Awakening guardian angels: drugging the p53 pathway

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

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

Structural Basis for Inhibition of the MDM2:p53 Interaction by an Optimized MDM2-Binding Peptide Selected with mRNA Display

Nagata, T., Shirakawa, K., Kobayashi, N., Shiheido, H., Tabata, N., Sakuma-Yonemura, Y., Horisawa, K., Katahira, M., Doi, N., & Yanagawa, H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109163 · Cited by 20

New small molecules, ISA27 and SM13, inhibit tumour growth inducing mitochondrial effects of p53

Sorriento, D., Giudice, C. D., Bertamino, A., Ciccarelli, M., Gomez-Monterrey, I. M., Campiglia, P., Novellino, E., Illario, M., Trimarco, B., LUCA, N. D., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.577 · Cited by 20

Inability of p53-reactivating compounds Nutlin-3 and RITA to overcome p53 resistance in tumor cells deficient in p53Ser46 phosphorylation

Ma, T., Yamada, S., Ichwan, S. J. A., Iseki, S., Ohtani, K., Otsu, M., & Ikeda, M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.11.161 · Cited by 19

Characterizing the conformational landscape of MDM2-binding p53 peptides using Molecular Dynamics simulations

Yadahalli, S., Li, J., Lane, D. P., Gosavi, S., & Verma, C. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-15930-4 · Cited by 19

Characterization of airborne PAHs and metals associated with PM10 fractions collected from an urban area of Sri Lanka and the impact on airway epithelial cells.

Abayalath, N., Malshani, I., Ariyaratne, R., Zhao, S., Zhong, G., Zhang, G., Manipura, A., SIRIBADDANA, A. A., Karunaratne, P., & Kodithuwakku, S. P. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2021.131741 · Cited by 20

Synthesis and Biological Evaluation of Novel Dispiro-Indolinones with Anticancer Activity

Ivanenkov, Y. A., Kukushkin, M. E., Beloglazkina, A. A., Shafikov, R. R., Barashkin, A. A., Ayginin, A. A., Serebryakova, M. S., Majouga, A. G., Skvortsov, D. A., Тафеенко, В. А., et al. (2023) · Molecules · doi:10.3390/molecules28031325 · Cited by 19

Targeting protein-protein interactions with low molecular weight and short peptide modulators: insights on disease pathways and starting points for drug discovery

Trisciuzzi, D., Villoutreix, B. O., Siragusa, L., Baroni, M., Cruciani, G., & Nicolotti, O. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2218641 · Cited by 19

Metastatic renal cell carcinoma without evidence of a renal primary

Costantino, C. A., THOMAS, G. V., Ryan, C. W., Coakley, F. V., & Troxell, M. L. (2015) · International Urology and Nephrology · doi:10.1007/s11255-015-1145-3 · Cited by 19

Ocotillol Enhanced the Antitumor Activity of Doxorubicin via p53-Dependent Apoptosis

Wang, H., Yu, P., Bai, J., Zhang, J., Kong, L., Zhang, F., Du, G., Pei, S., Zhang, L., Jiang, Y., et al. (2013) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2013/468537 · Cited by 19

Genomic profiling of small-cell lung cancer: the era of targeted therapies

Umemura, S., Tsuchihara, K., & Goto, K. (2015) · Japanese Journal of Clinical Oncology · doi:10.1093/jjco/hyv017 · Cited by 19

The p53 cofactor Strap exhibits an unexpected TPR motif and oligonucleotide-binding (OB)–fold structure

Adams, C. J., Pike, A., Maniam, S., Sharpe, T., Coutts, A., Knapp, S., Thangue, N. L., & Bullock, A. (2012) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1113731109 · Cited by 20

Identification of functional DNA variants in the constitutive promoter region of MDM2

Lalonde, M., Ouimet, M., Larivière, M., Kritikou, E. A., & Sinnett, D. (2012) · Human Genomics · doi:10.1186/1479-7364-6-15 · Cited by 19

Small-Molecule Inhibitors of Protein–Protein Interactions

Liu, Z., Chen, H., Wold, E. A., & Zhou, J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12326-1 · Cited by 19

Applications and genotoxicity of nanomaterials in the food industry

Manickam, V., Velusamy, R. K., Panchangam, R. L., Amiti, Rajendran, B., & Tamizhselvi, R. (2017) · Environmental Chemistry Letters · doi:10.1007/s10311-017-0633-3 · Cited by 19

p53 gene therapy of human breast carcinoma: using a transferrin-modified silica nanoparticles

Rejeeth, C., & Kannan, S. (2014) · Breast Cancer · doi:10.1007/s12282-014-0537-z · Cited by 19

Novel action modality of the diterpenoid anisomelic acid causes depletion of E6 and E7 viral oncoproteins in HPV-transformed cervical carcinoma cells

Paul, P., Rajendran, S. K., Peuhu, E., Alshatwi, A. A., Akbarsha, M. A., Hietanen, S., & Eriksson, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.02.011 · Cited by 19

Discovery of Novel 3,3-Disubstituted Piperidines as Orally Bioavailable, Potent, and Efficacious HDM2-p53 Inhibitors

Bogen, S. L., Pan, W., Gibeau, C. R., Lahue, B. R., Ma, Y., Nair, L. G., Seigel, E., Shipps, G. W., Tian, Y., Wang, Y., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00472 · Cited by 19

The dual role of p63 in cancer

Xu, Y., Yang, X., Xiong, Q., Han, J., & Zhu, Q. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1116061 · Cited by 19

Modeling and controlling the two-phase dynamics of the p53 network: a Boolean network approach

Lin, G., Ao, B., Chen, J., Wang, W., & Di, Z. (2014) · New Journal of Physics · doi:10.1088/1367-2630/16/12/125010 · Cited by 18

Simulating Molecular Mechanisms of the MDM2-Mediated Regulatory Interactions: A Conformational Selection Model of the MDM2 Lid Dynamics

Verkhivker, G. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040897 · Cited by 18

Evolution of Conformational Disorder & Diversity of the P53 Interactome

Huart, A.-S., & Hupp, T. R. (2013) · Biodiscovery · doi:10.7750/biodiscovery.2013.8.5 · Cited by 18

Concepts in MDM2 Signaling: Allosteric Regulation and Feedback Loops

Ponnuswamy, A., Hupp, T. R., & Fåhræus, R. (2012) · Genes & Cancer · doi:10.1177/1947601912454140 · Cited by 21

Structural determinants of benzodiazepinedione/peptide-based p53-HDM2 inhibitors using 3D-QSAR, docking and molecular dynamics

Wang, F., Li, Y., Ma, Z., Wang, X., & Wang, Y. (2011) · Journal of Molecular Modeling · doi:10.1007/s00894-011-1041-4 · Cited by 18

Targeting RNA Polymerase I with Hernandonine Inhibits Ribosomal RNA Synthesis and Tumor Cell Growth

Chen, Y., Chen, J., & Wang, H. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0402 · Cited by 18

Biomimetic Synthesis of Rhytidenone A and Mode of Action of Cytotoxic Rhytidenone F

Yue, Z., Lam, H. C., Chen, K., Siridechakorn, I., Liu, Y., Pudhom, K., & Lei, X. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201914257 · Cited by 18

Small-molecule modulation of p53 protein-protein interactions

Kuusk, A., Boyd, H., Chen, H., & Ottmann, C. (2020) · Biological Chemistry · doi:10.1515/hsz-2019-0405 · Cited by 18

HEXIM1, a New Player in the p53 Pathway

Lew, Q. J., Chu, K., Chia, Y. L., Cheong, N., & Chao, S. (2013) · Cancers · doi:10.3390/cancers5030838 · Cited by 19

Selective protein degradation in cell signalling

Liu, H., Urbé, S., & Clague, M. J. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.01.014 · Cited by 17

E3 ubiquitin ligase Cbl-b activates the p53 pathway by targeting Siva1, a negative regulator of ARF, in FLT3 inhibitor-resistant acute myeloid leukemia

Park, I.-K., Blum, W. G., Baker, S. D., & Caligiuri, M. A. (2016) · Leukemia · doi:10.1038/leu.2016.293 · Cited by 18

Induction of the p53 Tumor Suppressor in Cancer Cells through Inhibition of Cap-Dependent Translation

Harris, B., Wang, D., Zhang, Y., Ferrari, M. G., Okon, A. M., Cleary, M. P., Wagner, C. R., & Yang, D. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00367-17 · Cited by 18

Electromagnetic Energy as a Bridge Between Atomic and Cellular Levels in the Genetics Approach to Cancer Treatment

Tofani, S. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150225104217 · Cited by 17

Mdm2 inhibition confers protection of p53-proficient cells from the cytotoxic effects of Wee1 inhibitors

Li, Y., Saini, P., Sriraman, A., & Dobbelstein, M. (2015) · Oncotarget · doi:10.18632/oncotarget.5891 · Cited by 17

An updated meta-analysis of the p53 codon 72 polymorphism and gastric cancer risk

Liu, K., Qi, H., Yao, H., Lei, S.-L., Lei, Z.-D., Li, T., & Zhao, H. (2012) · Molecular Biology Reports · doi:10.1007/s11033-012-1674-0 · Cited by 17

Rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein–protein interactions by the MDM2 ligand nutlin‐3

Way, L., Faktor, J., Dvořáková, P., Nicholson, J., Vojtesek, B., Graham, D., Ball, K. L., & Hupp, T. R. (2016) · PROTEOMICS · doi:10.1002/pmic.201500501 · Cited by 16

Analysis of Genetic Alterations in Tunisian Patients with Lung Adenocarcinoma

Dhieb, D., Belguith, I., Capelli, L., Chiadini, E., Canale, M., Bravaccini, S., Yangui, I., Boudawara, O., JLIDI, R., Boudawara, T. S., et al. (2019) · Cells · doi:10.3390/cells8060514 · Cited by 17

A mini-review of the diffusion dynamics of DNA-binding proteins: experiments and models

Park, S., Lee, O.-C., Durang, X., & Jeon, J.-H. (2021) · Journal of the Korean Physical Society · doi:10.1007/s40042-021-00060-y · Cited by 17

Why is F19Ap53 unable to bind MDM2? Simulations suggest crack propagation modulates binding

Dastidar, S. G., Lane, D. P., & Verma, C. S. (2012) · Cell Cycle · doi:10.4161/cc.20333 · Cited by 17

Recognition Dynamics of p53 and MDM2: Implications for Peptide Design

ElSawy, K. M., Lane, D. P., Verma, C. S., & Caves, L. S. D. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b11162 · Cited by 17

P53 tumor suppressor is required for efficient execution of the death program following treatment with a cytotoxic limonoid obtained from Melia azedarach

Joray, M. B., Villafañez, F., González, M. L., Crespo, M. I., Laiolo, J., Palacios, S. M., Bocco, J. L., Soria, G., & Carpinella, M. C. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.04.039 · Cited by 17

Full-length mutation search of the TP53 gene in acute myeloid leukemia has increased significance as a prognostic factor

Terada, K., Yamaguchi, H., Ueki, T., Usuki, K., Kobayashi, Y., Tajika, K., Gomi, S., Kurosawa, S., Miyadera, K., Tokura, T., et al. (2017) · Annals of Hematology · doi:10.1007/s00277-017-3143-2 · Cited by 17

Mechanisms of oncogenic cell competition–Paths of victory

Gutiérrez-Martínez, A., Sew, W. Q. G., Molano-Fernández, M., Carretero, M., & Herranz, H. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.05.015 · Cited by 17

Splicing Modulation Results in Aberrant Isoforms and Protein Products of p53 Pathway Genes and the Sensitization of B Cells to Non-Genotoxic MDM2 Inhibition

Aptullahoğlu, E., Ciardullo, C., Wallis, J. P., Marr, H. J., Marshall, S. R., Bown, N. P., Willmore, E., & Lunec, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032410 · Cited by 15

The mechanistic role of NAT10 in cancer: Unraveling the enigmatic web of oncogenic signaling

Rodrigues, P., Bangali, H., Ali, E., Абдрешов, С. Н., Hjazi, A. M., Fenjan, M. N., Alawadi, A. H., Alsaalamy, A. H., Alasheqi, M. Q., & Mustafa, Y. F. (2023) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.154990 · Cited by 16

Delivery to, and Reactivation of, the p53 Pathway in Cancer Cells Using a Grafted Cyclotide Conjugated with a Cell-Penetrating Peptide

Philippe, G. J.-B., Huang, Y., Mittermeier, A., Brown, C. J., Kaas, Q., Ramlan, S. R., Wang, C. K. L., Lane, D. P., Loewer, A., Henriques, S. T., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01682 · Cited by 17

p14ARF Post-Transcriptional Regulation of Nuclear Cyclin D1 in MCF-7 Breast Cancer Cells: Discrimination between a Good and Bad Prognosis?

McGowan, E. M., Tran, N., Alling, N., Yagoub, D., Sedger, L. M., & Martiniello‐Wilks, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042246 · Cited by 16

Molecular genetics of high-risk chronic lymphocytic leukemia

Rossi, D., & Gaïdano, G. (2012) · Expert Review of Hematology · doi:10.1586/ehm.12.58 · Cited by 15

Deconstructing nucleotide binding activity of the Mdm2 RING domain

Priest, C., Prives, C. L., & Poyurovsky, M. V. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq669 · Cited by 16

PPARγ suppresses the proliferation of cardiac myxoma cells through downregulation of MEF2D in a miR-122-dependent manner

Qiu, Y., Yang, J., Bian, S., Chen, G., & Yu, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.112 · Cited by 16

Expression of transmembrane protein 26 (TMEM26) in breast cancer and its association with drug response

Naß, N., Dittmer, A., Hellwig, V. A. C. V., Lange, T., Beyer, J. M., Leyh, B., Ignatov, A., Weiβenborn, C., Kirkegaard, T., Lykkesfeldt, A. E., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9493 · Cited by 16

PDRG1 gene silencing contributes to inhibit the growth and induce apoptosis of gastric cancer cells

Zhang, Y., Li, J., Li, H.-Z., Song, H., Wei, C., & Zhang, S. (2019) · Pathology - Research and Practice · doi:10.1016/j.prp.2019.152567 · Cited by 17

TP53 and TP53-associated genes are correlated with the prognosis of paediatric neuroblastoma

Wang, H., Wang, X., Xu, L., & Zhang, J. (2022) · BMC Genomic Data · doi:10.1186/s12863-022-01059-5 · Cited by 16

Adoption of a Turn Conformation Drives the Binding Affinity of p53 C-Terminal Domain Peptides to 14-3-3σ

Kuusk, A., Neves, J. F., Bravo‐Rodriguez, K., Gunnarsson, A., Ruiz‐Blanco, Y. B., Ehrmann, M., Chen, H., Landrieu, I., Sánchez‐García, E., Boyd, H., et al. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00893 · Cited by 17

Discovery of 1-arylpyrrolidone derivatives as potent p53–MDM2 inhibitors based on molecule fusing strategy

Li, J., Wu, Y., Guo, Z., Zhuang, C., Yao, J., Dong, G., Yu, Z., Min, X., Wang, S., Liu, Y., et al. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.04.063 · Cited by 16

An anthraquinone derivative from Luffa acutangula induces apoptosis in human lung cancer cell line NCI-H460 through p53-dependent pathway

Vanajothi, R., & Srinivasan, P. (2015) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2015.1108335 · Cited by 16

Cedrus atlantica Extract Suppress Glioblastoma Growth through Promotion of Genotoxicity and Apoptosis: In Vitro and In Vivo Studies

Chang, K., Chang, J. T., Huang, X., Huang, Y., Li, C., Weng, J., Hsiao, C., Hsu, H.-J., & Tsai, N. (2021) · International Journal of Medical Sciences · doi:10.7150/ijms.54468 · Cited by 15

Small-Molecule Approaches to Target Transcription Factors

Cui, H., Stilgenbauer, M., & Koehler, A. N. (2024) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-062722-012209 · Cited by 19

p53 Actions on MicroRNA Expression and Maturation Pathway

Suzuki, H. I., & Miyazono, K. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-236-0_14 · Cited by 15

Gentian violet induces wtp53 transactivation in cancer cells

Garufi, A., D’Orazi, V., Arbiser, J. L., & D’Orazi, G. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2304 · Cited by 15

Identification and characterisation of Emp53, the homologue of human tumor suppressor p53, from Echinococcus multilocularis: its role in apoptosis and the oxidative stress response

Cheng, Z., Zhu, S., Wang, L., Liu, F., Tian, H., Pengsakul, T., & Wang, Y. (2015) · International Journal for Parasitology · doi:10.1016/j.ijpara.2015.02.010 · Cited by 15

Core modification of substituted piperidines as Novel inhibitors of HDM2–p53 protein–protein interaction

Pan, W., Lahue, B. R., Ma, Y., Nair, L. G., Shipps, G. W., Wang, Y., Doll, R. J., & Bogen, S. L. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.02.055 · Cited by 15

Human Serum Albumin and p53-Activating Peptide Fusion Protein Is Able to Promote Apoptosis and Deliver Fatty Acid-Modified Molecules

Joshi, M. R., Yao, N., Myers, K. A., & Li, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080926 · Cited by 15

Mechanism of Stapled Peptide Binding to MDM2: Possible Consequences for Peptide Design

Sim, A. Y. L., Joseph, T. L., Lane, D. P., & Verma, C. S. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct4009238 · Cited by 15

Impact of the Ki-67 labeling index and p53 expression status on disease-free survival in pT1 urothelial carcinoma of the bladder

Vetterlein, M. W., Roschinski, J., Gild, P., Marks, P., Soave, A., Doh, O., Hendrik Isbarn, A., Höppner, W., Wagner, W. P., Shariat, S. F., et al. (2017) · Translational Andrology and Urology · doi:10.21037/tau.2017.11.10 · Cited by 15

Interfaces with Structure Dynamics of the Workhorses from Cells Revealed through Cross-Linking Mass Spectrometry (CLMS)

Kalathiya, U., Padariya, M., Faktor, J., Coyaud, É., Alfaro, J. A., Fåhræus, R., Hupp, T. R., & Goodlett, D. R. (2021) · Biomolecules · doi:10.3390/biom11030382 · Cited by 14

Revisiting a challenging p53 binding site: a diversity-optimized HEFLib reveals diverse binding modes in T-p53C-Y220C

Stahlecker, J., Klett, T., Schwer, M., Jaag, S., Dammann, M., Ernst, L. N., Braun, M. B., Zimmermann, M. O., Krämer, M., Lämmerhofer, M., et al. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00246a · Cited by 15

Design, Synthesis and Evaluation of 2,5-Diketopiperazines as Inhibitors of the MDM2-p53 Interaction

Pettersson, M., Quant, M., Min, J., Iconaru, L. I., Kriwacki, R. W., Waddell, M. B., Guy, R. K., Luthman, K., & Grøtli, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137867 · Cited by 15

A Novel Aurora-A Inhibitor, BPR1K0609S1, Sensitizes Colorectal Tumor cells to 5-Fluorofracil (5-FU) Treatment

Shionome, Y., Lin, W., Shiao, H., Hsieh, H., Hsu, J. T., & Ouchi, T. (2013) · International Journal of Biological Sciences · doi:10.7150/ijbs.5806 · Cited by 16

Design of indole- and MCR-based macrocycles as p53-MDM2 antagonists

Neochoritis, C. G., Miraki, M. K., Abdelraheem, E. M. M., Surmiak, E., Zarganes‐Tzitzikas, T., Łabuzek, B., Holak, T. A., & Dömling, A. S. S. (2019) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.15.45 · Cited by 15

MD-4251: A First-in-Class Oral MDM2 Degrader Inducing Complete Tumor Regression with Single-Dose Administration

Acharyya, R. K., Huang, L., Aguilar, A., Hu, B., Bai, L., Metwally, H., McEachern, D., Jiang, W., Wang, Y., Li, Q., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00809 · Cited by 15

Pharmacoinformatics approach for the screening of Kovidra (Bauhinia variegata) phytoconstituents against tumor suppressor protein in triple negative breast cancer

More-Adate, P., Lokhande, K. B., Shrivastava, A., Doiphode, S., Nagar, S., Singh, A., & Baheti, A. M. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2219744 · Cited by 14

Targeted Polymersome Delivery of a Stapled Peptide for Drugging the Tumor Protein p53:BCL-2-Family Axis in Diffuse Large B-Cell Lymphoma

Schnorenberg, M. R., Hawley, K. M., Thomas-Toth, A. T., Watkins, E. A., Tian, Y. P., Ting, J., Leak, L. B., Kucera, I. M., Raczy, M. M., Kung, A. L., et al. (2023) · ACS Nano · doi:10.1021/acsnano.3c04112 · Cited by 14

Knockdown of microRNA‑29a regulates the expression of apoptosis‑related genes in MCF‑7 breast carcinoma cells

Khamisipour, G., Mansourabadi, E., Naeimi, B., Moazzeni, A., Tahmasebi, R., Hasanpour, M., Mohammadi, M. M., Mansourabadi, Z., & Shamsian, S. (2017) · Molecular and Clinical Oncology · doi:10.3892/mco.2017.1528 · Cited by 14

A protein folding molecular imaging biosensor monitors the effects of drugs that restore mutant p53 structure and its downstream function in glioblastoma cells

Paulmurugan, R., Afjei, R., Sekar, T. V., Babikir, H. A., & Massoud, T. F. (2018) · Oncotarget · doi:10.18632/oncotarget.25138 · Cited by 14

The Inability of the Choroid to Revascularize in Oxygen-Induced Retinopathy Results from Increased p53/miR-Let-7b Activity

Zhou, T. E., Zhu, T., Rivera, J. C., Omri, S., Tahiri, H., Lahaie, I., Rouget, R., Wirth, M., Nattel, S., Lodygensky, G. A., et al. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.07.009 · Cited by 14

Cyclic AMP-induced p53 destabilization is independent of EPAC in pre-B acute lymphoblastic leukemia cellsin vitro

Safa, M., Kazemi, A., Zaker, F., & Razmkhah, F. (2011) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2011.578140 · Cited by 14

Subchronic oral toxicity and metabolite profiling of the p53 stabilizing agent, CP-31398, in rats and dogs

Johnson, W. D., Muzzio, M., Detrisac, C. J., Kapetanović, I. M., Kopelovich, L., & McCormick, D. L. (2011) · Toxicology · doi:10.1016/j.tox.2011.08.009 · Cited by 14

RITA enhances chemosensivity of pre-B ALL cells to doxorubicin by inducing p53-dependent apoptosis

Kazemi, A., Safa, M., & Shahbazi, A. (2011) · Hematology · doi:10.1179/102453311x12953015767536 · Cited by 15

Inhibitors of the p53-Mdm2 interaction increase programmed cell death and produce abnormal phenotypes in the placozoon Trichoplax adhaerens (F.E. Schulze)

von der Chevallerie, K., Rolfes, S., & Schierwater, B. (2014) · Development Genes and Evolution · doi:10.1007/s00427-014-0465-0 · Cited by 16

Anti-Cancer Activity of a Novel Small Molecule Compound That Simultaneously Activates p53 and Inhibits NF-κB Signaling

Hwang, S. G., Park, J., Park, J. Y., Park, C. H., Lee, K.-H., Cho, J. W., Hwang, J., & Seong, J. Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044259 · Cited by 14

MDM4 binds ligands via a mechanism in which disordered regions become structured

Sanchez, M. C., Renshaw, J., Davies, G. M., Barlow, P. N., & Vogtherr, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.05.058 · Cited by 14

Highly reactive bis-cyclooctyne-modified diarylethene for SPAAC-mediated cross-linking

Strizhak, A. V., Sharma, K., Babii, O., Afonin, S., Ulrich, A. S., Komarov, I. V., & Spring, D. R. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob02428f · Cited by 15

p53-targeted cancer pharmacotherapy: move towards small molecule compounds

Kim, S.-H., & Dass, C. R. (2011) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.2010.01248.x · Cited by 14

A spatiotemporal characterization of the effect of p53 phosphorylation on its interaction with MDM2

ElSawy, K. M., Sim, A. Y. L., Lane, D. P., Verma, C. S., & Caves, L. S. D. (2015) · Cell Cycle · doi:10.4161/15384101.2014.989043 · Cited by 14

The TP53 signaling network in mammals and worms

Jolliffe, A. K., & Derry, W. B. (2012) · Briefings in Functional Genomics · doi:10.1093/bfgp/els047 · Cited by 14

Covalent Fragments Acting as Tyrosine Mimics for Mutant p53-Y220C Rescue by Nucleophilic Aromatic Substitution

Klett, T., Stahlecker, J., Jaag, S., Masberg, B., Knappe, C., Lämmerhofer, M., Coles, M. P., Stehle, T., & Boeckler, F. M. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00414 · Cited by 14

Dual Modulators of p53 and Cyclin D in ER Alpha Signaling by Albumin Nanovectors Bearing Zinc Chaperones for ER-positive Breast Cancer Therapy

Sundar, P. S., Naresh, P., Justin, A., Wadhwani, A., Mohankumar, S. K., & Selvaraj, J. (2020) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557520999201124212347 · Cited by 13

Helical sulfono-γ-AApeptides with predictable functions in protein recognition

Sang, P., Shi, Y., Wei, L., & Cai, J. (2022) · RSC Chemical Biology · doi:10.1039/d2cb00049k · Cited by 13

MDM2 inhibitors, nutlin-3a and navtemadelin, retain efficacy in human and mouse cancer cells cultured in hypoxia

Clavero, A. L., Boqvist, P. L., Ingelshed, K., Bosdotter, C., Sedimbi, S. K., Jiang, L., Wermeling, F., Vojtěšek, B., Lane, D. P., & Kannan, P. (2023) · Scientific Reports · doi:10.1038/s41598-023-31484-0 · Cited by 13

Multihit TP53 Mutations in Myeloproliferative Neoplasms and Acute Myeloid Leukemia: Comparative Analysis of Survival and Risk Factors in 142 Informative Cases

Fathima, S., Abdelmagid, M. G., Alsugair, A. K. A., Begna, K. H., Al‐Kali, A., Mangaonkar, A. A., Pardanani, A. D., Patnaik, M. M., Zepeda‐Mendoza, C. J., He, R. L., et al. (2025) · American Journal of Hematology · doi:10.1002/ajh.27670 · Cited by 13

Design, synthesis, and molecular modeling of coumarin derivatives as MDM2 inhibitors targeting breast cancer

Ahmed, E. Y., Latif, N. A. A., Nasr, T., Awad, H. M., & Abdelhafez, O. M. (2022) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14028 · Cited by 14

A matter of delicate balance: Loss and gain of Cockayne syndrome proteins in premature aging and cancer

Paccosi, E., Balajee, A. S., & Proietti‐De‐Santis, L. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.960662 · Cited by 14

Evolutionary determinants of curability in cancer

Mansur, M. B., deSouza, N. M., Natrajan, R., Abegglen, L. M., Schiffman, J. D., & Greaves, M. F. (2023) · Nature Ecology & Evolution · doi:10.1038/s41559-023-02159-w · Cited by 13

Mechanisms of p53 Functional De-Regulation: Role of the IκB-α/p53 Complex

Carrà, G., Crivellaro, S., Taulli, R., Guerrasio, A., Saglio, G. N., & Morotti, A. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17121997 · Cited by 14

Association between TP53 rs1042522 gene polymorphism and the risk of malignant bone tumors: a meta-analysis

Huang, X., Wu, F., Zhang, Z., & Shao, Z. (2019) · Bioscience Reports · doi:10.1042/bsr20181832 · Cited by 12

The C-terminal SAM domain of p73 binds to the N terminus of MDM2

Neira, J. L., Díaz-García, C., PRIETO, M. J. E., & Coutinho, A. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.01.019 · Cited by 13

A first report of a rare TP53 variant associated with Li-Fraumeni syndrome manifesting as invasive breast cancer and malignant solitary fibrous tumor

Prejac, J., Plavetić, N. D., Gotovac, K., & Borovečki, F. (2021) · World Journal of Surgical Oncology · doi:10.1186/s12957-021-02370-8 · Cited by 12

The human adenovirus E1B-55K oncoprotein coordinates cell transformation through regulation of DNA-bound host transcription factors

von Stromberg, K., Seddar, L., Ip, W.-H., Günther, T., Gornott, B., Weinert, S.-C., Hüppner, M., Bertzbach, L. D., & Dobner, T. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2310770120 · Cited by 11

Outcomes with allogeneic hematopoietic stem cell transplantation in TP53-mutated myelodysplastic syndrome: A systematic review and meta-analysis

Shahzad, M., Iqbal, Q., Tariq, E. F., Ammad-Ud-Din, M., Butt, A., Mushtaq, A. H., Ali, F., Chaudhary, S. G., Anwar, I., Gonzalez‐Lugo, J. D., et al. (2024) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2024.104310 · Cited by 12

Genetic mutations in chronic lymphocytic leukemia: impact on clinical treatment

Condoluci, A., & Rossi, D. (2019) · Expert Review of Hematology · doi:10.1080/17474086.2019.1575130 · Cited by 12

Molecular mechanisms in cancer development

Kashyap, A. K., & Dubey, S. K. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99883-3.00016-0 · Cited by 12

Drugging the p53 pathway: understanding the route to clinical efficacy

Khoo, K. H., Verma, C. S., & Lane, D. P. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4236 · Cited by 742

Small molecule compounds targeting the p53 pathway: are we finally making progress?

Yu, X., Narayanan, S., Vázquez, A., & Carpizo, D. R. (2014) · APOPTOSIS · doi:10.1007/s10495-014-0990-3 · Cited by 68

ORIGINAL PAPER Small molecule compounds targeting the p53 pathway: are we finally making progress?

Yu, X., Narayanan, S., Vazquez, A., & Carpizo, D. R. (2014)

The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches

Joerger, A. C., & Fersht, A. R. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014710 · Cited by 675

Translational approaches targeting the p53 pathway for anti‐cancer therapy

Essmann, F., & Schulze‐Osthoff, K. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01570.x · Cited by 77