Cited by 368Acute Myeloid Leukemia ResearchRetinoids in leukemia and cellular processesGenomics and Chromatin Dynamics

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The t(8;21) Fusion Protein Interferes with AML-1B-Dependent Transcriptional Activation

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Meyers, Shari, Lenny, Noel, Hiebert, Scott W.·1995·Molecular and Cellular Biology

DOI 10.1128/mcb.15.4.1974PMC PMC230424

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Abstract

The AML-1/CBF beta transcription factor complex is targeted by both the t(8;21) and the inv(16) chromosomal alterations, which are frequently observed in acute myelogenous leukemia. AML-1 is a site-specific DNA-binding protein that recognizes the enhancer core motif TGTGGT. The t(8;21) translocation fuses the first 177 amino acids of AML-1 to MTG8 (also known as ETO), generating a chimeric protein that retains the DNA-binding domain of AML-1. Analysis of endogenous AML-1 DNA-binding complexes suggested the presence of at least two AML-1 isoforms. Accordingly, we screened a human B-cell cDNA library and isolated a larger, potentially alternatively spliced, form of AML1, termed AML1B. AML-1B is a protein of 53 kDa that binds to a consensus AML-1-binding site and complexes with CBF beta. Subcellular fractionation experiments demonstrated that both AML-1 and AML-1/ETO are efficiently extracted from the nucleus under ionic conditions but that AML-1B is localized to a salt-resistant nuclear compartment. Analysis of the transcriptional activities of AML-1, AML-1B, and AML-1/ETO demonstrated that only AML-1B activates transcription from the T-cell receptor beta enhancer. Mixing experiments indicated that AML-1/ETO can efficiently block AML-1B-dependent transcriptional activation, suggesting that the t(8;21) translocation creates a dominant interfering protein.

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Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
Recombinant Genomes Which Express Chloramphenicol Acetyltransferase in Mammalian Cells
Gorman, C., Moffat, L. F., & Howard, B. H. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.9.1044 · Cited by 7,674
The scanning model for translation: an update.
Kozak, M. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.2.229 · Cited by 3,485
t(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene, AML1.
Miyoshi, H., Shimizu, K., Kozu, T., Maseki, N., Kaneko, Y., & Ohki, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10431 · Cited by 872
Multiple Point Mutations Affecting the Simian Virus 40 Enhancer
Weiher, H., König, M., & Gruß, P. (1983) · Science · doi:10.1126/science.6297005 · Cited by 803
Fusion Between Transcription Factor CBFβ/PEBP2β and a Myosin Heavy Chain in Acute Myeloid Leukemia
Liu, P., Tarlé, S. A., Hajra, A., Claxton, D. F., Marlton, P., Freedman, M., Siciliano, M. J., & Collins, F. S. (1993) · Science · doi:10.1126/science.8351518 · Cited by 732
Secreted placental alkaline phosphatase: a powerful new quantitative indicator of gene expression in eukaryotic cells
Berger, J., Hauber, J., Hauber, R., Geiger, R. E., & Cullen, B. R. (1988) · Gene · doi:10.1016/0378-1119(88)90219-3 · Cited by 667
Identification of breakpoints in t(8;21) acute myelogenous leukemia and isolation of a fusion transcript, AML1/ETO, with similarity to Drosophila segmentation gene, runt
Erickson, P., Gao, J., Chang, K., Look, T., Whisenant, E., Raimondi, S., Lasher, R., Trujillo, J., Rowley, J., & Drabkin, H. (1992) · Blood · doi:10.1182/blood.v80.7.1825.1825 · Cited by 631
PEBP2/PEA2 represents a family of transcription factors homologous to the products of the Drosophila runt gene and the human AML1 gene.
Ogawa, E., Maruyama, M., Kagoshima, H., Inuzuka, M., Lu, J., Satake, M., Shigesada, K., & Ito, Y. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6859 · Cited by 608
The interaction of RB with E2F coincides with an inhibition of the transcriptional activity of E2F.Preprint
Hiebert, S. W., Chellappan, S., Horowitz, J. M., & Nevins, J. R. (1992) · Genes & Development · doi:10.1101/gad.6.2.177 · Cited by 576
Self-citation

Flagged first, then by citations

Show all 46 references

Research works printed but not linked: 5

Bae S.-C., 1994, Mol. Cell. Biol., 14, 3242
Bae S. C., 1993, Oncogene, 8, 809
Gottschalk L. R., 1990, Mol. Cell. Biol., 10, 5486
Redondo J. M., 1991, Mol. Cell. Biol., 11, 5671
Wang S., 1993, EMBO J., 13, 3324

Sorted by citations

Items 201–300 of 367

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Positional differences of axon growth rates between sensory neurons encoded by runx3
Lallemend, F., Sterzenbach, U., Hadjab-Lallemend, S., Aquino, J. B., Castelo‐Branco, G., Sinha, I., Villaescusa, C., Levanon, D., Wang, Y., Franck, M. C. M., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.228 · Cited by 40
Worming out the biology of Runx
Nimmo, R. A., & Woollard, A. C. S. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2007.11.002 · Cited by 37
Shared and distinct roles mediated through C-terminal subdomains of acute myeloid leukemia/Runt-related transcription factor molecules in murine development
Fukushima‐Nakase, Y., Naoe, Y., Taniuchi, I., Hosoi, H., Sugimoto, T., & Okuda, T. (2005) · Blood · doi:10.1182/blood-2004-08-3372 · Cited by 37
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Staber, P. B., Zhang, P., Ye, M., Welner, R. S., Levantini, E., Di Ruscio, A., Ebralidze, A. K., Bach, C., Zhang, H., Zhang, J., et al. (2014) · Blood · doi:10.1182/blood-2014-01-550855 · Cited by 36
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Kohzaki, H., Ito, K., Huang, G., Wee, H., Murakami, Y., & Ito, Y. (1999) · Oncogene · doi:10.1038/sj.onc.1202735 · Cited by 36
Genome-wide co-occupancy of AML1-ETO and N-CoR defines the t(8;21) AML signature in leukemic cells
Trombly, D. J., Whitfield, T. W., Padmanabhan, S., Gordon, J. A. R., Lian, J. B., van Wijnen, A. J., Zaidi, S. K., Stein, J. L., & Stein, G. S. (2015) · BMC Genomics · doi:10.1186/s12864-015-1445-0 · Cited by 35
Study of Osteoblast-Specific Expression of One Mouse Osteocalcin Gene: Characterization of the Factor Binding to OSE2
Ducy, P. F., Geoffroy, V., & Karsenty, G. (1996) · Connective Tissue Research · doi:10.3109/03008209609029169 · Cited by 35
Implications for interrelationships between nuclear architecture and control of gene expression under microgravity conditions
Stein, G. S., van Wijnen, A. J., Stein, J. L., Lian, J. B., Pockwinse, S. M., & McNeil, S. M. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.9001.s157 · Cited by 35
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Le, X., Claxton, D. F., Kornblau, S. M., Fan, Y., Mu, Z., & Chang, K.-S. (1998) · European Journal Of Haematology · doi:10.1111/j.1600-0609.1998.tb01027.x · Cited by 35
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Barski, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gnh097 · Cited by 34
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Ashe, M., Pabón‐Peña, L. M., Dees, E., Price, K. L., & Bader, D. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308810200 · Cited by 34
Truncated RUNX1 protein generated by a novel t(1;21)(p32;q22) chromosomal translocation impairs the proliferation and differentiation of human hematopoietic progenitors
Rodríguez, S., Torres-Ruiz, R., Suela, J., Acquadro, F., Martin, M. C., Yebra, E., Ramı́rez, J. C., Álvarez, S., & Cigudosa, J. C. (2015) · Oncogene · doi:10.1038/onc.2015.70 · Cited by 32
Williams–Beuren syndrome critical region-5/non-T-cell activation linker: a novel target gene of AML1/ETO
Fliegauf, M., Stock, M., Berg, T., & Lübbert, M. (2004) · Oncogene · doi:10.1038/sj.onc.1208042 · Cited by 33
Potential involvement of the AML1-MTG8 fusion protein in the granulocytic maturation characteristic of the t(8;21) acute myelogenous leukemia revealed by microarray analysis
Shimada, H., Ichikawa, H., & Ohki, M. (2002) · Leukemia · doi:10.1038/sj.leu.2402465 · Cited by 33
ELA2 is regulated by hematopoietic transcription factors, but not repressed by AML1-ETO
Lausen, J., Liu, S., Fliegauf, M., Lübbert, M., & Werner, M. H. (2005) · Oncogene · doi:10.1038/sj.onc.1209181 · Cited by 32
c-Jun N-terminal kinase mediates AML1-ETO protein-induced connexin-43 expression
Gao, F., Wang, Q., Wu, Y., Li, X., Zhao, K.-W., & Chen, G. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.009 · Cited by 33
Nuclear microenvironments support assembly and organization of the transcriptional regulatory machinery for cell proliferation and differentiation
Stein, G. S., Lian, J. B., van Wijnen, A. J., Stein, J. L., Javed, A., Montecino, M. A., Zaidi, S. K., Young, D. W., Choi, J., Gutierrez, S. E., et al. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10777 · Cited by 33
PRISM offers a comprehensive genomic approach to transcription factor function predictionPreprint
Wenger, A. M., Clarke, S. L., Guturu, H., Chen, J., Schaar, B. T., McLean, C. Y., & Bejerano, G. (2013) · Genome Research · doi:10.1101/gr.139071.112 · Cited by 33
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Kummalue, T., Lou, J., & Friedman, A. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.23.8278-8291.2002 · Cited by 32
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Jin, Q., Ren, Y., Wang, M., Suraneni, P. K., Li, D., Crispino, J. D., Fan, J., & Huang, Z. (2016) · Blood Cancer Journal · doi:10.1038/bcj.2016.87 · Cited by 32
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Cooperative function of Aml1-ETO corepressor recruitment domains in the expansion of primary bone marrow cells.
Hug, B. A., Lee, S. Y. D., Kinsler, E. L., Zhang, J., & Lazar, M. A. (2002) · PubMed · Cited by 32
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Odaka, Y., Mally, A., Elliott, L. T., & Meyers, S. (2000) · Oncogene · doi:10.1038/sj.onc.1203689 · Cited by 31
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Corsetti, M. T., & Calabi, F. (1997) · Blood · doi:10.1182/blood.v89.7.2359 · Cited by 31
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Roh, S., Kasembeli, M. M., Galaz-Montoya, J. G., Trnka, M., Lau, W. C. Y., Burlingame, A. L., Chiu, W., & Tweardy, D. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.684878 · Cited by 30
Valproic acid triggers differentiation and apoptosis in AML1/ETO-positive leukemic cells specifically
Zápotocký, M., Mejstříková, E., Smetana, K., Starý, J., Trka, J., & Starková, J. (2012) · Cancer Letters · doi:10.1016/j.canlet.2011.12.041 · Cited by 29
Structural alterations in the transcription factor PEBP2/CBF linked to four different types of leukemia
Ito, Y. (1996) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/bf01261402 · Cited by 29
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Wigle, D. A., Thompson, K., Yablonsky, S., Zaidi, S. H. E., Coulber, C., Jones, P. L., & Rabinovitch, M. (1998) · Circulation Research · doi:10.1161/01.res.83.3.252 · Cited by 29
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Yun, C., Senju, S., Fujita, H., Tsuji, Y., Irie, A., Matsushita, S., & Nishimura, Y. (1999) · Tissue Antigens · doi:10.1034/j.1399-0039.1999.540206.x · Cited by 28
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Self-citation
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Ben-Aziz, R., Levanon, D., Karn, H. A., Kidron, D., Goldenberg, D., Lotem, J., Polak-Chaklon, S., & Groner, Y. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400415 · Cited by 28
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Multi-sites cleavage of leukemogenic AML1-ETO fusion protein by caspase-3 and its contribution to increased apoptotic sensitivity
Lu, Y., Peng, Z.-G., Yuan, T.-T., Yin, Q.-Q., Li, X., & Chen, G.-Q. (2007) · Leukemia · doi:10.1038/sj.leu.2405020 · Cited by 27
Regulation of Immature Myeloid Cell Differentiation by PEBP2/CBF, MYB, C/EBP and ETS Family Members
Friedman, A. D. (1996) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-85232-9_15 · Cited by 27
Co‐activator activator (CoAA) prevents the transcriptional activity of Runt domain transcription factors
Li, X., Hoeppner, L. H., Jensen, E. D., Gopalakrishnan, R., & Westendorf, J. J. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22263 · Cited by 26
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Lennartsson, A., Pieters, K., Ullmark, T., Vidovic, K., & Gullberg, U. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.10.067 · Cited by 27
Establishment and characterization of a stable cell line to evaluate cellular Runx2 activity
Kim, H. J., Park, H., Kim, J. H., Cho, J., Choi, J., Kim, J., Kim, H. J., Shin, H., & Ryoo, H. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20038 · Cited by 25
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Thiel, V. N., Giaimo, B. D., Schwarz, P., Soller, K., Vas, V., Bartkuhn, M., Blätte, T. J., Döhner, K., Bullinger, L., Borggrefe, T., et al. (2017) · Leukemia · doi:10.1038/leu.2017.105 · Cited by 25
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Hiebert, S. W., Reed-Inderbitzin, E. F., Amann, J. M., Irvin, B. J., Durst, K. L., & Linggi, B. E. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00021-4 · Cited by 26
Self-citation
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Zent, C. S., Kim, N., Hiebert, S. W., Zhang, D., Tenen, D. G., Rowley, J. D., & Nucifora, G. (1996) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-85232-9_24 · Cited by 25
Self-citation
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Bernard, O., Romana, S. P., Poirel, H. A., & Berger, R. (1996) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428199609054854 · Cited by 24
Temporal and Spatial Parameters of Skeletal Gene Expression: Targeting RUNX Factors and their Coregulatory Proteins to Subnuclear Domains
Stein, G. S., Lian, J. B., Stein, J. L., van Wijnen, A. J., Choi, J.-Y., Pratap, J., & Zaidi, S. K. (2003) · Connective Tissue Research · doi:10.1080/03008900390152241 · Cited by 24
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Davis, J. N., Rogers, D. L., Adams, L. K., Yong, T., Jung, J. S., Cheng, B., Fennell, K. A., Borazanci, E. H., Moustafa, Y. W., Sun, A., et al. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22298 · Cited by 24
Self-citation
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Contribution of oncogenes and tumor suppressor genes to myeloid leukemia
Wolff, L. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(97)00006-1 · Cited by 24
Cytogenetic biomarkers for human cancer
Keen‐Kim, D. (2008) · Frontiers in bioscience · doi:10.2741/3127 · Cited by 23
Loss of RUNX 1/ AML 1 arginine‐methylation impairs peripheral T cell homeostasis
Mizutani, S., Yoshida, T., Zhao, X., Nimer, S. D., Taniwaki, M., & Okuda, T. (2015) · British Journal of Haematology · doi:10.1111/bjh.13499 · Cited by 24
Correlation between karyotype and quantitative immunophenotype in acute myelogenous leukemia with t(8;21)
Khoury, H., Dalal, B. I., Nantel, S. H., Horsman, D. E., Lavoie, J. C., Shepherd, J. D., Hogge, D. E., Toze, C. L., Song, K., Forrest, D. L., et al. (2004) · Modern Pathology · doi:10.1038/modpathol.3800168 · Cited by 23
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van der Kouwe, E., & Staber, P. B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020350 · Cited by 24
Redistribution of H3K27me3 and acetylated histone H4 upon exposure to azacitidine and decitabine results in de-repression of the AML1/ETO target gene IL3
Buchi, F., Masala, E., Rossi, A., Valencia, A., Spinelli, E., Sanna, A., Gozzini, A., & Santini, V. (2013) · Epigenetics · doi:10.4161/epi.27322 · Cited by 22
Low frequency of TEL/AML1 in adult acute lymphoblastic leukemia
Kwong, Y., & Wong, K. F. (1997) · Cancer Genetics and Cytogenetics · doi:10.1016/s0165-4608(96)00418-9 · Cited by 22
ZFP36L2, a novel AML1 target gene, induces AML cells apoptosis and inhibits cell proliferation
Liu, J., Lu, W., Liu, S., Wang, Y., Li, S., Xu, Y., Xing, H., Tang, K., Tian, Z., Rao, Q., et al. (2018) · Leukemia Research · doi:10.1016/j.leukres.2018.02.017 · Cited by 20
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Moreno–Miralles, I., Pan, L., Keates‐Baleeiro, J., Goodwin, K. D., Yang, C., Kim, H., Thompson, M. A., Klug, C. A., Cleveland, J. L., & Hiebert, S. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506855200 · Cited by 21
Self-citation
Transcriptional and epigenetic regulation of the GM-CSF promoter by RUNX1
Taberlay, P. C., James, S. R., Qadi, A. A., West, A. C., Ray, S., Bert, A. G., Cockerill, P. N., & Holloway, A. F. (2010) · Leukemia Research · doi:10.1016/j.leukres.2010.03.029 · Cited by 22
Cooperation between Core Binding Factor and Adjacent Promoter Elements Contributes to the Tissue-specific Expression of Interleukin-3
Taylor, D. S., Laubach, J. P., Nathan, D. G., & Mathey-Prévôt, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.24.14020 · Cited by 21
BET inhibitors reduce cell size and induce reversible cell cycle arrest in AML
Zhang, S., Zhao, Y., Heaster, T. M., Fischer, M. A., Stengel, K. R., Zhou, X., Ramsey, H. E., Zhou, M., Savona, M. R., Skala, M. C., et al. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28005 · Cited by 21
Self-citation
Runx Protein Signaling in Human Cancers
Anglin, I. E., & Passaniti, A. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/1-4020-7847-1_10 · Cited by 21
Transcriptional Regulation by the t(8;21 )Fusion Protein, AML-1/ETO
Hiebert, S. W., Downing, J. R., Lenny, N. T., & Meyers, S. (1996) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-85232-9_25 · Cited by 20
Self-citation
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Chen, G., Liu, A., Xu, Y., Gao, L., Jiang, M., Li, Y., Lv, N., Zhou, L., Wang, L., Yu, L., et al. (2019) · FEBS Journal · doi:10.1111/febs.14751 · Cited by 20
The genome-wide molecular signature of transcription factors in leukemia
Prange, K. H. M., Singh, A. A., & Martens, J. H. A. (2014) · Experimental Hematology · doi:10.1016/j.exphem.2014.04.012 · Cited by 19
The PEBP2β/CBFβ-SMMHC chimeric protein is localized both in the cell membrane and nuclear subfractions of leukemic cells carrying chromosomal inversion 16
Kanto, S., Chiba, N., Tanaka, Y., Fujita, S., Endo, M., Kamada, N., Yoshikawa, K., Fukuzaki, A., Orikasa, S., Watanabe, T., et al. (2000) · Leukemia · doi:10.1038/sj.leu.2401821 · Cited by 20
RUNX3‐mediated repression of RUNX1 in B cells
Brady, G., & Farrell, P. J. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21880 · Cited by 19
AML1/ETO–induced survivin expression inhibits transcriptional regulation of myeloid differentiation
Balkhi, M. Y., Christopeit, M., Chen, Y. X., Geletu, M., & Behre, G. (2008) · Experimental Hematology · doi:10.1016/j.exphem.2008.05.008 · Cited by 19
Expression of steroidogenic enzyme messenger ribonucleic acid and cortisol production in adrenocortical cells isolated from halothane-sensitive and halothane-resistant pigs
Huang, H.-S., Wu, M.-C., & Li, P.-H. S. (2000) · Journal of Cellular Biochemistry · doi:10.1002/1097-4644(2000)79:1 · Cited by 10
Specific protein redirection as a transcriptional therapy approach for t(8;21) leukemia
Steffen, B., Serve, H. L., Berdel, W. E., Agrawal, S., Linggi, B. E., Büchner, T., Hiebert, S. W., & Müller‐Tidow, C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1330293100 · Cited by 19
Self-citation
Induction of apoptosis in myeloid leukaemic cells by ribozymes targeted against AML1/MTG8
Matsushita, H., Kizaki, M., Kobayashi, H., Muto, A., & Ikeda, Y. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6690214 · Cited by 19
Interactions between the leukaemia‐associated ETO homologues of nuclear repressor proteins
Lindberg, S. R., Olsson, A., Persson, A., & Olsson, I. (2003) · European Journal Of Haematology · doi:10.1046/j.0902-4441.2003.00166.x · Cited by 18
Comparison of the human genomic structure of the Runt domain-encoding PEBP2/CBFα gene family
Ahn, M., Bae, S., Maruyama, M., & Ito, Y. (1996) · Gene · doi:10.1016/0378-1119(95)00751-2 · Cited by 18
Review of current classification, molecular alterations, and tyrosine kinase inhibitor therapies in myeloproliferative disorders with hypereosinophilia
Demoulin, J., & Havelange, V. (2013) · Journal of Blood Medicine · doi:10.2147/jbm.s33142 · Cited by 17
Distinct mechanisms of regulation of the ITGA6 and ITGB4 genes by RUNX1 in myeloid cells
Phillips, J. L., Taberlay, P. C., Woodworth, A. M., Hardy, K., Brettingham‐Moore, K. H., Dickinson, J. L., & Holloway, A. F. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26197 · Cited by 17
Overexpression of RUNX3 Represses RUNX1 to Drive Transformation of Myelodysplastic Syndrome
Yokomizo‐Nakano, T., Kubota, S., Bai, J., Hamashima, A., Morii, M., Sun, Y., Katagiri, S., Iimori, M., Kanai, A., Tanaka, D., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3167 · Cited by 17
TEL/AML1 Overcomes Drug Resistance Through Transcriptional Repression of Multidrug Resistance-1 Gene Expression
Asakura, K., Uchida, H., Miyachi, H., Kobayashi, H., Miyakawa, Y., Nimer, S. D., Takahashi, H., Ikeda, Y., & Kizaki, M. (2004) · Molecular Cancer Research · doi:10.1158/1541-7786.339.2.6 · Cited by 17
1 Molecular and cytogenetic abnormalities in acute myeloid leukaemia and myelodysplastic syndromes
de Greef, G. E., & Hagemeijer, A. (1996) · Baillière s Clinical Haematology · doi:10.1016/s0950-3536(96)80034-5 · Cited by 17
Inducible overexpression of RUNX1b/c in human embryonic stem cells blocks early hematopoiesis from mesoderm
Chen, B., Teng, J., Liu, H., Pan, X., Zhou, Y., Huang, S.-K., Lai, M., Bian, G., Mao, B., Sun, W., et al. (2017) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjx032 · Cited by 16
AML1-Evi-1 specifically transforms hematopoietic stem cells through fusion of the entire Evi-1 sequence to AML1
Takeshita, M., Ichikawa, M., Nitta, E., Goyama, S., Asai, T., Ogawa, S., Chiba, S., & Kurokawa, M. (2008) · Leukemia · doi:10.1038/leu.2008.53 · Cited by 17
ALY Is a Common Coactivator of RUNX1 and c-Myb on the Type B Leukemogenic VirusEnhancer
Mertz, J. A., Kobayashi, R., & Dudley, J. P. (2007) · Journal of Virology · doi:10.1128/jvi.02253-06 · Cited by 16
Association of MTG8 (ETO/CDR), a Leukemia‐related Protein, with Serine/Threonine Protein Kinases and Heat Shock Protein HSP90 in Human Hematopoietic Cell Lines
Komori, A., Sueoka, E., Fujiki, H., Ishii, M., & Kozu, T. (1999) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.1999.tb00666.x · Cited by 16
The AML1/MTG8 Fusion Transcript in t(8;21) Positive AML and its Implication for the Detection of Minimal Residual Disease
Krauter, J., Heil, G., & Ganser, A. (2000) · Hematology · doi:10.1080/10245332.2000.11746532 · Cited by 16
Histone deacetylase 3 preferentially binds and collaborates with the transcription factor RUNX1 to repress AML1–ETO–dependent transcription in t(8;21) AML
Guo, C. H., Li, J., Steinauer, N., Wong, M., Wu, B., Dickson, A. M., Kalkum, M., & Zhang, J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010707 · Cited by 16
A Hematopoietic-Specific Transmembrane Protein, Art-1, Is Possibly Regulated by AML1
Harada, Y., Harada, H., Downing, J. R., & Kimura, A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5005 · Cited by 15
Transformation properties of the ETO gene, fusion partner in t(8:21) leukemias.
Wang, J., Wang, M., & Liu, J. M. (1997) · PubMed · Cited by 15
Hematopoietic Deficiencies and Core Binding Factor Expression in Murine Ts16, an Animal Model for Down Syndrome
Gjertson, C. K., Sturm, K. S., & Berger, C. N. (1999) · Clinical Immunology · doi:10.1006/clim.1998.4685 · Cited by 14
LPXN, a member of the paxillin superfamily, is fused to RUNX1 in an acute myeloid leukemia patient with a t(11;21)(q12;q22) translocation
Dai, H., Xue, Y., Zhou, J., Li, A., Wu, Y., Pan, J., Wang, Y., & Zhang, J. (2009) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20704 · Cited by 14
Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions
Roh, S., Kasembeli, M. M., Galaz-Montoya, J. G., Chiu, W., & Tweardy, D. J. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.04.045 · Cited by 14
Expression ofruntBIs Modulated during Chondrocyte Differentiation
Castagnola, P., Gennari, M., Gaggero, A., Rossi, F. M. V., Daga, A., Corsetti, M. T., Calabi, F., & Cancedda, R. (1996) · Experimental Cell Research · doi:10.1006/excr.1996.0075 · Cited by 14
Gene expression profiling for the diagnosis and prognosis of acute myeloid leukaemia
Mills, K. (2008) · Frontiers in bioscience · doi:10.2741/3026 · Cited by 12
PIG7, transactivated by AML1, promotes apoptosis and differentiation of leukemia cells with AML1–ETO fusion gene
Liu, J., Xing, H., Chen, Y., Wang, L., Wang, D., Rao, Q., Tang, K. J., Tian, Z., He, K., Wang, M., et al. (2011) · Leukemia · doi:10.1038/leu.2011.178 · Cited by 13
AML1–ETO promotes SIRT1 expression to enhance leukemogenesis of t(8;21) acute myeloid leukemia
Zhou, L., Wang, Q., Chen, X., Fu, L. N., Zhang, X., Wang, L., Deng, A., Li, D., Liu, J., Lv, N., et al. (2016) · Experimental Hematology · doi:10.1016/j.exphem.2016.09.013 · Cited by 13
Intranuclear organization of RUNX transcriptional regulatory machinery in biological control of skeletogenesis and cancer
Stein, G. S., Lian, J. B., Stein, J. L., van Wijnen, A. J., Montecino, M. A., Pratap, J., Choi, J., Zaidi, S. K., Javed, A., Gutierrez, S. E., et al. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00029-9 · Cited by 13
Tumourigenicity of MTG8, a leukaemia‐related gene, in concert with v‐Ha‐ras gene in BALB/3T3 cells
Sueoka, E., Sueoka, N., Okabe, S., Komori, A., Suganuma, M., Kozu, T., & Fujiki, H. (1998) · British Journal of Haematology · doi:10.1046/j.1365-2141.1998.00757.x · Cited by 13
Decreased intranuclear mobility of acute myeloid leukemia 1-containing fusion proteins is accompanied by reduced mobility and compartmentalization of core binding factor β
Qiu, J., Wong, J., Tweardy, D. J., & Dong, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209431 · Cited by 13
Control of TGF-beta receptor expression in bone
Centrella, M., Ji, C., & McCarthy, T. L. (1998) · Frontiers in bioscience · doi:10.2741/a268 · Cited by 13
Competitive binding of viral E2 protein and mammalian core-binding factor to transcriptional control sequences of human papillomavirus type 8 and bovine papillomavirus type 1
Schmidt, H. M., Steger, G., & Pfister, H. (1997) · Journal of Virology · doi:10.1128/jvi.71.10.8029-8034.1997 · Cited by 12
Proleukemic RUNX1 and CBFβ Mutations in the Pathogenesis of Acute Leukemia
Engel, M. E., & Hiebert, S. W. (2009) · Cancer treatment and research · doi:10.1007/978-0-387-69259-3_8 · Cited by 12
Self-citation
GENE THERAPY FOR LEUKEMIA AND LYMPHOMA
Adams, S., & Emerson, S. G. (1998) · Hematology/Oncology Clinics of North America · doi:10.1016/s0889-8588(05)70012-5 · Cited by 13
Epigenetic-based treatments emphasize the biologic differences of core-binding factor acute myeloid leukemias
Serrano, E., Carnicer, M. J., Lasa, A., Orantes, V., Peña, J., Brunet, S., Aventin, A. M., Sierra, J., & Nomdedeu, J. F. (2008) · Leukemia Research · doi:10.1016/j.leukres.2007.11.038 · Cited by 11
Expression of myeloperoxidase and gene mutations in AML patients with normal karyotype: double CEBPA mutations are associated with high percentage of MPO positivity in leukemic blasts
Tominaga, S., Tsushima, H., Ando, K., Itonaga, H., Imaizumi, Y., Imanishi, D., Iwanaga, M., Taguchi, J., Fukushima, T., Yoshida, S., et al. (2011) · International Journal of Hematology · doi:10.1007/s12185-011-0883-y · Cited by 11

Authors: Meyers, S., Lenny, N., & Hiebert, S. W.
Affiliations: St. Jude Children's Research Hospital (US)
ORCID: Hiebert, Scott W.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1995-04-01
Volume: 15
Issue: 4
Pages: 1974-1982
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.15.4.1974
PMC: PMC230424
OpenAlex: W2113086962
Cited by: 368
References: 46
Citations by year: 2025: 1 · 2023: 3 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 3 · 2018: 4 · 2017: 3 · 2016: 5 · 2015: 8 · 2014: 4 · 2013: 11 · 2012: 3
FWCI: 18.34
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: American Lebanese Syrian Associated Charities
National Institutes of Health
National Cancer Institute (R01CA064140, P30CA021765)
Topics: Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: ETO, CBFβ, acute myeloid leukemia, transcriptional activation, alternative splicing, DNA-binding domain, nuclear localization, chromosomal translocation
MeSH terms: RUNX1 Translocation Partner 1 Protein, Amino Acid Sequence, Base Sequence, Cell Compartmentation, Cell Nucleus, Cloning, Molecular, DNA-Binding Proteins, Enhancer Elements, Genetic, Gene Expression Regulation, Molecular Sequence Data, Neoplasm Proteins, Protein Binding, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Transcription Factors, Transcription, Genetic, Leukemia, Myeloid, Acute, Transcriptional Activation, Consensus Sequence, Alternative Splicing, DNA, Complementary, Core Binding Factors, Core Binding Factor Alpha 2 Subunit

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The t(8;21) Fusion Protein Interferes with AML-1B-Dependent Transcriptional Activation

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