torres, L., Delgado, T. C., García‐Rodríguez, J. L., Zubiete‐Franco, I., Fernández‐Ramos, D., Buqué, X., Cano, A., Juan, V. G., Fernández-Domínguez, I., Lopitz‐Otsoa, F., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.3191 · Cited by 87

New developments in the genetics and pathogenesis of tumours in tuberous sclerosis complex

Lam, H. C., Nijmeh, J., & Henske, E. P. (2016) · The Journal of Pathology · doi:10.1002/path.4827 · Cited by 86

Deregulation and Targeting of TP53 Pathway in Multiple Myeloma

Jovanović, K., Escure, G., Demonchy, J., Willaume, A., de Wyngaert, Z. V., Farhat, M.-M., Chauvet, P., Facon, T. T. F., Quesnel, B., & Manier, S. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2018.00665 · Cited by 86

PTEN in Colorectal Cancer: Shedding Light on Its Role as Predictor and Target

Salvatore, L., Calegari, M. A., Loupakis, F., Fassan, M., Stefano, B. D., Bensi, M., Bria, E., & Tortora, G. (2019) · Cancers · doi:10.3390/cancers11111765 · Cited by 86

Adult B-cell acute lymphoblastic leukemia cells display decreased PTEN activity and constitutive hyperactivation of PI3K/Akt pathway despite high PTEN protein levels

Gomes, A. M., Soares, M. V. D., Ribeiro, P. R., Caldas, J., Póvoa, V., Martins, L. R., Melão, A., Serra‐Caetano, A., Sousa, A. B., de Lacerda, J. F., et al. (2014) · Haematologica · doi:10.3324/haematol.2013.096438 · Cited by 86

Oncogene-induced senescence mediated by c-Myc requires USP10 dependent deubiquitination and stabilization of p14ARF

Ko, A., Han, S. Y., Choi, C. H., Cho, H., Lee, M.-S., Kim, S., Song, J. S., Hong, K., Lee, H., Hewitt, S. M., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0072-0 · Cited by 85

Prevalence and Prognostic Significance of PTEN Loss in African-American and European-American Men Undergoing Radical Prostatectomy

Tosoian, J. J., Almutairi, F., Morais, C. L., Glavaris, S. A., Hicks, J. L., Sundi, D., Humphreys, E. B., Han, M., Marzo, A. M. D., Ross, A. E., et al. (2016) · European Urology · doi:10.1016/j.eururo.2016.07.026 · Cited by 85

In vitro efficacy of ARQ 092, an allosteric AKT inhibitor, on primary fibroblast cells derived from patients with PIK3CA-related overgrowth spectrum (PROS)

Ranieri, C., Tommaso, S. D., Loconte, D. C., Grossi, V., Sanese, P., Bagnulo, R., Susca, F. C., Forte, G., Peserico, A., Luisi, A. D., et al. (2018) · Neurogenetics · doi:10.1007/s10048-018-0540-1 · Cited by 85

RB constrains lineage fidelity and multiple stages of tumour progression and metastasis

Walter, D. M., Yates, T. J., Ruiz-Torres, M., Kim-Kiselak, C., Gudiel, A. A., Deshpande, C. G., Wang, W., Cicchini, M., Stokes, K. L., Tobias, J. W., et al. (2019) · Nature · doi:10.1038/s41586-019-1172-9 · Cited by 84

Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein

Haluska, P. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.12.2538 · Cited by 84

p53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1

Santiago, A., Li, D., Zhao, L., Godsey, A. C., & Liao, D. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0771 · Cited by 83

Regulation of p53 family members by the ubiquitin-like SUMO system

Stehmeier, P., & Muller, S. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.002 · Cited by 83

The Oncoprotein Gankyrin Negatively Regulates Both p53 and RB by Enhancing Proteasomal Degradation

Higashitsuji, H., Liu, Y., Mayer, R. J., & Fujita, J. (2005) · Cell Cycle · doi:10.4161/cc.4.10.2107 · Cited by 82

Molecular and Functional Characterization of Three Different Postzygotic Mutations in PIK3CA-Related Overgrowth Spectrum (PROS) Patients: Effects on PI3K/AKT/mTOR Signaling and Sensitivity to PIK3 Inhibitors

Loconte, D. C., Grossi, V., Bozzao, C., Forte, G., Bagnulo, R., Stella, A., Lastella, P., Cutrone, M., Benedicenti, F., Susca, F. C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123092 · Cited by 82

The ARF tumour suppressor

Gallagher, S. J., Kefford, R. F., & Rizos, H. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.02.008 · Cited by 81

Crystal Structure of the Retinoblastoma Protein N Domain Provides Insight into Tumor Suppression, Ligand Interaction, and Holoprotein Architecture

Hassler, M., Singh, S., Yue, W. W., Luczynski, M. T., Lakbir, R., Sánchez‐Sánchez, F., Bader, T., Pearl, L. H., & Mittnacht, S. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.023 · Cited by 81

Haploinsufficiency of an RB–E2F1–Condensin II Complex Leads to Aberrant Replication and Aneuploidy

Coschi, C. H., Ishak, C. A., Gallo, D., Marshall, A. E., Talluri, S., Wang, J., Cecchini, M. J., Martens, A. L., Percy, V., Welch, I. D., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0215 · Cited by 81

Androgen induces G3BP2 and SUMO-mediated p53 nuclear export in prostate cancer

Ashikari, D., Takayama, K., Tanaka, T., Suzuki, Y., Obinata, D., Fujimura, T., Urano, T., Takahashi, S., & Inoue, S. (2017) · Oncogene · doi:10.1038/onc.2017.225 · Cited by 80

Identification of CDC25 as a Common Therapeutic Target for Triple-Negative Breast Cancer

Liu, J. C., Granieri, L., Shrestha, M., Wang, D., Vorobieva, I., Rubie, E. A., Jones, R. A., Ju, Y., Pellecchia, G., Jiang, Z., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.039 · Cited by 80

The C terminus of p53 regulates gene expression by multiple mechanisms in a target- and tissue-specific manner in vivoPreprint

Hamard, P.-J., Barthelery, N. J., Hogstad, B., Mungamuri, S. K., Tonnessen-Murray, C. A., Carvajal, L. A., Senturk, E., Gillespie, V., Aaronson, S. A., Mérad, M., et al. (2013) · Genes & Development · doi:10.1101/gad.224386.113 · Cited by 79

Tumor suppressor genes and their underlying interactions in paclitaxel resistance in cancer therapy

Xu, J., Hu, S., Shen, G., & Shen, G. (2016) · Cancer Cell International · doi:10.1186/s12935-016-0290-9 · Cited by 79

CDK4/6 inhibitors in breast cancer therapy: Current practice and future opportunities

Lynce, F. C., Shajahan‐Haq, A. N., & Swain, S. M. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.06.008 · Cited by 79

Roles of HAUSP-mediated p53 regulation in central nervous system development

Kon, N., Zhong, J., Kobayashi, Y., Li, M., Szabolcs, M., Ludwig, T., Canoll, P. D., & Gu, W. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.12 · Cited by 79

Bacterial CagA protein induces degradation of p53 protein in a p14ARF-dependent manner

Wei, J., Noto, J. M., Zaika, E. I., Romero–Gallo, J., Piazuelo, M. B., Schneider, B., El-Rifai, W. M., Correa, P., Peek, R. M., & Zaika, A. I. (2014) · Gut · doi:10.1136/gutjnl-2014-307295 · Cited by 76

E2F1 promotes the recruitment of DNA repair factors to sites of DNA double-strand breaks

Chen, J., Zhu, F., Weaks, R. L., Biswas, A., Guo, R. R., Li, Y., & Johnson, D. G. (2011) · Cell Cycle · doi:10.4161/cc.10.8.15341 · Cited by 76

Controlling the master—upstream regulation of the tumor suppressor LKB1

Kullmann, L., & Krahn, M. P. (2018) · Oncogene · doi:10.1038/s41388-018-0145-z · Cited by 75

Immune dysregulation in patients with PTEN hamartoma tumor syndrome: Analysis of FOXP3 regulatory T cells

Chen, H. H., Händel, N., Ngeow, J. Y. Y., Muller, J., Hühn, M. H., Yang, H.-T., Heindl, M., Berbers, R.-M., Hegazy, A. N., Kionke, J., et al. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.03.059 · Cited by 75

Palbociclib in combination with letrozole in patients with estrogen receptor–positive, human epidermal growth factor receptor 2–negative advanced breast cancer: PALOMA-2 subgroup analysis of Japanese patients

Mukai, H., Shimizu, C., Masuda, N., Ohtani, S., Ohno, S., Takahashi, M., Yamamoto, Y., Nishimura, R., Sato, N., Ohsumi, S., et al. (2018) · International Journal of Clinical Oncology · doi:10.1007/s10147-018-1353-9 · Cited by 74

Novel functional PI 3‐kinase antagonists inhibit cell growth and tumorigenicity in human cancer cell lines

Razzini, G., Berrie, C. P., Vignati, S., Broggini, M., Mascetta, G., Brancaccio, A., & Falasca, M. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.9.1179 · Cited by 74

Critical Role of PICT-1, a Tumor Suppressor Candidate, in Phosphatidylinositol 3,4,5-Trisphosphate Signals and Tumorigenic Transformation

Okahara, F., Itoh, K., Nakagawara, A., Murakami, M., Kanaho, Y., & Maehama, T. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-04-0301 · Cited by 74

Auto-ubiquitination of Mdm2 Enhances Its Substrate Ubiquitin Ligase Activity

Ranaweera, R. S., & Yang, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.454470 · Cited by 73

Ubiquitin, SUMO, and NEDD8: Key Targets of Bacterial Pathogens

Ribet, D., & Cossart, P. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.07.005 · Cited by 73

OTUB1 de-ubiquitinating enzyme promotes prostate cancer cell invasion in vitro and tumorigenesis in vivo

Iglesias‐Gato, D., Chuan, Y.-C., Jiang, N., Svensson, C., Bao, J., Paul, I., Egevad, L., Kessler, B. M., Wikström, P., Niu, Y., et al. (2015) · Molecular Cancer · doi:10.1186/s12943-014-0280-2 · Cited by 70

The Ataxia Telangiectasia–Mutated Target Site Ser18 Is Required for p53-Mediated Tumor Suppression

Armata, H. L., Garlick, D. S., & Sluss, H. K. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1610 · Cited by 69

USP14 regulates DNA damage repair by targeting RNF168-dependent ubiquitination

Sharma, A., Alswillah, T., Singh, K., Chatterjee, P., Willard, B., Venere, M., Summers, M. K., & Almasan, A. (2018) · Autophagy · doi:10.1080/15548627.2018.1496877 · Cited by 69

Regulation of the p53 Family Proteins by the Ubiquitin Proteasomal Pathway

Bang, S., Kaur, S., & Kurokawa, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010261 · Cited by 69

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Jain, A. K., & Barton, M. C. (2009) · Cell Cycle · doi:10.4161/cc.8.22.9979 · Cited by 68

Exosome-dependent immune surveillance at the metastatic niche requires BAG6 and CBP/p300-dependent acetylation of p53

Schuldner, M., Dörsam, B., Shatnyeva, O., Reiners, K. S., Kubarenko, A. V., Hansen, H. P., Finkernagel, F., Roth, K. S., Theurich, S., Nist, A., et al. (2019) · Theranostics · doi:10.7150/thno.36378 · Cited by 68

Functional evolution of the p53 regulatory network through its target response elements

Jegga, A. G., Inga, A., Menéndez, D., Aronow, B. J., & Resnick, M. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704694105 · Cited by 67

p53 status in the primary tumor predicts efficacy of subsequent abiraterone and enzalutamide in castration-resistant prostate cancer

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Cell Fate Regulation upon DNA Damage: p53 Serine 46 Kinases Pave the Cell Death Road

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Repression of AKT signaling by ARQ 092 in cells and tissues from patients with Proteus syndrome

Lindhurst, M. J., Yourick, M. R., Yu, Y., Savage, R. E., Ferrari, D., & Biesecker, L. G. (2015) · Scientific Reports · doi:10.1038/srep17162 · Cited by 67

USP2a Protein Deubiquitinates and Stabilizes the Circadian Protein CRY1 in Response to Inflammatory Signals

Tong, X., Buelow, K. L., Guha, A., Rausch, R., & Yin, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.340786 · Cited by 66

Decitabine in the treatment of myelodysplastic syndromes

Santos, F. P., Kantarjian, H. M., Garcia‐Manero, G., Issa, J. J., & Ravandi, F. (2009) · Expert Review of Anticancer Therapy · doi:10.1586/era.09.164 · Cited by 66

Thiosemicarbazones Functioning as Zinc Metallochaperones to Reactivate Mutant p53

Yu, X., Blanden, A. R., Tsang, A. T., Zaman, S., Liu, Y., Gilleran, J., Bencivenga, A. F., Kimball, S. D., Loh, S. N., & Carpizo, D. R. (2017) · Molecular Pharmacology · doi:10.1124/mol.116.107409 · Cited by 66

Origin and Function of Avian Retrovirus Transforming GenesPreprint

Bishop, J. M., Courtneidge, S. A., Levinson, A. D., Oppermann, H., Quintrell, N. A., Sheiness, D. K., Weiss, S. R., & Varmus, H. E. (1980) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1980.044.01.099 · Cited by 66

Illuminating p53 function in cancer with genetically engineered mouse models

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PHD3 Regulates p53 Protein Stability by Hydroxylating Proline 359

Rodríguez, J., Herrero, A., Li, S., Rauch, N., Quintanilla, A., Wynne, K. J., Krstić, A., Acosta, J. C., Taylor, C. T., Schlisio, S., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.108 · Cited by 64

Sirolimus treatment of severe PTEN hamartoma tumor syndrome: case report and in vitro studies

Schmid, G. L., Kaßner, F., Uhlig, H. H., Körner, A., Kratzsch, J., Händel, N., Zepp, F., Kowalzik, F., Laner, A., Starke, S., et al. (2013) · Pediatric Research · doi:10.1038/pr.2013.246 · Cited by 64

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Levine, A. J., & Berger, S. L. (2017) · Genes & Development · doi:10.1101/gad.298984.117 · Cited by 63

Chromatin Remodeling Factor LSH is Upregulated by the LRP6-GSK3β-E2F1 Axis Linking Reversely with Survival in Gliomas

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Post-translational modifications of tight junction transmembrane proteins and their direct effect on barrier function

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DNA‐damage‐responsive acetylation of pRb regulates binding to E2F‐1

Markham, D., Munro, S., Soloway, J., O'Connor, D. P., & La Thangue, N. B. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400591 · Cited by 62

Posttranslational regulation of phosphatase and tensin homolog (PTEN) and its functional impact on cancer behaviors

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UBE4B, a ubiquitin chain assembly factor, is required for MDM2-mediated p53 polyubiquitination and degradation

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Plk1 Protein Phosphorylates Phosphatase and Tensin Homolog (PTEN) and Regulates Its Mitotic Activity during the Cell Cycle

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DNA Damage Signals through Differentially Modified E2F1 Molecules To Induce Apoptosis

Carnevale, J., Palander, O., Seifried, L. A., & Dick, F. A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.06286-11 · Cited by 59

HAUSP , a novel deubiquitinase for Rb – MDM 2 the critical regulator

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PIASy-mediated Tip60 sumoylation regulates p53-induced autophagy

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Identification of TRIML2, a Novel p53 Target, that Enhances p53 SUMOylation and Regulates the Transactivation of Proapoptotic Genes

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Targeting p53 pathways: mechanisms, structures, and advances in therapy

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p53 signaling in cancer progression and therapy

Marei, H. E. S., Thani, A. A. A., Afifi, N. M., Hasan, A., Caceci, T., Pozzoli, G., Morrione, A., Giordano, A., & Cenciarelli, C. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02396-8 · Cited by 628

Mutant p53 in cancer: from molecular mechanism to therapeutic modulation

Chen, X., Zhang, T., Su, W., Dou, Z., Zhao, D., Jin, X., Lei, H., Wang, J., Xie, X., Cheng, B., et al. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05408-1 · Cited by 494

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

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Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response

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Post-translational modifications on the retinoblastoma protein

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Role of post-translational modifications in regulation of tumor suppressor p53 function

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Posttranslational regulation of phosphatase and tensin homolog (PTEN) and its functional impact on cancer behaviors

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Posttranslational Modifications of the Retinoblastoma Tumor Suppressor Protein as Determinants of Function

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p53: The Multifaceted Roles of Covalent Modifications in Cancer

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