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ASPP Proteins Specifically Stimulate the Apoptotic Function of p53
Open accessAbstract
We identified a family of proteins termed ASPP. ASPP1 is a protein homologous to 53BP2, the C-terminal half of ASPP2. ASPP proteins interact with p53 and specifically enhance p53-induced apoptosis but not cell cycle arrest. Inhibition of endogenous ASPP function suppresses the apoptotic function of endogenous p53 in response to apoptotic stimuli. ASPP enhance the DNA binding and transactivation function of p53 on the promoters of proapoptotic genes in vivo. Two tumor-derived p53 mutants with reduced apoptotic function were defective in cooperating with ASPP in apoptosis induction. The expression of ASPP is frequently downregulated in human breast carcinomas expressing wild-type p53 but not mutant p53. Therefore, ASPP regulate the tumor suppression function of p53 in vivo.
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“The miR-21 targets we identified included p53 homologue, p63, p53 activators JMY, TOPORS, TP53BP2, DAXX, and HNRPK, which can stabilize p53 protein levels by interfering with MDM2 and/or act as p53 transcriptional cofactors, assisting p53 in transactivating genes that can induce apoptosis and growth arrest (21)(22)(23)(24)(25)(26).”
From MicroRNA-21 Targets a Network of Key Tumor-Suppressive Pathways in Glioblastoma Cells (2008) · cites this paper as [23]
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Cites
Antibodies, a laboratory manual
(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90130-3 · Cited by 12,318
p53: puzzle and paradigm.Preprint
Ko, L. J., & Prives, C. L. (1996) · Genes & Development · doi:10.1101/gad.10.9.1054 · Cited by 2,346
Structure of the p53 Tumor Suppressor Bound to the Ankyrin and SH3 Domains of 53BP2
Gorina, S. S., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.1001 · Cited by 575
Two cellular proteins that bind to wild-type but not mutant p53.
Iwabuchi, K., Bartel, P. L., Li, B., Marraccino, R. L., & Fields, S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.6098 · Cited by 432
In vivo gene expression profile analysis of human breast cancer progression.
Sgroi, D. C., Teng, S., ROBINSON, G. C., LeVangie, R., Hudson, J. R., & Elkahloun, A. G. (1999) · PubMed · Cited by 390
Differential Activation of Target Cellular Promoters by p53 Mutants with Impaired Apoptotic Function
Ludwig, R. L., Bates, S., & Vousden, K. H. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4952 · Cited by 278
Hsieh, J.-K., Fredersdorf, S., Kouzarides, T., Martin, K., & Lü, X. (1997) · Genes & Development · doi:10.1101/gad.11.14.1840 · Cited by 278
Self-citationA Mutant p53 That Discriminates between p53-Responsive Genes Cannot Induce Apoptosis
Friedlander, P. A., Haupt, Y., Prives, C. L., & Oren, M. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4961 · Cited by 277
Stimulation of p53-mediated Transcriptional Activation by the p53-binding Proteins, 53BP1 and 53BP2
Iwabuchi, K., Li, B., Massa, H. F., Trask, B. J., Date, T., & Fields, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.26061 · Cited by 206
Crook, T., Brooks, L. A., Crossland, S., Osin, P., Barker, K. T., Waller, J., Philp, E., Smith, P. D., Yuluğ, I. G., Peto, J., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1202106 · Cited by 179
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Koeppel, M., van Heeringen, S. J., Smeenk, L., Navis, A. C., Janssen‐Megens, E. M., & Lohrum, M. A. E. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn940 · Cited by 57
Hwang, E., Zhang, Z., Cai, H., Huang, D. Y. C., Huong, S., Cha, C.-Y., & Huang, E. (2009) · Journal of Virology · doi:10.1128/jvi.00304-09 · Cited by 55
p53 and little brother p53/47: linking IRES activities with protein functions
Grover, R., Candeias, M. M., Fåhræus, R., & Das, S. (2009) · Oncogene · doi:10.1038/onc.2009.138 · Cited by 54
Hepatitis B virus-induced hepatocellular carcinoma: The role of the virus x protein
Motavaf, M., Safari, S., JOURSHARI, M. S., & Alavian, S. M. (2013) · Acta Virologica · doi:10.4149/av_2013_04_389 · Cited by 54
SEI family of nuclear factors regulates p53‐dependent transcriptional activation
Watanabe‐Fukunaga, R., Iida, S., Shimizu, Y., Nagata, S., & Fukunaga, R. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00881.x · Cited by 52
Janke, K., Brockmeier, U., Kuhlmann, K., Eisenacher, M., Nolde, J., Meyer, H. E., Mairbäurl, H., & Metzen, E. (2013) · Journal of Cell Science · doi:10.1242/jcs.117564 · Cited by 53
Lymphatic vessel assembly is impaired in Aspp1-deficient mouse embryos
Hirashima, M., Sano, K., Morisada, T., Murakami, K., Rossant, J., & Suda, T. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2008.01.023 · Cited by 53
Kampa-Schittenhelm, K. M., Acoba, J. D., Chen, D., Gay, J. W., Lee, H., Beemer, K., Padiernos, E., Boonmark, N. W., Zhu, Z., Fan, A. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809080106 · Cited by 52
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Determinants of p53 DNA binding, gene regulation, and cell fate decisions
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Zupnick, A., & Prives, C. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603387200 · Cited by 51
Insight into the Structural Basis of Pro- and Antiapoptotic p53 Modulation by ASPP Proteins
Ahn, J., Byeon, I. L., Byeon, C., & Gronenborn, A. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808821200 · Cited by 51
Katz, C., Benyamini, H., Rotem, S., Lebendiker, M., Danieli, T., Iosub‐Amir, A., Refaely, H., Dines, M., Bronner, V., Bravman, T., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711269105 · Cited by 51
RUNX Family Participates in the Regulation of p53-Dependent DNA Damage Response
Ozaki, T., Nakagawara, A., & Nagase, H. (2013) · International Journal of Genomics · doi:10.1155/2013/271347 · Cited by 53
Liu, Z., Lü, X., Zhang, Y., Zhong, S., Gu, S.-Z., Zhang, X., Yang, X. X., & Xin, H. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.069 · Cited by 51
Self-citationLiu, G., & Chen, X. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413889200 · Cited by 51
Herron, B. J., Rao, C., Liu, S., Laprade, L., Richardson, J. A., Olivieri, E. R., Semsarian, C., Millar, S. E., Stubbs, L. J., & Beier, D. R. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi063 · Cited by 50
Patel, S. V., George, R., Autore, F., Fraternali, F., Ladbury, J. E., & Nikolova, P. V. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn490 · Cited by 50
Identification of an NF-κB-Dependent Gene Network in Cells Infected by Mammalian Reovirus
O'Donnell, S. M., Holm, G. H., Pierce, J. M., Tian, B., Watson, M. J., Chari, R. S., Ballard, D. W., Brasier, A. R., & Dermody, T. S. (2006) · Journal of Virology · doi:10.1128/jvi.80.3.1077-1086.2006 · Cited by 51
Song, B., Bian, Q., Zhang, Y., Shao, C., Li, G., Liu, A., Jing, W., Liu, R., Zhou, Y., Jin, G., et al. (2015) · Molecular Cancer · doi:10.1186/s12943-015-0447-5 · Cited by 50
Lossos, I. S., Natkunam, Y., Levy, R., & Lopez, C. D. (2002) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/1042819021000040017 · Cited by 50
The changing face of p53 in head and neck cancer
Partridge, M., Costea, D. E., & Huang, X. (2007) · International Journal of Oral and Maxillofacial Surgery · doi:10.1016/j.ijom.2007.06.006 · Cited by 50
Wilson, A. M., Morquette, B., Abdouh, M., Unsain, N., Barker, P. A., Feinstein, E., Bernier, G., & Polo, A. D. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2635-12.2013 · Cited by 50
Inhaled resveratrol treatments slow ageing-related degenerative changes in mouse lung
Navarro, S., Reddy, R., Lee, J., Warburton, D., & Driscoll, B. (2017) · Thorax · doi:10.1136/thoraxjnl-2016-208964 · Cited by 50
Maillart, E., Brengel‐Pesce, K., Capela, D., Roget, A., Livache, T., Canva, M., Lévy, Y., & Soussi, T. (2004) · Oncogene · doi:10.1038/sj.onc.1207639 · Cited by 52
Multiple response elements and differential p53 binding control Perp expression during apoptosis.
Reczek, E. E., Flores, E. R., Tsay, A. S., Attardi, L. D., & Jacks, T. (2003) · PubMed · Cited by 49
MiRNAs Mediate GDNF-Induced Proliferation and Migration of Glioma Cells
Zhang, B., Dong, F.-L., Guo, T.-W., Gu, X.-H., Huang, L., & Gao, D. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485883 · Cited by 48
Notari, M., Hu, Y., Sutendra, G., Dedeić, Z., Lu, M. M., Dupays, L., Yavari, A., Carr, C. A., Zhong, S., Opel, A., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408111112 · Cited by 47
Self-citationLu, B., Guo, H., Zhao, J., Wang, C., Wu, G., Pang, M., Tong, X., Bu, F., Liang, A., Hou, S., et al. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.06.049 · Cited by 48
Apoptosis in health and disease and modulation of apoptosis for therapy: An overview
Singh, N. (2007) · Indian Journal of Clinical Biochemistry · doi:10.1007/bf02913307 · Cited by 49
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Tordella, L., Koch, S., Salter, V., Pagotto, A., Doondeea, J. B., Feller, S. M., Ratnayaka, I., Zhong, S., Goldin, R. D., Lozano, G., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309362110 · Cited by 48
Self-citationDevany, E., Park, J. Y., Murphy, M. R., Zakusilo, G., Baquero, J., Zhang, X., Hoque, M., Tian, B., & Kleiman, F. E. (2016) · Cell Discovery · doi:10.1038/celldisc.2016.13 · Cited by 52
Bhonde, M. R., Hanski, M.-L., Notter, M., Gillissen, B. F., Daniel, P. T., Zeitz, M., & Hanski, C. (2006) · Oncogene · doi:10.1038/sj.onc.1209017 · Cited by 47
Yang, Y., Zhang, Y., Yang, J.-Q., Zhang, M., Tian, T., Jiang, Y., Liu, X., Xue, G., Li, X., Zhang, X., et al. (2022) · Circulation Research · doi:10.1161/circresaha.122.321153 · Cited by 47
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Gasco, M., & Crook, T. (2003) · Drug Resistance Updates · doi:10.1016/j.drup.2003.11.001 · Cited by 47
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Kresty, L. A., Howell, A. B., & Baird, M. (2011) · Molecules · doi:10.3390/molecules16032375 · Cited by 45
Cai, Y., Qiu, S., Gao, X., Gu, S.-Z., & Liu, Z.-J. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0728-z · Cited by 45
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Li, N., & Richard, S. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw582 · Cited by 45
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Langton, P. F., Colombani, J., Aerne, B. L., & Tapon, N. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.11.005 · Cited by 45
Tidow, H., Veprintsev, D. B., Freund, S. M. V., & Fersht, A. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604725200 · Cited by 44
The chemosensitivity of testicular germ cell tumors
Voutsadakis, I. A. (2014) · Cellular Oncology · doi:10.1007/s13402-014-0168-6 · Cited by 43
The switch from survival responses to apoptosis after chromosomal breaks
Bree, R. T., Neary, C. L., Samali, A., & Lowndes, N. F. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.03.016 · Cited by 43
The ASPP family: deciding between life and death after DNA damage
Slee, E. A. (2003) · Toxicology Letters · doi:10.1016/s0378-4274(02)00421-6 · Cited by 44
Abnormal mRNA expression of ASPP members in leukemia cell lines
Liu, Z.-J., Zhang, Y., Zhang, X., & Yang, X. (2004) · Leukemia · doi:10.1038/sj.leu.2403300 · Cited by 43
Senescence-inducing stress promotes proteolysis of phosphoglycerate mutase via ubiquitin ligase Mdm2
Mikawa, T., Maruyama, T., Okamoto, K., Nakagama, H., LLeonart, M. E., Tsusaka, T., Hori, K., Murakami, I., Izumi, T., Takaori‐Kondo, A., et al. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201306149 · Cited by 45
p53 regulation upon genotoxic stress: intricacies and complexities
Kumari, R., Kohli, S., & Das, S. (2014) · Molecular & Cellular Oncology · doi:10.4161/23723548.2014.969653 · Cited by 41
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Ohata, H., Miyazaki, M., Otomo, R., Matsushima‐Hibiya, Y., Otsubo, C., Nagase, T., Arakawa, H., Yokota, J., Nakagama, H., Taya, Y., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01221-12 · Cited by 42
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Madar, S., Harel, E., Goldstein, I., Stein, Y., Kogan-Sakin, I., Kamer, I., Solomon, H., Dekel, E., Tal, P., Goldfinger, N., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061353 · Cited by 44
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Wang, X. D., Lapi, E., Sullivan, A., Ratnayaka, I., Goldin, R. D., Hay, R. T., & Lü, X. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.101 · Cited by 41
Jin, Y., Huang, R. Q., Xia, Y., Huang, C. Y., Qiu, F., Pu, J., He, X., & Zhao, X. J. (2020) · DNA and Cell Biology · doi:10.1089/dna.2020.5453 · Cited by 41
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Chen, Y., Fujita, T., Zhang, D., Doan, H. Q., Pinkaew, D., Liu, Z., Wu, J., Koide, Y., Chiu, A., Lin, C. C.-J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.217836 · Cited by 40
Wang, T., Zhao, M., Liang, D., Bose, U., Kaur, S., McManus, D. P., & Cummins, S. F. (2017) · Parasites & Vectors · doi:10.1186/s13071-017-2218-1 · Cited by 40
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Maas, A.-M., Bretz, A. C., Mack, E., & Stiewe, T. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.07.030 · Cited by 43
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Dreyfus, D. H., Nagasawa, M., Gelfand, E. W., & Ghoda, L. Y. (2005) · BMC Immunology · doi:10.1186/1471-2172-6-12 · Cited by 39
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Gene regulation by SMAR1: Role in cellular homeostasis and cancer
Malonia, S. K., Sinha, S., Lakshminarasimhan, P., Singh, K., Jalota‐Badhwar, A., Rampalli, S., Kaul-Ghanekar, R., & Chattopadhyay, S. (2010) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2010.08.003 · Cited by 39
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Bessette, D. C., Tilch, E., Seidens, T., Quinn, M. C. J., Wiegmans, A. P., Shi, W., Cocciardi, S., Reed, A. E. M., Saunus, J. M., Simpson, P. T., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125232 · Cited by 36
Chen, Y., Liu, W., Naumovski, L., & Neve, R. L. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01727.x · Cited by 38
Self-citationBudhram-Mahadeo, V. S., Bowen, S., Lee, S., Perez-Sanchez, C., Ensor, E. A., Morris, P. J., & Latchman, D. S. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl878 · Cited by 38
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Casamayor, A., & Ariño, J. (2020) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2020.06.004 · Cited by 36
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Ma, A., & Dai, X. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1403681 · Cited by 42
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Hirashima, M., Bernstein, A., Stanford, W. L., & Rossant, J. (2004) · Blood · doi:10.1182/blood-2004-01-0254 · Cited by 37
Llanos, S., Royer, C., Lu, M. M., Bergamaschi, D., Lee, W. H., & Lü, X. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.270751 · Cited by 35
Self-citationItoh, Y., Murata, A., Sakamoto, S., Nanatani, K., Wada, T., Takahashi, S., & Kamagata, K. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.06.001 · Cited by 36
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Sawai, S., Wong, P., & Ramasamy, T. S. (2022) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2022.2088684 · Cited by 34
Shi, Y., Han, Y., Xie, F., Wang, A., Feng, X., Li, N., Guo, H., & Chen, D. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12435 · Cited by 35
Royer, C., Koch, S., Qin, X., Žák, J., Buti, L., Dudziec, E., Zhong, S., Ratnayaka, I., Srinivas, S., & Lü, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111384 · Cited by 35
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Gen, Y., Yasui, K., Kitaichi, T., Iwai, N., Terasaki, K., Dohi, O., Hashimoto, H., Fukui, H., Inada, Y., Fukui, A., et al. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.04.002 · Cited by 35
Xie, Y., Li, Y., Chen, J., Ding, H., & Zhang, X. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1162662 · Cited by 36
Johnson, T. M., Meade, K. E., Pathak, N., Marques, M. R., & Attardi, L. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706764105 · Cited by 36
Wilson, A. M., Chiodo, V. A., Boye, S. L., Brecha, N. C., Hauswirth, W. W., & Polo, A. D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094175 · Cited by 34
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Stott, S., Randle, S. J., Rawi, S. A., Rowicka, P. A., Harris, R., Mason, B., Xia, J., Dalley, J. W., Barker, R. A., & Laman, H. (2019) · The Journal of Pathology · doi:10.1002/path.5312 · Cited by 34
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Wu, T., & Wu, L. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.655630 · Cited by 36
The variation game: Cracking complex genetic disorders with NGS and omics data
Cui, H., Dhroso, A., Johnson, N. T., & Korkin, D. (2015) · Methods · doi:10.1016/j.ymeth.2015.04.018 · Cited by 36
Forcing Cancer Cells to Commit Suicide
Vangestel, C., de Wiele, C. V., Mees, G., & Peeters, M. (2009) · Cancer Biotherapy and Radiopharmaceuticals · doi:10.1089/cbr.2008.0598 · Cited by 33
ASPP2 inhibits tumor growth by repressing the mevalonate pathway in hepatocellular carcinoma
Liang, B., Chen, R., Song, S., Wang, H., Sun, G., Yang, H., Jing, W., Zhou, X., Fu, Z., Huang, G., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2054-7 · Cited by 33
iASPP Inhibition: Increased Options in Targeting the p53 Family for Cancer Therapy
Bell, H. S., & Ryan, K. M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0182 · Cited by 33
53BP2 induces apoptosis through the mitochondrial death pathway
Kobayashi, S., Kajino, S., Takahashi, N., Kanazawa, S., Imai, K., Hibi, Y., Ohara, H., Itoh, M., & Okamoto, T. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00835.x · Cited by 33
Giampieri, S., García‐Escudero, R., Green, J. L., & Storey, A. (2004) · Oncogene · doi:10.1038/sj.onc.1207711 · Cited by 33
RetractedEffect of RNA Interference of iASPP on the Apoptosis in MCF-7 Breast Cancer Cells
Liu, Z., Cai, Y., Hou, L., Gao, X., Xin, H., Lü, X., Zhong, S., Gu, S.-Z., & Chen, J. (2008) · Cancer Investigation · doi:10.1080/07357900801965042 · Cited by 33
Self-citationThe relevance of protein-protein interactions for p53 function: the CPE contribution
Fernández-Fernández, M. R., & Sot, B. (2010) · Protein Engineering Design and Selection · doi:10.1093/protein/gzq074 · Cited by 33
Molecular mechanisms underlying the interaction of protein phosphatase-1c with ASPP proteins
Skene-Arnold, T. D., Luu, H. A., Uhrig, R. G., Wever, V. D., Nimick, M., Maynes, J. T., Fong, A., James, M. N. G., Trinkle‐Mulcahy, L., Moorhead, G. B. G., et al. (2012) · Biochemical Journal · doi:10.1042/bj20120506 · Cited by 33
Stimulus-Specific Transcriptional Regulation Within the p53 Network
Donner, A. J., Hoover, J. M., Szostek, S. A., & Espinosa, J. M. (2007) · Cell Cycle · doi:10.4161/cc.6.21.4893 · Cited by 33
Control of ASPP2/53BP2L Protein Levels by Proteasomal Degradation Modulates p53 Apoptotic Function
Zhu, Z., Ramos, J. A., Kampa-Schittenhelm, K. M., Adimoolam, S., Sirisawad, M., Yu, Z., Chen, D., Naumovski, L., & Lopez, C. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503736200 · Cited by 32
Self-citationCao, Y., Hamada, T., Matsui, T., Date, T., & Iwabuchi, K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.01.124 · Cited by 32
Metadata
- Authors
- Samuels-Lev, Y., O'Connor, D. J., Bergamaschi, D., Trigiante, G., Hsieh, J.-K., Zhong, S., Campargue, I., Naumovski, L., Crook, T., & Lu, X.
- Affiliations
- Ludwig Cancer Research (GB)
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2001-10
- Volume
- 8
- Issue
- 4
- Pages
- 781-794
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2087732778
- Cited by
- 664
- References
- 22
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 15 · 2023: 20 · 2022: 16 · 2021: 26 · 2020: 13 · 2019: 20 · 2018: 8 · 2017: 27 · 2016: 18 · 2015: 23 · 2014: 37 · 2013: 35 · 2012: 31
- FWCI
- 13.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- ASPP1, ASPP2, p53, apoptosis, p53 DNA binding, p53 transactivation, tumor suppression, breast cancer, mutant p53, cell cycle arrest
- MeSH terms
- Breast Neoplasms, Carcinoma, Carrier Proteins, Cell Separation, Female, Flow Cytometry, Humans, Microscopy, Fluorescence, Molecular Sequence Data, Peptide Fragments, Promoter Regions, Genetic, Proto-Oncogene Proteins, Tumor Cells, Cultured, Transcriptional Activation, Tumor Suppressor Protein p53, Cyclins, Apoptosis, Protein Structure, Tertiary, Proto-Oncogene Proteins c-bcl-2, Cyclin-Dependent Kinase Inhibitor p21, Apoptosis Regulatory Proteins, bcl-2-Associated X Protein
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