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Direct inhibition of the NOTCH transcription factor complex
Open accessAbstract
Direct inhibition of transcription factor complexes remains a central challenge in the discipline of ligand discovery. In general, these proteins lack surface involutions suitable for high-affinity binding by small molecules. Here we report the design of synthetic, cell-permeable, stabilized alpha-helical peptides that target a critical protein-protein interface in the NOTCH transactivation complex. We demonstrate that direct, high-affinity binding of the hydrocarbon-stapled peptide SAHM1 prevents assembly of the active transcriptional complex. Inappropriate NOTCH activation is directly implicated in the pathogenesis of several disease states, including T-cell acute lymphoblastic leukaemia (T-ALL). The treatment of leukaemic cells with SAHM1 results in genome-wide suppression of NOTCH-activated genes. Direct antagonism of the NOTCH transcriptional program causes potent, NOTCH-specific anti-proliferative effects in cultured cells and in a mouse model of NOTCH1-driven T-ALL.
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Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625
Notch Signaling: Cell Fate Control and Signal Integration in Development
Artavanis-Tsakonas, S., Rand, M. D., & Lake, R. J. (1999) · Science · doi:10.1126/science.284.5415.770 · Cited by 5,909
Lamb, J., Crawford, E. D., Peck, D., Modell, J. W., Blat, I. C., Wrobel, M. J., Lerner, J., Brunet, J.-P., Subramanian, A., Ross, K. N., et al. (2006) · Science · doi:10.1126/science.1132939 · Cited by 5,257
Activating Mutations of NOTCH1 in Human T Cell Acute Lymphoblastic Leukemia
Weng, A. P., Ferrando, A. A., Lee, W., Morris, J. P., Silverman, L. B., Sanchez-Irizarry, C., Blacklow, S. C., Look, A. T., & Aster, J. C. (2004) · Science · doi:10.1126/science.1102160 · Cited by 2,706
Self-citationNotch signalling: a simple pathway becomes complex
Bray, S. J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2009 · Cited by 2,620
A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
De Strooper, B., Annaert, W., Cupers, P., Saftig, P., Craessaerts, K., Mumm, J. S., Schroeter, E. H., Schrijvers, V., Wolfe, M. S., Ray, W. J., et al. (1999) · Nature · doi:10.1038/19083 · Cited by 2,100
Determination of the helix and β form of proteins in aqueous solution by circular dichroism
Chen, Y.-H., Yang, J. T., & Chau, K. H. (1974) · Biochemistry · doi:10.1021/bi00713a027 · Cited by 2,070
Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementia
Joutel, A., Corpechot, C., Ducros, A., Vahedi, K., Chabriat, H., Mouton, P., Alamowitch, S., Domenga, V., Cécillion, M., Maréchal, E., et al. (1996) · Nature · doi:10.1038/383707a0 · Cited by 2,068
Ellisen, L. W., Bird, J., West, D. C., Soreng, A. L., Reynolds, T. C., Smith, S. D., & Sklar, J. (1991) · Cell · doi:10.1016/0092-8674(91)90111-b · Cited by 1,691
Mutations in NOTCH1 cause aortic valve disease
Garg, V., Muth, A. N., Ransom, J. F., Schluterman, M. K., Barnes, R., King, I. N., Grossfeld, P. D., & Srivastava, D. (2005) · Nature · doi:10.1038/nature03940 · Cited by 1,509
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Recent advances in chemical protein synthesis: method developments and biological applications
Dong, S., Zheng, J., Li, Y., Wang, H., Chen, G., Chen, Y., Fang, G., Guo, J., He, C., Hu, H., et al. (2024) · Science China Chemistry · doi:10.1007/s11426-024-1950-1 · Cited by 167
Schreck, K. C., Taylor, P. H., Marchionni, L., Gopalakrishnan, V., Bar, E. E., Gaiano, N., & Eberhart, C. G. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-1624 · Cited by 169
Notch signalling in T‐cell lymphoblastic leukaemia/lymphoma and other haematological malignancies
Aster, J. C., Blacklow, S. C., & Pear, W. S. (2010) · The Journal of Pathology · doi:10.1002/path.2789 · Cited by 167
Self-citationStitched α-Helical Peptides via Bis Ring-Closing Metathesis
Hilinski, G. J., Kim, Y., Hong, J., Kutchukian, P. S., Nartey, C. M., Berkovitch, S. S., Chang, A. T., Ham, S., & Verdine, G. L. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505141j · Cited by 167
Self-citationDesign and Development of Peptides and Peptide Mimetics as Antagonists for Therapeutic Intervention
Mason, J. M. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.10.259 · Cited by 167
Notch Inhibition as a Promising New Approach to Cancer Therapy
Purow, B. W. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0899-4_23 · Cited by 157
Flexibility and small pockets at protein–protein interfaces: New insights into druggability
Jubb, H. C., Blundell, T. L., & Ascher, D. B. (2015) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2015.01.009 · Cited by 157
Laraia, L., McKenzie, G. J., Spring, D. R., Venkitaraman, A. R., & Huggins, D. J. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.04.019 · Cited by 154
Boersma, M., Haase, H. S., Peterson‐Kaufman, K. J., Lee, E. F., Clarke, O. B., Colman, P. M., Smith, B. J., Horne, W. S., Fairlie, W. D., & Gellman, S. H. (2011) · Journal of the American Chemical Society · doi:10.1021/ja207148m · Cited by 152
Bauer, D. E., & Orkin, S. H. (2015) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2015.08.001 · Cited by 143
Crosstalk between Notch, HIF-1α and GPER in Breast Cancer EMT
Francesco, E. M. D., Maggiolini, M., & Musti, A. M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19072011 · Cited by 148
Notch signaling in developmental and tumor angiogenesis
Kofler, N. M., Shawber, C. J., Kangsamaksin, T., Reed, H. O., Galatioto, J., & Kitajewski, J. (2011) · Genes & Cancer · doi:10.1177/1947601911423030 · Cited by 142
Ortmayr, K., Dubuis, S., & Zampieri, M. (2019) · Nature Communications · doi:10.1038/s41467-019-09695-9 · Cited by 142
Inhibition of Notch Signaling by a γ-Secretase Inhibitor Attenuates Hepatic Fibrosis in Rats
Chen, Y., Zheng, S., Qi, D., Zheng, S., Guo, J., Zhang, S., & Weng, Z. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046512 · Cited by 140
Therapeutic targets in triple negative breast cancer
O'Toole, S. A., Beith, J. M., Millar, E. K. A., West, R. H., McLean, A. E. B., Cazet, A., Swarbrick, A., & Oakes, S. R. (2013) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2012-201361 · Cited by 140
Molecular pathogenesis and targeted therapies for NOTCH1-induced T-cell acute lymphoblastic leukemia
Paganin, M., & Ferrando, A. A. (2010) · Blood Reviews · doi:10.1016/j.blre.2010.09.004 · Cited by 138
The Notch Pathway in Breast Cancer Progression
Kontomanolis, E. N., Kalagasidou, S., Pouliliou, S., Anthoulaki, X., Georgiou, N., Papamanolis, V., & Fasoulakis, Z. N. (2018) · The Scientific World JOURNAL · doi:10.1155/2018/2415489 · Cited by 141
Molecular engineering solutions for therapeutic peptide delivery
Acar, H., Ting, J., Srivastava, S., LaBelle, J. L., & Tirrell, M. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00536a · Cited by 139
Okamoto, T., Zobel, K., Fedorova, A., Quan, C., Yang, H., Fairbrother, W. J., Huang, D. C. S., Smith, B. J., Deshayes, K., & Czabotar, P. E. (2013) · ACS Chemical Biology · doi:10.1021/cb3005403 · Cited by 136
Role and potential for therapeutic targeting of MYB in leukemia
Pattabiraman, D. R., & Gonda, T. J. (2012) · Leukemia · doi:10.1038/leu.2012.225 · Cited by 138
A Thiol–Ene Coupling Approach to Native Peptide Stapling and Macrocyclization
Wang, Y., & Chou, D. H. (2015) · Angewandte Chemie · doi:10.1002/ange.201503975 · Cited by 134
Inhibition of leukemia cell engraftment and disease progression in mice by osteoblasts
Krevvata, M., Silva, B. C. C., Manavalan, J. S., Galán-Díez, M., Kode, A., Matthews, B. G., Park, D. S., Zhang, C. A., Galili, N., Nickolas, T. L., et al. (2014) · Blood · doi:10.1182/blood-2013-07-517219 · Cited by 138
Notch Activity Modulates the Responsiveness of Neural Progenitors to Sonic Hedgehog Signaling
Kong, J. H., Yang, L., Dessaud, É., Chuang, K., Moore, D. M., Rohatgi, R., Briscoe, J., & Novitch, B. G. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.03.005 · Cited by 141
Notch signaling regulates PD‐1 expression during CD8 + T‐cell activation
Mathieu, M., Cotta‐Grand, N., Daudelin, J., Thébault, P., & Labrecque, N. (2012) · Immunology and Cell Biology · doi:10.1038/icb.2012.53 · Cited by 136
Emerging topics in Reelin function
Förster, E., Bock, H. H., Herz, J., Chai, X., Frotscher, M., & Zhao, S. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07222.x · Cited by 130
Objective assessment of cancer genes for drug discovery
Patel, M. N., Halling‐Brown, M., Tym, J. E., Workman, P., & Al‐Lazikani, B. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3913 · Cited by 133
Dees, C., Zerr, P., Tomčík, M., Beyer, C., Horn, A., Akhmetshina, A., Palumbo, K., Reich, N., Zwerina, J., Sticherling, M., et al. (2011) · Arthritis & Rheumatism · doi:10.1002/art.30254 · Cited by 129
Moore, G., Annett, S., McClements, L., & Robson, T. (2020) · Cells · doi:10.3390/cells9061503 · Cited by 129
Bautista, A. D., Appelbaum, J., Craig, C. J., Michel, J., & Schepartz, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910715u · Cited by 130
Pattabiraman, D. R., McGirr, C., Shakhbazov, K., Barbier, V., Krishnan, K., Mukhopadhyay, P., Hawthorne, P. L., Trezise, A. E. O., Ding, J., Grimmond, S. M., et al. (2014) · Blood · doi:10.1182/blood-2012-02-413187 · Cited by 127
Descatoire, M., Weller, S., Irtan, S., Sarnacki, S., Feuillard, J., Storck, S., Guiochon‐Mantel, A., Bouligand, J., Morali, A., Cohen, J., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20132203 · Cited by 127
Dietrich, L., Rathmer, B., Ewan, K., Bange, T., Heinrichs, S., Dale, T. C., Schade, D., & Grossmann, T. N. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.06.013 · Cited by 126
Protein–protein interactions as druggable targets: recent technological advances
Higueruelo, A. P., Jubb, H. C., & Blundell, T. L. (2013) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2013.05.009 · Cited by 131
Computational Peptidology: A New and Promising Approach to Therapeutic Peptide Design
Zhou, P., Wang, C., Ren, Y., Yang, C., & Tian, F. (2013) · Current Medicinal Chemistry · doi:10.2174/0929867311320150005 · Cited by 124
Sharma, V. P., Tang, B., Wang, Y., Duran, C. L., Karagiannis, G. S., Xue, E. A., Entenberg, D. R., Borriello, L., Coste, A., Eddy, R. J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27308-2 · Cited by 122
Therapeutic approaches to modulating Notch signaling: Current challenges and future prospects
Groth, C., & Fortini, M. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.01.016 · Cited by 121
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Yan, C., & Higgins, P. J. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.11.002 · Cited by 126
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Bonnet, C., González, S., Roberts, J. S., Robertson, S. Y. T., Ruiz, M., Zheng, J., & Deng, S. X. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2021.100956 · Cited by 121
Notch1 loss of heterozygosity causes vascular tumors and lethal hemorrhage in mice
Liu, Z., Turkoz, A., Jackson, E. N., Corbo, J. C., Engelbach, J. A., Garbow, J. R., Piwnica-Worms, D. R., & Kopan, R. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43114 · Cited by 119
Directly targeting transcriptional dysregulation in cancer
Gonda, T. J., & Ramsay, R. G. (2015) · Nature reviews. Cancer · doi:10.1038/nrc4018 · Cited by 121
LaRochelle, J. R., Cobb, G., Steinauer, A., Rhoades, E. R., & Schepartz, A. (2015) · Journal of the American Chemical Society · doi:10.1021/ja510391n · Cited by 124
Targeting protein–protein interactions, a wide open field for drug design
Bakail, M., & Ochsenbein, F. (2016) · Comptes Rendus. Chimie · doi:10.1016/j.crci.2015.12.004 · Cited by 117
Advances and challenges in targeting IRF5, a key regulator of inflammation
Almuttaqi, H., & Udalova, I. A. (2018) · FEBS Journal · doi:10.1111/febs.14654 · Cited by 116
Notch Signalling in Breast Development and Cancer
Edwards, A., & Brennan, K. R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.692173 · Cited by 116
Introduction of All-Hydrocarbon i,i+3 Staples into α-Helices via Ring-Closing Olefin Metathesis
Kim, Y., Kutchukian, P. S., & Verdine, G. L. (2010) · Organic Letters · doi:10.1021/ol1010449 · Cited by 116
Self-citationA Left‐Handed Solution to Peptide Inhibition of the p53–MDM2 Interaction
Liu, M., Pazgier, M., Li, C., Yuan, W., Li, C., & Lu, W. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201000329 · Cited by 115
Winter, A., Higueruelo, A. P., Marsh, M., Sigurdardottir, A., Pitt, W. R., & Blundell, T. L. (2012) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583512000108 · Cited by 119
What makes a good drug target?
Gashaw, I., Ellinghaus, P., Sommer, A., & Asadullah, K. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.12.008 · Cited by 121
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Koch, U., & Radtke, F. (2010) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(10)92013-9 · Cited by 114
Mazur, P. K., & Siveke, J. T. (2011) · Gut · doi:10.1136/gutjnl-2011-300756 · Cited by 113
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Wang, N., Wang, S., Li, M., Hu, B., Liu, L., Yang, S., Yang, S., Gong, Z., Lai, P. B. S., & Chen, G. G. (2018) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758835918816287 · Cited by 116
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BeLow, M., & Osipo, C. (2020) · Cells · doi:10.3390/cells9102204 · Cited by 112
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Tan, Y. S., Lane, D. P., & Verma, C. S. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.06.012 · Cited by 113
Targeting transcription factors
Yeh, J., Toniolo, P. A., & Frank, D. A. (2013) · Current Opinion in Oncology · doi:10.1097/01.cco.0000432528.88101.1a · Cited by 109
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Durinck, K., Goossens, S., Peirs, S., Wallaert, A., Loocke, W. V., Matthijssens, F., Pieters, T., Milani, G., Lammens, T., Rondou, P., et al. (2015) · Experimental Hematology · doi:10.1016/j.exphem.2015.05.017 · Cited by 111
AKAPs: The architectural underpinnings of local cAMP signaling
Kritzer, M. D., Li, J., Dodge‐Kafka, K. L., & Kapiloff, M. S. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.05.002 · Cited by 109
Pharmacological disruption of the Notch transcription factor complex
Lehal, R., Zarić, J., Vigolo, M., Urech, C., Frismantas, V., Zangger, N., Cao, L., Berger, A., Chicote, I., Loubéry, S., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1922606117 · Cited by 113
Self-citationThe Notch signaling pathway: Molecular basis of cell context dependency
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Madden, M. M., Muppidi, A., Li, Z., Li, X., Chen, J., & Lin, Q. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.01.004 · Cited by 104
Inhibition of Notch Signaling Blocks Growth of Glioblastoma Cell Lines and Tumor Neurospheres
Chen, J., Kesari, S., Rooney, C., Strack, P. R., Chen, J., Shen, H., Wu, L., & Griffin, J. D. (2010) · Genes & Cancer · doi:10.1177/1947601910383564 · Cited by 104
Samon, J. B., Castillo-Martín, M., Hadler, M., Ambesi-Impiobato, A., Paietta, E. M., Racevskis, J., Wiernik, P. H., Rowe, J. M., Jakubczak, J. L., Randolph, S., et al. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0938 · Cited by 104
Nichols, C. A., Gibson, W. J., Brown, M. S., Kosmicki, J. A., Busanovich, J. P., Wei, H. Y., Urbanski, L. M., Currimjee, N., Berger, A. C., Gao, G. F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16399-y · Cited by 107
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Groot, A. J., & Vooijs, M. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0899-4_2 · Cited by 110
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Lanigan, F., Geraghty, J. G., & Bracken, A. P. (2011) · Oncogene · doi:10.1038/onc.2011.34 · Cited by 95
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Chenoweth, D. M., & Dervan, P. B. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105068b · Cited by 95
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CANALIS, E. M., & Zanotti, S. (2014) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-014-0200-y · Cited by 95
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Sabatino, V., Rebelein, J. G., & Ward, T. R. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b07193 · Cited by 95
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Wang, X. Q., Zhang, W., Lui, E. L. H., Zhu, Y., Lü, P., Yu, X., Sun, J.-S., Yang, S., Poon, R. T. P., & Fan, S. T. (2011) · International Journal of Cancer · doi:10.1002/ijc.27336 · Cited by 95
Descatoire, M., Weller, S., Irtan, S., Sarnacki, S., Feuillard, J., Storck, S., Guiochon‐Mantel, A., Bouligand, J., Morali, A., Cohen, J., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.2013220304222014c · Cited by 95
Stapling of unprotected helical peptides via photo-induced intramolecular thiol–yne hydrothiolation
Tian, Y., Li, J., Zhao, H., Zeng, X., Wang, D., Liu, Q., Niu, X., Huang, X., Xu, N., & Li, Z. (2016) · Chemical Science · doi:10.1039/c6sc00106h · Cited by 96
Tosello, V., & Ferrando, A. A. (2013) · Therapeutic Advances in Hematology · doi:10.1177/2040620712471368 · Cited by 92
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Lin, S., Tian, L., Shen, H., Gu, Y., Li, J., Chen, Z., Sun, X., You, M. J., & Wu, L. (2012) · Oncogene · doi:10.1038/onc.2012.482 · Cited by 91
Pelay‐Gimeno, M., Glas, A., Koch, O., & Grossmann, T. N. (2015) · Angewandte Chemie · doi:10.1002/ange.201412070 · Cited by 90
Cromm, P. M., Schaubach, S., Spiegel, J., Fürstner, A., Grossmann, T. N., & Waldmann, H. (2016) · Nature Communications · doi:10.1038/ncomms11300 · Cited by 93
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Feng, P., Chen, D., Wang, X., Li, Y., Li, Z., Li, B., Zhang, Y., Li, W., Zhang, J., Ye, J., et al. (2022) · Leukemia · doi:10.1038/s41375-022-01651-9 · Cited by 90
Ashworth, T. D., Pear, W. S., Chiang, M. Y., Blacklow, S. C., Mastio, J., Xu, L., Kelliher, M. A., Kastner, P., Chan, S. H., & Aster, J. C. (2010) · Blood · doi:10.1182/blood-2010-05-286328 · Cited by 89
Self-citationImpact of Notch Signaling on Inflammatory Responses in Cardiovascular Disorders
Quillard, T., & Charreau, B. L. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14046863 · Cited by 94
Notch signaling in prostate cancer: A moving target
Carvalho, F. L. F., Simons, B. W., Eberhart, C. G., & Berman, D. M. (2014) · The Prostate · doi:10.1002/pros.22811 · Cited by 91
Relapsed T Cell ALL: Current Approaches and New Directions
McMahon, C. M., & Luger, S. M. (2019) · Current Hematologic Malignancy Reports · doi:10.1007/s11899-019-00501-3 · Cited by 87
Direct Targeting of Rab‐GTPase–Effector Interactions
Spiegel, J., Cromm, P. M., Itzen, A., Goody, R. S., Grossmann, T. N., & Waldmann, H. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201308568 · Cited by 88
Birts, C. N., Nijjar, S. K., Mardle, C. A., Hoakwie, F., Duriez, P. J., Blaydes, J. P., & Tavassoli, A. (2013) · Chemical Science · doi:10.1039/c3sc50481f · Cited by 85
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Metadata
- Authors
- Moellering, R. E., Cornejo, M., Davis, T. N., Bianco, C. D., Aster, J. C., Blacklow, S. C., Kung, A. L., Gilliland, D. G., Verdine, G. L., & Bradner, J. E.
- Affiliations
- Broad Institute (US)
- Brigham and Women's Hospital (US)
- Dana-Farber Cancer Institute (US)
- Harvard University (US)
- Corresponding author
- Verdine, Gregory L.
- Bradner, James E.
- ORCID
- Venue
- Nature
- Published
- 2009-11-12
- Volume
- 462
- Issue
- 7270
- Pages
- 182-188
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2951323
- OpenAlex
- W2085948054
- Cited by
- 752
- References
- 51
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 12 · 2023: 30 · 2022: 21 · 2021: 28 · 2020: 43 · 2019: 35 · 2018: 47 · 2017: 43 · 2016: 34 · 2015: 56 · 2014: 70 · 2013: 76 · 2012: 75
- FWCI
- 32.31
- Type
- journal article
- Language
- en
- Update notices
- erratum (2010-01-21)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Iris (University of Trento) (submittedVersion)
- Funders
- National Institutes of Health (n01co12400-79-0-22, 5t32gm007598-41)
- National Cancer Institute (N01CO12400, N01-CO-012400, P01CA119070, R01CA092433, R56CA092433)
- National Institute of General Medical Sciences (5T32GM007598, T32-GM007598)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- Notch signaling, hydrocarbon-stapled peptides, protein-protein interaction inhibition, T-cell acute lymphoblastic leukemia, Notch1, transcription factor antagonism, cell-permeable peptide
- MeSH terms
- Animals, Binding, Competitive, Cell Membrane Permeability, Disease Models, Animal, DNA-Binding Proteins, Humans, Models, Molecular, Nuclear Proteins, Peptides, Protein Binding, Substrate Specificity, Transcription Factors, Signal Transduction, Transcriptional Activation, Gene Expression Regulation, Neoplastic, Genome, Protein Structure, Secondary, Protein Structure, Tertiary, Drosophila Proteins, Cell Line, Tumor, Cell Proliferation, Mice, Immunoglobulin J Recombination Signal Sequence-Binding Protein, Receptor, Notch1, Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
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