Regulating tumor suppressor genes: post-translational modifications
Open accessAbstract
Tumor suppressor genes cooperate with each other in tumors. Three important tumor suppressor proteins, retinoblastoma (Rb), p53, phosphatase, and tensin homolog deleted on chromosome ten (PTEN) are functionally associated and they regulated by post-translational modification (PTMs) as well. PTMs include phosphorylation, SUMOylation, acetylation, and other novel modifications becoming growing appreciated. Because most of PTMs are reversible, normal cells use them as a switch to control the state of cells being the resting or proliferating, and PTMs also involve in cell survival and cell cycle, which may lead to abnormal proliferation and tumorigenesis. Although a lot of studies focus on the importance of each kind of PTM, further discoveries shows that tumor suppressor genes (TSGs) form a complex “network” by the interaction of modification. Recently, there are several promising strategies for TSGs for they change more frequently than carcinogenic genes in cancers. We here review the necessity, characteristics, and mechanisms of each kind of post-translational modification on Rb, p53, PTEN, and its influence on the precise and selective function. We also discuss the current antitumoral therapies of Rb, p53 and PTEN as predictive, prognostic, and therapeutic target in cancer.
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PTMs are known to function as molecular switches by affecting protein-protein interactions.
“PTMs are known to function as molecular switches by affecting protein-protein interactions (Chen, Liu et al., 2020, Nishi, Hashimoto et al., 2011).”
From SHARPIN S146 phosphorylation mediates ARP2/3 interaction, cancer cell invasion and metastasis (2022) · cites this paper as Chen, Liu et al., 2020
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1 retracted
Song, P., Wu, Y., Xu, J., Xie, Z., Dong, Y., Zhang, M., & Zou, M. (2007) · Circulation · doi:10.1161/circulationaha.107.716498 · Cited by 143 · see citing works
RetractedHershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018 · see citing works
Comprehensive genomic characterization defines human glioblastoma genes and core pathways
The Cancer Genome Atlas Research Network (2008) · Nature · doi:10.1038/nature07385 · Cited by 7,735 · see citing works
p53, the cellular gatekeeper for growth and division
Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693 · see citing works
Mutation and cancer: statistical study of retinoblastoma
Knudson, A. G. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.4.820 · Cited by 7,612 · see citing works
Nowell, P. C. (1976) · Science · doi:10.1126/science.959840 · Cited by 6,471 · see citing works
AKT/PKB signaling: navigating downstream
Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115 · see citing works
An Integrated Genomic Analysis of Human Glioblastoma Multiforme
Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857 · see citing works
The retinoblastoma protein and cell cycle control
Weinberg, R. A. (1995) · Cell · doi:10.1016/0092-8674(95)90385-2 · Cited by 4,862 · see citing works
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661 · see citing works
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506 · see citing works
Integrative Genomic Profiling of Human Prostate Cancer
Taylor, B. S., Schultz, N. D., Hieronymus, H., Gopalan, A., Xiao, Y., Carver, B. S., Arora, V. K., Kaushik, P., Cerami, E. G., Reva, B. A., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.05.026 · Cited by 3,653 · see citing works
Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
Olsen, J. V., Blagoev, B., Gnad, F., Maček, B., Kumar, C., Mortensen, P., & Mann, M. (2006) · Cell · doi:10.1016/j.cell.2006.09.026 · Cited by 3,484 · see citing works
Mutations in the p53 tumor suppressor gene: clues to cancer etiology and molecular pathogenesis.
Greenblatt, M. S., Bennett, W. P., Hollstein, M., & Harris, C. C. (1994) · PubMed · Cited by 3,463 · see citing works
A human DNA segment with properties of the gene that predisposes to retinoblastoma and osteosarcoma
Friend, S. H., Bernards, R., Rogelj, S., Weinberg, R. A., Rapaport, J. M., Albert, D. M., & Dryja, T. P. (1986) · Nature · doi:10.1038/323643a0 · Cited by 2,948 · cited 2× · see citing works
“Therefore, in 1969, the presence of TSGs based on the developmental dynamics of sporadic and hereditary retinoblastoma, which suggested a carcinogenic “2-hit” model, and was eventually accepted and successfully cloned Rb1 in 1986.(9,10) One of the early famous arguments aimed at the being of TSG was because it is irre…”
BackgroundActivation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559 · see citing works
The regulation of E2F by pRB-family proteins.
Dyson, N. (1998) · Genes & Development · doi:10.1101/gad.12.15.2245 · Cited by 2,317 · see citing works
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206 · see citing works
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100 · see citing works
Swatek, K. N., & Komander, D. (2016) · Cell Research · doi:10.1038/cr.2016.39 · Cited by 2,070 · see citing works
Liaw, D., Marsh, D. J., Li, J., Dahia, P. L. M., Wang, S. I., Zheng, Z., Bose, S., Call, K. M., Tsou, H. C., Peacoke, M., et al. (1997) · Nature Genetics · doi:10.1038/ng0597-64 · Cited by 2,067 · see citing works
The functions and regulation of the PTEN tumour suppressor
Song, M. S., Salmena, L., & Pandolfi, P. P. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3330 · Cited by 1,926 · see citing works
Programmed Cell Death in Animal Development and Disease
Fuchs, Y., & Steller, H. (2011) · Cell · doi:10.1016/j.cell.2011.10.033 · Cited by 1,915 · see citing works
Kastenhuber, E. R., & Lowe, S. W. (2017) · Cell · doi:10.1016/j.cell.2017.08.028 · Cited by 1,906 · see citing works
Finn, R. S., Crown, J. P., Lang, I., Boer, K., Bondarenko, I. M., Kulyk, S. O., Ettl, J., Patel, R., Pinter, T., Schmidt, M., et al. (2015) · The Lancet Oncology · doi:10.1016/s1470-2045(14)71159-3 · Cited by 1,900 · see citing works
Cell cycle proteins as promising targets in cancer therapy
Otto, T., & Siciński, P. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2016.138 · Cited by 1,875 · see citing works
The p53-mdm-2 autoregulatory feedback loop.
Wu, X., Bayle, J. H., Olson, D., & Levine, A. J. (1993) · Genes & Development · doi:10.1101/gad.7.7a.1126 · Cited by 1,801 · see citing works
p53 Has a Direct Apoptogenic Role at the Mitochondria
Mihara, M., Erster, S. H., Zaika, A. I., Petrenko, O., Chittenden, T. D., Pančoška, P., & Moll, U. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00050-9 · Cited by 1,771 · see citing works
The ATM protein kinase: regulating the cellular response to genotoxic stress, and more
Shiloh, Y., & Ziv, Y. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3546 · Cited by 1,649 · see citing works
AMP-activated protein kinase induces a p53-dependent metabolic checkpoint
Jones, R. G., Plas, D. R., Kubek, S., Buzzai, M., Mu, J., Xu, Y., Birnbaum, M. J., & Thompson, C. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.027 · Cited by 1,619 · see citing works
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A. P., Sowa, M. E., Rad, R., Rush, A. J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,582 · 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
Chk1 and Chk2 kinases in checkpoint control and cancer
Bartek, J., & Lukas, J. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00110-7 · Cited by 1,513 · see citing works
Defining the Human Deubiquitinating Enzyme Interaction Landscape
Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,512 · see citing works
Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53
Oliner, J. D., Pietenpol, J. A., Thiagalingam, S., Gyuris, J., Kinzler, K. W., & Vogelstein, B. (1993) · Nature · doi:10.1038/362857a0 · Cited by 1,447 · see citing works
Ubiquitination in disease pathogenesis and treatment
Popovic, D., Vucic, D., & Đikić, I. (2014) · Nature Medicine · doi:10.1038/nm.3739 · Cited by 1,405 · see citing works
The tripartite motif family identifies cell compartments
Reymond, A., Meroni, G., Fantozzi, A., Merla, G., Cairo, S., Luzi, L., Riganelli, D., Zanaria, E., Messali, S., Cainarca, S., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.9.2140 · Cited by 1,366 · see citing works
Loss of tumor suppressor PTEN function increases B7-H1 expression and immunoresistance in glioma
Parsa, A. T., Waldron, J. S., Panner, A., Crane, C. A., Parney, I. F., Barry, J. J., Cachola, K. E., Murray, J. C., Tihan, T., Jensen, M. C., et al. (2006) · Nature Medicine · doi:10.1038/nm1517 · Cited by 1,341 · see citing works
Regulating the p53 pathway: in vitro hypotheses, in vivo veritas
Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286 · see citing works
MDM2, MDMX and p53 in oncogenesis and cancer therapy
Wade, M., Li, Y.-C., & Wahl, G. M. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3430 · Cited by 1,279 · cited 1× · see citing works
“The MDM2 oncoprotein is overexpressed in many types of human cancers and is a critical component of the p53 pathway.(262,263) MDM2 targets p53 for ubiquitination, and for proteasome-mediated degradation, and it maintains an appropriately low level of p53 under unstressed cell conditions.”
BackgroundPost-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270 · see citing works
Kinzler, K. W., & Vogelstein, B. (1997) · Nature · doi:10.1038/386761a0 · Cited by 1,240 · see citing works
Fry, D. W., Harvey, P. J., Keller, P. R., Elliott, W. L., Meade, M., Trachet, E., Albassam, M., Zheng, X., Leopold, W. R., Pryer, N. K., et al. (2004) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.1427.3.11 · Cited by 1,236 · see citing works
Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis
Cully, M., You, H., Levine, A. J., & Mak, T. W. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1819 · Cited by 1,233 · see citing works
Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling
Mukhopadhyay, D., & Riezman, H. (2007) · Science · doi:10.1126/science.1127085 · Cited by 1,221 · see citing works
DNA damage activates p53 through a phosphorylation–acetylation cascade
Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204 · see citing works
DNA damage and the balance between survival and death in cancer biology
Roos, W. P., Thomas, A. D., & Kaina, B. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.2 · Cited by 1,189 · see citing works
The Multiple Roles of PTEN in Tumor Suppression
Di Cristofano, A., & Pandolfi, P. P. (2000) · Cell · doi:10.1016/s0092-8674(00)80674-1 · Cited by 1,182 · see citing works
Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, A. J., Hochstrasser, M., Finley, D. J., & Peng, J. (2009) · Cell · doi:10.1016/j.cell.2009.01.041 · Cited by 1,125 · see citing works
Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
Bykov, V. J. N., Issaeva, N., Shilov, A., Hultcrantz, M., Pugacheva, E., Chumakov, P., Bergman, J., Wiman, K. G., & Selivanova, G. (2002) · Nature Medicine · doi:10.1038/nm0302-282 · Cited by 1,067 · see citing works
A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly
Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999) · Cell · doi:10.1016/s0092-8674(00)80574-7 · Cited by 1,056 · see citing works
Mechanisms of Deubiquitinase Specificity and Regulation
Mevissen, T. E. T., & Komander, D. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044916 · Cited by 1,035 · see citing works
Principles of Tumor Suppression
Sherr, C. J. (2004) · Cell · doi:10.1016/s0092-8674(03)01075-4 · Cited by 1,028 · see citing works
Tenets of PTEN Tumor Suppression
Salmena, L., Carracedo, A., & Pandolfi, P. P. (2008) · Cell · doi:10.1016/j.cell.2008.04.013 · Cited by 1,027 · see citing works
Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., & Gu, W. J. (2002) · Nature · doi:10.1038/nature737 · Cited by 1,027 · see citing works
Correction of a pathogenic gene mutation in human embryos
Ma, H., Marti-Gutierrez, N., Park, S.-W., Wu, J., Lee, Y., Suzuki, K., Koski, A., Ji, D., Hayama, T., Ahmed, R., et al. (2017) · Nature · doi:10.1038/nature23305 · Cited by 969 · cited 1× · see citing works
“Although gene editing has brought many challenges, including miss target effect and induction of adaptive immune response, recent progress shows hope in reducing these results.(188,430) There is no doubt that gene editing Regulating tumor suppressor genes: post-translational modifications Chen et al.”
BackgroundBRCA1 and BRCA2: 1994 and beyond
Narod, S. A., & Foulkes, W. D. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1431 · Cited by 967 · see citing works
HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation
Zhou, B. P., Liao, Y., Xia, W., Zou, Y., Spohn, B., & Hung, M.-C. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-973 · Cited by 951 · see citing works
APC, Signal transduction and genetic instability in colorectal cancer
Fodde, R., Smits, R., & Clevers, H. (2001) · Nature Reviews Cancer · doi:10.1038/35094067 · Cited by 937 · see citing works
Targeting CDK4 and CDK6: From Discovery to Therapy
Sherr, C. J., Beach, D., & Shapiro, G. I. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0894 · Cited by 936 · see citing works
p53 ubiquitination: Mdm2 and beyond
Brooks, C. L., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.020 · Cited by 924 · see citing works
ARF family G proteins and their regulators: roles in membrane transport, development and disease
Donaldson, J. G., & Jackson, C. L. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3117 · Cited by 914 · see citing works
Regulation of the specific DNA binding function of p53
Hupp, T. R., Meek, D. W., Midgley, C., & Lane, D. P. (1992) · Cell · doi:10.1016/0092-8674(92)90562-q · Cited by 905 · see citing works
Wagner, S., Beli, P., Weinert, B. T., Nielsen, M. L., Cox, J., Mann, M., & Choudhary, C. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013284 · Cited by 889 · see citing works
The long tail of oncogenic drivers in prostate cancer
PCF/SU2C International Prostate Cancer Dream Team, Armenia, J., Wankowicz, S. A. M., Liu, D., Gao, J., Kundra, R., Reznik, E., Chatila, W. K., Chakravarty, D., Han, G. C., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0078-z · Cited by 873 · see citing works
p53 induces differentiation of mouse embryonic stem cells by suppressing Nanog expression
Lin, T., Chao, C., Saito, S., Mazur, S. J., Murphy, M. E., Appella, E., & Xu, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1211 · Cited by 859 · see citing works
Regulation of p53 activity through lysine methylation
Chuikov, S., Kurash, J. K., Wilson, J. R., Xiao, B., Justin, N., Ivanov, G. S., McKinney, K. M., Tempst, P., Prives, C. L., Gamblin, S. J., et al. (2004) · Nature · doi:10.1038/nature03117 · Cited by 820 · see citing works
p53 is regulated by the lysine demethylase LSD1
Huang, J. L., Sengupta, R., Espejo, A. B., Lee, M. G., Dorsey, J. A., Richter, M., Opravil, S., Shiekhattar, R., Bedford, M. T., Jenuwein, T., et al. (2007) · Nature · doi:10.1038/nature06092 · Cited by 820 · see citing works
Serrano-Gomez, S. J., Maziveyi, M., & Alahari, S. K. (2016) · Molecular Cancer · doi:10.1186/s12943-016-0502-x · Cited by 817 · see citing works
Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2
Li, M., Brooks, C. L., Wu-Baer, F., Chen, D., Baer, R., & Gu, W. (2003) · Science · doi:10.1126/science.1091362 · Cited by 804 · cited 1× · see citing works
“Further, MDM2 mediates the nuclear export of p53.(266) Moreover, when p53 is ubiquitinated by MDM2, it cannot be acetylated by p300/ CBP, and, therefore, rapid proteasome-mediated degradation takes place.”
BackgroundPharmacological Rescue of Mutant p53 Conformation and Function
Foster, B. A., Coffey, H. A., Morin, M. J., & Rastinejad, F. (1999) · Science · doi:10.1126/science.286.5449.2507 · Cited by 802 · see citing works
Proteogenomic Analysis of Human Colon Cancer Reveals New Therapeutic Opportunities
Vasaikar, S., Huang, C., Wang, X., Petyuk, V. A., Savage, S. R., Wen, B., Dou, Y., Zhang, Y., Shi, Z., Arshad, O. A., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.030 · Cited by 799 · see citing works
p53: oncogene or anti-oncogene?Preprint
Lane, D. P., & Benchimol, S. (1990) · Genes & Development · doi:10.1101/gad.4.1.1 · Cited by 796 · see citing works
The broken cycle: E2F dysfunction in cancer
Kent, L. N., & Leone, G. W. (2019) · Nature reviews. Cancer · doi:10.1038/s41568-019-0143-7 · Cited by 786 · see citing works
Lastwika, K. J., Wilson, W., Li, Q. K., Norris, J., Xu, H., Ghazarian, S. R., Kitagawa, H., Kawabata, S., Taube, J. M., Yao, S., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-14-3362 · Cited by 785 · see citing works
A Mutant-p53/Smad Complex Opposes p63 to Empower TGFβ-Induced Metastasis
Adorno, M., Cordenonsi, M., Montagner, M., Dupont, S., Wong, C., Hann, B. C., Solari, A., Bobisse, S., Rondina, M. B., Guzzardo, V., et al. (2009) · Cell · doi:10.1016/j.cell.2009.01.039 · Cited by 783 · see citing works
Phosphorylation of the PTEN Tail Regulates Protein Stability and Function
Vázquez, F., Ramaswamy, S., Nakamura, N., & Sellers, W. R. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.14.5010-5018.2000 · Cited by 777 · see citing works
The p53–Mdm2 module and the ubiquitin system
Michael, D., & Oren, M. (2002) · Seminars in Cancer Biology · doi:10.1016/s1044-579x(02)00099-8 · Cited by 759 · see citing works
Goldstein, G., Scheid, M. P., Hämmerling, U., Schlesinger, D. H., Niall, H. D., & Boyse, E. A. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.11 · Cited by 752 · see citing works
The retinoblastoma tumour suppressor in development and cancer
Classon, M., & Harlow, E. (2002) · Nature Reviews Cancer · doi:10.1038/nrc950 · Cited by 738 · see citing works
Stommel, J. M., Marchenko, N. D., Jimenez, G. S., Moll, U. M., Hope, T. J., & Wahl, G. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1660 · Cited by 738 · see citing works
Ubiquitylation and cell signaling
Haglund, K., & Đikić, I. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600808 · Cited by 736 · see citing works
TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases
Meroni, G., & Diez‐Roux, G. (2005) · BioEssays · doi:10.1002/bies.20304 · Cited by 731 · see citing works
NEDD4-1 Is a Proto-Oncogenic Ubiquitin Ligase for PTEN
Wang, X., Trotman, L. C., Koppie, T. M., Alimonti, A., Chen, Z., Gao, Z., Wang, J., Erdjument‐Bromage, H., Tempst, P., Cordon‐Cardo, C., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.039 · Cited by 720 · see citing works
Pirh2, a p53-Induced Ubiquitin-Protein Ligase, Promotes p53 Degradation
Leng, R. P., Lin, Y., Ma, W., Wu, H., Lemmers, B., Chung, S., Parant, J. M., Lozano, G., Hakem, R., & Benchimol, S. (2003) · Cell · doi:10.1016/s0092-8674(03)00193-4 · Cited by 717 · see citing works
ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage
Maya, R., Balass, M., Kim, S.-T., Shkedy, D., Leal, J.-F. M., Shifman, O., Moas, M., Buschmann, T., Ronai, Z., Shiloh, Y., et al. (2001) · Genes & Development · doi:10.1101/gad.886901 · Cited by 716 · cited 2× · see citing works
“interaction between p53 and MDM2 is broken, such as during a DNA damage event in which MDM2 is phosphorylated at serine 395.(268) Notably, low level of MDM2 activity induces p53 monoubiquitination and nuclear output, while high level of MDM2 activity promotes p53 polyubiquitination and nuclear degradation.”
BackgroundThe ubiquitin ligase COP1 is a critical negative regulator of p53
Dornan, D., Wertz, I. E., Shimizu, H., Arnott, D. P., Frantz, G. D., Dowd, P., Rourke, K. O., Koeppen, H., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02514 · Cited by 700 · see citing works
Structural Biology of the Tumor Suppressor p53
Joerger, A. C., & Fersht, A. R. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.060806.091238 · Cited by 699 · see citing works
Binding and modulation of p53 by p300/CBP coactivators
Lill, N. L., Grossman, S. R., Ginsberg, D., DeCaprio, J. A., & Livingston, D. M. (1997) · Nature · doi:10.1038/42981 · Cited by 693 · see citing works
A dynamic role of HAUSP in the p53-Mdm2 pathway
Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679 · see citing works
Recruitment of p300/CBP in p53-Dependent Signal Pathways
Avantaggiati, M. L., Ogryzko, V. V., Gardner, K., Giordano, A., Levine, A. S., & Kelly, K. (1997) · Cell · doi:10.1016/s0092-8674(00)80304-9 · Cited by 668 · see citing works
Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.-W., Gu, W. J., Cohen, R. E., & Shi, Y. (2002) · Cell · doi:10.1016/s0092-8674(02)01199-6 · Cited by 648 · see citing works
MDM2 — master regulator of the p53 tumor suppressor protein
Momand, J., Wu, H.-H., & Dasgupta, G. (2000) · Gene · doi:10.1016/s0378-1119(99)00487-4 · Cited by 641 · see citing works
SUMO‐1 modification activates the transcriptional response of p53
Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Midgley, C., Lane, D. P., & Hay, R. T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6455 · Cited by 639 · see citing works
USP10 Regulates p53 Localization and Stability by Deubiquitinating p53
Yuan, J., Luo, K., Zhang, L., Cheville, J. C., & Lou, Z. (2010) · Cell · doi:10.1016/j.cell.2009.12.032 · Cited by 637 · cited 2× · see citing works
“Upon DNA damage, USP10 is phosphorylated by ATM, after which it is re-localized to the nucleus where p53 de-ubiquitination occurs, which is the reverse of the function of residual MDM2, which ubiquitinates p53.(329,330) As USP10 plays an anti-cancer role by regulating the nuclear output and degradation of p53 induced…”
BackgroundThe Tumor Suppressor PTEN Is Phosphorylated by the Protein Kinase CK2 at Its C Terminus
Torres, J., & Pulido, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009134200 · Cited by 630 · see citing works
Repression of p53 activity by Smyd2-mediated methylation
Huang, J. L., Perez-Burgos, L., Placek, B. J., Sengupta, R., Richter, M., Dorsey, J. A., Kubicek, S., Opravil, S., Jenuwein, T., & Berger, S. L. (2006) · Nature · doi:10.1038/nature05287 · Cited by 626 · see citing works
Why are there hotspot mutations in the TP53 gene in human cancers?
Baugh, E. H., Ke, H., Levine, A. J., Bonneau, R., & Chan, C. S. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.180 · Cited by 609 · see citing works
Tumour suppression by p53: a role for the DNA damage response?
Meek, D. W. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2716 · Cited by 604 · see citing works
Divorcing ARF and p53: an unsettled case
Sherr, C. J. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1954 · Cited by 595 · see citing works
PTEN: Tumor Suppressor and Metabolic Regulator
Chen, C.-Y., Chen, J., He, L., & Stiles, B. L. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00338 · Cited by 589 · see citing works
Targeted therapy in patients with PIK3CA-related overgrowth syndrome
Venot, Q., Blanc, T., Hadj-Rabia, S., Berteloot, L., Ladraa, S., Huyen, J. D. V., Blanc, E., Johnson, S. C., Hoguin, C., Boccara, O., et al. (2018) · Nature · doi:10.1038/s41586-018-0217-9 · Cited by 588 · see citing works
Chromatin replication and epigenome maintenance
Alabert, C., & Groth, A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3288 · Cited by 586 · see citing works
Lundblad, J. R., Kwok, R. P. S., Laurance, M. E., Harter, M. L., & Goodman, R. H. (1995) · Nature · doi:10.1038/374085a0 · Cited by 585 · see citing works
Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage.
Chehab, N. H., Malikzay, A., Stavridi, E. S., & Halazonetis, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13777 · Cited by 583 · see citing works
p300/CBP‐mediated p53 acetylation is commonly induced by p53‐activating agents and inhibited by MDM2
Ito, A., Lai, C.-H., Zhao, X., Saito, S., Hamilton, M. H., Appella, E., & Yao, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1331 · Cited by 582 · see citing works
Molecular mechanisms underlying RB protein function
Dick, F. A., & Rubin, S. M. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3567 · Cited by 570 · see citing works
Ubiquitin chain diversity at a glance
Akutsu, M., Đikić, I., & Bremm, A. (2016) · Journal of Cell Science · doi:10.1242/jcs.183954 · Cited by 555 · see citing works
ARF-BP1/Mule Is a Critical Mediator of the ARF Tumor Suppressor
Chen, D., Kon, N., Li, M., Zhang, W., Qin, J., & Gu, W. J. (2005) · Cell · doi:10.1016/j.cell.2005.03.037 · Cited by 539 · see citing works
Wang, M., Mao, C., Ouyang, L., Liu, Y., Lai, W., Liu, N., Shi, Y., Chen, L., Xiao, D., Yu, F., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0304-y · Cited by 530 · see citing works
Self-citationp53 post-translational modification: deregulated in tumorigenesis
Dai, C., & Gu, W. J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.09.002 · Cited by 523 · see citing works
Therapeutic targeting of p53: all mutants are equal, but some mutants are more equal than others
Sabapathy, K., & Lane, D. P. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2017.151 · Cited by 517 · see citing works
Discovery of a potent and selective inhibitor of cyclin-dependent kinase 4/6
Toogood, P. L., Harvey, P. J., Repine, J. T., Sheehan, D. J., VanderWel, S. N., Zhou, H., Keller, P. R., McNamara, D. J., Sherry, D., Zhu, T., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049354h · Cited by 513 · see citing works
Activation of p53 by conjugation to the ubiquitin‐like protein SUMO‐1
Gostissa, M., Hengstermann, A., Fogal, V., Sandy, P., Schwarz, S. E., Scheffner, M., & Sal, G. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6462 · Cited by 512 · see citing works
Critical role of FOXO3a in carcinogenesis
Liu, Y., Ao, X., Ding, W., Ponnusamy, M., Wu, W., Hao, X., Yu, W., Wang, Y., Li, P., & Wang, J. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0856-3 · Cited by 508 · see citing works
Acetylation of p53 inhibits its ubiquitination by Mdm2
Li, M., Luo, J., Brooks, C. L., & Gu, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200578200 · Cited by 503 · see citing works
CDK4/6 Inhibition in Cancer: Beyond Cell Cycle Arrest
Goel, S., DeCristo, M. J., McAllister, S. S., & Zhao, J. J. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.07.002 · Cited by 495 · see citing works
Mao, C., Wang, X., Liu, Y., Wang, M., Yan, B., Jiang, Y., Shi, Y., Shen, Y., Liu, X., Lai, W., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-3454 · Cited by 493 · see citing works
Self-citationArginine methylation regulates the p53 response
Jansson, M., Durant, S., Cho, E., Sheahan, S., Edelmann, M. J., Kessler, B., & Thangue, N. L. (2008) · Nature Cell Biology · doi:10.1038/ncb1802 · Cited by 492 · see citing works
Posttranslational Modification of p53: Cooperative Integrators of FunctionPreprint
Meek, D. W., & Anderson, C. W. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000950 · Cited by 487 · see citing works
George, S., Miao, D., Demetri, G. D., Adeegbe, D. O., Rodig, S. J., Shukla, S. A., Lipschitz, M., Amin‐Mansour, A., Raut, C. P., Carter, S. L., et al. (2017) · Immunity · doi:10.1016/j.immuni.2017.02.001 · Cited by 476 · see citing works
PTEN: Multiple Functions in Human Malignant Tumors
Milella, M., Falcone, I., Conciatori, F., Incani, U. C., Curatolo, A. D., Inzerilli, N., Nuzzo, C. M. A., Vaccaro, V., Vari, S., Cognetti, F., et al. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00024 · Cited by 469 · see citing works
Modulation of p53 Function by SET8-Mediated Methylation at Lysine 382
Shi, X., Kachirskaia, I., Yamaguchi, H., West, L. E., Wen, H., Wang, E. W., Dutta, S. M., Appella, E., & Gozani, O. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.012 · Cited by 463 · see citing works
A General Theory of Carcinogenesis
Comings, D. E. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.12.3324 · Cited by 462 · see citing works
Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7
Lee, J., Russo, A. A., & Pavletich, N. P. (1998) · Nature · doi:10.1038/36038 · Cited by 459 · see citing works
ATM Mutations in Cancer: Therapeutic Implications
Choi, M. P., Kipps, T. J., & Kurzrock, R. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0945 · Cited by 456 · see citing works
Polyubiquitination of p53 by a Ubiquitin Ligase Activity of p300
Grossman, S. R., Deato, M. D. E., Brignone, C., Chan, H. M., Kung, A. L., Tagami, H., Nakatani, Y., & Livingston, D. M. (2003) · Science · doi:10.1126/science.1080386 · Cited by 454 · see citing works
Involvement of PIAS1 in the Sumoylation of Tumor Suppressor p53
Kahyo, T., Nishida, T., & Yasuda, H. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00349-5 · Cited by 449 · see citing works
Signaling by the Phosphoinositide 3-Kinase Family in Immune Cells
Okkenhaug, K. (2013) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-095946 · Cited by 446 · see citing works
RB1 : a prototype tumor suppressor and an enigmaPreprint
Dyson, N. J. (2016) · Genes & Development · doi:10.1101/gad.282145.116 · Cited by 437 · see citing works
Walther, J. B., Loh, T., & Granka, L. A. (2005) · Journal of Language and Social Psychology · doi:10.1177/0261927x04273036 · Cited by 436 · see citing works
Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains
Emmerich, C. H., Ordureau, A., Strickson, S., Arthur, J. S. C., Pedrioli, P. G. A., Komander, D., & Cohen, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314715110 · Cited by 425 · see citing works
2011: the immune hallmarks of cancer
Cavallo, F., Giovanni, C. D., Nanni, P., Forni, G., & Lollini, P. (2011) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-010-0968-0 · Cited by 417 · see citing works
The PTEN, Mdm2, p53 tumor suppressor–oncoprotein network
Mayo, L. D., & Donner, D. B. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02166-7 · Cited by 408 · see citing works
Two distinct modes for propagation of histone PTMs across the cell cyclePreprint
Alabert, C., Barth, T. K., Reverón-Gómez, N., Sidoli, S., Schmidt, A., Jensen, O. N., Imhof, A., & Groth, A. (2015) · Genes & Development · doi:10.1101/gad.256354.114 · Cited by 404 · see citing works
PTEN, more than the AKT pathway
Blanco‐Aparicio, C., Renner, O., Martínez-Leal, J. F., & Carnero, A. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm052 · Cited by 403 · see citing works
Drugs and Lactation Database: LactMed
Chelf, C. J. (2012) · Journal of Electronic Resources in Medical Libraries · doi:10.1080/15424065.2012.735134 · Cited by 401 · see citing works
Discovery of RG7112: a small-molecule MDM2 inhibitor in clinical development
Vu, B., Wovkulich, P., Pizzolato, G., Lovey, A., Ding, Q., Jiang, N., Liu, J.-J., Zhao, C., Glenn, K., Wen, Y., et al. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml4000657 · Cited by 395 · see citing works
Loss of Lkb1 and Pten Leads to Lung Squamous Cell Carcinoma with Elevated PD-L1 Expression
Xu, C., Brainson, C. F., Koyama, S., Wu, H., Zhao, Y., Chen, Z., Herter-Sprie, G. S., Akbay, E. A., Tchaicha, J. H., Altabef, A. B., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.03.033 · Cited by 394 · see citing works
Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation
Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Lane, D. P., & Hay, R. T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8458-8467.2000 · Cited by 386 · see citing works
Inhibitors of cyclin-dependent kinases as cancer therapeutics.
Whittaker, S. R., Mallinger, A., Workman, P., & Clarke, P. A. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.008 · Cited by 384 · see citing works
A p53 Amino-Terminal Nuclear Export Signal Inhibited by DNA Damage-Induced Phosphorylation
Zhang, Y., & Xiong, Y. (2001) · Science · doi:10.1126/science.1058637 · Cited by 378 · cited 1× · see citing works
“The N-terminal transactivation domain of p53 seems containing another NES, in which phosphorylation blocks the nuclear output of p53, bring about its nuclear accumulation.(210) SUMOylation occurs at K386 of p53 and SUMO-1, SUMO-2, or SUMO-3 that accelerates the output of the p53 from nucleus.”
BackgroundCDK4/6 Inhibitors: The Mechanism of Action May Not Be as Simple as Once Thought
Klein, M. E., Kovatcheva, M., Davis, L. E., Tap, W. D., & Koff, A. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.023 · Cited by 378 · see citing works
The antitumorigenic roles of BRCA1–BARD1 in DNA repair and replication
Tarsounas, M., & Sung, P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0218-z · Cited by 366 · see citing works
Ma, C. X., Gao, F., Luo, J. R., Northfelt, D., Goetz, M. P., Forero, A., Hoog, J., Naughton, M., Ademuyiwa, F. O., Suresh, R., et al. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-3206 · Cited by 360 · see citing works
The role of PTEN signaling perturbations in cancer and in targeted therapy
Keniry, M. E., & Parsons, R. E. (2008) · Oncogene · doi:10.1038/onc.2008.248 · Cited by 358 · see citing works
Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1
Nakada, S., Tai, I., Panier, S., Al-Hakim, A., Iemura, S.-I., Juang, Y.-C., O’Donnell, L., Kumakubo, A., Munro, M., Sicheri, F., et al. (2010) · Nature · doi:10.1038/nature09297 · Cited by 357 · see citing works
Mechanism of action of the immunosuppressant rapamycin
Dumont, F. J., & Su, Q. (1995) · Life Sciences · doi:10.1016/0024-3205(95)02233-3 · Cited by 356 · see citing works
Stress Signals Utilize Multiple Pathways To Stabilize p53
Ashcroft, M. A., Taya, Y., & Vousden, K. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.9.3224-3233.2000 · Cited by 356 · see citing works
Oncogenic lncRNA downregulates cancer cell antigen presentation and intrinsic tumor suppression
Hu, Q., Ye, Y., Chan, L.-C., Li, Y., Liang, K., Lin, A., Egranov, S. D., Zhang, Y., Xia, W., Gong, J., et al. (2019) · Nature Immunology · doi:10.1038/s41590-019-0400-7 · Cited by 353 · see citing works
Self-citationPTEN Protects p53 from Mdm2 and Sensitizes Cancer Cells to Chemotherapy
Mayo, L. D., Dixon, J. E., Durden, D. L., Tonks, N. K., & Donner, D. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108302200 · Cited by 351 · see citing works
Tailoring to RB: tumour suppressor status and therapeutic response
Knudsen, E. S., & Knudsen, K. E. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2401 · Cited by 345 · see citing works
Protein Language: Post-Translational Modifications Talking to Each Other.
Vu, L. D., Gevaert, K., & Smet, I. D. (2018) · Trends in Plant Science · doi:10.1016/j.tplants.2018.09.004 · Cited by 340 · see citing works
Principles of Ubiquitin-Dependent Signaling
Oh, E., Akopian, D., & Rape, M. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062802 · Cited by 339 · see citing works
The post-translational modification, SUMOylation, and cancer (Review)
Han, Z., Feng, Y.-H., Gu, B.-H., Li, Y., & Chen, H. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4280 · Cited by 337 · see citing works
Asselin, É., Mills, G. B., & Tsang, B. K. (2001) · PubMed · Cited by 336 · see citing works
Loss of Tumor Suppressor Gene Function in Human Cancer: An Overview
Wang, L., Wu, C., Rajasekaran, N., & Shin, Y. K. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000495956 · Cited by 334 · see citing works
Lee, Y.-R., Chen, M., Lee, J. D., Zhang, J., Lin, S., Fu, T., Chen, H., Ishikawa, T., Chiang, S.-Y., Katon, J. M., et al. (2019) · Science · doi:10.1126/science.aau0159 · Cited by 331 · see citing works
Klughammer, J., Kiesel, B., Roetzer-Pejrimovsky, T., Fortelny, N., Nemc, A., Nenning, K., Furtner, J., Sheffield, N. C., Datlinger, P., Peter, N., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0156-x · Cited by 326 · see citing works
A Secreted PTEN Phosphatase That Enters Cells to Alter Signaling and Survival
Hopkins, B. D., Fine, B. M., Steinbach, N., Dendy, M., Rapp, Z., Shaw, J. M., Pappas, K., Yu, J. S., Hodakoski, C., Mense, S. M., et al. (2013) · Science · doi:10.1126/science.1234907 · Cited by 325 · see citing works
Allele-Specific p53 Mutant Reactivation
Yu, X., Vázquez, A., Levine, A. J., & Carpizo, D. R. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.03.042 · Cited by 321 · see citing works
The next level of complexity: Crosstalk of posttranslational modifications
Venne, A. S., Kollipara, L., & Zahedi, R. P. (2013) · PROTEOMICS · doi:10.1002/pmic.201300344 · Cited by 320 · see citing works
Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle and Protein Quality Control
Yau, R. G., Dörner, K., Castellanos, E. R., Haakonsen, D. L., Werner, A. A., Wang, N., Yang, X. W., Martinez-Martín, N., Matsumoto, M. L., Dixit, V. M., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.040 · Cited by 315 · see citing works
Lin, Z., Yang, H., Kong, Q., Li, J., Lee, S.-M., Gao, B., Dong, H., Wei, J., Song, J., Zhang, D. D., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.03.024 · Cited by 315 · see citing works
Rb regulates fate choice and lineage commitment in vivo
Calo, E., Quintero-Estades, J. A., Danielian, P. S., Nedelcu, S., Berman, S. D., & Lees, J. A. (2010) · Nature · doi:10.1038/nature09264 · Cited by 313 · see citing works
The mdm-2 oncogene can overcome wild-type p53 suppression of transformed cell growth.
Finlay, C. A. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.301 · Cited by 311 · see citing works
Loughery, J., Cox, M. L., Smith, L. M., & Meek, D. W. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku501 · Cited by 308 · see citing works
WWP2 is an E3 ubiquitin ligase for PTEN
Maddika, S., Kavela, S., Rani, N., Palicharla, V. R., Pokorny, J. L., Sarkaria, J. N., & Chen, J. (2011) · Nature Cell Biology · doi:10.1038/ncb2240 · Cited by 306 · see citing works
Ha, N., Tonozuka, T., Stamos, J. L., Choi, H., & Weis, W. I. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.010 · Cited by 304 · see citing works
Targeting the MDM2–p53 Protein–Protein Interaction for New Cancer Therapy: Progress and Challenges
Wang, S., Zhao, Y., Aguilar, A., Bernard, D., & Yang, C.-Y. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026245 · Cited by 300 · see citing works
Trim24 targets endogenous p53 for degradation
Allton, K., Jain, A. K., Herz, H.-M., Tsai, W.-W., Jung, S. Y., Qin, J., Bergmann, A., Johnson, R. L., & Barton, M. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813177106 · Cited by 292 · see citing works
The regulation of protein phosphorylation
Johnson, L. N. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370627 · Cited by 292 · see citing works
Chow, L. M. L., Endersby, R., Zhu, X., Rankin, S. L., Qu, C., Zhang, J., Broniscer, A., Ellison, D. W., & Baker, S. J. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.01.039 · Cited by 291 · see citing works
Regulation of the p53 response and its relationship to cancer
Meek, D. W. (2015) · Biochemical Journal · doi:10.1042/bj20150517 · Cited by 291 · see citing works
Is there a code embedded in proteins that is based on post-translational modifications?
Sims, R. J., & Reinberg, D. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2502 · Cited by 289 · see citing works
CHK2 kinase: cancer susceptibility and cancer therapy – two sides of the same coin?
Antoni, L., Sodha, N., Collins, I., & Garrett, M. D. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2251 · Cited by 287 · see citing works
Distinct p53 acetylation cassettes differentially influence gene-expression patterns and cell fate
Knights, C. D., Catania, J., Giovanni, S. D., Muratoglu, S. C., Perez, R. E., Swartzbeck, A., Quong, A. A., Zhang, X., Beerman, T. A., Pestell, R. G., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512059 · Cited by 284 · see citing works
Acetylation control of the retinoblastoma tumour-suppressor protein
Chan, H. M., Krstic–Demonacos, M., Smith, L. M., Demonacos, C., & Thangue, N. B. L. (2001) · Nature Cell Biology · doi:10.1038/35083062 · Cited by 282 · see citing works
The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2
Stevenson, L. F., Sparks, A., Allende‐Vega, N., Xirodimas, D. P., Lane, D. P., & Saville, M. K. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601567 · Cited by 280 · see citing works
Hamid, A., Gray, K. P., Shaw, G., MacConaill, L. E., Evan, C. P., Bernard, B. D., Loda, M. F., Corcoran, N. M., Allen, E. M. V., Choudhury, A. D., et al. (2018) · European Urology · doi:10.1016/j.eururo.2018.11.045 · Cited by 276 · see citing works
Cytoplasmic destruction of p53 by the endoplasmic reticulum‐resident ubiquitin ligase ‘Synoviolin’
Yamasaki, S., Yagishita, N., Sasaki, T., Nakazawa, M., Kato, Y., Yamadera, T., Bae, E.-K., Toriyama, S., Ikeda, R., Zhang, L., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601490 · Cited by 275 · see citing works
Rahdar, M., Inoue, T., Meyer, T., Zhang, J., Vázquez, F., & Devreotes, P. N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811212106 · Cited by 266 · see citing works
Phosphorylated RB Promotes Cancer Immunity by Inhibiting NF-κB Activation and PD-L1 Expression
Jin, X., Ding, D., Yan, Y., Li, H., Wang, B., Ma, L., Ye, Z., Ma, T., Wu, Q., Rodrigues, D. N., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.034 · Cited by 261 · see citing works
Meulmeester, E., Maurice, M. M., Boutell, C., Teunisse, A. F. A. S., Ovaa, H., Abraham, T. E., Dirks, R. W., & Jochemsen, A. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.024 · Cited by 260 · see citing works
Al-Khouri, A. M., Ma, Y., Togo, S. H., Williams, S., & Mustelin, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503045200 · Cited by 254 · see citing works
Rubin, S. M., Gall, A.-L., Zheng, N., & Pavletich, N. P. (2005) · Cell · doi:10.1016/j.cell.2005.09.044 · Cited by 253 · see citing works
Stable expansion of high‐grade serous ovarian cancer organoids requires a low‐Wnt environment
Hoffmann, K., Berger, H., Kulbe, H., Thillainadarasan, S., Mollenkopf, H., Żemojtel, T., TAUBE, E. T., Darb‐Esfahani, S., Mangler, M., Sehouli, J., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019104013 · Cited by 252 · see citing works
The management of retinoblastoma
Fabian, I. D., Onadim, Z., Karaa, E. K., Duncan, C., Chowdhury, T., Scheimberg, I. B., Ohnuma, S., Reddy, M. A., & Sagoo, M. S. (2018) · Oncogene · doi:10.1038/s41388-017-0050-x · Cited by 251 · see citing works
Hu, M., Gu, L., Li, M., Jeffrey, P. D., Gu, W., & Shi, Y. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040027 · Cited by 251 · see citing works
The mechanism of OTUB1-mediated inhibition of ubiquitination
Wiener, R., Zhang, X., Wang, T., & Wolberger, C. (2012) · Nature · doi:10.1038/nature10911 · Cited by 248 · see citing works
Tripathy, D., Bardia, A., & Sellers, W. R. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-3157 · Cited by 247 · see citing works
Molecular pathways: CDK4 inhibitors for cancer therapy
Dickson, M. A. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1551 · Cited by 245 · see citing works
Deciphering the retinoblastoma protein phosphorylation code
Rubin, S. M. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.10.007 · Cited by 244 · see citing works
Kaiser, S. E., Riley, B. E., Shaler, T. A., Trevino, R., Becker, C. H., Schulman, H., & Kopito, R. R. (2011) · Nature Methods · doi:10.1038/nmeth.1649 · Cited by 242 · see citing works
Cam, L. L., Linares, L. K., Paul, C., Julien, E., Lacroix, M., Hatchi, E., Triboulet, R., Bossis, G., Shmueli, A., Rodríguez, M. S., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.031 · Cited by 241 · see citing works
The genomic landscape of tuberous sclerosis complex
Martin, K. R., Zhou, W., Bowman, M. J., Shih, J., Au, K. S., Dittenhafer-Reed, K. E., Sisson, K. A., Koeman, J., Weisenberger, D. J., Cottingham, S. L., et al. (2017) · Nature Communications · doi:10.1038/ncomms15816 · Cited by 238 · see citing works
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 · see citing works
Surf the Post-translational Modification Network of p53 Regulation
Gu, B., & Zhu, W. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.4283 · Cited by 234 · see citing works
Mennerich, D., Kubaichuk, K. I., & Kietzmann, T. (2019) · Trends in cancer · doi:10.1016/j.trecan.2019.08.005 · Cited by 232 · see citing works
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Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016 · see citing works
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 602 · see citing works
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 · see citing works
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works
Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response
Snyder, N. A., & Silva, G. M. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101077 · Cited by 352 · see citing works
Deubiquitinase-targeting chimeras for targeted protein stabilization
Henning, N. J., Boike, L., Spradlin, J. N., Ward, C. C., Liu, G., Zhang, E., Belcher, B. P., Brittain, S. M., Hesse, M. J., Dovala, D., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-00971-2 · Cited by 344 · see citing works
Application of Proteomics in Cancer: Recent Trends and Approaches for Biomarkers Discovery
Kwon, Y. W., Jo, H.-S., Bae, S., Seo, Y., Song, P., Song, M., & Yoon, J. H. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.747333 · Cited by 270 · see citing works
Pathological implication of protein post-translational modifications in cancer
Pan, S., & Chen, R. (2022) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2022.101097 · Cited by 272 · see citing works
Targeted therapy for head and neck cancer: signaling pathways and clinical studies
Li, Q., Tie, Y., Alu, A., Ma, X., & Shi, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01297-0 · Cited by 269 · see citing works
Multi-omics approaches for biomarker discovery in early ovarian cancer diagnosis
Xiao, Y., Bi, M., Guo, H., & Li, M. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104001 · Cited by 256 · see citing works
Progress and prospects of mRNA-based drugs in pre-clinical and clinical applications
Shi, Y., Shi, M., Wáng, Y., & You, J. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02002-z · Cited by 231 · see citing works
Rah, B., Rather, R. A., Bhat, G. R., Baba, A. B., Mushtaq, I., Farooq, M., Yousuf, T., Dar, S. B., Parveen, S., Hassan, R., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.821344 · Cited by 202 · see citing works
A Systematic Review of Biosynthesized Metallic Nanoparticles as a Promising Anti-Cancer-Strategy
Andleeb, A., Andleeb, A., Asghar, S., Zaman, G., Tariq, M., Mehmood, A., Nadeem, M., Hano, C., Lorenzo, J. M., & Abbasi, B. H. (2021) · Cancers · doi:10.3390/cancers13112818 · Cited by 173 · see citing works
PTEN Alterations and Their Role in Cancer Management: Are We Making Headway on Precision Medicine?
Fusco, N., Sajjadi, E., Venetis, K., Gaudioso, G., Lopez, G., Corti, C., Guerini‐Rocco, E., Criscitiello, C., Malapelle, U., & Invernizzi, M. (2020) · Genes · doi:10.3390/genes11070719 · Cited by 167 · see citing works
Posttranslational Modifications in Ferroptosis
Wei, X., Yi, X., Zhu, X., & Jiang, D. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8832043 · Cited by 165 · see citing works
Hepatitis Virus and Hepatocellular Carcinoma: Recent Advances
Shen, C., Jiang, X., Li, M., & Luo, Y. (2023) · Cancers · doi:10.3390/cancers15020533 · Cited by 158 · see citing works
The landscape of T cell antigens for cancer immunotherapy
Peri, A., Salomon, N., Wolf, Y., Kreiter, S., Diken, M., & Samuels, Y. (2023) · Nature Cancer · doi:10.1038/s43018-023-00588-x · Cited by 130 · see citing works
Altered glycosylation in cancer: molecular functions and therapeutic potential
Xu, X., Peng, Q., Jiang, X., Tan, S., Yang, W., Han, Y., Oyang, L., Lin, J., Shen, M., Wang, J., et al. (2024) · 癌症:英文版 · doi:10.1002/cac2.12610 · Cited by 131 · see citing works
Overcoming anti-cancer drug resistance via restoration of tumor suppressor gene function
Gao, L., Wu, Z., Assaraf, Y. G., Chen, Z., & Wang, L. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100770 · Cited by 118 · see citing works
Oncogenes and tumor suppressor genes: functions and roles in cancers
Dakal, T. C., Dhabhai, B., Pant, A., Moar, K., Chaudhary, K., Yadav, V., Ranga, V., Sharma, N. K., Kumar, A., Maurya, P. K., et al. (2024) · MedComm · doi:10.1002/mco2.582 · Cited by 125 · see citing works
Genetic expression in cancer research: Challenges and complexity
Liu, H., Guo, Z., & Wang, P. (2024) · Gene Reports · doi:10.1016/j.genrep.2024.102042 · Cited by 104 · see citing works
Therapeutic Potential of Targeting the SUMO Pathway in Cancer
Kukkula, A., Ojala, V. K., Mendez, L., Sistonen, L., Elenius, K., & Sundvall, M. (2021) · Cancers · doi:10.3390/cancers13174402 · Cited by 92 · see citing works
Arshad, F., Nabi, F., Iqbal, S., & Khan, R. H. (2022) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2022.112356 · Cited by 91 · see citing works
Wang, Z., Wang, Y., Shen, N., Liu, Y., Xu, X., Zhu, R., Jiang, H., Wu, X., Wei, Y., & Tang, J. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216619 · Cited by 88 · see citing works
The roles of KRAS in cancer metabolism, tumor microenvironment and clinical therapy
Ma, Q., Zhang, W., Wu, K., & Shi, L. (2025) · Molecular Cancer · doi:10.1186/s12943-024-02218-1 · Cited by 92 · see citing works
Thioredoxin (Trx): A redox target and modulator of cellular senescence and aging-related diseases
Yang, B., Lin, Y., Huang, Y., Shen, Y.-Q., & Chen, Q. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103032 · Cited by 90 · see citing works
Ferroptosis: an important player in the inflammatory response in diabetic nephropathy
Li, J., Li, L., Zhang, Z., Chen, P., Shu, H., Yang, C., Chu, Y., & Liu, J. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1294317 · Cited by 82 · see citing works
Liposomes for the Treatment of Brain Cancer—A Review
Raju, R., Abuwatfa, W. H., Pitt, W. G., & Husseini, G. A. (2023) · Pharmaceuticals · doi:10.3390/ph16081056 · Cited by 76 · see citing works
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 72 · see citing works
p53: From Fundamental Biology to Clinical Applications in Cancer
Capuozzo, M., Santorsola, M., Bocchetti, M., Perri, F., Cascella, M., Granata, V., Celotto, V., Gualillo, O., Cossu, A. M., Nasti, G., et al. (2022) · Biology · doi:10.3390/biology11091325 · Cited by 70 · see citing works
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 · see citing works
Mafi, A., Rahmati, A., Aghdam, Z. B., Salami, R., Salami, M., Vakili, O., & Aghadavod, E. (2022) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-022-00354-4 · Cited by 66 · see citing works
Acetylation targeting chimera enables acetylation of the tumor suppressor p53
Kabir, M., Sun, N., Hu, X., Martin, T. C., Yi, J., Zhong, Y., Xiong, Y., Kaniskan, H. Ü., Gu, W., Parsons, R., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c04640 · Cited by 65 · see citing works
Role of Immune Cells and Receptors in Cancer Treatment: An Immunotherapeutic Approach
Mukherjee, A. G., Wanjari, U. R., Namachivayam, A., Murali, R., Prabakaran, D. S., Ganesan, R., Renu, K., Dey, A., Vellingiri, B., Ramanathan, G., et al. (2022) · Vaccines · doi:10.3390/vaccines10091493 · Cited by 67 · see citing works
GINS4 suppresses ferroptosis by antagonizing p53 acetylation with Snail
Chen, L., Cai, Q., Yang, R., Wang, H., Ling, H., Li, T., Liu, N., Wang, Z., Sun, J., Tao, T., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219585120 · Cited by 64 · see citing works
Self-citationBiological effects and mechanisms of fisetin in cancer: a promising anti-cancer agent
Zhou, C., Huang, Y., Nie, S., Zhou, S., Gao, X., & Chen, G. (2023) · European journal of medical research · doi:10.1186/s40001-023-01271-8 · Cited by 63 · see citing works
PRMT5-mediated arginine methylation stabilizes GPX4 to suppress ferroptosis in cancer
Fan, Y., Wang, Y., Dan, W., Zhang, Y., Nie, L., Ma, Z., Zhuang, Y., Liu, B., Li, M., Liu, T., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01610-3 · Cited by 62 · see citing works
PCDHB14 promotes ferroptosis and is a novel tumor suppressor in hepatocellular carcinoma
Liu, Y., Ouyang, L., Mao, C., Chen, Y., Li, T., Liu, N., Wang, Z., Lai, W., Zhou, Y., Cao, Y., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02370-2 · Cited by 58 · see citing works
Self-citationZhao, S., Zhang, X., Chen, S., & Zhang, S. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01700-0 · Cited by 58 · see citing works
Advancement in Biopolymer Assisted Cancer Theranostics
Bhattacharya, T., Preetam, S., Ghosh, B., Chakrabarti, T., Chakrabarti, P., Samal, S., & Thorat, N. D. (2023) · ACS Applied Bio Materials · doi:10.1021/acsabm.3c00458 · Cited by 42 · see citing works
Liquid-liquid phase separation in DNA double-strand breaks repair
Wang, Y., Zhao, W.-W., Shi, J., Wan, X., Zheng, J., & Fan, X. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06267-0 · Cited by 59 · see citing works
Ye, Z., Xia, Y., Li, L., Li, B., Chen, L., Yu, W., Ruan, Y., Rao, T., Zhou, X., & Fan, C. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114925 · Cited by 53 · see citing works
Self-citationMultiple aspects of matrix stiffness in cancer progression
Mancini, A., Gentile, M. T., Pentimalli, F., Cortellino, S., Grieco, M., & Giordano, A. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1406644 · Cited by 52 · see citing works
PDLIM2: Signaling pathways and functions in cancer suppression and host immunity
Guo, Z. S., & Qu, Z. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188630 · Cited by 50 · see citing works
Yadollahi, P., Jeon, Y., Ng, W. L., & Choi, I. (2021) · BMB Reports · doi:10.5483/bmbrep.2021.54.1.241 · Cited by 45 · see citing works
Long, Y., Guo, J., Chen, J., Sun, J., Wang, H., Peng, X., Wang, Z., Lai, W., Liu, N., Shu, L., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01224-3 · Cited by 45 · see citing works
Self-citationTRIM21‐Promoted FSP1 Plasma Membrane Translocation Confers Ferroptosis Resistance in Human Cancers
Gong, J., Liu, Y., Wang, W., He, R., Xia, Q., Chen, L., Zhao, C., Gao, Y., Shi, Y., Bai, Y., et al. (2023) · Advanced Science · doi:10.1002/advs.202302318 · Cited by 45 · see citing works
Self-citationLi, M., Shi, M., Hu, C., Chen, B., & Li, S. (2021) · Oncogene · doi:10.1038/s41388-021-01816-3 · Cited by 45 · see citing works
Huang, X., Yang, Z., Zhang, J., Wang, R., Fan, J., Zhang, H., Xu, R., Li, X., Yu, S., Long, L., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.712732 · Cited by 45 · see citing works
The Functional Roles of ISG15/ISGylation in Cancer
Yin, Y., Qin, H., Li, H., Shi, W., Bao, L., Xu, S., Yin, J., & Zheng, L. (2023) · Molecules · doi:10.3390/molecules28031337 · Cited by 43 · see citing works
TRP Channels Interactome as a Novel Therapeutic Target in Breast Cancer
Saldías, M. P., Maureira, D., Orellana‐Serradell, O., Silva, I., Lavanderos, B. J., Cruz, P., Torres, C., Cáceres, M., & Cerda, O. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.621614 · Cited by 42 · see citing works
Post-Translational Modifications of BRD4: Therapeutic Targets for Tumor
Liu, N., Ling, R., Tang, X., Yu, Y., Zhou, Y., & Chen, D. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.847701 · Cited by 42 · see citing works
Tu, Y., Xu, L., Fu, G., Wang, J., Xia, P., Tao, Z., Ye, Y., Hu, J., Cai, W., Zhu, H., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01494-8 · Cited by 48 · see citing works
Potential Biomarkers for Liver Cancer Diagnosis Based on Multi-Omics Strategy
Chen, F., Wang, J., Wu, Y. C., Gao, Q., & Zhang, S. J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.822449 · Cited by 41 · see citing works
Guo, Y., Tang, Y., Lu, G., & Gu, J. (2023) · Nutrients · doi:10.3390/nu15102259 · Cited by 39 · see citing works
Lin, Y., Lin, P., Lu, Y., Zheng, J., Zheng, Y., Huang, X., Zhao, X., & Cui, L. (2024) · Advanced Science · doi:10.1002/advs.202406318 · Cited by 39 · see citing works
Chen, Y., Yue, S., Yu, L., Cao, J., Liu, Y., Deng, A., Lu, Y., Yang, J., Li, Y., Du, J., et al. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s501773 · Cited by 39 · see citing works
Post-Translational Modifications That Drive Prostate Cancer Progression
Samaržija, I. (2021) · Biomolecules · doi:10.3390/biom11020247 · Cited by 39 · see citing works
Amani, J., Gorjizadeh, N., Younesi, S., Najafi, M., Ashrafi, A. M., Irian, S., Gorjizadeh, N., & Azizian, K. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103103 · Cited by 39 · see citing works
The molecular code of kidney cancer: A path of discovery for gene mutation and precision therapy
Xie, D., Li, G., Zheng, Z., Zhang, X., Wang, S., Jiang, B., Li, X., Wang, X., & Wu, G. (2024) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2024.101335 · Cited by 38 · see citing works
Wang, Q., Feng, Y., Peng, W., Ji, D., Zhang, Z., Qian, W., Li, J., Gu, Q., Zhang, D., Tang, J., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.02.041 · Cited by 38 · see citing works
Wang, X., Lv, X., Ma, J., & Xu, G. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108680 · Cited by 37 · see citing works
Clark, J., Kayed, R., Abate, G., Uberti, D. L., Kinnon, P., & Piccirella, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.835288 · Cited by 37 · see citing works
p53 at the crossroad between mitochondrial reactive oxygen species and necroptosis
Rius‐Pérez, S. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.07.022 · Cited by 37 · see citing works
Loss of SMURF2 expression enhances RACK1 stability and promotes ovarian cancer progression
Pi, Y., Feng, Q., Sun, F., Wang, Z., Zhao, Y., Chen, D., Liu, Y., & Lou, G. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01226-w · Cited by 36 · see citing works
Song, F., Hou, C., Huang, Y., Liang, J., Cai, H., Tian, G., Jiang, Y., Wang, Z., & Hou, J. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111228 · Cited by 34 · see citing works
Advancements in CRISPR/Cas systems for disease treatment
Xu, Y., Le, H., Wu, Q., Wang, N., & Gong, C. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.05.007 · Cited by 35 · see citing works
Regulation of Inflammatory Cell Death by Phosphorylation
Xu, W., & Huang, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.851169 · Cited by 34 · see citing works
The Elephant Evolved p53 Isoforms that Escape MDM2-Mediated Repression and Cancer
Padariya, M., Jooste, M.-L., Hupp, T., Fåhraeus, R., Vojtesek, B., Vollrath, F., Kalathiya, U., & Karakostis, K. (2022) · Molecular Biology and Evolution · doi:10.1093/molbev/msac149 · Cited by 33 · see citing works
Ismail, T., Alzneika, S., Riguene, E., Al-Maraghi, S., Alabdulrazzak, A., Al-Khal, N., Fetais, S., Thanassoulas, A., Farsi, H. F. A., & Nomikos, M. (2024) · Pharmaceuticals · doi:10.3390/ph17030333 · Cited by 32 · see citing works
Post-Translational Modification of ZEB Family Members in Cancer Progression
Park, M. K., Lee, H., & Lee, C. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315127 · Cited by 32 · see citing works
Lenvatinib resistance mechanism and potential ways to conquer
Bo, W., & Chen, Y. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1153991 · Cited by 32 · see citing works
Zagirova, D., Pushkov, S., Leung, G. H. D., Liu, B. H. M., Urban, A., Sidorenko, D., Kalashnikov, A., Kozlova, E., Naumov, V., Pun, F. W., et al. (2023) · Aging · doi:10.18632/aging.205055 · Cited by 32 · see citing works
The role of acetylation and deacetylation in cancer metabolism
Wang, C., & Ma, X. (2025) · Clinical and Translational Medicine · doi:10.1002/ctm2.70145 · Cited by 31 · see citing works
Alharbi, H. M. (2024) · Drug Design, Development and Therapy · doi:10.2147/dddt.s441325 · Cited by 22 · see citing works
Garufi, A., Pistritto, G., D’Orazi, V., Cirone, M., & D’Orazi, G. (2022) · Biomolecules · doi:10.3390/biom12030461 · Cited by 30 · see citing works
Yousuf, M., Shamsi, A., Khan, S., Κhan, P., Shahwan, M. J., Elasbali, A. M., Haque, Q. M. R., & Hassan, M. I. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.06.013 · Cited by 33 · see citing works
DUSP4 promotes esophageal squamous cell carcinoma progression by dephosphorylating HSP90β
Zhou, L., Yao, N., Yang, L., Liu, K., Qiao, Y., Huang, C., Du, R., Yeung, Y. T., Liu, W., Cheng, D., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112445 · Cited by 29 · see citing works
Huaier Extract Inhibits Prostate Cancer Growth via Targeting AR/AR-V7 Pathway
Liu, Z., Liu, C., Yan, K., Liu, J., Fang, Z., & Fan, Y. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.615568 · Cited by 29 · see citing works
Protein Acetylation at the Interface of Genetics, Epigenetics and Environment in Cancer
Harachi, M., Masui, K., Cavenee, W. K., Mischel, P. S., & Shibata, N. (2021) · Metabolites · doi:10.3390/metabo11040216 · Cited by 29 · see citing works
Optimized data-independent acquisition approach for proteomic analysis at single-cell level
Wang, Y., Lih, T. M., Chen, L., Xu, Y., Kuczler, M. D., Cao, L., Pienta, K. J., Amend, S. R., & Zhang, H. (2022) · Clinical Proteomics · doi:10.1186/s12014-022-09359-9 · Cited by 29 · see citing works
Self-citationAshrafian, S., Zarrineh, M., Jensen, P., Nawrocki, A., Rezadoost, H., Ansari, A. M., Farahmand, L., Ghassempour, A., & Larsen, M. R. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00168 · Cited by 28 · see citing works
Sheng, Z., Yu, J., Deng, K., Andrade-Barazarte, H., Zemmar, A., Li, S., Li, N., Yan, Z., Chen, Z., Sun, Y. Y., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.584988 · Cited by 28 · see citing works
Xia, Q., Sun, J., Xun, Y., Xiao, J., Liu, C., Xu, J., An, Y., Xu, M., Liu, Z., Wang, S., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.864156 · Cited by 28 · see citing works
Ali, S., Noreen, A., Qamar, A., Zafar, I., Ain, Q., Nafidi, H., Jardan, Y. A. B., Bourhia, M., Rashid, S., & Sharma, R. (2023) · Frontiers in Chemistry · doi:10.3389/fchem.2023.1174363 · Cited by 28 · see citing works
Therapeutic Implications of PTEN in Non-Small Cell Lung Cancer
Sirhan, Z., Alojair, R., Thyagarajan‐Sahu, A., & Sahu, R. P. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15082090 · Cited by 28 · see citing works
Harnessing the therapeutic potential of extracellular vesicles for cancer treatment
Zhang, Y., Xiao, Y., Sun, G., Jin, X., Guo, L., Li, T., & Yin, H. H. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.05.001 · Cited by 27 · see citing works
Significance of African Diets in Biotherapeutic Modulation of the Gut Microbiome
Isibor, P. O., Akinduti, P. A., Aworunse, O. S., Oyewale, J., Oshamika, O. O., Ugboko, H. U., Taiwo, O., Ahuekwe, E. F., Obafemi, Y. D., Onibokun, E. A., et al. (2021) · Bioinformatics and Biology Insights · doi:10.1177/11779322211012697 · Cited by 30 · see citing works
Ubiquitination and SUMOylation: Protein Homeostasis Control Over Cancer
Dai, X., Zhang, T., & Hua, D. (2021) · Epigenomics · doi:10.2217/epi-2021-0371 · Cited by 27 · see citing works
HuR Protein in Hepatocellular Carcinoma: Implications in Development, Prognosis and Treatment
Papatheofani, V., Levidou, G., Sarantis, P., Koustas, E., Karamouzis, M. V., Pergaris, A., Kouraklis, G. P., & Theocharis, S. E. (2021) · Biomedicines · doi:10.3390/biomedicines9020119 · Cited by 26 · see citing works
Mao, F., Liu, K., Wong, N.-K., Zhang, X., Yi, W., Xiang, Z., Xiao, S., Yu, Z., & Zhang, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.746017 · Cited by 26 · see citing works
Planas‐Paz, L., Pliego‐Mendieta, A., Hagedorn, C., Aguilera‐Garcia, D., Haberecker, M., Arnold, F. M., Herzog, M., Bankel, L., Guggenberger, R., Steiner, S., et al. (2023) · EMBO Molecular Medicine · doi:10.15252/emmm.202216863 · Cited by 26 · see citing works
Colorectal cancer: the APC-lncRNA link
Morin, P. J. (2019) · Journal of Clinical Investigation · doi:10.1172/jci125985 · Cited by 25 · see citing works
SUMOylation and NEDDylation in Primary and Metastatic Cancers to Bone
Gomarasca, M., Lombardi, G., & Maroni, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.889002 · Cited by 25 · see citing works
Liu, W., Zeng, Y., Hao, X., Wang, X., Liu, J., Gao, T., Wang, M., Zhang, J., Huo, M., Hu, T., et al. (2023) · 癌症:英文版 · doi:10.1002/cac2.12479 · Cited by 25 · see citing works
Hu, Q., Shi, Y., Wang, H., Li, B., & Xu, Z. (2025) · Experimental Hematology and Oncology · doi:10.1186/s40164-025-00627-6 · Cited by 26 · see citing works
Analysis of tripartite motif (TRIM) family gene expression in prostate cancer bone metastases
Offermann, A., Kang, D., Watermann, C., Weingart, A., Hupe, M. C., Saraji, A. A., Stegmann-Frehse, J., Kruper, R., Schüle, R., Pantel, K., et al. (2021) · Carcinogenesis · doi:10.1093/carcin/bgab083 · Cited by 24 · see citing works
E3 ubiquitin ligase TRIM31: A potential therapeutic target
Deng, N.-H., Tian, Z., Zou, Y.-J., & Quan, S.-B. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116846 · Cited by 23 · see citing works
Catalpol Ameliorates Neurotoxicity in N2a/APP695swe Cells and APP/PS1 Transgenic Mice
Du, J., Liu, J., Huang, X., Li, Y., Song, D., Li, Q., Lin, J., Li, B., & Li, L. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00524-4 · Cited by 23 · see citing works
Plasma exosome-derived circGAPVD1 as a potential diagnostic marker for colorectal cancer
Li, T., Zhou, T., Wu, J., Lv, H., Zhou, H., Du, M., Zhang, X., Wu, N., Gong, S., Ren, Z., et al. (2023) · Translational Oncology · doi:10.1016/j.tranon.2023.101652 · Cited by 23 · see citing works
- Authors
- Chen, L., Liu, S., & Tao, Y.
- Affiliations
- Central South University (CN)
- Corresponding author
- Tao, Yongguang
- Venue
- Signal Transduction and Targeted Therapy
- Published
- 2020-06-10
- Volume
- 5
- Issue
- 1
- Pages
- 90-90
- ISSN
- 2059-3635 (ISSN-L)
- PMC
- PMC7293209
- OpenAlex
- W3035758066
- Cited by
- 449
- References
- 522
- Citations by year
- 2026: 52 · 2025: 89 · 2024: 110 · 2023: 87 · 2022: 65 · 2021: 38 · 2020: 3 · 2019: 4 · 2018: 1
- FWCI
- 5.23
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Signal Transduction and Targeted Therapy (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81672787, 111 Project, 81672991, 81874139)
- Higher Education Discipline Innovation Project
- Overseas Expertise Introduction Project for Discipline Innovation (“111” Project)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- tumor suppressor, post-translational modification, retinoblastoma protein, p53, PTEN, phosphorylation, SUMOylation, acetylation, tumor suppressor network, cell cycle regulation, carcinogenesis, cancer therapy, therapeutic target
- MeSH terms
- Humans, Neoplasms, Protein Processing, Post-Translational, Genes, Tumor Suppressor, Tumor Suppressor Protein p53, Retinoblastoma Protein, PTEN Phosphohydrolase, Carcinogenesis
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