The Drug-Induced Degradation of Oncoproteins: An Unexpected Achilles' Heel of Cancer Cells?
Abstract
Many targeted therapies against cancer are aimed at inhibiting the enzymatic activity of kinases. Thus far, this approach has undoubtedly yielded significant clinical improvements, but has only rarely achieved cures. Other drugs, which selectively elicit proteasome-dependent degradation of oncoproteins, induce the loss of cancer cell self-renewal and promote cell differentiation and/or apoptosis. In acute promyelocytic leukemia, the cooperative degradation of PML/RARA by arsenic and retinoic acid cures most patients. In this condition and others, drug-induced proteolysis of oncoproteins is feasible and underlies improved clinical outcome. Several transcription factors, nuclear receptors, or fusion proteins driving cancer growth could be candidates for proteolysis-based drug-discovery programs. Summary: Some cancer therapies may degrade oncoproteins. Loss of the driver oncoprotein is associated with loss of cancer cell self-renewal. Leukemia- or sarcoma-associated fusion proteins are the best candidates for small-molecule screens aimed at initiating oncoprotein degradation. Cancer Discovery; 1(2). 117–27. ©2011 AACR.
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Targeted protein degradation has recently gained significant interest as an alternative cancer therapy approach.
“Notably, targeted protein degradation has recently gained significant interest as an alternative cancer therapy approach [40,41].”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [40]
Cites
Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works
Patterns of somatic mutation in human cancer genomes
Greenman, C. D., Stephens, P., Smith, R., Dalgliesh, G. L., Hunter, C., Bignell, G. R., Davies, H. R., Teague, J. W., Butler, A. P., Stevens, C., et al. (2007) · Nature · doi:10.1038/nature05610 · Cited by 3,062 · see citing works
Development of a second-generation antiandrogen for treatment of advanced prostate cancer.
Tran, C., Ouk, S., Clegg, N. J., Chen, Y., Watson, P. A., Arora, V., Wongvipat, J., Smith-Jones, P. M., Yoo, D., Kwon, A., et al. (2009) · Science · doi:10.1126/science.1168175 · Cited by 2,292 · see citing works
Shah, N. P., Nicoll, J. M., Nagar, B., Gorre, M. E., PAQUETTE, R. L., Kuriyan, J., & Sawyers, C. L. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00096-x · Cited by 1,608 · see citing works
Mahon, F., Réa, D., Guilhot, J., Guilhot, F., Huguet, F., Nicolini, F. E., Legros, L., Charbonnier, A., Guerci‐Bresler, A., Varet, B. R., et al. (2010) · The Lancet Oncology · doi:10.1016/s1470-2045(10)70233-3 · Cited by 1,541 · see citing works
de Thé, H., Lavau, C., Marchio, A., Chomienne, C., Degos, L., & Dejean, A. (1991) · Cell · doi:10.1016/0092-8674(91)90113-d · Cited by 1,331 · see citing works
Acute promyelocytic leukemia: from highly fatal to highly curable
Wang, Z., & Chen, Z. (2008) · Blood · doi:10.1182/blood-2007-07-102798 · Cited by 1,283 · see citing works
Oncogenic Transcription Factors in the Human Acute Leukemias
Look, A. T. (1997) · Science · doi:10.1126/science.278.5340.1059 · Cited by 1,206 · see citing works
Conversion of Bcl-2 to a Bax-like Death Effector by Caspases
Cheng, E. H. Y., Kirsch, D. G., Clem, R. J., Ravi, R. K., Kastan, M. B., Bedi, A., Ueno, K., & Hardwick, J. M. (1997) · Science · doi:10.1126/science.278.5345.1966 · Cited by 1,106 · see citing works
Welcker, M., & Clurman, B. E. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2290 · Cited by 1,084 · see citing works
Melnick, A. M., & Licht, J. D. (1999) · Blood · doi:10.1182/blood.v93.10.3167.410k44_3167_3215 · Cited by 1,024 · see citing works
Craft, N., Shostak, Y., Carey, M., & Sawyers, C. L. (1999) · Nature Medicine · doi:10.1038/6495 · Cited by 980 · see citing works
Enhancement of proteasome activity by a small-molecule inhibitor of USP14
Lee, B., Lee, M. J., Park, S., Oh, D., Elsasser, S., Chen, P., Gartner, C. A., Dimova, N. V., Hanna, J. W., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 943 · see citing works
Transcriptome sequencing to detect gene fusions in cancer
Maher, C. A., Kumar‐Sinha, C., Cao, X., Sundaram, S. K., Han, B., Jing, X., Sam, L. T., Barrette, T. R., Palanisamy, N., & Chinnaiyan, A. M. (2009) · Nature · doi:10.1038/nature07638 · Cited by 887 · see citing works
Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
Bernardi, R., & Pandolfi, P. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2277 · Cited by 876 · see citing works
Carvalho, A. L., Nishimoto, I. N., Califano, J. A., & Kowalski, L. P. (2004) · International Journal of Cancer · doi:10.1002/ijc.20740 · Cited by 867 · see citing works
Chen, G.-Q., Zhu, J., Shi, X., Ni, J., Zhong, H., Si, G., Jin, X., Tang, W., Li, X., Xong, S., et al. (1996) · Blood · doi:10.1182/blood.v88.3.1052.1052 · Cited by 863 · see citing works
Dynamics of chronic myeloid leukaemia
Franziska Michor, A., Hughes, T. P., Iwasa, Y., Branford, S., Shah, N. P., Sawyers, C. L., & Nowak, M. A. (2005) · Nature · doi:10.1038/nature03669 · Cited by 834 · see citing works
Complex landscapes of somatic rearrangement in human breast cancer genomes
Stephens, P. J., McBride, D. J., Lin, M., Varela, I., Pleasance, E., Simpson, J. T., Stebbings, L. A., Leroy, C., Edkins, S., Mudie, L. J., et al. (2009) · Nature · doi:10.1038/nature08645 · Cited by 833 · see citing works
Human T-cell leukaemia virus type 1 (HTLV-1) infectivity and cellular transformation
Matsuoka, M., & Jeang, K.-T. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2111 · Cited by 829 · see citing works
Genetic variegation of clonal architecture and propagating cells in leukaemia
Anderson, K., Lutz, C., van Delft, F. W., Bateman, C. M., Guo, Y., Colman, S., Kempski, H. M., Moorman, A. V., Titley, I., Swansbury, J. G., et al. (2010) · Nature · doi:10.1038/nature09650 · Cited by 803 · see citing works
How the ubiquitin–proteasome system controls transcription
Muratani, M., & Tansey, W. P. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1049 · Cited by 803 · see citing works
Chen, G., Shi, X., Tang, W., Xiong, S. M., Zhu, J., Cai, X., Han, Z., Ni, J.-H., Shi, G., Jia, P.-M., et al. (1997) · PubMed · Cited by 787 · see citing works
Reid, G., Hübner, M. R., Métivier, R., Brand, H., Denger, S., Manu, D., Beaudouin, J., Ellenberg, J., & Gannon, F. (2003) · Molecules and Cells · doi:10.1016/s1097-2765(03)00090-x · Cited by 787 · see citing works
PAX8-PPAR γ 1 Fusion in Oncogene Human Thyroid Carcinoma
Kroll, T. G., Sarraf, P., Pecciarini, L., Chen, C., Mueller, E., Spiegelman, B. M., & Fletcher, J. A. (2000) · Science · doi:10.1126/science.289.5483.1357 · Cited by 780 · see citing works
Arsenic degrades PML or PML–RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathway
Lallemand-Breitenbach, V., Jeanne, M., Benhenda, S., Nasr, R., Lei, M., Pérès, L., Zhou, J., Zhu, J., Raught, B., & de Thé, H. (2008) · Nature Cell Biology · doi:10.1038/ncb1717 · Cited by 726 · see citing works
Self-citationTP53 Mutation and Survival in Chronic Lymphocytic Leukemia
Zenz, T., Eichhorst, B. F., Busch, R. M., Denzel, T., Häbe, S., Winkler, D. F. H., Bühler, A., Edelmann, J., Bergmann, M., Hopfinger, G., et al. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.27.8762 · Cited by 617 · see citing works
Proteasome-dependent degradation of the human estrogen receptor
Nawaz, Z., Lonard, D. M., Dennis, A. P., Smith, C. L., & O’Malley, B. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1858 · Cited by 589 · see citing works
Shen, Z., Shi, Z., Fang, J., Gu, B.-W., Li, J., Zhu, Y., Shi, J., Zheng, P., Yan, H., Liu, Y., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400053101 · Cited by 583 · see citing works
The Role of PML in Tumor Suppression
Salomoni, P., & Pandolfi, P. P. (2002) · Cell · doi:10.1016/s0092-8674(02)00626-8 · Cited by 564 · see citing works
PML Nuclear BodiesPreprint
Lallemand-Breitenbach, V., & de Thé, H. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000661 · Cited by 561 · see citing works
Immunoproteasomes Preserve Protein Homeostasis upon Interferon-Induced Oxidative Stress
Seifert, U., Biały, Ł. P., Ebstein, F., Bech‐Otschir, D., Beling, A., Schröter, F., Prozorovski, T., Lange, N., Steffen, J., Rieger, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.036 · Cited by 554 · see citing works
PML targeting eradicates quiescent leukaemia-initiating cells
Ito, K., Bernardi, R., Morotti, A., Matsuoka, S., Saglio, G. N., Ikeda, Y., Rosenblatt, J. M., Avigan, D., Teruya‐Feldstein, J., & Pandolfi, P. P. (2008) · Nature · doi:10.1038/nature07016 · Cited by 538 · see citing works
Use of arsenic trioxide (As2O3) in the treatment of patients with acute promyelocytic leukemia
Lazo, G., Kantarjian, H. M., Estey, E. H., Thomas, D. A., O'Brien, S. M., & Cortes, J. E. (2003) · Cancer · doi:10.1002/cncr.11314 · Cited by 493 · see citing works
Acute promyelocytic leukaemia: novel insights into the mechanisms of cure
de Thé, H., & Zhu, C. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2943 · Cited by 490 · see citing works
Lallemand-Breitenbach, V., Zhu, J., Puvion-dutilleul, F., Koken, M. H. M., Honoré, N., Doubeikovsky, A., Duprez, E., Pandolfi, P. P., Puvion, E., Freemont, P. S., et al. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.12.1361 · Cited by 488 · see citing works
Staudt, L. M. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000109 · Cited by 485 · see citing works
In utero rearrangements in the trithorax-related oncogene in infant leukaemias
Ford, A. M., Ridge, S. A., Cabrera, M. E., et al. (1993) · Nature · doi:10.1038/363358a0 · Cited by 459 · see citing works
Zhu, J., Koken, M. H. M., Quignon, F., Chelbi‐Alix, M. K., Degos, L., Wang, Z. Y., Chen, Z., & de Thé, H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3978 · Cited by 426 · see citing works
Hu, J., Liu, Y.-F., Wu, C.-F., Xu, F., Shen, Z.-X., Zhu, Y., Li, J., Tang, W., Zhao, W.-L., Wu, W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813280106 · Cited by 425 · see citing works
Initiating and Cancer-Propagating Cells in TEL-AML1 -Associated Childhood Leukemia
Hong, D., Gupta, R., Ancliff, P., Atzberger, A., Brown, J., Soneji, S., Green, J., Colman, S., Piacibello, W., Buckle, V. J., et al. (2008) · Science · doi:10.1126/science.1150648 · Cited by 393 · see citing works
FLT3 as a therapeutic target in AML: still challenging after all these years
Kindler, T., Lipka, D. B., & Fischer, T. (2010) · Blood · doi:10.1182/blood-2010-04-261867 · Cited by 384 · see citing works
Zhu, J., Gianni’, M., Kopf, E., Honoré, N., Chelbi‐Alix, M. K., Koken, M. H. M., Quignon, F., Rochette‐Egly, C., & de Thé, H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14807 · Cited by 371 · see citing works
Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy
Goldberg, A. L. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350012 · Cited by 370 · see citing works
Hauser, S., Adelmant, G., Sarraf, P., Wright, H. M., Mueller, E., & Spiegelman, B. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001297200 · Cited by 367 · see citing works
Eradication of acute promyelocytic leukemia-initiating cells through PML-RARA degradation
Nasr, R., Guillemin, M.-C., Ferhi, O., Soilihi, H., Pérès, L., Berthier, C., Rousselot, P. H., Robledo-Sarmiento, M., Lallemand-Breitenbach, V., Gourmel, B., et al. (2008) · Nature Medicine · doi:10.1038/nm.1891 · Cited by 354 · see citing works
Self-citationShao, W., Fanelli, M., Ferrara, F. F., Riccioni, R., Rosenauer, A., Davison, K. L., Lamph, W. W., Waxman, S., Pelicci, P. G., Lo‐Coco, F., et al. (1998) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/90.2.124 · Cited by 342 · see citing works
Ingle, J. N., Ahmann, D. L., Green, S., et al. (1981) · New England Journal of Medicine · doi:10.1056/nejm198101013040104 · Cited by 337 · see citing works
PML/RARA Oxidation and Arsenic Binding Initiate the Antileukemia Response of As2O3
Jeanne, M., Lallemand-Breitenbach, V., Ferhi, O., Koken, M. H. M., Bras, M. L., Duffort, S., Pérès, L., Berthier, C., Soilihi, H., Raught, B., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.06.003 · Cited by 332 · see citing works
Lallemand-Breitenbach, V., Guillemin, M.-C., Janin, A., Daniel, M., Degos, L., Kogan, S. C., Bishop, J. M., & de Thé, H. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.7.1043 · Cited by 306 · see citing works
How I treat acute promyelocytic leukemia
Tallman, M. S., & Altman, J. K. (2009) · Blood · doi:10.1182/blood-2009-07-216457 · Cited by 284 · see citing works
Hasegawa, H., Sawa, H., Lewis, M. J., Orba, Y., Sheehy, N., Yamamoto, Y., Ichinohe, T., Tsunetsugu‐Yokota, Y., Katano, H., Takahashi, H., et al. (2006) · Nature Medicine · doi:10.1038/nm1389 · Cited by 282 · see citing works
Varshavsky, A. J. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.04.005 · Cited by 281 · see citing works
Zuber, J., McJunkin, K., Fellmann, C., Dow, L. E., Taylor, M. J., Hannon, G., & Lowe, S. (2010) · Nature Biotechnology · doi:10.1038/nbt.1720 · Cited by 277 · see citing works
Autophagy contributes to therapy-induced degradation of the PML/RARA oncoprotein
Isakson, P., Bjørås, M., Bøe, S. O., & Simonsen, A. (2010) · Blood · doi:10.1182/blood-2010-01-261040 · Cited by 269 · see citing works
Marcucci, F., & Mele, A. (2010) · Blood · doi:10.1182/blood-2010-06-275818 · Cited by 266 · see citing works
Mathews, V., George, B., Chendamarai, E., Lakshmi, K. M., Desire, S., Balasubramanian, P., Viswabandya, A., Rajashekar, T., Abraham, A., Velayudhan, S. R., et al. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2010.28.5031 · Cited by 250 · see citing works
Wu, X., Hawse, J. R., Subramaniam, M., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3933 · Cited by 225 · see citing works
Rational Combinations Using HDAC Inhibitors
Bots, M. L., & Johnstone, R. W. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2786 · Cited by 218 · see citing works
Cheskis, B. J., Greger, J., Nagpal, S., & Freedman, L. P. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21253 · Cited by 212 · see citing works
Advances in estrogen receptor biology: prospects for improvements in targeted breast cancer therapy
Shao, W., & Brown, M. A. (2003) · Breast Cancer Research · doi:10.1186/bcr742 · Cited by 201 · see citing works
Kchour, G., Tarhini, M., Kooshyar, M. M., Hajj, H. E., Wattel, E., Mahmoudi, M., Hatoum, H. A., Rahimi, H., Maleki, M., Rafatpanah, H., et al. (2009) · Blood · doi:10.1182/blood-2009-03-211821 · Cited by 199 · see citing works
Self-citationMiyamoto, T., Nagafuji, K., Akashi, K., Harada, M., Kyo, T., Akashi, T., Takenaka, K., Mizuno, S., Gondo, H., Okamura, T., et al. (1996) · Blood · doi:10.1182/blood.v87.11.4789.bloodjournal87114789 · Cited by 195 · see citing works
Bazarbachi, A. A., El-Sabban, M. E., Nasr, R., Quignon, F., Awaraji, C., Kersual, J., Dianoux, L., Zermati, Y., Haidar, J. H., Hermine, O., et al. (1999) · Blood · doi:10.1182/blood.v93.1.278 · Cited by 179 · see citing works
Self-citationNervi, C., Ferrara, F. F., Fanelli, M., Rippo, M. R., Tomassini, B., Ferrucci, P. F., Ruthardt, M., Gelmetti, V., Gambacorti-Passerini, C. B., Diverio, D., et al. (1998) · PubMed · doi:10.1182/blood.v92.7.2244 · Cited by 171 · 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
Muratani, M., Kung, C. K.-H., Shokat, K. M., & Tansey, W. P. (2005) · Cell · doi:10.1016/j.cell.2004.12.025 · Cited by 157 · see citing works
Minireview: Extranuclear Steroid Receptors: Roles in Modulation of Cell Functions
Levin, E. R. (2010) · Molecular Endocrinology · doi:10.1210/me.2010-0284 · Cited by 153 · see citing works
Zhu, J., Lallemand-Breitenbach, V., & de Thé, H. (2001) · Oncogene · doi:10.1038/sj.onc.1204852 · Cited by 151 · see citing works
Shih, L.-Y., Huang, C.-F., Wang, P.-N., Jh, W., Lin, T.-L., Dunn, P., & Kuo, M.-C. (2004) · Leukemia · doi:10.1038/sj.leu.2403274 · Cited by 145 · see citing works
El-Sabban, M. E., Nasr, R., Dbaibo, G. S., Hermine, O., Abboushi, N., Quignon, F., Ameisen, J., Bex, F., de Thé, H., & Bazarbachi, A. A. (2000) · PubMed · doi:10.1182/blood.v96.8.2849 · Cited by 139 · see citing works
Self-citationPositive and negative regulation of granulopoiesis by endogenous RARα
Kastner, P., Lawrence, H. J., Waltzinger, C., Ghyselinck, N. B., Chambon, P., & Chan, S. H. (2001) · Blood · doi:10.1182/blood.v97.5.1314 · Cited by 133 · see citing works
Copland, J. A., Marlow, L. A., Kurakata, S., Fujiwara, K., Wong, A., Kreinest, P. A., Williams, S. F., Haugen, B. R., Klopper, J. P., & Smallridge, R. C. (2005) · Oncogene · doi:10.1038/sj.onc.1209267 · Cited by 133 · see citing works
Nasr, R. (2003) · Blood · doi:10.1182/blood-2002-09-2986 · Cited by 103 · see citing works
Self-citationTherapy-induced selective loss of leukemia-initiating activity in murine adult T cell leukemia
Hajj, H. E., El-Sabban, M. E., Hasegawa, H., Zaatari, G. S., Ablain, J., Saab, S. T., Janin, A., Mahfouz, R. A., Nasr, R., Kfoury, Y. S., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20101095 · Cited by 94 · see citing works
Self-citationMao, J.-H., Sun, X., Liu, J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016311108 · Cited by 88 · see citing works
Ligands specify estrogen receptor alpha nuclear localization and degradation
Kocanova, S., Mazaheri, M., Caze-Subra, S., et al. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-98 · Cited by 87 · see citing works
Epping, M. T., Wang, L., Plumb, J. A., Lieb, M., Gronemeyer, H., Brown, R. E., & Bernards, R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702518104 · Cited by 79 · see citing works
Combined effects of As4S4 and imatinib on chronic myeloid leukemia cells and BCR-ABL oncoprotein
Yin, T., Wu, Y., Sun, H., et al. (2004) · Blood · doi:10.1182/blood-2004-04-1433 · Cited by 78 · see citing works
Biological characteristics of the pure antiestrogen fulvestrant: overcoming endocrine resistance
Dowsett, M., Nicholson, R. I., & Pietras, R. J. (2005) · Breast Cancer Research and Treatment · doi:10.1007/s10549-005-9037-3 · Cited by 77 · see citing works
Bour, G., Lalevée, S., & Rochette‐Egly, C. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.04.003 · Cited by 69 · see citing works
Gu, Z., Wu, Y., Zhou, M., Liu, C., Xu, H., Yan, H., Zhao, Y., Huang, Y., Sun, H., & Chen, G. (2010) · Blood · doi:10.1182/blood-2010-02-267963 · Cited by 51 · see citing works
PAX5–PML acts as a dual dominant-negative form of both PAX5 and PML
Kurahashi, S., Hayakawa, F., Miyata, Y., Yasuda, T., Minami, Y., Tsuzuki, S., Abe, A., & Naoe, T. (2011) · Oncogene · doi:10.1038/onc.2010.554 · Cited by 44 · see citing works
Bäsecke, J., Cepek, L., Mannhalter, C., et al. (2002) · Blood · doi:10.1182/blood-2002-06-1673 · Cited by 39 · see citing works
Retinoic acid and arsenic: towards oncogene-targeted treatments of acute promyelocytic leukaemia
Quignon, F., Chen, Z., & de Thé, H. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(97)00025-5 · Cited by 37 · see citing works
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di Masi, A., Leboffe, L., De Marinis, E., Pagano, F., Cicconi, L., Rochette-Egly, C., Lo-Coco, F., Ascenzi, P., & Nervi, C. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.12.003 · Cited by 403 · see citing works
Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56
Wang, J., Okkeri, J., Pavic, K., Wang, Z., Kauko, O., Halonen, T., Sarek, G., Ojala, P. M., Rao, Z., Xu, W., et al. (2017) · The EMBO Reports · doi:10.15252/embr.201642788 · Cited by 95 · see citing works
Leiva, M., Moretti, S., Soilihi, H., Pallavicini, I., Peres, L., Mercurio, C., Dal Zuffo, R., Minucci, S., & de Thé, H. (2012) · Leukemia · doi:10.1038/leu.2012.39 · Cited by 58 · see citing works
Self-citationTargeting post-translational modification of transcription factors as cancer therapy
Qian, M., Yan, F., Yuan, T., Yang, B., He, Q., & Zhu, H. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.06.005 · Cited by 47 · see citing works
- Authors
- Ablain, J., Nasr, R., Bazarbachi, A., & de Thé, H.
- Affiliations
- Inserm (FR)
- Authors' Affiliations: 1Université Paris Diderot, Sorbonne Paris Cité, UMR 944/7212, 2INSERM UMR 944, 3CNRS UMR 7212, Equipe labellisée par la Ligue Nationale contre le Cancer, Institut Universitaire d'Hématologie, and 4Assistance Publique Hôpitaux de Paris (AP-HP), Service de Biochimie, Hôpital St. Louis, Paris, France; Departments of 5Cell Biology, Anatomy, and Physiological Sciences, and 6Internal Medicine, American University of Beirut, Beirut, Lebanon
- Venue
- Cancer Discovery
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- 2011-07-01
- Volume
- 1
- Issue
- 2
- Pages
- 117-127
- ISSN
- 2159-8274 (ISSN-L)
- 2159-8290
- OpenAlex
- W2130158187
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- 44
- References
- 85
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- journal article
- Language
- en
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- closed
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- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Keywords
- oncoprotein degradation, proteasomal degradation, targeted cancer therapy, kinase inhibitors, acute promyelocytic leukemia, PML-RARA fusion, arsenic, retinoic acid, fusion protein, nuclear receptors, transcription factors, small molecule screening, apoptosis, cell differentiation
- MeSH terms
- Animals, Antineoplastic Agents, Cell Differentiation, Humans, Neoplasms, Oncogene Proteins, Apoptosis, Drug Discovery, Proteolysis
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 ›
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