Cited by 914Cancer-related Molecular PathwaysPI3K/AKT/mTOR signaling in cancerCancer Mechanisms and Therapy

The DOI matches its Crossref record; 148 of the 149 references it cites were found in a registry or an index.

Awakening guardian angels: drugging the p53 pathway

Brown, Christopher J., Lain, Sonia, Verma, Chandra S., Fersht, Alan R., Lane, David P.·2009·Nature Reviews Cancer

Open this paper in CoChat — free account

Abstract

Currently, around 11 million people are living with a tumour that contains an inactivating mutation of TP53 (the human gene that encodes p53) and another 11 million have tumours in which the p53 pathway is partially abrogated through the inactivation of other signalling or effector components. The p53 pathway is therefore a prime target for new cancer drug development, and several original approaches to drug discovery that could have wide applications to drug development are being used. In one approach, molecules that activate p53 by blocking protein-protein interactions with MDM2 are in early clinical development. Remarkable progress has also been made in the development of p53-binding molecules that can rescue the function of certain p53 mutants. Finally, cell-based assays are being used to discover compounds that exploit the p53 pathway by either seeking targets and compounds that show synthetic lethality with TP53 mutations or by looking for non-genotoxic activators of the p53 response.

Integrity signals

Registry

Crossref · 10.1038/nrc2763

Cites

148 of 148 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Activating Mutations in the Epidermal Growth Factor Receptor Underlying Responsiveness of Non–Small-Cell Lung Cancer to Gefitinib
Lynch, T. J., Bell, D. W., Sordella, R., Gurubhagavatula, S., Okimoto, R. A., Brannigan, B. W., Harris, P. L., Haserlat, S. M., Supko, J. G., Haluska, F. G., et al. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040938 · Cited by 11,486
EGFR Mutations in Lung Cancer: Correlation with Clinical Response to Gefitinib Therapy
Paez, J. G., Jänne, P. A., Lee, J. C., Tracy, S., Greulich, H., Gabriel, S., Herman, P., Kaye, F. J., Lindeman, N., Boggon, T. J., et al. (2004) · Science · doi:10.1126/science.1099314 · Cited by 9,368
Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
Farmer, H., McCabe, N., Lord, C. J., Tutt, A. N. J., Johnson, D. A., Richardson, T. B., Santarosa, M., Dillon, K. J., Hickson, I., Knights, C., et al. (2005) · Nature · doi:10.1038/nature03445 · Cited by 6,683
p53, guardian of the genome
Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138
Self-citation
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
EGF receptor gene mutations are common in lung cancers from “never smokers” and are associated with sensitivity of tumors to gefitinib and erlotinib
Pao, W., Miller, V., Zakowski, M., Doherty, J., Politi, K., Sarkaria, I., Singh, B., Heelan, R., Rusch, V., Fulton, L., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405220101 · Cited by 4,338
An inhibitor of Bcl-2 family proteins induces regression of solid tumours
Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,407
The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
Momand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
Xue, W., Zender, L., Miething, C., Dickins, R. A., Hernando, E., Krizhanovsky, V., Cordon-Cardo, C., & Lowe, S. W. (2007) · Nature · doi:10.1038/nature05529 · Cited by 2,473

Flagged first, then by citations

Show all 149 references

1 of the 149 references couldn’t be matched to a known paper.

Sorted by citations

Items 601–700 of 914

Antitumor Activity of Bioactive Compounds from Rapana venosa against Human Breast Cell Lines
Petrova, M., Vlahova, Z., Schröder, M., Todorova, J., Tzintzarov, A., Gospodinov, A. G., Velkova, L. G., Kaynarov, D., Dolashki, A., Dolashka, P. A., et al. (2023) · Pharmaceuticals · doi:10.3390/ph16020181 · Cited by 12
Convergent TP53 loss and evolvability in cancer
Mansur, M. B., & Greaves, M. F. (2023) · BMC Ecology and Evolution · doi:10.1186/s12862-023-02146-6 · Cited by 13
Non-Structural protein 1 (NS1) gene of Canine Parvovirus-2 regresses chemically induced skin tumors in Wistar rats
Santra, L., Rajmani, R. S., Kumar, G. V. P. P. S. R., Saxena, S., Dhara, S. K., Kumar, A., Sahoo, A. P., Singh, L. V., Desai, G. S., Chaturvedi, U., et al. (2014) · Research in Veterinary Science · doi:10.1016/j.rvsc.2014.07.024 · Cited by 12
Endosomal sorting complexes required for ESCRTing cells toward death during neurogenesis, neurodevelopment and neurodegeneration
Kaul, Z., & Chakrabarti, O. (2018) · Traffic · doi:10.1111/tra.12569 · Cited by 12
Multifaceted behavior of PEST sequence enriched nuclear proteins in cancer biology and role in gene therapy
Sarfraz, M., Afzal, A., Khattak, S., Saddozai, U. A. K., Li, H., Zhang, Q., Madni, A., Haleem, K. S., Duan, S., Wu, D., et al. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30011 · Cited by 14
Characteristics and survival of patients with advanced cancer and p53 mutations
Said, R., Ye, Y., Hong, D. S., Jankú, F., Fu, S., Naing, A., Wheler, J. J., Kurzrock, R., Thomas, C. G., Palmer, G. A., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2004 · Cited by 12
Counteracting MDM2‐induced HIPK2 downregulation restores HIPK2/p53 apoptotic signaling in cancer cells
Nardinocchi, L., Puca, R., Givol, D., & D’Orazi, G. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.09.018 · Cited by 12
A p53 Axis Regulates B Cell Receptor-Triggered, Innate Immune System-Driven B Cell Clonal Expansion
Lee, H., Haque, S., Nieto, J., Trott, J., Inman, J. K., McCormick, S. A., Chiorazzi, N., & Mongini, P. K. A. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103037 · Cited by 13
Phase Separation Enhanced PROTAC for Highly Efficient Protein Degradation
Yu, X., Hu, W., Dong, H., Zhao, T., Wang, X., Chen, L., Xue, S., Li, J., & Luo, S. (2024) · Biomacromolecules · doi:10.1021/acs.biomac.4c00424 · Cited by 11
Female‐specific mechanisms of meiotic initiation and progression in mammalian oocyte development
Shimada, R., & Ishiguro, K. (2024) · Genes to Cells · doi:10.1111/gtc.13152 · Cited by 11
The broad-spectrum anti-DNA virus agent cidofovir inhibits lung metastasis of virus-independent, FGF2-driven tumors
Liekens, S., Noppen, S., Gijsbers, S., Sienaert, R., Ronca, R., Tobia, C., & Presta, M. (2014) · Oncotarget · doi:10.18632/oncotarget.3079 · Cited by 11
Ion mobility and Top-down MS complementary approaches for the structural analysis of protein models bound to anticancer metallodrugs
Escribano, E., Madurga, S., Vilaseca, M., & Moreno, V. (2014) · Inorganica Chimica Acta · doi:10.1016/j.ica.2014.07.052 · Cited by 11
TP53 mutant cell lines selected for resistance to MDM2 inhibitors retain growth inhibition by MAPK pathway inhibitors but a reduced apoptotic response
Wu, C., Koay, T. S., Ho, Y.-H., Lovat, P. E., & Lunec, J. (2019) · Cancer Cell International · doi:10.1186/s12935-019-0768-3 · Cited by 11
WIP1 Inhibition by GSK2830371 Potentiates HDM201 through Enhanced p53 Phosphorylation and Activation in Liver Adenocarcinoma Cells
Wu, C., Mahdi, A., Huang, C., Chen, C., Pan, Y., Chang, J. W., Chen, J., Yeh, C., & Lunec, J. (2021) · Cancers · doi:10.3390/cancers13153876 · Cited by 11
Therapeutic reactivation of mutant p53 protein by quinazoline derivatives
Sutherland, H. S., Hwang, I. Y., Marshall, E. S., Lindsay, B. S., Denny, W. A., Gilchrist, C. A., Joseph, W. R., Greenhalgh, D., Richardson, E., Kestell, P., et al. (2011) · Investigational New Drugs · doi:10.1007/s10637-011-9744-z · Cited by 13
PRIMA-1 induces caspase-mediated apoptosis in acute promyelocytic leukemia NB4 cells by inhibition of nuclear factor-κB and downregulation of Bcl-2, XIAP, and c-Myc
Farhadi, E., Safa, M., Sharifi, A. M., & Bashash, D. (2016) · Anti-Cancer Drugs · doi:10.1097/cad.0000000000000426 · Cited by 11
E3 Ubiquitin Ligases: Structures, Biological Functions, Diseases, and Therapy
Wang, H., Peng, J., Li, H., Lan, Y., Guo, J., Qiu, Q., & Huang, X. (2025) · MedComm · doi:10.1002/mco2.70528 · Cited by 13
Elucidating the Mechanisms of R248Q Mutation-Enhanced p53 Aggregation and Its Inhibition by Resveratrol
Liu, Q., Li, L., Yu, Y., & Wei, G. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c04700 · Cited by 11
New Nano-Silica Supported Basic Ionic Liquids-Catalyzed Multicomponent Synthesis of imidazo [1,2-a] Pyridines Under Solvent-Free Conditions
Kheradmand, Y. A., Salimi, F., & Moghanlou, A. O. (2023) · Catalysis Letters · doi:10.1007/s10562-023-04534-5 · Cited by 10
Donafenib activates the p53 signaling pathway in hepatocellular carcinoma, induces ferroptosis, and enhances cell apoptosis
Liang, J., Chen, M., Yan, G., Hoa, P. T. T., Wei, S., Huang, H., Xie, Q., Luo, X., Mo, S., & Han, C. (2025) · Clinical and Experimental Medicine · doi:10.1007/s10238-024-01550-6 · Cited by 10
MDM2 in Tumor Biology and Cancer Therapy: A Review of Current Clinical Trials
Russano, F., Sturlese, M., Dall’Olmo, L., Callegarin, F., Brugnolo, D., Fiore, P. D., Patti, V., Purpura, A. H.-S., Moro, S., Rastrelli, M., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010099 · Cited by 14
Lessons from microRNA biology: Top key cellular drivers of Autosomal Dominant Polycystic Kidney Disease
Fragiadaki, M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166358 · Cited by 10
G-Network Modelling Based Abnormal Pathway Detection in Gene Regulatory Networks
Kim, H., Çetin-Atalay, R., & Erol Gelenbe, A. (2011) · Springer eBooks · doi:10.1007/978-1-4471-2155-8_32 · Cited by 10
Decrease of mitochondrial p53 during late apoptosis is linked to its dephosphorylation on serine 20
Castrogiovanni, C., Vandaudenard, M., Waterschoot, B., Backer, O. D., & Dumont, P. (2015) · Cancer Biology & Therapy · doi:10.1080/15384047.2015.1070978 · Cited by 11
D ‐Peptide‐Based Drug Discovery Aided by Chemical Protein Synthesis
Zhao, L., & Lu, W. (2011) · Israel Journal of Chemistry · doi:10.1002/ijch.201100085 · Cited by 10
The Roles of MicroRNAs in Glioblastoma Biology and Biomarker
Sasayama, T., Tanaka, K., & Kohmura, E. (2016) · InTech eBooks · doi:10.5772/63243 · Cited by 9
p53 in the Clinics
Hainaut, P. L., Wiman, K. G., & Olivier, M. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3676-8 · Cited by 10
Isolation of a peptide containing d-amino acid residues that inhibits the α-helix-mediated p53–MDM2 interaction from a one-bead one-compound library
Morimoto, J., Hosono, Y., & Sando, S. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.01.001 · Cited by 10
Prognostic value of the combined expression of tumor-associated trypsin inhibitor (TATI) and p53 in patients with bladder cancer undergoing radical cystectomy
Liu, A., Xue, Y., Liu, F., Tan, H., Xiong, Q., Zeng, S., Zhang, Z., Gao, X., Sun, Y., & Xu, C. (2019) · Cancer Biomarkers · doi:10.3233/cbm-182143 · Cited by 10
Cisplatin binds to the MDM2 RING finger domain and inhibits the ubiquitination activity
Cao, K., Ding, X., Sheng, Y., Wang, Y., & Liu, Y. (2020) · Chemical Communications · doi:10.1039/d0cc00203h · Cited by 9
Mutant TP53 interacts with BCAR1 to contribute to cancer cell invasion
Guo, A. K., Itahana, Y., Seshachalam, V. P., Chow, H. Y., Ghosh, S., & Itahana, K. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-01124-9 · Cited by 10
Tracing the protectors path from the germ line to the genome
Coutandin, D., Ou, H. D., Löhr, F., & Dötsch, V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001069107 · Cited by 10
IGF2: The Achilles' heel of p53‐deficiency?
Clermont, F. F., Nittner, D., & Marine, J. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201201509 · Cited by 10
Bridged Analogues for p53-Dependent Cancer Therapy Obtained by S-Alkylation
Micewicz, E. D., Sharma, S. K., Waring, A. J., Luong, H. T., McBride, W. H., & Ruchala, P. P. (2015) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-015-9487-3 · Cited by 11
Identification of p53 Activators in a Human Microarray Compendium
Corton, J. C., Witt, K. L., & Yauk, C. L. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00052 · Cited by 10
Structural Studies on Mechanisms to Activate Mutant p53
Viadiu, H., Fronza, G., & Inga, A. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9211-0_7 · Cited by 10
Avian Models for Human Carcinogenesis—Recent Findings from Molecular and Clinical Research
Niebora, J., Data, K., Domagała, D., Józkowiak, M., Barrett, S., Abbariki, T. N., Bryja, A., Kulus, M., Woźniak, S., Ziemak, H., et al. (2024) · Cells · doi:10.3390/cells13211797 · Cited by 9
The Roles of Ubiquitination Factor E4B (UBE4B) in the Postoperative Prognosis of Patients with Renal Cell Carcinoma and in Renal Tumor Cells Growth and Metastasis
Huang, X., Hao, S., Zhou, Z.-Q., Huang, B., Fang, J., Tang, Y., Zhang, J., & Xia, J. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s229577 · Cited by 10
A small peptide derived from p53 linker region can resume the apoptotic activity of p53 by sequestering iASPP with p53
Qiu, S., Cai, Y., Gao, X., Gu, S.-Z., & Liu, Z.-J. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.10.044 · Cited by 9
Synthesis of Chiral Alkenyl Cyclopropane Amino Acids for Incorporation into Stapled Peptides
Yuen, T. Y., Brown, C. J., Tan, Y. S., & Johannes, C. W. (2019) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.9b02659 · Cited by 9
Self-citation
How does a hydrocarbon staple affect peptide hydrophobicity?
Sim, A. Y. L., & Verma, C. S. (2015) · Journal of Computational Chemistry · doi:10.1002/jcc.23859 · Cited by 10
Self-citation
p53 transcriptional pathways in breast cancer: the good, the bad and the complex
Thompson, A. M., & Lane, D. P. (2009) · The Journal of Pathology · doi:10.1002/path.2674 · Cited by 9
Self-citation
A subset of microRNAs potentially acts as a convergent hub for upstream transcription factors in cancer cells
Yoshida (2010) · Oncology Reports · doi:10.3892/or_00000995 · Cited by 9
Studies on the role of NS3 and NS5A non-structural genes of hepatitis C virus genotype 3a local isolates in apoptosis
Sabri, S., Idrees, M., Rafique, S., Ali, A., & Iqbal, M. (2014) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2014.01.010 · Cited by 9
Immunohistochemical study of p53, Ki-67, epidermal growth factor receptor, and sex-determining region Y-box 2 in squamous cell carcinoma of tongue
Gaopande, V. L., Bhayekar, P., Joshi, A. R., & Jadhav, A. (2016) · BLDE University Journal of Health Sciences · doi:10.4103/2468-838x.196089 · Cited by 9
Tetra-substituted pyrrole derivatives act as potent activators of p53 in melanoma cells
Proto, M., Fiore, D., Forte, G., Cuozzo, P., Ramunno, A., Fattorusso, C., Gazzerro, P., Pascale, M. C., & Franceschelli, S. (2019) · Investigational New Drugs · doi:10.1007/s10637-019-00813-4 · Cited by 9
Optimized Inhibitors of MDM2 via an Attempted Protein‐Templated Reductive Amination
van der Vlag, R., Ünver, M. Y., Felicetti, T., Twarda‐Clapa, A., Kassim, F., Ermiş, Ç., Neochoritis, C. G., Musielak, B., Łabuzek, B., Dömling, A. S. S., et al. (2019) · ChemMedChem · doi:10.1002/cmdc.201900574 · Cited by 8
Targeting p53 activation: Recent therapeutic advances in cancer and diabetic macular edema
Wang, Z., Zhang, S., Mélita, I. L., & Zhao, Y. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117909 · Cited by 10
Emerging Target Families: Intractable Targets
Knapp, S. (2015) · Handbook of experimental pharmacology · doi:10.1007/164_2015_28 · Cited by 9
A Left‐Handed Solution to Peptide Inhibition of the p53–MDM2 Interaction
Liu, M., Pazgier, M., Li, C., Yuan, W., Li, C., & Lu, W. (2010) · Angewandte Chemie · doi:10.1002/ange.201000329 · Cited by 10
Clinical Significance of the Wild Type p53-Induced Phosphatase 1 Expression in Invasive Breast Cancer
Inoue, Y., Yamashita, N., Kitao, H., Tanaka, K., Saeki, H., Oki, E., Oda, Y., Tokunaga, E., & Maehara, Y. (2017) · Clinical Breast Cancer · doi:10.1016/j.clbc.2017.11.008 · Cited by 10
Homogenous TP53mut-associated tumor biology across mutation and cancer types revealed by transcriptome analysis
Romanovsky, E., Kluck, K., Ourailidis, I., Menzel, M., Beck, S., Ball, M., Kazdal, D. N., Christopoulos, P., Schirmacher, P., Stiewe, T., et al. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01413-1 · Cited by 9
Anticancer agents derived from marine algae
Boopathy, N. S., & Kathiresan, K. (2013) · Elsevier eBooks · doi:10.1533/9780857098689.2.307 · Cited by 9
Role of altholactone in inducing type II apoptosis signalling pathway and expression of cancer‐related genes in cervical carcinoma HeLa cell line
Uthaisang‐Tanechpongtamb, W., Sriyabhaya, P., & Wilairat, P. (2013) · Cell Biology International · doi:10.1002/cbin.10059 · Cited by 8
Molecular biomarkers of glioblastoma: current targets and clinical implications
Yoshimoto, K., Mizoguchi, Hata, Amano, Nakamizo, & Sasaki (2012) · Current Biomarker Findings · doi:10.2147/cbf.s25590 · Cited by 7
Role of Wnt-p53-Nox Signaling Pathway in Cancer Development and Progression
Kumar, D., Sharma, S., Verma, S., Kumar, P., & Ambasta, R. K. (2015) · Journal of Advances in Medicine and Medical Research · doi:10.9734/bjmmr/2015/17996 · Cited by 9
The tobacco carcinogen NNK disturbs mitotic chromosome alignment by interrupting p53 targeting to the centrosome
Park, J. E., Jang, Y. L., & Jang, C. (2017) · Toxicology Letters · doi:10.1016/j.toxlet.2017.09.019 · Cited by 8
Novel 4-(3-phenylpropionamido), 4-(2-phenoxyacetamido) and 4-(cinnamamido) substituted benzamides bearing the pyrazole or indazole nucleus: synthesis, biological evaluation and mechanism of action
Raffa, D., D’Anneo, A., Plescia, F., Daidone, G., Lauricella, M., & Maggio, B. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.10.055 · Cited by 8
Tumor Suppressor Genes
Cheng, Y. (2012) · InTech eBooks · doi:10.5772/1337 · Cited by 9
Characterisation of the p53 pathway in cell lines established from TH-MYCN transgenic mouse tumours
Chen, L., Esfandiari, A., Reaves, W., Vu, A. T., Hogarty, M. D., Lunec, J., & Tweddle, D. A. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4261 · Cited by 8
Leveraging protein quaternary structure to identify oncogenic driver mutations
Ryslik, G., Cheng, Y., Modis, Y., & Zhao, H. (2016) · BMC Bioinformatics · doi:10.1186/s12859-016-0963-3 · Cited by 7
The Crusade against Mutant p53: Does the COMPASS Point to the Holy Grail?
Abraham, C. G., & Espinosa, J. M. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.09.019 · Cited by 7
MPK-09, a Small Molecule Inspired from Bioactive Styryllactone Restores the Wild-Type Function of Mutant p53
Metri, P. K., Naz, S., Kondaiah, P., & Prasad, K. R. (2013) · ACS Chemical Biology · doi:10.1021/cb3005929 · Cited by 7
p53 in Head and Neck Squamous Cell Carcinoma
Philips, R. H. W., & Pan, Q. (2017) · Springer eBooks · doi:10.1007/978-94-024-1084-6_5 · Cited by 7
LQFM030 reduced Ehrlich ascites tumor cell proliferation and VEGF levels
da Mota, M. F., de Carvalho, F. S., de Ávila, R. I., de Ávila, P. H. M., Cortez, A. P., Menegatti, R., Sabino, J. R., dos Santos, T. R. M., Gomes, S. A., da Cunha, L. C., et al. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.12.029 · Cited by 7
Sensitive and simultaneous surface plasmon resonance detection of free and p53-bound MDM2 proteins from human sarcomas
Wu, L., Tang, H., Hu, S., Xia, Y., Lu, Z., Fan, Y., Wang, Z., Yi, X., Zhou, F., & Wang, J. (2018) · The Analyst · doi:10.1039/c7an01918a · Cited by 7
Simultaneous measurement of p53:Mdm2 and p53:Mdm4 protein-protein interactions in whole cells using fluorescence labelled foci
Frosi, Y., Inoue, K., Ramlan, S. R., Lane, D. P., Watanabe, T., & Brown, C. J. (2019) · Scientific Reports · doi:10.1038/s41598-019-54123-z · Cited by 7
Self-citation
Protein destabilization and degradation as a mechanism for hereditary disease
Nielsen, S. V., Schenstrøm, S. M., Christensen, C. E., Stein, A., Lindorff‐Larsen, K., & Hartmann‐Petersen, R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819132-3.00006-3 · Cited by 8
Design, Synthesis, and Biological Evaluation of Aromatic Amide-Substituted Benzimidazole-Derived Chalcones. The Effect of Upregulating TP53 Protein Expression
Wu, L., Yang, Y., Wang, Z., Wu, X., Su, F., Li, M., Jing, X., & Han, C. (2020) · Molecules · doi:10.3390/molecules25051162 · Cited by 8
Design and Preparation of β‐Lactam Derivatives Bearing Phenanthrenimidazole as Cytotoxic Agents
Alborz, M., Pournejati, R., Rad, J. A., Jarrahpour, A., Karbalaei‐Heidari, H. R., Brunel, J. M., & Turos, E. (2022) · ChemistrySelect · doi:10.1002/slct.202202306 · Cited by 7
Alternative strategies for targeting mouse double minute 2 activity with small molecules: novel patents on the horizon?
Macchiarulo, A., Giacchè, N., Mancini, F., Puxeddu, E., Moretti, F., & Pellicciari, R. (2011) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2011.546349 · Cited by 7
Jetzt wird es ernst: strukturbasiertes Design von Mdm2/Mdmx‐p53‐Inhibitoren
Popowicz, G. M., Dömling, A. S. S., & Holak, T. A. (2011) · Angewandte Chemie · doi:10.1002/ange.201003863 · Cited by 7
Biological evaluation of MR36, a novel non-polyglutamatable thymidylate synthase inhibitor that blocks cell cycle progression in melanoma cell lines
Giudice, S., Benassi, L., Bertazzoni, G., Veratti, E., Morini, D., Azzoni, P., Costi, M. P., Venturelli, A., Pirondi, S., Seidenari, S., et al. (2011) · Investigational New Drugs · doi:10.1007/s10637-011-9733-2 · Cited by 7
Natural Functions and Structure–Activity Relationships of Cyclotides
Oguis, G. K., Kan, M., & Craik, D. J. (2015) · Advances in botanical research · doi:10.1016/bs.abr.2015.10.001 · Cited by 7
Pro‑apoptotic effects of Kangfuxin on human stomach cancer cells and its underlying mechanism
Ma, X., Sun, J., Ye, W., Huang, Y., Sun, C. M., Tao, Y., Wang, T., Cong, W., & Geng, F. (2018) · Oncology Letters · doi:10.3892/ol.2018.8713 · Cited by 7
Sliding mode controller–observer pair for p53 pathway
Azam, M. R., Utkin, V. I., Uppal, A. A., & Bhatti, A. I. (2019) · IET Systems Biology · doi:10.1049/iet-syb.2018.5121 · Cited by 7
Inhibiting mechanism of small molecule toward the p53‐ MDM 2 interaction: A molecular dynamic exploration
Chen, J., Wang, J., Pang, L., & Zhu, W. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13345 · Cited by 7
MDM4 as a Prognostic Factor for Patients With Gastric Cancer With Low Expression of p53
Zhang, X., Yamamoto, Y., Wang, X., Sato, M., Imanishi, M., Sugaya, A., Hirose, M., Endo, S., Moriwaki, T., Yamato, K., et al. (2021) · Anticancer Research · doi:10.21873/anticanres.14906 · Cited by 6
Structural Basis of Mutation-Dependent p53 Tetramerization Deficiency
Rigoli, M., Spagnolli, G., Lorengo, G., Monti, P., Potestio, R., Biasini, E., & Inga, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147960 · Cited by 6
Conformationally Controlled sp 3 ‐Hydrocarbon‐Based α‐Helix Mimetics
Dewis, L. I., Madhavachary, R., Williams, C., Chiarparin, E., Myers, E. L., Butts, C. P., & Aggarwal, V. K. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202301209 · Cited by 7
The end of KRAS, and other, cancers? A new way forward
Mallucci, L., & Wells, V. E. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.11.018 · Cited by 6
Hitting a Moving Target: Targeting Transient Protein States
Bauer, M. R., & Boeckler, F. M. (2013) · Structure · doi:10.1016/j.str.2013.11.003 · Cited by 6
MicroRNAs in breast cancer and breast cancer stem cells and their potential for breast cancer therapy
Li, J., Shen, L., Xiao, X., & Fang, L. (2013) · Chinese Medical Journal · doi:10.3760/cma.j.issn.0366-6999.20111729 · Cited by 6
Nutlin-3 inhibits androgen receptor-driven c-FLIP expression, resulting in apoptosis of prostate cancer cells
Logan, I. R., McClurg, U. L., Jones, D. L., O’Neill, D. J., Shaheen, F. S., Lunec, J., Gaughan, L., & Robson, C. N. (2016) · Oncotarget · doi:10.18632/oncotarget.12542 · Cited by 6
Case report: A unique presentation of a high-grade neuroepithelial tumor with EWSR1::PATZ1 fusion with diagnostic, molecular, and therapeutic insights
Ene, A., Di, J., Neltner, J. H., Pittman, T. A., Arnold, S. M., Kolesar, J., Villano, J. L., Bachert, S. E., & Allison, D. B. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1094274 · Cited by 6
Therapeutic Targeting of p53-Mediated Apoptosis Pathway in Head and Neck Squamous Cell Carcinomas: Current Progress and Challenges
Ichwan, S. J. A., Taher, M., Ohtani, K., & Ike, M.-A. (2012) · InTech eBooks · doi:10.5772/27968 · Cited by 8
Characterization of Hydration Properties in Structural Ensembles of Biomolecules
Pradhan, M. R., Nguyen, M. N., Kannan, S., Fox, S. J., Kwoh, C. K., Lane, D. P., & Verma, C. S. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00453 · Cited by 6
Self-citation
Targeting Protein Synthesis, Folding, and Degradation Pathways in Cancer
Pasqua, E., Wilding, B., Cheeseman, M. D., & Jones, K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12395-9 · Cited by 6
Oncogenic R248W mutation induced conformational perturbation of the p53 core domain and the structural protection by proteomimetic amyloid inhibitor ADH-6
Liu, Q., Yu, Y., & Wei, G. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d4cp02046d · Cited by 5
SNAr Reactive Pyrazine Derivatives as p53-Y220C Cleft Binders with Diverse Binding Modes
Klett, T., Stahlecker, J., Schwer, M., Jaag, S., Masberg, B., Knappe, C., Lämmerhofer, M., Stehle, T., & Boeckler, F. M. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s513792 · Cited by 6
In-silico approaches to unravel the efficacy of naturally occurring C–C and C–O–C type biflavonoids towards the inhibition of MDM2–p53 interactions
Karmakar, S., Sen, A., Majumdar, S., Singh, B., Pramanik, A., & Mondal, S. (2025) · Discover Chemistry. · doi:10.1007/s44371-025-00167-2 · Cited by 5
Trp53 regulates platelets in bone marrow via the PI3K pathway
Yang, M., Liu, Q., Niu, T., Kuang, J., Zhang, X., Jiang, L., Li, S., He, X., Wang, L., & Li, J. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8850 · Cited by 5
Network Analysis of Molecular Dynamics Sectors in the p53 Protein
Fabry, J. D., & Thayer, K. M. (2022) · ACS Omega · doi:10.1021/acsomega.2c05635 · Cited by 6
Ectopically Expressed Meiosis-Specific Cancer Testis Antigen HORMAD1 Promotes Genomic Instability in Squamous Cell Carcinomas
Gantchev, J. K., Messina‐Pacheco, J., Villarreal, A. M., Ramchatesingh, B. L., Lefrançois, P., Xie, P., Amar, L., Xu, H. H., Raveendra, K., Sikorski, D., et al. (2023) · Cells · doi:10.3390/cells12121627 · Cited by 5
Nutlin's two roads toward apoptosis
Zhang, Q., & Lu, H. (2010) · Cancer Biology & Therapy · doi:10.4161/cbt.10.6.13127 · Cited by 6
Functional Interrogation of the N-Terminal Lid of MDMX in p53 Binding via Native Chemical Ligation
Chen, X., & Lu, W. (2016) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c15-00975 · Cited by 5
Highly Potent Clickable Probe for Cellular Imaging of MDM2 and Assessing Dynamic Responses to MDM2-p53 Inhibition
Lebraud, H., Noble, R. A., Phillips, N., Heam, K., Castro, J., Zhao, Y., Newell, D. R., Lunec, J., Wedge, S. R., & Heightman, T. D. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00315 · Cited by 5
A dimethylbromobenzene-cysteine stapled peptide dual inhibitor of the p53-MDM2/MDMX interactions
Jiang, W., Jin, L., Liu, M., Hou, P., & He, W. (2019) · Hepatoma Research · doi:10.20517/2394-5079.2018.97 · Cited by 5
Analytical discovery of water disinfection byproducts of toxicological relevance: highlighting halobenzoquinones
Craven, C. B., Blackstock, L. K. J., Xie, J., Li, J., Yuan, C., & Li, X. (2021) · Canadian Journal of Chemistry · doi:10.1139/cjc-2021-0036 · Cited by 5
Proteasome Based Molecular Strategies Against Improper Cellular Proliferation
Dubey, A. R., Kinger, S., Jagtap, Y. A., Patwa, S. M., Kumar, P., Singh, S., Kumar, A., Kumar, A., & Mishra, A. (2021) · Cellular Physiology and Biochemistry · doi:10.33594/000000439 · Cited by 5

Authors: Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R., & Lane, D. P.
Affiliations: Agency for Science, Technology and Research (SG)
Medical Research Council (GB)
Corresponding author: Lane, David P.
ORCID: Brown, Christopher J.
Verma, Chandra S.
Lane, David P.
Venue: Nature Reviews Cancer
Publisher: Springer Science and Business Media LLC
Published: 2009-12
Volume: 9
Issue: 12
Pages: 862-873
ISSN: 1474-175X (ISSN-L)
1474-1768
DOI: 10.1038/nrc2763
OpenAlex: W2093775600
Cited by: 881
References: 149
Citations by year: 2026: 5 · 2025: 24 · 2024: 21 · 2023: 64 · 2022: 27 · 2021: 32 · 2020: 37 · 2019: 49 · 2018: 42 · 2017: 59 · 2016: 58 · 2015: 76 · 2014: 91 · 2013: 74 · 2012: 82
FWCI: 6.45
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature reviews. Cancer (publishedVersion)
PubMed (publishedVersion)
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 › Cancer Research › Cancer Mechanisms and Therapy
Keywords: p53 pathway, TP53 mutation, MDM2, p53 activation, mutant p53, synthetic lethality, cell-based assays, anticancer drug development, protein-protein interaction inhibitors
MeSH terms: Antineoplastic Agents, Humans, Mutation, Neoplasms, Drug Design, Signal Transduction, Genes, p53, Tumor Suppressor Protein p53, Drug Delivery Systems, Proto-Oncogene Proteins c-mdm2

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Awakening guardian angels: drugging the p53 pathway

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks