Dual inhibition of MDMX and MDM2 as a therapeutic strategy in leukemia

In Vivo Gene Delivery and Stable Transduction of Nondividing Cells by a Lentiviral Vector

Naldini, L., Blömer, U., Gallay, P., Ory, D., Mulligan, R., Gage, F. H., Verma, I. M., & Trono, D. (1996) · Science · doi:10.1126/science.272.5259.263 · Cited by 4,903 · see citing works

A cell initiating human acute myeloid leukaemia after transplantation into SCID mice

Lapidot, T., Sirard, C., Vormoor, J., Murdoch, B., Hoang, T., Caceres-Cortes, J., Minden, M., Paterson, B., Caligiuri, M. A., & Dick, J. E. (1994) · Nature · doi:10.1038/367645a0 · Cited by 4,783 · 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

Mutational landscape and significance across 12 major cancer types

Kandoth, C., McLellan, M. D., Vandin, F., Ye, K., Niu, B., Lu, C., Xie, M., Zhang, Q., McMichael, J. F., Wyczalkowski, M. A., et al. (2013) · Nature · doi:10.1038/nature12634 · Cited by 4,419 · see citing works

Regulation of p53 stability by Mdm2

Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · see citing works

Double nicking by RNA-guided CRISPR Cas9 for enhanced genome editing specificity

Ran, F. A., Hsu, P. D., Lin, C.-Y., Gootenberg, J. S., Konermann, S., Trevino, A. E., Scott, D. A., Inoue, A., Matoba, S., Zhang, Y., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.021 · Cited by 3,299 · see citing works

Blinded by the Light: The Growing Complexity of p53

Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163 · see citing works

p53 in health and disease

Vousden, K. H., & Lane, D. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2147 · Cited by 2,275 · see citing works

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951 · see citing works

p53 mutations in cancer

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

Localization of ASH1 mRNA particles in living yeast.

Bertrand, E., Chartrand, P., Schaefer, M., Shenoy, S., Singer, R., & Long, R. M. (1998) · Molecules and Cells · doi:10.1016/s1097-2765(00)80143-4 · Cited by 1,597 · 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

Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53

de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420 · see citing works

Unravelling mechanisms of p53-mediated tumour suppression

Bieging-Rolett, K. T., Mello, S. S., & Attardi, L. D. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3711 · Cited by 1,389 · see citing works

Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53

Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280 · 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 · see citing works

Chemotherapy-resistant human AML stem cells home to and engraft within the bone-marrow endosteal region

Ishikawa, F., Yoshida, S., Saito, Y., Hijikata, A., Kitamura, H., Tanaka, S., Nakamura, R., Tanaka, T., Tomiyama, H., Saito, N., et al. (2007) · Nature Biotechnology · doi:10.1038/nbt1350 · Cited by 993 · see citing works

Mammalian genes are transcribed with widely different bursting kinetics

Suter, D. M., Molina, N., Gatfield, D., Schneider, K., Schibler, U., & Naef, F. (2011) · Science · doi:10.1126/science.1198817 · Cited by 927 · see citing works

Normal and leukemic hematopoiesis: Are leukemias a stem cell disorder or a reacquisition of stem cell characteristics?

Passegue, E. A., Jamieson, C. H. M., Ailles, L., & Weissman, I. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2034201100 · Cited by 685 · see citing works

TP53 alterations in acute myeloid leukemia with complex karyotype correlate with specific copy number alterations, monosomal karyotype, and dismal outcome

Rücker, F. G., Schlenk, R. F., Bullinger, L., Käyser, S., Teleanu, V., Kett, H., Habdank, M., Kugler, C.-M., Holzmann, K., Gaidzik, V. I., et al. (2011) · Blood · doi:10.1182/blood-2011-08-375758 · Cited by 680 · see citing works

Stapled α−helical peptide drug development: A potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy

Chang, Y. S., Graves, B. J., Guerlavais, V., Tovar, C., Packman, K. E., To, K.-H., Olson, K. A., Kesavan, K. P., Gangurde, P., Mukherjee, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303002110 · Cited by 666 · see citing works

MDMX: a novel p53‐binding protein with some functional properties of MDM2.

Shvarts, A., Steegenga, W. T., Riteco, N., van Laar, T., Dekker, P., Bazuine, M., van Ham, R. C., van der Houven van Oordt, W., Hateboer, G., van der Eb, A. J., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00919.x · Cited by 648 · see citing works

Discovery of RG7388, a Potent and Selective p53–MDM2 Inhibitor in Clinical Development

Ding, Q., Zhang, Z., Liu, J.-J., Jiang, N., Zhang, J., Ross, T. M., Chu, X.-J., Bartkovitz, D., Podlaski, F., Janson, C., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400487c · Cited by 595 · see citing works

Reactivation of the p53 Tumor Suppressor Pathway by a Stapled p53 Peptide

Bernal, F., Tyler, A. F., Korsmeyer, S. J., Walensky, L. D., & Verdine, G. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0693587 · Cited by 559 · see citing works

Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53

Parant, J., Chavez-Reyes, A., Little, N. A., Yan, W., Reinke, V., Jochemsen, A. G., & Lozano, G. (2001) · Nature Genetics · doi:10.1038/ng714 · Cited by 517 · see citing works

Efficient method to generate single‐copy transgenic mice by site‐specific integration in embryonic stem cells

Beard, C., Hochedlinger, K., Plath, K., Wutz, A., & Jaenisch, R. (2006) · genesis · doi:10.1002/gene.20180 · Cited by 482 · see citing works

Small-Molecule Inhibitors of the MDM2–p53 Protein–Protein Interaction (MDM2 Inhibitors) in Clinical Trials for Cancer Treatment

Zhao, Y., Aguilar, A., Bernard, D., & Wang, S. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501092z · Cited by 462 · see citing works

Small molecules enhance CRISPR genome editing in pluripotent stem cells

Yu, C., Liu, Y., Ma, T., Liu, K., Xu, S., Zhang, Y., Liu, H., La Russa, M., Xie, M., Ding, S., et al. (2015) · Cell stem cell · doi:10.1016/j.stem.2015.01.003 · Cited by 455 · see citing works

Activation of p53 by SIRT1 Inhibition Enhances Elimination of CML Leukemia Stem Cells in Combination with Imatinib

Li, L., Wang, L., Li, L., Wang, Z., Ho, Y., McDonald, T., Holyoake, T. L., Chen, W., & Bhatia, R. (2012) · Cancer Cell · doi:10.1016/j.ccr.2011.12.020 · Cited by 410 · see citing works

MDM2 antagonists induce p53-dependent apoptosis in AML: implications for leukemia therapy

Kojima, K., Konopleva, M. Y., Samudio, I. J., Shikami, M., Cabreira-Hansen, M. D. G., McQueen, T. J., Ruvolo, V. R., Tsao, T., Zeng, Z., Vassilev, L. T., et al. (2005) · Blood · doi:10.1182/blood-2005-02-0553 · Cited by 407 · 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

Overexpression of Mdm2 in mice reveals a p53-independent role for Mdm2 in tumorigenesis

Jones, S. N., Hancock, A. R., Vogel, H., Donehower, L. A., & Bradley, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15608 · Cited by 386 · see citing works

Results of the Phase I trial of RG7112, a small-molecule MDM2 antagonist in leukemia

Andreeff, M., Kelly, K. R., Yee, K., Assouline, S., Strair, R., Popplewell, L., Bowen, D., Martinelli, G., Drummond, M. W., Vyas, P., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-0481 · Cited by 352 · see citing works

MDM4 is a key therapeutic target in cutaneous melanoma

Gembarska, A., Luciani, F., Fedele, C., Russell, E. A., Dewaele, M., Villar, S., Zwolinska, A., Haupt, S., de Lange, J., Yip, D., et al. (2012) · Nature Medicine · doi:10.1038/nm.2863 · Cited by 327 · see citing works

MDM2 interacts with MDMX through their RING finger domains

Tanimura, S., Ohtsuka, S., Mitsui, K., Shirouzu, K., Yoshimura, A., & Ohtsubo, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00254-9 · Cited by 324 · see citing works

Clinical Overview of MDM2/X-Targeted Therapies

Burgess, A., Chia, K. M., Haupt, S., Thomas, D., Haupt, Y., & Lim, E. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00007 · Cited by 315 · see citing works

Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development

Migliorini, D., Denchi, E. L., Danovi, D., Jochemsen, A., Capillo, M., Gobbi, A., Helin, K., Pelicci, P. G., & Marine, J.-C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5527-5538.2002 · Cited by 313 · see citing works

The human MDM-2 oncogene is overexpressed in leukemias

Bueso-Ramos, C., Yang, Y. S., deLeon, E., McCown, P., Stass, S. A., & Albitar, M. X. (1993) · Blood · doi:10.1182/blood.v82.9.2617.bloodjournal8292617 · Cited by 292 · see citing works

Stabilization of the MDM2 Oncoprotein by Interaction with the Structurally Related MDMX Protein

Sharp, D. A., Kratowicz, S. A., Sank, M. J., & George, D. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38189 · Cited by 286 · see citing works

A Stapled p53 Helix Overcomes HDMX-Mediated Suppression of p53

Bernal, F., Wade, M. R., Godes, M., Davis, T. N., Whitehead, D. G., Kung, A. L., Wahl, G. M., & Walensky, L. D. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.024 · Cited by 284 · see citing works

Mutual Dependence of MDM2 and MDMX in Their Functional Inactivation of p53

Gu, J., Kawai, H., Nie, L., Kitao, H., Wiederschain, D., Jochemsen, A. G., Parant, J. M., Lozano, G., & Yuan, Z.-M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200150200 · Cited by 265 · see citing works

TP53 mutations in newly diagnosed acute myeloid leukemia: Clinicomolecular characteristics, response to therapy, and outcomes

Kadia, T. M., Jain, P., Ravandi, F., Garcia‐Manero, G., Andreef, M., Takahashi, K., Borthakur, G. M., Jabbour, E. J., Konopleva, M. Y., Daver, N. G., et al. (2016) · Cancer · doi:10.1002/cncr.30203 · Cited by 261 · see citing works

Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells <i>in vivo</i>

Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260 · see citing works

Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms

Stad, R., Little, N. A., Xirodimas, D. P., Frenk, R., van der Eb, A. J., Lane, D. P., Saville, M. K., & Jochemsen, A. G. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve227 · Cited by 234 · see citing works

Dual targeting of p53 and c-MYC selectively eliminates leukaemic stem cells

Abraham, S. A., Hopcroft, L. E. M., Carrick, E., Drotar, M. E., Dunn, K., Williamson, A. J. K., Korfi, K., Baquero, P., Park, L. E., Scott, M. T., et al. (2016) · Nature · doi:10.1038/nature18288 · Cited by 225 · see citing works

Efficient p53 Activation and Apoptosis by Simultaneous Disruption of Binding to MDM2 and MDMX

Hu, B., Gilkes, D. M., & Chen, J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1140 · Cited by 214 · see citing works

Fluorescence Fluctuation Spectroscopy Enables Quantitative Imaging of Single mRNAs in Living Cells

Wu, B., Chao, J. A., & Singer, R. H. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.05.017 · Cited by 205 · see citing works

Overexpression of IL-1 receptor accessory protein in stem and progenitor cells and outcome correlation in AML and MDS

Barreyro, L., Will, B., Bartholdy, B., Zhou, L., Todorova, T. I., Stanley, R. F., Ben-Neriah, S., Montagna, C., Parekh, S., Pellagatti, A., et al. (2012) · Blood · doi:10.1182/blood-2012-01-404699 · Cited by 201 · see citing works

Ablation of Fbxw7 Eliminates Leukemia-Initiating Cells by Preventing Quiescence

Takeishi, S., Matsumoto, A., Onoyama, I., Naka, K., Hirao, A., & Nakayama, K. I. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.01.026 · Cited by 177 · see citing works

Structure-based Design of High Affinity Peptides Inhibiting the Interaction of p53 with MDM2 and MDMX

Phan, J., Li, Z., Kasprzak, A., Li, B., Sebti, S., Guida, W., Schönbrunn, E., & Chen, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.073056 · Cited by 173 · see citing works

Antisense oligonucleotide–mediated MDM4 exon 6 skipping impairs tumor growth

Dewaele, M., Tabaglio, T., Willekens, K., Bezzi, M., Teo, S. X., Low, D. H. P., Koh, C. M., Rambow, F., Fiers, M. W. E. J., Rogiers, A., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci82534 · Cited by 173 · see citing works

Long-term haematopoietic reconstitution by Trp53-/-p16Ink4a-/-p19Arf-/- multipotent progenitors

Akala, O. O., Park, I.-K., Qian, D., Pihalja, M., Becker, M. W., & Clarke, M. F. (2008) · Nature · doi:10.1038/nature06869 · Cited by 168 · see citing works

p53 loss promotes acute myeloid leukemia by enabling aberrant self-renewalPreprint

Zhao, Z., Zuber, J. A., Díaz-Flores, E., Lintault, L., Kogan, S. C., Shannon, K., & Lowe, S. W. (2010) · Genes & Development · doi:10.1101/gad.1940710 · Cited by 167 · see citing works

Synergistic roles of Mdm2 and Mdm4 for p53 inhibition in central nervous system development

Xiong, S., Van Pelt, C. S., Elizondo-Fraire, A. C., Liu, G., & Lozano, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508500103 · Cited by 155 · see citing works

E2F7, a novel target, is up-regulated by p53 and mediates DNA damage-dependent transcriptional repression

Carvajal, L. A., Hamard, P.-J., Tonnessen, C., & Manfredi, J. J. (2012) · Genes &amp; Development · doi:10.1101/gad.184911.111 · Cited by 151 · see citing works

Hdmx Stabilizes Mdm2 and p53

Stad, R., Ramos, Y. F. M., Little, N., Grivell, S., Attema, J., van der Eb, A. J., & Jochemsen, A. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003496200 · Cited by 145 · see citing works

Mdm2 Is Required for Survival of Hematopoietic Stem Cells/Progenitors via Dampening of ROS-Induced p53 Activity

Abbas, H. A., Macció, D. R., Coşkun, S., Jackson, J. G., Hazen, A. L., Sills, T., You, M. J., Hirschi, K. K., & Lozano, G. (2010) · Cell stem cell · doi:10.1016/j.stem.2010.09.013 · Cited by 141 · see citing works

TP53 in hematological cancer: Low incidence of mutations with significant clinical relevance

PELLER, S., & Rotter, V. (2003) · Human Mutation · doi:10.1002/humu.10190 · Cited by 141 · see citing works

TXNIP maintains the hematopoietic cell pool by switching the function of p53 under oxidative stress

Jung, H., Kim, M. J., Kim, D. O., Kim, W. S., Yoon, S.-J., Park, Y.-J., Yoon, S. R., Kim, T.-D., Suh, H.-W., Yun, S., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.06.002 · Cited by 132 · see citing works

Molecular Basis for the Inhibition of p53 by Mdmx

Popowicz, G. M., Czarna, A., Rothweiler, U., Szwagierczak, A., Krajewski, M., Weber, L., & Holak, T. A. (2007) · Cell Cycle · doi:10.4161/cc.6.19.4740 · Cited by 131 · see citing works

HDAC8 Inhibition Specifically Targets Inv(16) Acute Myeloid Leukemic Stem Cells by Restoring p53 Acetylation

Qi, J., Singh, S., Hua, W.-K., Cai, Q., Chao, S.-W., Li, L., Liu, H., Ho, Y., McDonald, T., Lin, A., et al. (2015) · Cell stem cell · doi:10.1016/j.stem.2015.08.004 · Cited by 117 · see citing works

A Small-Molecule Inhibitor of MDMX Activates p53 and Induces Apoptosis

Wang, H., Ma, X., Ren, S., Buolamwini, J. K., & Yan, C. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0581 · Cited by 117 · see citing works

Mutations of the P53 gene in acute myeloid leukaemia

Fenaux, P., Preudhomme, C., Quiquandon, I., Jonveaux, P., Laı̈, J. L., Vanrumbeke, M., Loucheux‐Lefebvre, M. H., Bauters, F., Berger, R., & Kerckaert, J. P. (1992) · British Journal of Haematology · doi:10.1111/j.1365-2141.1992.tb08897.x · Cited by 117 · see citing works

Single-Cell and Single-Molecule Analysis of Gene Expression Regulation

Vera, M., Biswas, J., Senecal, A., Singer, R. H., & Park, H. Y. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-120215-034854 · Cited by 109 · see citing works

Acute myeloid leukemia patients clinical response to idasanutlin (RG7388) is associated with pre-treatment MDM2 protein expression in leukemic blasts

Reis, B., Jukofsky, L., Chen, G., Martinelli, G., Zhong, H., So, W. V., Dickinson, M. J., Drummond, M., Assouline, S., Hashemyan, M., et al. (2016) · Haematologica · doi:10.3324/haematol.2015.139717 · Cited by 91 · see citing works

SnapShot: Acute Myeloid Leukemia

Zeisig, B. B., Kulasekararaj, A. G., Mufti, G. J., & So, C. W. E. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.10.017 · Cited by 89 · see citing works

Mdm2 and Mdm4 Loss Regulates Distinct p53 Activities

Barboza, J., Iwakuma, T., Terzian, T., El‐Naggar, A. K., & Lozano, G. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-2079 · Cited by 89 · see citing works

Serum clinical chemistry and hematology reference values in outbred stocks of albino mice from three commonly used vendors and two inbred strains of albino mice.

Serfilippi, L. M., Pallman, D. R. S., & Russell, B. (2003) · PubMed · Cited by 89 · see citing works

The prognostic significance of p16INK4a/p14ARF locus deletion and MDM-2 protein expression in adult acute myelogenous leukemia

Faderl, S., Kantarjian, H. M., Estey, E. H., Manshouri, T., Chan, C., Elsaied, A. R., Kornblau, S. M., Cortes, J. E., Thomas, D. A., Pierce, S. A., et al. (2000) · Cancer · doi:10.1002/1097-0142(20001101)89:9 · Cited by 88 · see citing works

Spontaneous Tumorigenesis in Mice Overexpressing the p53-Negative Regulator Mdm4

Xiong, S., Pant, V., Suh, Y.-A., Van Pelt, C. S., Wang, Y., Valentin-Vega, Y. A., Post, S. M., & Lozano, G. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1457 · Cited by 82 · see citing works

Phase I trial of a novel stapled peptide ALRN-6924 disrupting MDMX- and MDM2-mediated inhibition of WT p53 in patients with solid tumors and lymphomas.

Meric‐Bernstam, F., Saleh, M. N., Infante, J. R., Goel, S., Falchook, G. S., Shapiro, G. I., Chung, K. Y., Conry, R. M., Hong, D. S., Wang, J. S.-Z., et al. (2017) · Journal of Clinical Oncology · doi:10.1200/jco.2017.35.15_suppl.2505 · Cited by 79 · see citing works

Whole genome sequence analysis links chromothripsis to EGFR, MDM2, MDM4, and CDK4 amplification in glioblastoma

Furgason, J. M., Koncar, R. F., Michelhaugh, S. K., Sarkar, F. H., Mittal, S., Sloan, A. E., Barnholtz‐Sloan, J. S., & Bahassi, E. M. (2015) · Oncoscience · doi:10.18632/oncoscience.178 · Cited by 65 · see citing works

The p53 tumor suppressor protein is a critical regulator of hematopoietic stem cell behavior

Liu, Y., Elf, S., Asai, T., Miyata, Y., Liu, Y., Sashida, G., Huang, G., Giandomenico, S. D., Koff, A., & Nimer, S. D. (2009) · Cell Cycle · doi:10.4161/cc.8.19.9627 · Cited by 65 · see citing works

Necdin, a p53 target gene, regulates the quiescence and response to genotoxic stress of hematopoietic stem/progenitor cells

Asai, T., Liu, Y., Giandomenico, S. D., Bae, N., Ndiaye‐Lobry, D., DeBlasio, A., Menéndez, S., Antipin, Y., Reva, B. A., Wevrick, R., et al. (2012) · Blood · doi:10.1182/blood-2011-11-393983 · Cited by 65 · see citing works

Alternate Splicing of the p53 Inhibitor HDMX Offers a Superior Prognostic Biomarker than p53 Mutation in Human Cancer

Lenos, K., Grawenda, A. M., Lodder, K., Kuijjer, M. L., Teunisse, A. F. A. S., Repapi, E., Grochola, L. F., Bartel, F., Hogendoorn, P. C. W., Wuerl, P., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0215 · Cited by 65 · see citing works

PAK1 is a therapeutic target in acute myeloid leukemia and myelodysplastic syndrome

Pandolfi, A., Stanley, R. F., Yu, Y., Bartholdy, B., Pendurti, G., Gritsman, K., Boultwood, J., Chernoff, J., Verma, A., & Steidl, U. G. (2015) · Blood · doi:10.1182/blood-2014-12-618801 · Cited by 60 · see citing works

Analysis of the p53 and MDM‐2 gene in acute myeloid leukemia

Seliger, B., Papadileris, S., Vogel, D. W., Heß, G., Brendel, C. A., Störkel, S., örtel, J., Kolbe, K., Huber, C. H., Huhn, D., et al. (1996) · European Journal Of Haematology · doi:10.1111/j.1600-0609.1996.tb01369.x · Cited by 56 · see citing works

Fine-tuning p53 activity through C-terminal modification significantly contributes to HSC homeostasis and mouse radiosensitivity

Wang, Y. V., Leblanc, M., Fox, N., Mao, J.-H., Tinkum, K. L., Krummel, K., Engle, D., Piwnica-Worms, D., Piwnica-Worms, H., Balmain, A., et al. (2011) · Genes &amp; Development · doi:10.1101/gad.2024411 · Cited by 53 · see citing works

p53 Basic C Terminus Regulates p53 Functions through DNA Binding Modulation of Subset of Target Genes

Hamard, P.-J., Lukin, D. J., & Manfredi, J. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.331298 · Cited by 48 · see citing works

Mechanistic validation of a clinical lead stapled peptide that reactivates p53 by dual HDM2 and HDMX targeting

Wachter, F., Morgan, A. M., Godes, M., Mourtada, R., Bird, G. H., & Walensky, L. D. (2016) · Oncogene · doi:10.1038/onc.2016.361 · Cited by 45 · see citing works

Targeting Mdmx to treat breast cancers with wild-type p53

Haupt, S., Buckley, D., Pang, J.-M., Panimaya, J., Paul, P. J., Gamell, C., Takano, E. A., Lee, Y. Y., Hiddingh, S., Rogers, T.-M., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.173 · Cited by 42 · see citing works

Assessing the Efficacy of Mdm2/Mdm4-Inhibiting Stapled Peptides Using Cellular Thermal Shift Assays

Tan, B. X., Brown, C. J., Ferrer, F. J., Yuen, T. Y., Quah, S. T., Chan, B. H., Jansson, A. E., Teo, H., Nordlund, P., & Lane, D. P. (2015) · Scientific Reports · doi:10.1038/srep12116 · Cited by 40 · see citing works

High Mdm4 levels suppress p53 activity and enhance its half-life in acute myeloid leukaemia

Tan, B. X., Khoo, K. H., Lim, T. M., & Lane, D. P. (2013) · Oncotarget · doi:10.18632/oncotarget.1559 · Cited by 34 · see citing works

TP53 mutations in older adults with acute myeloid leukemia

Yanada, M., Yamamoto, Y., Iba, S., Okamoto, A., Inaguma, Y., Tokuda, M., Morishima, S., Kanie, T., Mizuta, S., Akatsuka, Y., et al. (2016) · International Journal of Hematology · doi:10.1007/s12185-016-1942-1 · Cited by 34 · see citing works

MDM4 Overexpressed in Acute Myeloid Leukemia Patients with Complex Karyotype and Wild-Type TP53

Li, L., Tan, Y., Chen, X., Xu, Z., Yang, S., Ren, F., Guo, H., Wang, X., Chen, Y., Li, G., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113088 · Cited by 29 · see citing works

MDM4 (MDMX) is overexpressed in chronic lymphocytic leukaemia (CLL) and marks a subset of p53wild‐type CLL with a poor cytotoxic response to Nutlin‐3

Bo, M. D., Secchiero, P., Degan, M., Marconi, D., Bomben, R., Pozzato, G., Gaïdano, G., Poeta, G. D., Forconi, F., Zauli, G., et al. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08185.x · Cited by 26 · see citing works

High Expression of Human Homologue of Murine Double Minute 4 and the Short Splicing Variant, HDM4-S, in Bone Marrow in Patients With Acute Myeloid Leukemia or Myelodysplastic Syndrome

Han, X., Medeiros, L. J., Zhang, Y. H., You, M. J., Andreeff, M., Konopleva, M. Y., & Bueso-Ramos, C. (2016) · Clinical Lymphoma Myeloma & Leukemia · doi:10.1016/j.clml.2016.03.012 · Cited by 20 · see citing works

An observational study on the expression levels of MDM2 and MDMX proteins, and associated effects on P53 in a series of human liposarcomas

Touqan, N., Diggle, C. P., Verghese, E. T., Perry, S., Horgan, K. J., Merchant, W., Anwar, R., Markham, A. F., Carr, I., & Achuthan, R. (2013) · BMC Clinical Pathology · doi:10.1186/1472-6890-13-32 · Cited by 18 · see citing works

Aspiration method to collect epithelial cells from mouse, rat, and monkey oviducts.

Okada, H., Hirose, Y., Ito, M., & Sankai, T. (2003) · PubMed · Cited by 6 · see citing works

Targeting apoptosis in cancer therapy

Carneiro, B. A., & El‐Deiry, W. S. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0341-y · Cited by 2,594 · see citing works

Therapeutic Peptides: Current Applications and Future Directions

Wang, L., Wang, N., Zhang, W., Cheng, X., Yan, Z., Shao, G., Wang, X., Wang, R., & Fu, C. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00904-4 · Cited by 2,131 · see citing works

Trends in peptide drug discovery

Muttenthaler, M., King, G. F., Adams, D. J., & Alewood, P. F. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-00135-8 · Cited by 2,022 · see citing works

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

Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials

Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891 · see citing works

Tumor suppressor p53: Biology, signaling pathways, and therapeutic targeting

Borrero, L. J. H., & El‐Deiry, W. S. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188556 · Cited by 773 · see citing works

Drugging p53 in cancer: one protein, many targets

Hassin, O., & Oren, M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00571-8 · Cited by 736 · see citing works

Targeting mutant p53 for cancer therapy: direct and indirect strategies

Hu, J., Cao, J., Topatana, W., Juengpanich, S., Li, S., Zhang, B., Shen, J., Cai, L., Cai, X., & Chen, M. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01169-0 · Cited by 557 · see citing works

Understanding the complexity of p53 in a new era of tumor suppression

Liu, Y., Su, Z., Tavana, O., & Gu, W. J. (2024) · Cancer Cell · doi:10.1016/j.ccell.2024.04.009 · Cited by 519 · see citing works

Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials

Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · see citing works

Targeting p53 for the treatment of cancer

Duffy, M. J., Synnott, N. C., O’Grady, S., & Crown, J. P. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.07.005 · Cited by 351 · see citing works

Targeting p53–MDM2 interaction by small-molecule inhibitors: learning from MDM2 inhibitors in clinical trials

Zhu, H., Gao, H., Ji, Y., Zhou, Q., Du, Z., Tian, L., Jiang, Y., Yao, K., & Zhou, Z. (2022) · Journal of Hematology &amp; Oncology · doi:10.1186/s13045-022-01314-3 · Cited by 223 · see citing works

Dysregulated haematopoietic stem cell behaviour in myeloid leukaemogenesis

Yamashita, M., Dellorusso, P. V., Olson, O. C., & Passegue, E. A. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-0260-3 · Cited by 182 · see citing works

Phase 1 Trial of ALRN-6924, a Dual Inhibitor of MDMX and MDM2, in Patients with Solid Tumors and Lymphomas Bearing Wild-type <i>TP53</i>

Saleh, M. N., Patel, M. R., Bauer, T. M., Goel, S., Falchook, G. S., Shapiro, G. I., Chung, K. Y., Infante, J. R., Conry, R. M., Rabinowits, G., et al. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-0715 · Cited by 159 · see citing works

Current developments of targeting the p53 signaling pathway for cancer treatment

Huang, J. L. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107720 · Cited by 155 · see citing works

From Discovery to Bedside: Targeting the Ubiquitin System

Wertz, I. E., & Wang, X. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.10.022 · Cited by 157 · see citing works

Rational Design of Peptide-Based Inhibitors Disrupting Protein-Protein Interactions

Wang, X., Ni, D., Liu, Y., & Lu, S. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.682675 · Cited by 153 · see citing works

MDM2 Inhibitors for Cancer Therapy: The Past, Present, and Future

Wang, W., Albadari, N. G., Du, Y., Fowler, J. F., Sang, H. T., Xian, W., McKeon, F., Li, W., Zhou, J., & Zhang, R. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.123.001026 · Cited by 147 · see citing works

Discovery of Sulanemadlin (ALRN-6924), the First Cell-Permeating, Stabilized α-Helical Peptide in Clinical Development

Guerlavais, V., Sawyer, T. K., Carvajal, L. A., Chang, Y. S., Graves, B. J., Ren, J.-G., Sutton, D., Olson, K. A., Packman, K. E., Darłak, K., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00623 · Cited by 145 · see citing works

Charge-specific adverse effects of polystyrene nanoplastics on zebrafish (Danio rerio) development and behavior

Teng, M., Zhao, X., Wu, F., Wang, C., Wang, C., White, J. C., Zhao, W., Zhou, L., Yan, S., & Tian, S. (2022) · Environment International · doi:10.1016/j.envint.2022.107154 · Cited by 120 · see citing works

A DNA repair pathway can regulate transcriptional noise to promote cell fate transitions

Desai, R. V., Chen, X., Martin, B., Chaturvedi, S., Hwang, D.-W., Li, W., Chen, Y., Ding, S., Thomson, M. W., Singer, R. H., et al. (2021) · Science · doi:10.1126/science.abc6506 · Cited by 116 · see citing works

The role of TP53 in acute myeloid leukemia: Challenges and opportunities

Barbosa, K., Li, S., Adams, P. D., & Deshpande, A. J. (2019) · Genes Chromosomes and Cancer · doi:10.1002/gcc.22796 · Cited by 115 · see citing works

Peptide-Based Agents for Cancer Treatment: Current Applications and Future Directions

Nhàn, N. T. T., Yamada, T., & Yamada, K. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612931 · Cited by 109 · see citing works

Cyclic Peptides in Pipeline: What Future for These Great Molecules?

Costa, L., Sousa, E., & Fernandes, C. (2023) · Pharmaceuticals · doi:10.3390/ph16070996 · Cited by 106 · see citing works

Current challenges and unmet medical needs in myelodysplastic syndromes

Platzbecker, U., Kubasch, A. S., Homer-Bouthiette, C., & Prébet, T. (2021) · Leukemia · doi:10.1038/s41375-021-01265-7 · Cited by 102 · see citing works

Ubiquitin–proteasome system and the role of its inhibitors in cancer therapy

Aliabadi, F., Sohrabi, B., Mostafavi, E., Pazoki–Toroudi, H., & Webster, T. J. (2021) · Open Biology · doi:10.1098/rsob.200390 · Cited by 100 · see citing works

Precision medicine by designer interference peptides: applications in oncology and molecular therapeutics

Sorolla, A., Wang, E., Golden, E., Duffy, C., Henriques, S. T., Redfern, A. D., & Blancafort, P. (2019) · Oncogene · doi:10.1038/s41388-019-1056-3 · Cited by 94 · see citing works

Cell fate regulation governed by p53: Friends or reversible foes in cancer therapy

Song, B., Yang, P., & Zhang, S. (2024) · 癌症：英文版 · doi:10.1002/cac2.12520 · Cited by 97 · see citing works

Targeting MDM2 for novel molecular therapy: Beyond oncology

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

Human Oncoviruses and p53 Tumor Suppressor Pathway Deregulation at the Origin of Human Cancers

Tornesello, M. L., Annunziata, C., Tornesello, A. L., Buonaguro, L., & Buonaguro, F. M. (2018) · Cancers · doi:10.3390/cancers10070213 · Cited by 87 · see citing works

Pharmacological reactivation of p53 in the era of precision anticancer medicine

Tuval, A., Strandgren, C., Heldin, A., Palomar-Siles, M., & Wiman, K. G. (2023) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-023-00842-2 · Cited by 84 · see citing works

Targeting the Ubiquitin-Proteasome System for Cancer Therapeutics by Small-Molecule Inhibitors

LaPlante, G., & Zhang, W. (2021) · Cancers · doi:10.3390/cancers13123079 · Cited by 82 · see citing works

Redesigning of Cell-Penetrating Peptides to Improve Their Efficacy as a Drug Delivery System

Szabó, I., Yousef, M., Soltész, D. B., Bató, C., Mező, G., & Bánóczi, Z. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14050907 · Cited by 80 · see citing works

Therapeutic stapled peptides: Efficacy and molecular targets

Li, Y., Wu, M., Fu, Y., Xue, J., Yuan, F., Qu, T., Rissanou, A. N., Wang, Y., Li, X., & Hu, H. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107137 · Cited by 85 · see citing works

WWP2 regulates pathological cardiac fibrosis by modulating SMAD2 signaling

Chen, H., Moreno‐Moral, A., Pesce, F., Devapragash, N., Mancini, M., Heng, E. L., Rotival, M., Srivastava, P. K., Harmston, N., Shkura, K., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11551-9 · Cited by 75 · see citing works

Clonal hematopoiesis driven by chromosome 1q/MDM4 trisomy defines a canonical route toward leukemia in Fanconi anemia

Sébert, M., Gachet, S., Leblanc, T. M., Rousseau, A., Bluteau, O., Kim, R., Abdelali, R. B., de Fontbrune, F. S., Maillard, L., Fédronie, C., et al. (2023) · Cell stem cell · doi:10.1016/j.stem.2023.01.006 · Cited by 79 · see citing works

Programmed cell death, redox imbalance, and cancer therapeutics

Dai, X., Wang, D., & Zhang, J. (2021) · APOPTOSIS · doi:10.1007/s10495-021-01682-0 · Cited by 78 · see citing works

Prolonged Idasanutlin (RG7388) Treatment Leads to the Generation of p53-Mutated Cells

Skalniak, Ł., Kocik-Krol, J., Polak, J., Skalniak, A., Rak, M., Wolnicka-Głubisz, A., & Holak, T. A. (2018) · Cancers · doi:10.3390/cancers10110396 · Cited by 76 · see citing works

The Mettl3 epitranscriptomic writer amplifies p53 stress responses

Raj, N., Wang, M., Seoane, J. A., Zhao, R. L., Kaiser, A. M., Moonie, N. A., Demeter, J., Boutelle, A. M., Kerr, C. H., Mulligan, A. S., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.010 · Cited by 74 · see citing works

First in class dual MDM2/MDMX inhibitor ALRN-6924 enhances antitumor efficacy of chemotherapy in TP53 wild-type hormone receptor-positive breast cancer models

Pairawan, S., Zhao, M., Yuca, E., Annis, A., Evans, K., Sutton, D., Carvajal, L., Ren, J.-G., Santiago, S., Guerlavais, V., et al. (2021) · Breast Cancer Research · doi:10.1186/s13058-021-01406-x · Cited by 73 · see citing works

Cytotoxic and antitumor peptides as novel chemotherapeutics

Luan, X., Wu, Y., Shen, Y., Zhang, H., Zhou, Y., Chen, H., Nagle, D. G., & Zhang, W. (2020) · Natural Product Reports · doi:10.1039/d0np00019a · Cited by 72 · see citing works

Nanoparticle Conjugation Stabilizes and Multimerizes β-Hairpin Peptides To Effectively Target PD-1/PD-L1 β-Sheet-Rich Interfaces

Jeong, W., Bu, J., Han, Y., Drelich, A. J., Nair, A., Král, P., & Hong, S. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10160 · Cited by 70 · see citing works

The Renaissance of Cyclin Dependent Kinase Inhibitors

Ettl, T., Schulz, D., & Bauer, R. J. (2022) · Cancers · doi:10.3390/cancers14020293 · Cited by 71 · see citing works

Advanced Strategies for Therapeutic Targeting of Wild-Type and Mutant p53 in Cancer

Zhang, S., Carlsen, L., Borrero, L. J. H., Seyhan, A. A., Tian, X., & El‐Deiry, W. S. (2022) · Biomolecules · doi:10.3390/biom12040548 · Cited by 71 · see citing works

The long and the short of it: the MDM4 tail so far

Haupt, S., Mejía-Hernández, J. O., Vijayakumaran, R., Keam, S. P., & Haupt, Y. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz007 · Cited by 69 · see citing works

Resistance mechanisms to inhibitors of p53-MDM2 interactions in cancer therapy: can we overcome them?

Hároníková, L., Bonczek, O., Zatloukalová, P., Kokas, F. Z., Kucerikova, M., Coates, P. J., Fåhræus, R., & Vojtěšek, B. (2021) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-021-00293-6 · Cited by 71 · see citing works

Bioactive peptides: an alternative therapeutic approach for cancer management

Ghadiri, N., Javidan, M., Sheikhi, S., Taştan, Ö., Parodi, A., Liao, Z., Azar, M. T., & Ganjalıkhani-Hakemi, M. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1310443 · Cited by 66 · see citing works

The nucleolus, an ally, and an enemy of cancer cells

Stępiński, D. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1706-5 · Cited by 66 · see citing works

It’s Getting Complicated—A Fresh Look at p53-MDM2-ARF Triangle in Tumorigenesis and Cancer Therapy

Kung, C.-P., & Weber, J. D. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.818744 · Cited by 68 · see citing works

Targeting the p53 signaling pathway in cancers: Molecular mechanisms and clinical studies

Shen, J., Wang, Q., Mao, Y., Gao, W., & Duan, S. (2023) · MedComm · doi:10.1002/mco2.288 · Cited by 66 · see citing works

The p53/MDM2/MDMX-targeted therapies – a clinical synopsis

Jiang, L., & Zawacka-Pankau, J. (2020) · Cell Death &amp; Disease · doi:10.1038/s41419-020-2445-9 · Cited by 62 · see citing works

A Balancing Act: p53 Activity from Tumor Suppression to Pathology and Therapeutic Implications

Wang, M., & Attardi, L. D. (2021) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-042320-025840 · Cited by 60 · see citing works

Molecular glues modulate protein functions by inducing protein aggregation: A promising therapeutic strategy of small molecules for disease treatment

Wu, H., Yao, H., He, C., Jia, Y., Zhu, Z., Xu, S., Li, D., & Xu, J. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.03.019 · Cited by 60 · see citing works

Targeting the MDM2-p53 pathway in dedifferentiated liposarcoma

Traweek, R. S., Cope, B. M., Roland, C. L., Keung, E. Z.-Y., Nassif, E. F., & Erstad, D. J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1006959 · Cited by 61 · see citing works

Studying protein–protein interactions: Latest and most popular approaches

Akbarzadeh, S., Coşkun, Ö., & Günçer, B. (2024) · Journal of Structural Biology · doi:10.1016/j.jsb.2024.108118 · Cited by 58 · see citing works

Incorporation of Putative Helix-Breaking Amino Acids in the Design of Novel Stapled Peptides: Exploring Biophysical and Cellular Permeability Properties

Partridge, A. W., Kaan, H. Y. K., Juang, Y.-C. A., Sadruddin, A., Lim, S., Brown, C. J., Ng, S., Thean, D., Ferrer, F. J., Johannes, C. W., et al. (2019) · Molecules · doi:10.3390/molecules24122292 · Cited by 57 · see citing works

Structure-Based Design of Potent and Orally Active Isoindolinone Inhibitors of MDM2-p53 Protein–Protein Interaction

Chessari, G., Hardcastle, I. R., Ahn, J. S., Anil, B., Anscombe, E., Bawn, R. H., Bevan, L., Blackburn, T. J., Buck, I. M., Cano, C., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02188 · Cited by 58 · see citing works

Paralog-specific signaling by IRAK1/4 maintains MyD88-independent functions in MDS/AML

Bennett, J. R., Ishikawa, C., Agarwal, P., Yeung, J., Sampson, A. M., Uible, E. E., Vick, E. J., Bolanos, L. C., Hueneman, K. M., Wunderlich, M., et al. (2023) · Blood · doi:10.1182/blood.2022018718 · Cited by 56 · see citing works

Bioactive Peptides and Proteins from Wasp Venoms

Luo, L., Kamau, P. M., & Lai, R. (2022) · Biomolecules · doi:10.3390/biom12040527 · Cited by 55 · see citing works

Harnessing the Therapeutic Potential of Biomacromolecules through Intracellular Delivery of Nucleic Acids, Peptides, and Proteins

Tian, Y. P., Tirrell, M., & LaBelle, J. L. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202102600 · Cited by 51 · see citing works

Targeting the MTF2–MDM2 Axis Sensitizes Refractory Acute Myeloid Leukemia to Chemotherapy

Maganti, H. B., Jrade, H., Cafariello, C., Rothberg, J. L. M., Porter, C. J., Yockell‐Lelièvre, J., Battaion, H. L., Khan, S. T., Howard, J. P., Li, Y., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-0841 · Cited by 60 · see citing works

Recent CPP-based applications in medicine

Kurrikoff, K., & Langel, Ü. (2019) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2019.1665021 · Cited by 52 · see citing works

Targeting MDMX for Cancer Therapy: Rationale, Strategies, and Challenges

Yu, D.-H., Xu, Z., Mo, S., Li, Y., Cheng, X., & Qin, J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01389 · Cited by 51 · see citing works

TP53 in Acute Myeloid Leukemia: Molecular Aspects and Patterns of Mutation

George, B., Kantarjian, H. M., Baran, N., Krocker, J. D., & Rios, A. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910782 · Cited by 50 · see citing works

Relapsed pediatric acute myeloid leukaemia: state-of-the-art in 2023

Egan, G., & Tasian, S. K. (2023) · Haematologica · doi:10.3324/haematol.2022.281106 · Cited by 47 · see citing works

Recent Progress and Clinical Development of Inhibitors that Block MDM4/p53 Protein–Protein Interactions

Zhang, S., Lou, J., Li, Y., Zhou, F., Yan, Z., Lyu, X., & Zhao, Y. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00940 · Cited by 47 · see citing works

An improved imaging system that corrects MS2-induced RNA destabilization

Li, W., Maekiniemi, A., Sato, H., Osman, C., & Singer, R. H. (2022) · Nature Methods · doi:10.1038/s41592-022-01658-1 · Cited by 46 · see citing works

Targeting Mitochondrial Metabolic Reprogramming as a Potential Approach for Cancer Therapy

Zhang, L., Wei, Y., Yuan, S., & Sun, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054954 · Cited by 48 · see citing works

A therapeutic patent overview of MDM2/X-targeted therapies (2014–2018)

Skalniak, Ł., Surmiak, E., & Holak, T. A. (2019) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2019.1582645 · Cited by 45 · see citing works

Genetic biomarkers of drug resistance: A compass of prognosis and targeted therapy in acute myeloid leukemia

Long, L., Assaraf, Y. G., Lei, Z., Peng, H., Yang, L., Chen, Z., & Ren, S. (2020) · Drug Resistance Updates · doi:10.1016/j.drup.2020.100703 · Cited by 45 · see citing works

TP53 Status, Patient Sex, and the Immune Response as Determinants of Lung Cancer Patient Survival

Freudenstein, D., Litchfield, C., Caramia, F., Wright, G. M., Solomon, B., Ball, D., Keam, S. P., Neeson, P. J., Haupt, Y., & Haupt, S. (2020) · Cancers · doi:10.3390/cancers12061535 · Cited by 44 · see citing works

Computational Modeling as a Tool to Investigate PPI: From Drug Design to Tissue Engineering

Pérez, J. J., Pérez, R. A., & Pérez, A. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.681617 · Cited by 43 · see citing works

TP53 in MDS and AML: Biological and clinical advances

Zhao, Y., Chen, W., Yu, J., Pei, S., Zhang, Q., Shi, J., Huang, H., & Zhao, Y. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216767 · Cited by 44 · see citing works

Landscape of Tumor Suppressor Mutations in Acute Myeloid Leukemia

Panuzzo, C., Signorino, E., Calabrese, C., Ali, M. S., Petiti, J., Bracco, E., & Cilloni, D. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9030802 · Cited by 42 · see citing works

Emerging Pharmacotherapeutic Strategies to Overcome Undruggable Proteins in Cancer

Lu, Y., Yang, Y., Zhu, G., Zeng, H., Fan, Y., Guo, F., Xu, D., Wang, B., Chen, D., & Ge, G. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.83026 · Cited by 41 · see citing works

Strategies for development of synthetic heart valve tissue engineering scaffolds

Snyder, Y., & Jana, S. (2023) · Progress in Materials Science · doi:10.1016/j.pmatsci.2023.101173 · Cited by 39 · see citing works

A tetrameric protein scaffold as a nano-carrier of antitumor peptides for cancer therapy

Ma, B., Niu, F., Qu, X., He, W., Feng, C., Wang, S., Ouyang, Z., Yan, J., Wen, Y., Xu, D., et al. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.03.004 · Cited by 39 · see citing works

Towards design of drugs and delivery systems with the Martini coarse-grained model

Kjølbye, L. R., Pereira, G. P., Bartocci, A., Pannuzzo, M., Albani, S., Marchetto, A., Jiménez‐García, B., Martin, J., Rossetti, G., Cecchini, M., et al. (2022) · QRB Discovery · doi:10.1017/qrd.2022.16 · Cited by 39 · see citing works

Leukemic stem cells as a target for eliminating acute myeloid leukemia: Gaps in translational research

Khaldoyanidi, S. K., Hindoyan, A. A., Stein, A. S., & Subklewe, M. (2022) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2022.103710 · Cited by 38 · see citing works

Emerging concepts and challenges in the development of disease-modifying osteoarthritis drugs – a more refined perspective

Jenei-Lanzl, Z., Maurer, S., Brenner, R. E., Zaucke, F., Fuchs, M., & Riegger, J. (2025) · Archives of pharmacal research · doi:10.1007/s12272-025-01551-3 · Cited by 35 · see citing works

Polymeric nanomedicines targeting hematological malignancies

Gu, W., Qu, R., Meng, F., Cornelissen, J. J. L. M., & Zhong, Z. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.08.001 · Cited by 35 · see citing works

p53 and Myofibroblast Apoptosis in Organ Fibrosis

McElhinney, K., Irnaten, M., & O'Brien, C. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076737 · Cited by 33 · see citing works

MDMX acts as a pervasive preleukemic-to-acute myeloid leukemia transition mechanism

Ueda, K., Kumari, R., Schwenger, E., Wheat, J. C., Bohorquez, O., Narayanagari, S.-R., Taylor, S. J., Carvajal, L. A., Pradhan, K., Bartholdy, B., et al. (2021) · Cancer Cell · doi:10.1016/j.ccell.2021.02.006 · Cited by 33 · see citing works

Dissecting the Transcriptional and Chromatin Accessibility Heterogeneity of Proliferating Cone Precursors in Human Retinoblastoma Tumors by Single Cell Sequencing—Opening Pathways to New Therapeutic Strategies?

Collin, J., Queen, R. A., Zerti, D., STEEL, D. H., Bowen, C., Parulekar, M., & Lako, M. (2021) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.62.6.18 · Cited by 34 · see citing works

Targeting protein-protein interactions in drug discovery: Modulators approved or in clinical trials for cancer treatment

Camps-Fajol, C., Cavero, D., Minguillón, J., & Surrallés, J. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107544 · Cited by 35 · see citing works

Hitting Undruggable Targets: Viewing Stabilized Peptide Development through the Lens of Quantitative Systems Pharmacology

Atangcho, L., Navaratna, T. A., & Thurber, G. M. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.11.008 · Cited by 31 · see citing works

Targeting WEE1/AKT Restores p53-Dependent Natural Killer–Cell Activation to Induce Immune Checkpoint Blockade Responses in “Cold” Melanoma

Dinavahi, S. S., Chen, Y., Punnath, K., Berg, A. S., Herlyn, M., Foroutan, M., Huntington, N. D., & Robertson, G. P. (2022) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-21-0587 · Cited by 31 · see citing works

MDM2 inhibition in the treatment of glioblastoma: From concept to clinical investigation

Pellot Ortiz, K. I., Rechberger, J. S., Nonnenbroich, L. F., Daniels, D. J., & Sarkaria, J. N. (2023) · Biomedicines · doi:10.3390/biomedicines11071879 · Cited by 30 · see citing works

MiR-1205 functions as a tumor suppressor by disconnecting the synergy between KRAS and MDM4/E2F1 in non-small cell lung cancer.

Yan, H., Chen, X., Li, Y., Fan, L., Tai, Y., Zhou, Y., Chen, Y., Qi, X., Huang, R., & Ren, J. (2019) · Europe PMC (PubMed Central) · Cited by 30 · see citing works

TIFA and TIFAB: FHA-domain proteins involved in inflammation, hematopoiesis, and disease

Niederkorn, M., Agarwal, P., & Starczynowski, D. T. (2020) · Experimental Hematology · doi:10.1016/j.exphem.2020.08.010 · Cited by 30 · see citing works

Structural States of Hdm2 and HdmX: X‐ray Elucidation of Adaptations and Binding Interactions for Different Chemical Compound Classes

Kallen, J. A., Izaac, A., Chau, S., Wirth, E., Schoepfer, J. G., Mah, R., Schlapbach, A., Stutz, S., Vaupel, A., Guagnano, V., et al. (2019) · ChemMedChem · doi:10.1002/cmdc.201900201 · Cited by 30 · see citing works

Advances in the Study of Structural Modification and Biological Activities of Anoplin

Wu, Y., Huang, R., Jin, J., Zhang, L., Zhang, H., Chen, H., Chen, L.-L., & Luan, X. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00519 · Cited by 30 · see citing works

Structure-Based Discovery of MDM2/4 Dual Inhibitors that Exert Antitumor Activities against MDM4-Overexpressing Cancer Cells

Zhang, S., Yan, Z., Li, Y., Gong, Y., Lyu, X., Lou, J., Zhang, D., Meng, X., & Zhao, Y. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00095 · Cited by 29 · see citing works

Application of omics in the diagnosis, prognosis, and treatment of acute myeloid leukemia

Zhang, Z., Huang, J., Zhang, Z., Shen, H., Tang, X., Wu, D., Bao, X., Xu, G., & Chen, S. (2024) · Biomarker Research · doi:10.1186/s40364-024-00600-1 · Cited by 30 · see citing works

Cell-penetrating peptides as part of therapeutics used in cancer research

Matijass, M., & Neundorf, I. (2021) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2021.100092 · Cited by 28 · see citing works

Current insights into the regulation of programmed cell death by TP53 mutation in cancer

Su, Y., Sai, Y., Zhou, L., Liu, Z., Du, P., Wu, J., & Zhang, J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1023427 · Cited by 28 · see citing works

Salvation of the fallen angel: Reactivating mutant p53

Yang, L., Wang, Z., Chen, Y., Petersen, R. B., Zheng, L., & Huang, K. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14572 · Cited by 26 · see citing works

Therapeutic Strategies to Activate p53

Aguilar, A., & Wang, S. (2022) · Pharmaceuticals · doi:10.3390/ph16010024 · Cited by 27 · see citing works

MDM2-p53 Interaction Inhibitors: The Current State-of-Art and Updated Patent Review (2010-Present)

Rusiecki, R., Witkowski, J., & Jaszczewska‐Adamczak, J. A. (2019) · Recent Patents on Anti-Cancer Drug Discovery · doi:10.2174/1574892814666191022163540 · Cited by 27 · see citing works

Targeting Apoptosis in AML: Where Do We Stand?

Krawiec, K. M., Strzałka, P., Czemerska, M., Wiśnik, A., Zawlik, I., Wierzbowska, A., & Pluta, A. (2022) · Cancers · doi:10.3390/cancers14204995 · Cited by 26 · see citing works

Dual Inhibition of Mdmx and Mdm2 Using an Alpha-Helical P53 Stapled Peptide (ALRN-6924) As a Novel Therapeutic Strategy in Acute Myeloid Leukemia

Carvajal, L. A., Neriah, D. B., Senecal, A., Bernard, L., Narayanagari, S.-R., Kenworthy, C. A., Thiruthuvanathan, V. J., Guerlavais, V., Annis, D. A., Bartholdy, B., et al. (2017) · Blood · doi:10.1182/blood.v130.suppl_1.795.795 · Cited by 7 · see citing works

Dual inhibition of HDMX and HDM2 in acute myeloid leukemia

Carvajal, L. A., Neriah, D. B., Senecal, A., Benard, L., Narayanagari, S.-R., Kenworhty, C., Thiruthuvanathan, V. J., Guerlavais, V., Annis, A., Bartholdy, B., et al. (2017) · Experimental Hematology · doi:10.1016/j.exphem.2017.06.058

Dual Targeting of MDMX and MDM2 Has Antileukemic Activity

(2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-rw2018-068

SBMB-004: A first-in-class dual MDM2/BRD4 inhibitor restoring p53 function and suppressing oncogenic transcription in acute myeloid leukemia

Abohassan, M., Shahrani, M. M. A., & Rajagopalan, P. (2026) · Journal of Biomedical Research · doi:10.7555/jbr.39.20250492

Restoring p53 activity

Crunkhorn, S. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.81 · Cited by 2 · see citing works