Cited by 243HER2/EGFR in Cancer ResearchLung Cancer Treatments and MutationsCancer Genomics and Diagnostics

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Pan-Cancer Landscape and Analysis of ERBB2 Mutations Identifies Poziotinib as a Clinically Active Inhibitor and Enhancer of T-DM1 Activity

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Robichaux, Jacqulyne P., Elamin, Yasir Y., Vijayan, R.S.K., Nilsson, Monique B., Hu, Lemei, He, Junqin, Zhang, Fahao, Pisegna, Marlese, Poteete, Alissa, Sun, Huiying, Li, Shuai, Chen, Ting, Han, Han, Negrao, Marcelo Vailati, Ahnert, Jordi Rodon, Diao, Lixia, Wang, Jing, Le, Xiuning, Meric-Bernstam, Funda, Routbort, Mark, Roeck, Brent, Yang, Zane, Raymond, Victoria M., Lanman, Richard B., Frampton, Garrett M., Miller, Vincent A., Schrock, Alexa B., Albacker, Lee A., Wong, Kwok-kin, Cross, Jason B., Heymach, John V.·2019·Cancer Cell

DOI 10.1016/j.ccell.2019.09.001PMC PMC6944069

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Abstract

We characterized the landscape and drug sensitivity of ERBB2 (HER2) mutations in cancers. In 11 datasets (n = 211,726), ERBB2 mutational hotspots varied across 25 tumor types. Common HER2 mutants yielded differential sensitivities to eleven EGFR/HER2 tyrosine kinase inhibitors (TKIs) in vitro, and molecular dynamics simulations revealed that mutants with a reduced drug-binding pocket volume were associated with decreased affinity for larger TKIs. Overall, poziotinib was the most potent HER2 mutant-selective TKI tested. Phase II clinical testing in ERBB2 exon 20-mutant non-small cell lung cancer resulted in a confirmed objective response rate of 42% in the first 12 evaluable patients. In pre-clinical models, poziotinib upregulated HER2 cell-surface expression and potentiated the activity of T-DM1, resulting in complete tumor regression with combination treatment.

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Comparison of simple potential functions for simulating liquid water
Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,397
Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems
Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,638
New response evaluation criteria in solid tumours: revised RECIST guideline (version 1.1)
Eisenhauer, E. A., Therasse, P., Bogaerts, J., Schwartz, L. H., Sargent, D., Ford, R., Dancey, J., Arbuck, S., Gwyther, S., Mooney, M., et al. (2009) · European Journal of Cancer · doi:10.1016/j.ejca.2008.10.026 · Cited by 29,534
Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
Ryckaert, J.-P., Ciccotti, G., & Berendsen, H. J. C. (1977) · Journal of Computational Physics · doi:10.1016/0021-9991(77)90098-5 · Cited by 21,430
Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914
ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB
Maier, J., Martinez, C., Kasavajhala, K., Wickstrom, L., Hauser, K., & Simmerling, C. L. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00255 · Cited by 11,141
The Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity
Barretina, J., Caponigro, G., Stransky, N., Venkatesan, K., Margolin, A. A., Kim, S., Wilson, C. J., Lehár, J., Kryukov, G. V., Sonkin, D., et al. (2012) · Nature · doi:10.1038/nature11003 · Cited by 7,950
Trastuzumab in combination with chemotherapy versus chemotherapy alone for treatment of HER2-positive advanced gastric or gastro-oesophageal junction cancer (ToGA): a phase 3, open-label, randomised controlled trial
Bang, Y.-J., Van Cutsem, E., Feyereislova, A., Chung, H. C., Shen, L., Sawaki, A., Lordick, F., Ohtsu, A., Omuro, Y., Satoh, T., et al. (2010) · The Lancet · doi:10.1016/s0140-6736(10)61121-x · Cited by 7,302
Pembrolizumab versus docetaxel for previously treated, PD-L1-positive, advanced non-small-cell lung cancer (KEYNOTE-010): a randomised controlled trial
Herbst, R. S., Baas, P., Kim, D.-W., Felip, E., Pérez-Gracia, J. L., Han, J.-Y., Molina, J., Kim, J.-H., Arvis, C. D., Ahn, M.-J., et al. (2016) · The Lancet · doi:10.1016/s0140-6736(15)01281-7 · Cited by 6,449
Atezolizumab versus docetaxel in patients with previously treated non-small-cell lung cancer (OAK): a phase 3, open-label, multicentre randomised controlled trial
Rittmeyer, A., Barlési, F., Waterkamp, D., Park, K., Ciardiello, F., von Pawel, J., Gadgeel, S. M., Hida, T., Kowalski, D. M., Cobo, M., et al. (2016) · The Lancet · doi:10.1016/s0140-6736(16)32517-x · Cited by 4,718
Trastuzumab emtansine for HER2-positive advanced breast cancer
Verma, S., Miles, D., Gianni, L., Krop, I. E., Welslau, M., Baselga, J., Pegram, M., Oh, D.-Y., Diéras, V., Guardino, E., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1209124 · Cited by 3,834
Phase III Study of Afatinib or Cisplatin Plus Pemetrexed in Patients With Metastatic Lung Adenocarcinoma With EGFR Mutations
Sequist, L. V., Yang, J. C.-H., Yamamoto, N., O'Byrne, K., Hirsh, V., Mok, T., Geater, S. L., Orlov, S., Tsai, C.-M., Boyer, M., et al. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.44.2806 · Cited by 3,228
Adjuvant Trastuzumab in HER2-Positive Breast Cancer
Slamon, D. J., EIERMANN, W., Robert, N. J., Pieńkowski, T., Martín, M., Press, M. F., Mackey, J. R., Glaspy, J. A., Chan, A., Pawlicki, M., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa0910383 · Cited by 2,833
Pertuzumab plus Trastuzumab plus Docetaxel for Metastatic Breast Cancer
Baselga, J., Cortés, J., Kim, S.-B., Im, S.-A., Hegg, R., Im, Y.-H., Roman, L., Pedrini, J. L., Pienkowski, T., Knott, A., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1113216 · Cited by 2,532
Randomized Phase III Trial of Pemetrexed Versus Docetaxel in Patients With Non–Small-Cell Lung Cancer Previously Treated With Chemotherapy
Hanna, N., Shepherd, F. A., Fossella, F. V., Pereira, J. R., De Marinis, F., von Pawel, J., Gatzemeier, U., Tsao, T. C. Y., Pless, M., Muller, T., et al. (2004) · Journal of Clinical Oncology · doi:10.1200/jco.2004.08.163 · Cited by 2,426
Prospective Randomized Trial of Docetaxel Versus Best Supportive Care in Patients With Non–Small-Cell Lung Cancer Previously Treated With Platinum-Based Chemotherapy
Shepherd, F. A., Dancey, J. E., Ramlau, R., Mattson, K. V., Gralla, R. J., O’Rourke, M. A., Levitan, N. I., Gressot, L., Vincent, M. D., Burkes, R. L., et al. (2000) · Journal of Clinical Oncology · doi:10.1200/jco.2000.18.10.2095 · Cited by 2,178
The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP
Yun, C.-H., Mengwasser, K. E., Toms, A. V., Woo, M. S., Greulich, H., Wong, K.-K., Meyerson, M., & Eck, M. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709662105 · Cited by 2,118
Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation 1 1Edited by J. Thornton
Word, J. M., Lovell, S. C., Richardson, J. S., & Richardson, D. C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2401 · Cited by 1,432
Lapatinib with trastuzumab for HER2-positive early breast cancer (NeoALTTO): a randomised, open-label, multicentre, phase 3 trial
Baselga, J. M., Bradbury, I., Eidtmann, H., Cosimo, S. D., de Azambuja, E., Aura, C. M., Gómez, H., Dinh, P., Fauria, K., Dooren, V. V., et al. (2012) · The Lancet · doi:10.1016/s0140-6736(11)61847-3 · Cited by 1,324
Langevin stabilization of molecular dynamics
Izaguirre, J. A., Catarello, D. P., Wozniak, J. M., & Skeel, R. D. (2001) · The Journal of Chemical Physics · doi:10.1063/1.1332996 · Cited by 1,086
Activating HER2 Mutations in HER2 Gene Amplification Negative Breast Cancer
Bose, R., Kavuri, S. M., Searleman, A. C., Shen, W., Shen, D., Koboldt, D. C., Monsey, J. D., Goel, N. J., Aronson, A. B., Li, S., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0349 · Cited by 886
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Nivolumab Versus Docetaxel in Previously Treated Patients With Advanced Non–Small-Cell Lung Cancer: Two-Year Outcomes From Two Randomized, Open-Label, Phase III Trials (CheckMate 017 and CheckMate 057)
Horn, L., Spigel, D. R., Vokes, E. E., Holgado, E., Ready, N., Steins, M. B., Poddubskaya, E. V., Borghaei, H., Felip, E., Paz-Ares, L. G., et al. (2017) · Journal of Clinical Oncology · doi:10.1200/jco.2017.74.3062 · Cited by 875
A phase III randomized comparison of lapatinib plus capecitabine versus capecitabine alone in women with advanced breast cancer that has progressed on trastuzumab: updated efficacy and biomarker analyses
Cameron, D., Casey, M., Press, M. F., Lindquist, D. L., Pieńkowski, T., Romieu, C. G., Chan, S. Y. T., Jagiełło-Gruszfeld, A., Kaufman, B., Crown, J. P., et al. (2008) · Breast Cancer Research and Treatment · doi:10.1007/s10549-007-9885-0 · Cited by 795
HER kinase inhibition in patients with HER2- and HER3-mutant cancers
Hyman, D. M., Piha-Paul, S. A., Won, H., Rodon, J., Saura, C., Shapiro, G. I., Juric, D., Quinn, D. I., Moreno, V., Doger, B., et al. (2018) · Nature · doi:10.1038/nature25475 · Cited by 780
Self-citation
Ado-Trastuzumab Emtansine for Patients With HER2-Mutant Lung Cancers: Results From a Phase II Basket Trial
Li, B. T., Shen, R., Buonocore, D. J., Olah, Z. T., Ni, A., Ginsberg, M. S., Ulaner, G. A., Offin, M. D., Feldman, D., Hembrough, T., et al. (2018) · Journal of Clinical Oncology · doi:10.1200/jco.2018.77.9777 · Cited by 562
Routine Access to Millisecond Time Scale Events with Accelerated Molecular Dynamics
Pierce, L., Salomón–Ferrer, R., de Oliveira, C. A. F., McCammon, J. A., & Walker, R. C. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300284c · Cited by 515
Targeted therapy for advanced solid tumors on the basis of molecular profiles: Results from MyPathway, an open-label, phase IIa multiple basket study
Hainsworth, J. D., Meric-Bernstam, F., Swanton, C., Hurwitz, H., Spigel, D. R., Sweeney, C., Burris, H. A., Bose, R., Yoo, B., Stein, A., et al. (2018) · Journal of Clinical Oncology · doi:10.1200/jco.2017.75.3780 · Cited by 506
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Ettinger, D. S., Aisner, D. L., Wood, D. E., Akerley, W., Bauman, J. R., Chang, J. Y., Chirieac, L. R., D’Amico, T. A., Dilling, T. J., Dobelbower, M. C., et al. (2018) · Journal of the National Comprehensive Cancer Network · doi:10.6004/jnccn.2018.0062 · Cited by 469
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Robichaux, J. P., Elamin, Y. Y., Tan, Z., Carter, B. W., Zhang, S., Liu, S., Li, S., Chen, T., Poteete, A., Estrada-Bernal, A., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0007-9 · Cited by 468
Self-citation
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Park, J. W., Liu, M., Yee, D., Yau, C. S. F., Veer, L. V. ‘., Symmans, W. F., Paoloni, M. C., Perlmutter, J., Hylton, N. M., Hogarth, M. A., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1513750 · Cited by 456
Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein
Aertgeerts, K., Skene, R. J., Yano, J. K., Sang, B., Zou, H., Snell, G., Jennings, A. J., Iwamoto, K., Habuka, N., Hirokawa, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.206193 · Cited by 448
Lapatinib, a HER2 tyrosine kinase inhibitor, induces stabilization and accumulation of HER2 and potentiates trastuzumab-dependent cell cytotoxicity
Scaltriti, M., Verma, C. S., Guzmán, M., Jimenez, J., Parra, J.-L., Pedersen, K., Smith, D. J., Landolfi, S., y Cajal, S. R., Arribas, J., et al. (2008) · Oncogene · doi:10.1038/onc.2008.432 · Cited by 440
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Mok, T. S., Cheng, Y., Zhou, X., Lee, K. H., Nakagawa, K., Niho, S., Lee, M., Linke, R., Rosell, R., Corral, J., et al. (2018) · Journal of Clinical Oncology · doi:10.1200/jco.2018.78.7994 · Cited by 439
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Odegaard, J. I., Vincent, J. J., Mortimer, S., Vowles, J. V., Ulrich, B. C., Banks, K. C., Fairclough, S. R., Zill, O. A., Sikora, M., Mokhtari, R. B., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3831 · Cited by 437
Self-citation
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Leo, A. D., Gómez, H., Aziz, Z., Zvirbule, Z., Bines, J., Arbushites, M. C., Guerrera, S., Koehler, M. T., Oliva, C., Stein, S. H., et al. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2008.16.2578 · Cited by 417
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Meric‐Bernstam, F., Johnson, A. M., Dumbrava, E. E. I., Raghav, K. P. S., Balaji, K., Bhatt, M., Murthy, R. K., Rodon, J. A., & Piha-Paul, S. A. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-2275 · Cited by 348
Self-citation
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Gómez, H., Doval, D. C., Chavez, M. A., Ang, P., Aziz, Z., Nag, S. M., Ng, C., Franco, S. X., Chow, L. W. C., Arbushites, M. C., et al. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.14.0590 · Cited by 338
Targeting HER2 aberrations as actionable drivers in lung cancers: phase II trial of the pan-HER tyrosine kinase inhibitor dacomitinib in patients with HER2-mutant or amplified tumors
Kris, M. G., Camidge, D. R., Giaccone, G., Hida, T., Li, B. T., O'Connell, J., Taylor, I., Zhang, H., Arcila, M. E., Goldberg, Z., et al. (2015) · Annals of Oncology · doi:10.1093/annonc/mdv186 · Cited by 334
Lung cancer patients with HER2 mutations treated with chemotherapy and HER2-targeted drugs: results from the European EUHER2 cohort
Mazières, J., Barlési, F., Filleron, T., Besse, B., Monnet, I., Beau‐Faller, M., Peters, S., Dansin, É., Früh, M., Pless, M., et al. (2015) · Annals of Oncology · doi:10.1093/annonc/mdv573 · Cited by 326
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Chen, H., Ma, J., Li, W., Eliseenkova, A. V., Xu, C., Neubert, T. A., Miller, W. T., & Mohammadi, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.028 · Cited by 300
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Li, B. T., Michelini, F., Misale, S., Cocco, E., Baldino, L., Cai, Y., Shifman, S. G., Tu, H., Myers, M. L., Xu, C., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0215 · Cited by 293
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Greulich, H. E., Kaplan, B., Mertins, P., Chen, T.-H., Tanaka, K., Yun, C., Zhang, X., Lee, S., Cho, J., Ambrogio, L., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203201109 · Cited by 288
Self-citation
Sampling of slow diffusive conformational transitions with accelerated molecular dynamics
Hamelberg, D., de Oliveira, C. A. F., & McCammon, J. A. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2789432 · Cited by 253
Ba/F3 cells and their use in kinase drug discovery
Warmuth, M., Kim, S., Gu, X.-J., Xia, G., & Adrián, F. (2007) · Current Opinion in Oncology · doi:10.1097/cco.0b013e328011a25f · Cited by 240
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Ma, C. X., Bose, R., Gao, F., Freedman, R. A., Telli, M. L., Kimmick, G., Winer, E., Naughton, M., Goetz, M. P., Russell, C., et al. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-0900 · Cited by 193
Self-citation
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Perera, S. A., Li, D., Shimamura, T., Raso, M. G., Ji, H., Chen, L., Borgman, C. L., Zaghlul, S., Brandstetter, K. A., Kubo, S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808930106 · Cited by 189
Activating HER2 mutations as emerging targets in multiple solid cancers
Connell, C. M., & Doherty, G. J. (2017) · ESMO Open · doi:10.1136/esmoopen-2017-000279 · Cited by 169
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the NCI PRO-CTCAE Study Group, Hay, J. L., Atkinson, T. M., Reeve, B. B., Mitchell, S. A., Mendoza, T. R., Willis, G., Minasian, L. M., Clauser, S. B., Denicoff, A. M., et al. (2013) · Quality of Life Research · doi:10.1007/s11136-013-0470-1 · Cited by 163
Implementation of accelerated molecular dynamics in NAMD
Wang, Y., Harrison, C. B., Schulten, K. J., & McCammon, J. A. (2011) · Computational Science & Discovery · doi:10.1088/1749-4699/4/1/015002 · Cited by 147
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Hartmaier, R. J., Albacker, L. A., Chmielecki, J., Bailey, M., He, J., Goldberg, M. E., Ramkissoon, S. H., Suh, J. H., Elvin, J. A., Chiacchia, S., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2479 · Cited by 139
Self-citation
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Kosaka, T., Tanizaki, J., Paranal, R. M., Endoh, H., Lydon, C., Capelletti, M., Repellin, C. E., Choi, J., Ogino, A., Calles, A., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-3404 · Cited by 131
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Möbitz, H. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.03.009 · Cited by 105
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Nagano, M., Kohsaka, S., Ueno, T., Kojima, S., Saka, K., Iwase, H., Kawazu, M., & Mano, H. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-0991 · Cited by 79
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Xu, Z., Zhang, Y., Li, N., Liu, P., Gao, L., Gao, X. Y., & Tie, X. (2017) · BMJ Open · doi:10.1136/bmjopen-2016-013053 · Cited by 64
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Sultan, M. M., Denny, R. A., Unwalla, R. J., Lovering, F., & Pande, V. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-10697-0 · Cited by 49
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Negrao, M. V., Reuben, A., Robichaux, J. P., Le, X., Nilsson, M. B., Wu, C., Zhang, J., Landry, L. C. A. D. L., Roarty, E. B., Rinsurongkawong, W., et al. (2018) · Journal of Clinical Oncology · doi:10.1200/jco.2018.36.15_suppl.9052 · Cited by 46
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Oh, I., Hur, J. Y., Park, C., Kim, Y., Kim, S. J., Lee, M. K., Kim, H. J., Lee, K. Y., Lee, J. C., & Choi, C. (2018) · Clinical Lung Cancer · doi:10.1016/j.cllc.2018.05.018 · Cited by 32
Pharmacodynamics, pharmacokinetics and clinical efficacy of neratinib in HER2-positive breast cancer and breast cancer with HER2 mutations
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Shan, L., Qiu, T., Ling, Y., Guo, L., Zheng, B. J., Wang, B., Li, W., Li, L., & Ying, J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130447 · Cited by 22
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Shen, X., Chen, B., Ma, Z., Xie, B., Cao, X., Yang, T., Zhao, Y., Qin, J., Li, J., Cao, F., et al. (2015) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2015.1049361 · Cited by 10
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In the literature: December 2019
Gambardella, V., Insa, A., Cejalvo, J. M., & Cervantes, A. M. R. (2020) · ESMO Open · doi:10.1136/esmoopen-2019-000642 · Cited by 1

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Trastuzumab Deruxtecan in HER2 -Mutant Non–Small-Cell Lung Cancer
Li, B. T., Smit, E. F., Goto, Y., Nakagawa, K., Udagawa, H., Mazières, J., Nagasaka, M., Bazhenova, L. A., Saltos, A. N., Felip, E., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2112431 · Cited by 1,068
Structure-based classification predicts drug response in EGFR-mutant NSCLC
Robichaux, J. P., Le, X., Vijayan, R. S. K., Hicks, J. K., Heeke, S., Elamin, Y. Y., Lin, H. Y., Udagawa, H., Skoulidis, F., Tran, H., et al. (2021) · Nature · doi:10.1038/s41586-021-03898-1 · Cited by 490
Self-citation
Targeting HER2 with Trastuzumab Deruxtecan: A Dose-Expansion, Phase I Study in Multiple Advanced Solid Tumors
Tsurutani, J., Iwata, H., Krop, I. E., Janne, P. A., Doi, T., Takahashi, S., Park, H., Redfern, C. H., Tamura, K., Wise-Draper, T. M., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-1014 · Cited by 359
HER2-Mediated Internalization of Cytotoxic Agents in ERBB2 Amplified or Mutant Lung Cancers
Li, B. T., Michelini, F., Misale, S., Cocco, E., Baldino, L., Cai, Y., Shifman, S. G., Tu, H., Myers, M. L., Xu, C., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0215 · Cited by 293
Endocytosis in cancer and cancer therapy
Banushi, B., Joseph, S. R., Lum, B., Lee, J. J., & Simpson, F. (2023) · Nature reviews. Cancer · doi:10.1038/s41568-023-00574-6 · Cited by 252

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Authors: Robichaux, J. P., Elamin, Y. Y., Vijayan, R. S. K., Nilsson, M. B., Hu, L., He, J., Zhang, F., Pisegna, M., Poteete, A., Sun, H., Li, S., Chen, T., Han, H., Negrao, M. V., Ahnert, J. R., Diao, L., Wang, J., Le, X., Meric-Bernstam, F., Routbort, M., Roeck, B., Yang, Z., Raymond, V. M., Lanman, R. B., Frampton, G. M., Miller, V. A., Schrock, A. B., Albacker, L. A., Wong, K.-K., Cross, J. B., & Heymach, J. V.
Affiliations: The University of Texas MD Anderson Cancer Center (US)
NYU Langone Health (US)
Spectrum Pharmaceuticals (United States) (US)
Guardant (United States) (US)
Foundation Medicine (United States) (US)
Corresponding author: Heymach, John V.
ORCID: Robichaux, Jacqulyne P.
Elamin, Yasir Y.
Vijayan, R.S.K.
Nilsson, Monique B.
He, Junqin
Zhang, Fahao
Poteete, Alissa
Sun, Huiying
Li, Shuai
Chen, Ting
Han, Han
Negrao, Marcelo Vailati
Diao, Lixia
Wang, Jing
Le, Xiuning
Raymond, Victoria M.
Lanman, Richard B.
Frampton, Garrett M.
Miller, Vincent A.
Schrock, Alexa B.
Albacker, Lee A.
Wong, Kwok-kin
Cross, Jason B.
Heymach, John V.
Venue: Cancer Cell
Publisher: Elsevier BV
Published: 2019-10
Volume: 36
Issue: 4
Pages: 444-457.e7
ISSN: 1535-6108 (ISSN-L)
DOI: 10.1016/j.ccell.2019.09.001
PMC: PMC6944069
OpenAlex: W2977889895
Cited by: 242
References: 66
Citations by year: 2026: 21 · 2025: 34 · 2024: 33 · 2023: 40 · 2022: 43 · 2021: 43 · 2020: 28
FWCI: 12.00
Type: journal article
Language: en
Update notices: erratum (2020-03-16)
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 379 d)
Locations: Cancer Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Cancer Institute
Topics: Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Lung Cancer Treatments and Mutations
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Genomics and Diagnostics
Keywords: ERBB2 mutations, HER2, poziotinib, tyrosine kinase inhibitors, trastuzumab emtansine, non-small cell lung cancer, drug sensitivity, molecular dynamics simulation, drug-binding pocket, combination therapy
MeSH terms: Antineoplastic Agents, Immunological, Progression-Free Survival, Ado-Trastuzumab Emtansine, Adult, Animals, Antineoplastic Combined Chemotherapy Protocols, Disease Models, Animal, DNA Mutational Analysis, Drug Synergism, Female, Humans, Male, Mice, Transgenic, Mutation, Neoplasms, Quinazolines, Erb-b2 Receptor Tyrosine Kinases, Drug Resistance, Neoplasm, Protein Kinase Inhibitors, Mice, Datasets as Topic

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Pan-Cancer Landscape and Analysis of ERBB2 Mutations Identifies Poziotinib as a Clinically Active Inhibitor and Enhancer of T-DM1 Activity

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