Untangling the ErbB signalling network

Yarden, Yosef; Sliwkowski, Mark X.

doi:10.1038/35052073

Cited by 6,974HER2/EGFR in Cancer ResearchPI3K/AKT/mTOR signaling in cancerLung Cancer Treatments and Mutations

Untangling the ErbB signalling network

Yarden, Yosef, Sliwkowski, Mark X.·2001·Nature Reviews Molecular Cell Biology

DOI 10.1038/35052073

Open this paper in CoChat — free account

Abstract

When epidermal growth factor and its relatives bind the ErbB family of receptors, they trigger a rich network of signalling pathways, culminating in responses ranging from cell division to death, motility to adhesion. The network is often dysregulated in cancer and lends credence to the mantra that molecular understanding yields clinical benefit: over 25,000 women with breast cancer have now been treated with trastuzumab (Herceptin), a recombinant antibody designed to block the receptor ErbB2. Likewise, small-molecule enzyme inhibitors and monoclonal antibodies to ErbB1 are in advanced phases of clinical testing. What can this pathway teach us about translating basic science into clinical use?

Integrity signals

Registry

Crossref · 10.1038/35052073

Cites

111 of 111 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

EGFR is a member of the receptor tyrosine kinase family and a typical transmembrane receptor that initiates signaling cascades upon ligand-stimulated dimerization, thereby activating its tyrosine kinase and multiple downstream effectors.
“Epidermal growth factor receptor (EGFR), a member of the receptor tyrosine kinase family, is a typical transmembrane receptor that initiates signaling cascades upon ligand-stimulated dimerization, thereby activating its tyrosine kinase and multiple downstream effectors.99–101”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [99]
EGFR is implicated in cell proliferation, mitosis, and cancer development.
“and is implicated in cell proliferation, mitosis, and cancer development.99,103,104”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [99]
EGFR is a member of the ErbB family that drives the initiation and development of multiple types of cancers.
“EGFR is a member of ErbB family driving the initiation and development of multiple types of cancers [181].”
From Combination strategies with PD-1/PD-L1 blockade: current advances and future directions (2022) · cites this paper as [181]
HER3 features very low catalytic activity but engages in oncogenic signaling by acting as a scaffold to enable receptor heterodimerization.
“HER3 features very low catalytic activity but engages in oncogenic signaling by acting as a scaffold to enable receptor heterodimerization.8−10”
From Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence (2023) · cites this paper as [9]
TGFα is co-overexpressed with EGFR in lung, colorectal, ovary and head and neck squamous cancers, where it is associated with poor patient prognosis.
“TGFα is also co-overexpressed with EGFR in lung, colorectal, ovary and head and neck squamous cancers, where it is associated with poor patient prognosis (Grandis et al., 1998; Yarden and Sliwkowski, 2001) (Table 1).”
From ERBB Receptors: From Oncogene Discovery to Basic Science to Mechanism-Based Cancer Therapeutics (2014) · cites this paper as Yarden and Sliwkowski, 2001

Human Breast Cancer: Correlation of Relapse and Survival with Amplification of the HER-2/ neu Oncogene
Slamon, D. J., Clark, G. M., Wong, S. G., Levin, W. J., Ullrich, A., & McGuire, W. L. (1987) · Science · doi:10.1126/science.3798106 · Cited by 11,760 · see citing works
Epidermal growth factor-related peptides and their receptors in human malignancies.
Salomon, D., Brandt, R., Ciardiello, F., & Normanno, N. (1995) · Critical reviews in oncology/hematology · doi:10.1016/1040-8428(94)00144-i · Cited by 2,860 · see citing works
Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets
Clynes, R. A., Towers, T. L., Presta, L. G., & Ravetch, J. V. (2000) · Nature Medicine · doi:10.1038/74704 · Cited by 2,768 · see citing works
Multinational Study of the Efficacy and Safety of Humanized Anti-HER2 Monoclonal Antibody in Women Who Have HER2-Overexpressing Metastatic Breast Cancer That Has Progressed After Chemotherapy for Metastatic Disease
Cobleigh, M., Vogel, C. L., Tripathy, D., Robert, N. J., Scholl, S., Fehrenbacher, L., Wolter, J. M., Paton, V. E., Shak, S., Lieberman, G., et al. (1999) · Journal of Clinical Oncology · doi:10.1200/jco.1999.17.9.2639 · Cited by 2,767 · see citing works
The ErbB signaling network: receptor heterodimerization in development and cancer
Olayioye, M. A., Neve, R. M., Lane, H. A., & Hynes, N. E. (2000) · The EMBO Journal · doi:10.1093/emboj/19.13.3159 · Cited by 2,438 · see citing works
Tyrosine Kinase Inhibition: An Approach to Drug Development
Levitzki, A., & Gazit, A. (1995) · Science · doi:10.1126/science.7892601 · Cited by 1,635 · see citing works
ErbB‐2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
Graus-Porta, D., Beerli, R. R., Daly, J. M., & Hynes, N. E. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1647 · Cited by 1,593 · see citing works
EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
Prenzel, N., Zwick, E., Daub, H., Leserer, M., Abraham, R., Wallasch, C., & Ullrich, A. (1999) · Nature · doi:10.1038/47260 · Cited by 1,507 · see citing works
β-Arrestin-Dependent Formation of β 2 Adrenergic Receptor-Src Protein Kinase Complexes
Luttrell, L. M., Ferguson, S. S. G., Daaka, Y., Miller, W. E., Maudsley, S. R., Rocca, G. J. D., Lin, F., Kawakatsu, H., Owada, K. M., Luttrell, D. K., et al. (1999) · Science · doi:10.1126/science.283.5402.655 · Cited by 1,473 · see citing works
Targeted Disruption of Mouse EGF receptor: Effect of Genetic Background on Mutant Phenotype
Threadgill, D. W., Dlugosz, A. A., Hansen, L. A., Tennenbaum, T., Lichti, U. F., Yee, D., LaMantia, C., Mourton, T., Herrup, K., Harris, R. C., et al. (1995) · Science · doi:10.1126/science.7618084 · Cited by 1,460 · see citing works
Phase II study of weekly intravenous recombinant humanized anti-p185HER2 monoclonal antibody in patients with HER2/neu-overexpressing metastatic breast cancer.
Baselga, J. M., Tripathy, D., Mendelsohn, J. M., Baughman, S. A., Benz, C. C., Dantis, L., Sklarin, N. T., Seidman, A. D., Hudis, C. A., Moore, J. L., et al. (1996) · Journal of Clinical Oncology · doi:10.1200/jco.1996.14.3.737 · Cited by 1,382 · see citing works
A Hierarchical Network of Interreceptor Interactions Determines Signal Transduction by Neu Differentiation Factor/Neuregulin and Epidermal Growth Factor
Tzahar, E., Waterman, H., Chen, X., Levkowitz, G., Karunagaran, D., Lavi, S., Ratzkin, B. J., & Yarden, Y. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5276 · Cited by 1,039 · see citing works
Self-citation
Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor
Miettinen, P. J., Berger, J. E., Meneses, J. J., Phung, Y. T., Pedersen, R. A., Werb, Z., & Derynck, R. (1995) · Nature · doi:10.1038/376337a0 · Cited by 1,038 · see citing works
The HER‐2/ neu Oncogene in Breast Cancer: Prognostic Factor, Predictive Factor, and Target for Therapy
Ross, J. S., & Fletcher, J. A. (1998) · Stem Cells · doi:10.1002/stem.160413 · Cited by 990 · see citing works
c-erbB-2 Expression and Response to Adjuvant Therapy in Women with Node-Positive Early Breast Cancer
Muss, H. B., Thor, A. D., Berry, D. A., Kute, T. E., Liu, E. T., Koerner, F., Cirrincione, C., Budman, D. R., Wood, W. C., Barcos, M. P., et al. (1994) · New England Journal of Medicine · doi:10.1056/nejm199405053301802 · Cited by 960 · see citing works
A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
Đikić, I., Tokiwa, G. Y., Lev, S., Courtneidge, S. A., & Schlessinger, J. (1996) · Nature · doi:10.1038/383547a0 · Cited by 955 · see citing works
c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptorPreprint
Levkowitz, G., Waterman, H., Zamir, E., Kam, Z., Oved, S., Langdon, W. Y., Beguinot, L., Geiger, B., & Yarden, Y. (1998) · Genes & Development · doi:10.1101/gad.12.23.3663 · Cited by 865 · see citing works
Self-citation
Structural alterations of the epidermal growth factor receptor gene in human gliomas.
Wong, A. J., Ruppert, J. M., Bigner, S. H., Grzeschik, C. H., Humphrey, P. A., Bigner, D. S., & Vogelstein, B. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.2965 · Cited by 851 · see citing works
EGF receptor
Wells, A. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00015-1 · Cited by 819 · see citing works
HER-2/neu gene amplification characterized by fluorescence in situ hybridization: poor prognosis in node-negative breast carcinomas.
Press, M. F., Bernstein, L., THOMAS, P. A., Meisner, L. F., Zhou, J. Y., Ma, Y., Hung, G., Robinson, R. A., Harris, C., El‐Naggar, A. K., et al. (1997) · Journal of Clinical Oncology · doi:10.1200/jco.1997.15.8.2894 · Cited by 803 · see citing works
Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions.
Pinkas‐Kramarski, R., Soussan, L., Waterman, H., Levkowitz, G., Alroy, I., Klapper, L. N., Lavi, S., Seger, R., Ratzkin, B. J., Sela, M., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00603.x · Cited by 770 · see citing works
Self-citation
Severe neuropathies in mice with targeted mutations in the ErbB3 receptor
Riethmacher, D., Sonnenberg-Riethmacher, E., Brinkmann, V., Yamaai, T., Lewin, G. R., & Birchmeier, C. (1997) · Nature · doi:10.1038/39593 · Cited by 729 · see citing works
Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity.
Guy, P. M., Platko, J. V., Cantley, L. C., Cerione, R. A., & Carraway, K. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8132 · Cited by 698 · see citing works
TGFα deficiency results in hair follicle and eye abnormalities in targeted and waved-1 mice
Luetteke, N., Qiu, T. H., Peiffer, R. L., Oliver, P. M., Smithies, O., & Lee, D. C. (1993) · Cell · doi:10.1016/0092-8674(93)90228-i · Cited by 658 · see citing works
Nonclinical studies addressing the mechanism of action of trastuzumab (Herceptin).
Sliwkowski, M. X., Ja, L., Gd, L., Te, H., FENDLY, B. M., & Fox, J. A. (1999) · PubMed · Cited by 653 · see citing works
Self-citation
Signal characteristics of G protein‐transactivated EGF receptor
Daub, H., Wallasch, C., Lankenau, A., Herrlich, A., & Ullrich, A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.23.7032 · Cited by 647 · see citing works
Frequent expression of a mutant epidermal growth factor receptor in multiple human tumors.
Moscatello, D. K., Holgado-Madruga, M., Godwin, A. K., Ramirez, G., Gunn, G. R., Zoltick, P. W., Biegel, J. A., Hayes, R. L., & Wong, A. J. (1995) · PubMed · Cited by 637 · see citing works
HER-2 tyrosine kinase pathway targets estrogen receptor and promotes hormone-independent growth in human breast cancer cells.
Pietras, R. J., Arboleda, J., Dm, R., Wongvipat, N., Pegram, M. D., Ramos, L., Cm, G., Mg, P., Sliwkowski, M. X., & Dj, S. (1995) · PubMed · Cited by 603 · see citing works
Self-citation
Mice with a null mutation of the TGFα gene have abnormal skin architecture, wavy hair, and curly whiskers and often develop corneal inflammation
Mann, G. B., Fowler, K. J., Gabriel, A., Nice, E. C., Williams, R. L., & Dunn, A. R. (1993) · Cell · doi:10.1016/0092-8674(93)90227-h · Cited by 583 · see citing works
Estrogenic Regulation of Growth and Polypeptide Growth Factor Secretion in Human Breast Carcinoma
Dickson, R. B., & Lippman, M. E. (1987) · Endocrine Reviews · doi:10.1210/edrv-8-1-29 · Cited by 566 · see citing works
Cooperative signaling of ErbB3 and ErbB2 in neoplastic transformation and human mammary carcinomas.
Alimandi, M., Romano, A., Curia, M. C., Muraro, R., Fedi, P., Aaronson, S. A., Fiore, P. P. D., & Kraus, M. H. (1995) · PubMed · Cited by 548 · see citing works
Human epidermal growth factor: isolation and chemical and biological properties.
Cohen, S., & Carpenter, G. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.4.1317 · Cited by 511 · see citing works
Neuregulins and Their Receptors: A Versatile Signaling Module in Organogenesis and Oncogenesis
Burden, S. J., & Yarden, Y. (1997) · Neuron · doi:10.1016/s0896-6273(00)80324-4 · Cited by 479 · see citing works
Self-citation
ErbB3 is required for normal cerebellar and cardiac development: a comparison with ErbB2- and heregulin-deficient mice
Erickson, S. L., O’Shea, K. S., Ghaboosi, N., Loverro, L., Frantz, G. D., Bauer, M., Lu, L. H., & Moore, M. W. (1997) · Development · doi:10.1242/dev.124.24.4999 · Cited by 467 · see citing works
Gβγ Subunits Mediate Src-dependent Phosphorylation of the Epidermal Growth Factor Receptor
Luttrell, L. M., Rocca, G. J. D., van Biesen, T., Luttrell, D. K., & Lefkowitz, R. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4637 · Cited by 457 · see citing works
The ErbB-2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derived growth factors
Klapper, L. N., Glathe, S., Vaisman, N., Hynes, N. E., Andrews, G. C., Sela, M., & Yarden, Y. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4995 · Cited by 455 · see citing works
Self-citation
All ErbB Receptors Other Than the Epidermal Growth Factor Receptor Are Endocytosis Impaired
Baulida, J., Kraus, M. H., Alimandi, M., Fiore, P. P. D., & Carpenter, G. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.5251 · Cited by 453 · see citing works
Specific, irreversible inactivation of the epidermal growth factor receptor and erbB2, by a new class of tyrosine kinase inhibitor
Fry, D. W., Bridges, A. J., Denny, W. A., Doherty, A. M., Greis, K. D., Hicks, J. L., Hook, K. E., Keller, P. R., Leopold, W. R., Loo, J. A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.12022 · Cited by 424 · see citing works
Differential endocytic routing of homo‐ and hetero‐dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers
Lenferink, A. E. G., Pinkas‐Kramarski, R., van de Poll, M. L. M., van Vugt, M. J. H., Klapper, L. N., Tzahar, E., Waterman, H., Sela, M., van Zoelen, E. J. J., & Yarden, Y. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3385 · Cited by 413 · see citing works
Self-citation
Coexpression of epidermal growth factor receptor and ligands in human pancreatic cancer is associated with enhanced tumor aggressiveness.
Yamanaka, Y., Frieß, H., Kobrin, M. S., et al. (1993) · PubMed · Cited by 411 · see citing works
c-erb B2 overexpression decreases the benefit of adjuvant tamoxifen in early-stage breast cancer without axillary lymph node metastases.
Carlomagno, C., Perrone, F., Gallo, C., et al. (1996) · Journal of Clinical Oncology · doi:10.1200/jco.1996.14.10.2702 · Cited by 409 · see citing works
Heregulin‐dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3.
Wallasch, C., Weiss, F. U., Niederfellner, G., Jallal, B., Issing, W., & Ullrich, A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00101.x · Cited by 406 · see citing works
Binding specificities and affinities of egf domains for ErbB receptors
Jones, J. T., Akita, R. W., & Sliwkowski, M. X. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00283-5 · Cited by 387 · see citing works
Self-citation
The Cellular Response to Neuregulins Is Governed by Complex Interactions of the erbB Receptor Family
Riese, D. J., van Raaij, T. M., Plowman, G. D., Andrews, G. C., & Stern, D. F. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.10.5770 · Cited by 368 · see citing works
Controlled Dimerization of ErbB Receptors Provides Evidence for Differential Signaling by Homo- and Heterodimers
Muthuswamy, S. K., Gilman, M. Z., & Brugge, J. S. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.6845 · Cited by 366 · see citing works
The ErbB2 and ErbB3 receptors and their ligand, neuregulin-1, are essential for development of the sympathetic nervous systemPreprint
Britsch, S., Li, L., Kirchhoff, S., Theuring, F., Brinkmann, V., Birchmeier, C., & Riethmacher, D. (1998) · Genes & Development · doi:10.1101/gad.12.12.1825 · Cited by 344 · see citing works
A strain‐independent postnatal neurodegeneration in mice lacking the EGF receptor
Sibilia, M. C., Steinbach, J. P., Stingl, L., Aguzzi, A., & Wagner, E. F. (1998) · The EMBO Journal · doi:10.1093/emboj/17.3.719 · Cited by 325 · see citing works
Secreted Spitz triggers the DER signaling pathway and is a limiting component in embryonic ventral ectoderm determination.
Schweitzer, R., Shaharabany, M., Seger, R., & Shilo, B. Z. (1995) · Genes & Development · doi:10.1101/gad.9.12.1518 · Cited by 317 · see citing works
ERBIN: a basolateral PDZ protein that interacts with the mammalian ERBB2/HER2 receptor
Borg, J., Marchetto, S., Bivic, A. L., Ollendorff, V., Jaulin‐Bastard, F., Saito, H., Fournier, E., Adélaı̈de, J., Margolis, B. L., & Birnbaum, D. (2000) · Nature Cell Biology · doi:10.1038/35017038 · Cited by 311 · see citing works
Synergistic interaction of p185c-neu and the EGF receptor leads to transformation of rodent fibroblasts
Kokai, Y., Myers, J. N., Wada, T., Brown, V. I., LeVea, C., Davis, J. G., Dobashi, K., & Greene, M. I. (1989) · Cell · doi:10.1016/0092-8674(89)90843-x · Cited by 308 · see citing works
Combination of EGFR, HER-2/neu, and HER-3 is a stronger predictor for the outcome of oral squamous cell carcinoma than any individual family members.
Xia, W., Lau, Y. K. J., Zhang, H. Z., Xiao, F. Y., Johnston, D. A., Liu, A. R., Li, L., Katz, R. L., & Hung, M. (1999) · PubMed · Cited by 295 · see citing works
Tyrosine phosphorylation of the EGF receptor by the kinase Jak2 is induced by growth hormone
Yamauchi, T., Ueki, K., Tobe, K., Tamemoto, H., Sekine, N., Wada, M., Honjo, M., Takahashi, M., Takahashi, T., Hirai, H., et al. (1997) · Nature · doi:10.1038/36369 · Cited by 284 · see citing works
ARIA: A Neuromuscular Junction Neuregulin
Fischbach, G. D., & Rosen, K. M. (1997) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.20.1.429 · Cited by 281 · see citing works
Requirement of ErbB2 for signalling by interleukin-6 in prostate carcinoma cells
Qiu, Y., Ravi, L., & Kung, H.-J. (1998) · Nature · doi:10.1038/30012 · Cited by 280 · see citing works
Employment of the Epidermal Growth Factor Receptor in Growth Factor–Independent Signaling Pathways
Carpenter, G. F. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.4.697 · Cited by 272 · see citing works
Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor
Dong, J., Opresko, L. K., Dempsey, P. J., Lauffenburger, D. A., Coffey, R. J., & Wiley, H. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6235 · Cited by 263 · see citing works
ErbB-1 and ErbB-2 Acquire Distinct Signaling Properties Dependent upon Their Dimerization Partner
Olayioye, M. A., Graus-Porta, D., Beerli, R. R., Rohrer, J., Gay, B., & Hynes, N. E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5042 · Cited by 262 · see citing works
Neuregulin-β induces expression of an NMDA-receptor subunit
Ozaki, M., Sasner, M., Yano, R., Lu, H. S., & Buonanno, A. (1997) · Nature · doi:10.1038/37795 · Cited by 257 · see citing works
The E5 oncoprotein of human papillomavirus type 16 inhibits the acidification of endosomes in human keratinocytes
Straight, S. W., Herman, B. A., & McCance, D. J. (1995) · Journal of Virology · doi:10.1128/jvi.69.5.3185-3192.1995 · Cited by 255 · see citing works
The influence of heregulins on human Schwann cell proliferation
Levi, A., Bunge, R. P., Lofgren, J. A., et al. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-02-01329.1995 · Cited by 251 · see citing works
Inhibition of Drosophila EGF receptor activation by the secreted protein Argos
Schweitzer, R., Howes, R., Smith, R. J., Shilo, B., & Freeman, M. (1995) · Nature · doi:10.1038/376699a0 · Cited by 249 · see citing works
ERBB2 amplification is associated with tamoxifen resistance in steroid-receptor positive breast cancer
Borg, Å., Baldetorp, B., Fernö, M., Killander, D., Olsson, H. L., Rydén, S., & Sigurdsson, H. (1994) · Cancer Letters · doi:10.1016/0304-3835(94)90194-5 · Cited by 246 · see citing works
The Epstein-Barr virus latent membrane protein 1 induces expression of the epidermal growth factor receptor
Miller, W. E., Earp, H. S., & Raab‐Traub, N. (1995) · Journal of Virology · doi:10.1128/jvi.69.7.4390-4398.1995 · Cited by 236 · see citing works
Involvement of p27KIP1 in G1 arrest mediated by an anti-epidermal growth factor receptor monoclonal antibody.
Wu, X., Rubin, M., Fan, Z., DeBlasio, T., Soos, T. J., Koff, A., & Mendelsohn, J. M. (1996) · PubMed · Cited by 228 · see citing works
Efficient coupling with phosphatidylinositol 3-kinase, but not phospholipase C gamma or GTPase-activating protein, distinguishes ErbB-3 signaling from that of other ErbB/EGFR family members.
Fedi, P., Pierce, J. H., Fiore, P. P. D., & Kraus, M. H. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.492 · Cited by 228 · see citing works
Bivalence of EGF‐like ligands drives the ErbB signaling network
Tzahar, E., Pinkas‐Kramarski, R., Moyer, J. D., Klapper, L. N., Alroy, I., Levkowitz, G., Shelly, M., Henis, S., Eisenstein, M., Ratzkin, B. J., et al. (1997) · The EMBO Journal · doi:10.1093/emboj/16.16.4938 · Cited by 228 · see citing works
Self-citation
Neuregulins with an Ig-like domain are essential for mouse myocardial and neuronal development.
Kramer, R., Bucay, N., Kane, D. J., Martin, L. E., Tarpley, J. E., & Theill, L. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4833 · Cited by 227 · see citing works
Changing pattern of expression of the epidermal growth factor receptor and transforming growth factor alpha in the progression of prostatic neoplasms.
Scher, H. I., Sarkis, A. S., Reuter, V., Cohen, D., Netto, G. J., Petrylak, D. P., LIANES, P., FUKS, Z. Y., Mendelsohn, J. M., & Cordon‐Cardo, C. (1995) · PubMed · Cited by 214 · see citing works
Alternative Intracellular Routing of ErbB Receptors May Determine Signaling Potency
Waterman, H., Sabanay, I., Geiger, B., & Yarden, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13819 · Cited by 207 · see citing works
Self-citation
Unarmed, tumor-specific monoclonal antibody effectively treats brain tumors
Sampson, J. H., Alexander, L. E. C., Lee, S., Archer, G. E., Ashley, D. M., Wikstrand, C. J., Hale, L. P., Small, C. G., Dranoff, G., Friedman, A. H., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130166597 · Cited by 188 · see citing works
Heparin Blockade of Thrombin-Induced Smooth Muscle Cell Migration Involves Inhibition of Epidermal Growth Factor (EGF) Receptor Transactivation by Heparin-Binding EGF-Like Growth Factor
Kalmes, A., Vesti, B. R., Daum, G., Abraham, J. A., & Clowes, A. W. (2000) · Circulation Research · doi:10.1161/01.res.87.2.92 · Cited by 182 · see citing works
Multiple functions of let-23, a Caenorhabditis elegans receptor tyrosine kinase gene required for vulval induction.
Aroian, R. V., & Sternberg, P. W. (1991) · Genetics · doi:10.1093/genetics/128.2.251 · Cited by 173 · see citing works
The class III variant of the epidermal growth factor receptor (EGFRvIII): characterization and utilization as an immunotherapeutic target
Wikstrand, C. J., Reist, C. J., Archer, G. E., Zalutsky, M. R., & Bigner, D. D. (1998) · Journal of NeuroVirology · doi:10.3109/13550289809114515 · Cited by 172 · see citing works
HER-2/neu Protein: A Target for Antigen-Specific Immunotherapy of Human Cancer
Disis, M. L., & Cheever, M. A. (1997) · Advances in cancer research · doi:10.1016/s0065-230x(08)60103-7 · Cited by 170 · see citing works
Characterization of a naturally occurring ErbB4 isoform that does not bind or activate phosphatidyl inositol 3-kinase
Elenius, K., Choi, C. J., Paul, S., Santiestevan, E., Nishi, E., & Klagsbrun, M. (1999) · Oncogene · doi:10.1038/sj.onc.1202612 · Cited by 170 · see citing works
A Natural ErbB4 Isoform That Does Not Activate Phosphoinositide 3-Kinase Mediates Proliferation but Not Survival or Chemotaxis
Kainulainen, V., Sundvall, M., Määttä, J. A., Santiestevan, E., Klagsbrun, M., & Elenius, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8641 · Cited by 161 · see citing works
Intracellular expression of single chain antibodies reverts ErbB-2 transformation.
Beerli, R. R., Wels, W. S., & Hynes, N. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51027-4 · Cited by 155 · see citing works
Enhanced expression of cyclooxygenase (COX)-2 in human skin epidermal cancer cells: Evidence for growth suppression by inhibiting COX-2 expression
Higashi, Y., Kanekura, T., & Kanzaki, T. (2000) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(20000601)86:5 · Cited by 155 · see citing works
Extracellular domains drive homo‐ but not hetero‐dimerization of erbB receptors
Ferguson, K. M., Darling, P. J., Mohan, M. J., Macatee, T. L., & Lemmon, M. A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4632 · Cited by 153 · see citing works
Implication of a multisubunit Ets‐related transcription factor in synaptic expression of the nicotinic acetylcholine receptor
Schaeffer, L., Duclert‐Savatier, N., Huchet, M., & Changeux, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.3078 · Cited by 149 · see citing works
p120 Is a Cytosolic Adapter Protein That Associates with Phosphoinositide 3-Kinase in Response to Epidermal Growth Factor in PC12 and Other Cells
Soltoff, S. P., & Cantley, L. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.563 · Cited by 143 · see citing works
THE RECEPTOR FOR EGF AND ITS LIGANDS - EXPRESSION, PROGNOSTIC VALUE AND TARGET FOR THERAPY IN CANCER (REVIEW)
Modjtahedi, H., & Dean, C. (1994) · International Journal of Oncology · doi:10.3892/ijo.4.2.277 · Cited by 138 · see citing works
Singling out Drosophila tendon cells: a dialogue between two distinct cell types
Volk, T. (1999) · Trends in Genetics · doi:10.1016/s0168-9525(99)01862-4 · Cited by 123 · see citing works
NDF/heregulin induces persistence of terminal end buds and adenocarcinomas in the mammary glands of transgenic mice.
Im, K., & Leder, P. (1996) · PubMed · Cited by 121 · see citing works
The carboxyl terminus of epidermal growth factor receptor/erbB-2 chimerae is internalization impaired.
Sorkin, A. D., Fiore, P. P. D., & Carpenter, G. (1993) · PubMed · Cited by 109 · see citing works
Tissue expression of neu differentiation factor/heregulin and its receptor complex in prostate cancer and its biologic effects on prostate cancer cells in vitro.
Lyne, J. C., Melhem, M. F., Finley, G., et al. (1997) · PubMed · Cited by 108 · see citing works
c-erbB-4 protein expression in human breast cancer
Kew, T. Y., Bell, J. A., Pinder, S. E., et al. (2000) · British Journal of Cancer · doi:10.1054/bjoc.1999.1057 · Cited by 105 · see citing works
New Intracellular Targets for Therapeutic Drug Design
Brugge, J. S. (1993) · Science · doi:10.1126/science.8388123 · Cited by 95 · see citing works
Domain-specific gene disruption reveals critical regulation of neuregulin signaling by its cytoplasmic tail
Liu, X., Hwang, H., Cao, L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13024 · Cited by 92 · see citing works
ErbB‐4 Activation Promotes Neurite Outgrowth in PC12 Cells
Vaskovsky, A., Lupowitz, Z., Erlich, S., et al. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0740979.x · Cited by 92 · see citing works
Oncogenes in head and neck cancer
Irish, J. C., & Bernstein, A. (1993) · The Laryngoscope · doi:10.1288/00005537-199301000-00009 · Cited by 89 · see citing works
Expression of EGF, TGF-alpha and EGFR in squamous cell lung carcinomas.
Gorgoulis, V. G., Aninos, D., Mikou, P., Kanavaros, P., Karameris, A., Joardanoglou, J., Rasidakis, A., Veslemes, M., Ozanne, B. W., & Spandidos, D. A. (1992) · PubMed · Cited by 84 · see citing works
The Role of Cultured Schwann Cell Grafts in the Repair of Gaps within the Peripheral Nervous System of Primates
Levi, A. D., Sonntag, V. K. H., Dickman, C. A., et al. (1997) · Experimental Neurology · doi:10.1006/exnr.1996.6344 · Cited by 83 · see citing works
The tumor suppression activity of E1A in HER-2/neu-overexpressing breast cancer
Chang, J. Y., Xia, W., Shao, R., et al. (1997) · Oncogene · doi:10.1038/sj.onc.1200861 · Cited by 82 · see citing works
Triplex formation inhibits HER-2/neu transcription in vitro.
Ebbinghaus, S., Gee, J. E., Rodu, B., et al. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116850 · Cited by 81 · see citing works
Trans-Activation of Epidermal Growth Factor Receptor Gene by the Hepatitis B Virus X-Gene Product
Menzo, S., Clementi, M., Alfani, E., et al. (1993) · Virology · doi:10.1006/viro.1993.1550 · Cited by 71 · see citing works
Kinase-deficient neu proteins suppress epidermal growth factor receptor function and abolish cell transformation.
Qian, X., Dougall, W. C., Hellman, M., et al. (1994) · PubMed · Cited by 69 · see citing works
Localization of Heparin-Binding Epidermal Growth Factor–Like Growth Factor in Human Coronary Arteries
Nakata, A., Miyagawa, J., Yamashita, S., Nishida, M., Tamura, R., Yamamori, K., Nakamura, T., Nozaki, S., Kameda-Takemura, K., Kawata, S., et al. (1996) · Circulation · doi:10.1161/01.cir.94.11.2778 · Cited by 67 · see citing works
Neuregulin-1 and Human Epidermal Growth Factor Receptors 2 and 3 Play a Role in Human Lung Development In Vitro
Patel, N. V., Acarregui, M. J., Snyder, J. M., et al. (2000) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.22.4.3854 · Cited by 67 · see citing works
Computer simulated evolution of a network of cell-signaling molecules
Bray, D., & Lay, S. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80878-1 · Cited by 65 · see citing works
Increased expression of c-erbB-2 in hormone-dependent breast cancer cells inhibits cell growth and induces differentiation
Giani, C., Casalini, P., Pupa, S. M., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1201954 · Cited by 56 · see citing works
Antisense DNA downregulation of the ERBB2 oncogene measured by a flow cytometric assay.
Vaughn, J. P., Iglehart, J. D., Demirdji, S. H., et al. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8338 · Cited by 54 · see citing works
Prognostic significance of ERRB3 overexpression in oral squamous cell carcinoma
Shintani, S., FUNAYAMA, T., Yoshihama, Y., et al. (1995) · Cancer Letters · doi:10.1016/0304-3835(95)03866-u · Cited by 52 · see citing works
Heregulin Reverses the Oligomerization of HER3
Landgraf, R., & Eisenberg, D. S. (2000) · Biochemistry · doi:10.1021/bi000953+ · Cited by 52 · see citing works
Transforming Growth Factor Alpha, Shope Fibroma Growth Factor, and Vaccinia Growth Factor Can Replace Myxoma Growth Factor in the Induction of Myxomatosis in Rabbits
Opgenorth, A., Nation, N., Graham, K., et al. (1993) · Virology · doi:10.1006/viro.1993.1092 · Cited by 44 · see citing works
Molecular requirements for the effect of neuregulin on cell spreading, motility and colony organization
Chausovsky, A., Waterman, H., Elbaum, M., Yarden, Y., Geiger, B., & Bershadsky, A. D. (2000) · Oncogene · doi:10.1038/sj.onc.1203410 · Cited by 42 · see citing works
Self-citation
Structural Aspects of the Epidermal Growth Factor Receptor Required for Transmodulation of erbB-2/neu
Worthylake, R. A., & Wiley, H. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8594 · Cited by 40 · see citing works
Inhibitors of Tyrosine Kinases in the Treatment of Psoriasis
Ben‐Bassat, H., & Klein, B. (2000) · Current Pharmaceutical Design · doi:10.2174/1381612003400182 · Cited by 39 · see citing works
A Phase I Study of Recombinant Adenovirus Vector-Mediated Delivery of an Anti-erbB-2 Single-Chain (sFv) Antibody Gene for Previously Treated Ovarian and Extraovarian Cancer Patients. University of Alabama at Birmingham, Birmingham, Alabama
Alvarez, R. D., & Curiel, D. T. (1997) · Human Gene Therapy · doi:10.1089/hum.1997.8.2-229 · Cited by 29 · see citing works
Ligand-independent dimerization of oncogenic v-erbB products involves covalent interactions
Adelsman, M. A., Huntley, B. K., & Maihle, N. J. (1996) · Journal of Virology · doi:10.1128/jvi.70.4.2533-2544.1996 · Cited by 25 · see citing works
HER2 as a Predictor of Therapeutic Response in Breast Cancer
Paik, S., & Liu, E. T. (2000) · Breast Disease · doi:10.3233/bd-1999-11108 · Cited by 24 · see citing works

Flagged first, then by citations

Sorted by citations

Genes that mediate breast cancer metastasis to lung
Minn, A. J., Gupta, G. P., Siegel, P. M., Bos, P. D., Shu, W., Giri, D. D., Viale, A., Olshen, A. B., Gerald, W. L., & Massagué, J. (2005) · Nature · doi:10.1038/nature03799 · Cited by 2,922 · see citing works
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 · see citing works
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
Zhang, X., Gureasko, J., Shen, K., Cole, P. A., & Kuriyan, J. (2006) · Cell · doi:10.1016/j.cell.2006.05.013 · Cited by 1,650 · see citing works
Epidermal growth factor receptor: Mechanisms of activation and signalling
Jorissen, R. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00098-8 · Cited by 1,565 · see citing works
Combination strategies with PD-1/PD-L1 blockade: current advances and future directions
Yi, M., Zheng, X., Niu, M., Zhu, S., Ge, H., & Wu, K. (2022) · Molecular Cancer · doi:10.1186/s12943-021-01489-2 · Cited by 1,445 · see citing works
Cell-signalling dynamics in time and space
Kholodenko, B. N. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1838 · Cited by 1,347 · see citing works
Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity
Yun, C.-H., Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., & Eck, M. J. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.12.017 · Cited by 1,192 · see citing works
Neuregulin 1 in neural development, synaptic plasticity and schizophrenia
Mei, L., & Xiong, W.-C. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2392 · Cited by 1,030 · see citing works
ERBB Receptors: From Oncogene Discovery to Basic Science to Mechanism-Based Cancer Therapeutics
Arteaga, C. L., & Engelman, J. A. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.02.025 · Cited by 1,048 · see citing works
ErbB receptors and signaling pathways in cancer
Hynes, N. E., & MacDonald, G. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.12.010 · Cited by 956 · see citing works
The Epidermal Growth Factor Receptor Pathway: A Model for Targeted Therapy
Scaltriti, M., & Baselga, J. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-1554 · Cited by 913 · see citing works
Target Binding Properties and Cellular Activity of Afatinib (BIBW 2992), an Irreversible ErbB Family Blocker
Solca, F., Dahl, G., Zoephel, A., Bader, G., Sanderson, M., Klein, C., Kraemer, O., Himmelsbach, F., Haaksma, E., & Adolf, G. R. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.197756 · Cited by 865 · see citing works
Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth
Agus, D. B., Akita, R. W., Fox, W. D., Lewis, G. D., Higgins, B., Pisacane, P. I., Lofgren, J. A., Tindell, C., Evans, D. P., Maiese, K., et al. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00097-1 · Cited by 873 · see citing works
Self-citation
Oncogenic Activation of the RAS/RAF Signaling Pathway Impairs the Response of Metastatic Colorectal Cancers to Anti–Epidermal Growth Factor Receptor Antibody Therapies
Benvenuti, S., Sartore-Bianchi, A., Di Nicolantonio, F., Zanon, C., Moroni, M., Veronese, S., Siena, S., & Bardelli, A. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4158 · Cited by 830 · see citing works
Signaling pathways in cancer-associated fibroblasts and targeted therapy for cancer
Wu, F., Yang, J., Liu, J., Wang, Y., Mu, J., Zeng, Q., Deng, S., & Zhou, H. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00641-0 · Cited by 773 · see citing works
Phosphotyrosine interactome of the ErbB‐receptor kinase family
Schulze, W. X., Deng, L., & Mann, M. (2005) · Molecular Systems Biology · doi:10.1038/msb4100012 · Cited by 753 · see citing works
Understanding resistance to EGFR inhibitors—impact on future treatment strategies
Wheeler, D. L., Dunn, E. F., & Harari, P. M. (2010) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2010.97 · Cited by 683 · see citing works
MEK1 and MEK2 inhibitors and cancer therapy: the long and winding road
Caunt, C. J., Sale, M. J., Smith, P. D., & Cook, S. J. (2015) · Nature Reviews Cancer · doi:10.1038/nrc4000 · Cited by 606 · see citing works
Herceptin acts as an anti-angiogenic cocktail
Izumi, Y., Xu, L., di Tomaso, E., Fukumura, D., & Jain, R. K. (2002) · Nature · doi:10.1038/416279b · Cited by 623 · see citing works
Peptide-Based Vaccines: Current Progress and Future Challenges
Malonis, R. J., Lai, J. R., & Vergnolle, O. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00472 · Cited by 602 · see citing works
Mutations of the epidermal growth factor receptor gene and related genes as determinants of epidermal growth factor receptor tyrosine kinase inhibitors sensitivity in lung cancer
Mitsudomi, T., & Yatabe, Y. (2007) · Cancer Science · doi:10.1111/j.1349-7006.2007.00607.x · Cited by 606 · see citing works
EGFR in Cancer: Signaling Mechanisms, Drugs, and Acquired Resistance
Uribe, M. L., Marrocco, I., & Yarden, Y. (2021) · Cancers · doi:10.3390/cancers13112748 · Cited by 604 · see citing works
Self-citation
Epidermal growth factor receptor targeting in cancer: a review of trends and strategies
Yewale, C., Baradia, D., Vhora, I., Patil, S., & Misra, A. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.07.100 · Cited by 533 · see citing works
Human Breast Cancer Cells Selected for Resistance to Trastuzumab In vivo Overexpress Epidermal Growth Factor Receptor and ErbB Ligands and Remain Dependent on the ErbB Receptor Network
Ritter, C. A., Perez-Torres, M., Rinehart, C., Guix, M., Dugger, T., Engelman, J. A., & Arteaga, C. L. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-0701 · Cited by 497 · see citing works
Epithelial versus Mesenchymal Phenotype Determines In vitro Sensitivity and Predicts Clinical Activity of Erlotinib in Lung Cancer Patients
Yauch, R. L., Januario, T., Eberhard, D. A., Cavet, G., Zhu, W., Fu, L., Pham, T. Q., Soriano, R., Stinson, J., Seshagiri, S., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-1492 · Cited by 495 · see citing works
Biological activities and potential industrial applications of fucose rich sulfated polysaccharides and fucoidans isolated from brown seaweeds: A review
Wijesinghe, W. A. J. P., & Jeon, Y.-J. (2012) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2011.12.029 · Cited by 449 · see citing works
Epidermal growth factor receptor inhibition strategies in oncology
Harari, P. M. (2004) · Endocrine-Related Cancer · doi:10.1677/erc.1.00600 · Cited by 423 · see citing works
Input–output behavior of ErbB signaling pathways as revealed by a mass action model trained against dynamic data
Chen, W. W., Schoeberl, B., Jasper, P. J., Niepel, M., Nielsen, U. B., Lauffenburger, D. A., & Sorger, P. K. (2009) · Molecular Systems Biology · doi:10.1038/msb.2008.74 · Cited by 391 · see citing works
EGF Receptor Signaling Is Essential for K-Ras Oncogene-Driven Pancreatic Ductal Adenocarcinoma
Navas, C., Hernández-Porras, I., Schuhmacher, A. J., Sibilia, M., Guerra, C., & Barbacid, M. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.08.001 · Cited by 391 · see citing works
“These observations are intriguing because the EGFR is known to signal upstream of K-RAS and hence, its inhibition should have little or no effect on downstream K-RAS-driven oncogenic signals (Yarden and Sliwkowski, 2001).”
The Cbl interactome and its functions
Schmidt, M. H. H., & Dikic, I. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1762 · Cited by 395 · see citing works
Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials
Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · see citing works
The Neuregulin-1 Receptor ErbB4 Controls Glutamatergic Synapse Maturation and Plasticity
Li, B., Woo, R.-S., Mei, L., & Malinow, R. (2007) · Neuron · doi:10.1016/j.neuron.2007.03.028 · Cited by 354 · see citing works
Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
Jura, N., Shan, Y., Cao, X., Shaw, D. E., & Kuriyan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912101106 · Cited by 338 · see citing works
Mechanisms of resistance to anti-EGFR therapy in colorectal cancer
Zhao, B., Wang, L., Qiu, H., Zhang, M., Sun, L., Peng, P., Yu, Q., & Yuan, X. (2017) · Oncotarget · doi:10.18632/oncotarget.14012 · Cited by 319 · see citing works
Phenotypic and functional characterisation of the luminal cell hierarchy of the mammary gland
Shehata, M., Teschendorff, A., Sharp, G., Novcic, N., Russell, I. A., Avril, S., Prater, M., Eirew, P., Caldas, C., Watson, C. J., et al. (2012) · Breast Cancer Research · doi:10.1186/bcr3334 · Cited by 306 · see citing works
An oxygen-regulated switch in the protein synthesis machinery
Uniacke, J., Holterman, C. E., Lachance, G., Franovic, A., Jacob, M. D., Fabian, M. R., Payette, J., Holcik, M., Pause, A., & Lee, S. (2012) · Nature · doi:10.1038/nature11055 · Cited by 319 · see citing works
Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms
Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310 · see citing works
The function and clinical application of extracellular vesicles in innate immune regulation
Zhou, X., Xie, F., Wang, L., Zhang, L., Zhang, S., Fang, M., & Zhou, F. (2020) · Cellular & Molecular Immunology · doi:10.1038/s41423-020-0391-1 · Cited by 294 · see citing works
Clinical, histopathologic, and molecular markers of prognosis: toward a new disease risk stratification system for medulloblastoma
Gajjar, A., Hernan, R., Kocak, M., Fuller, C., Lee, Y., McKinnon, P. J., Wallace, D., Lau, C., Chintagumpala, M., Ashley, D. M., et al. (2004) · Journal of Clinical Oncology · doi:10.1200/jco.2004.06.032 · Cited by 279 · see citing works
A computational model on the modulation of mitogen-activated protein kinase (MAPK) and Akt pathways in heregulin-induced ErbB signalling
HATAKEYAMA, M., KIMURA, S., NAKA, T., KAWASAKI, T., YUMOTO, N., ICHIKAWA, M., KIM, J.-H., SAITO, K., SAEKI, M., SHIROUZU, M., et al. (2003) · Biochemical Journal · doi:10.1042/bj20021824 · Cited by 233 · see citing works
Affibody molecules as engineered protein drugs
Frejd, F. Y., & Kim, K.-T. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.35 · Cited by 225 · see citing works
Biosynthesis of tumorigenic HER2 C-terminal fragments by alternative initiation of translation
Anido, J., Scaltriti, M., Bech Serra, J. J., Josefat, B. S., Rojo Todo, F., Baselga, J., & Arribas, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601191 · Cited by 231 · see citing works
Biology of Interactions: Antiepidermal Growth Factor Receptor Agents
Harari, P. M., Allen, G. W., & Bonner, J. A. (2007) · Journal of Clinical Oncology · doi:10.1200/jco.2007.11.8984 · Cited by 214 · see citing works
Pharmacological targeting of the pseudokinase Her3
Xie, T., Lim, S. M., Westover, K. D., Dodge, M. E., Ercan, D., Ficarro, S. B., Udayakumar, D., Gurbani, D., Tae, H. S., Riddle, S. M., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1658 · Cited by 205 · see citing works
Direct delivery of functional proteins and enzymes to the cytosol using nanoparticle-stabilized nanocapsules
Tang, R., Kim, C. S., Solfiell, D. J., Rana, S., Mout, R., Velázquez-Delgado, E. M., Chompoosor, A., Jeong, Y., Yan, B., Zhu, Z.-J., et al. (2013) · ACS Nano · doi:10.1021/nn402753y · Cited by 188 · see citing works
Anti-HER2 scFv-Directed Extracellular Vesicle-Mediated mRNA-Based Gene Delivery Inhibits Growth of HER2-Positive Human Breast Tumor Xenografts by Prodrug Activation
Wang, J.-H., Forterre, A. V., Zhao, J., Frimannsson, D. O., Delcayre, A., Antes, T. J., Efron, B., Jeffrey, S. S., Pegram, M. D., & Matin, A. C. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0827 · Cited by 181 · see citing works
Phase I Dose-Escalation Study of the Pan-HER Inhibitor, PF299804, in Patients with Advanced Malignant Solid Tumors
Jänne, P. A., Boss, D. S., Camidge, D. R., Britten, C. D., Engelman, J. A., Garon, E. B., Guo, F., Wong, S., Liang, J., Letrent, S., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-1220 · Cited by 181 · see citing works
Aptamer to ErbB-2/HER2 enhances degradation of the target and inhibits tumorigenic growth
Mahlknecht, G., Maron, R., Mancini, M., Schechter, B., Sela, M., & Yarden, Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302594110 · Cited by 169 · see citing works
Self-citation
Sloppy models, parameter uncertainty, and the role of experimental design
Apgar, J. F., Witmer, D. K., White, F. M., & Tidor, B. (2010) · Molecular BioSystems · doi:10.1039/b918098b · Cited by 146 · see citing works
Clinical benefit of lapatinib-based therapy in patients with human epidermal growth factor receptor 2-positive breast tumors coexpressing the truncated p95HER2 receptor
Scaltriti, M., Chandarlapaty, S., Prudkin, L., Aura, C., Jimenez, J., Angelini, P. D., Sánchez, G., Guzman, M., Parra, J. L., Ellis, C., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-3407 · Cited by 151 · see citing works
An LGG-derived protein promotes IgA production through upregulation of APRIL expression in intestinal epithelial cells
Wang, Y., Liu, L., Moore, D. J., Shen, X., Peek, R. M., Acra, S. A., Li, H., Ren, X., Polk, D. B., & Yan, F. (2017) · Mucosal Immunology · doi:10.1038/mi.2016.57 · Cited by 149 · see citing works
Phosphoproteomic mass spectrometry profiling links Src family kinases to escape from HER2 tyrosine kinase inhibition
Rexer, B. N., Ham, A.-J. L., Rinehart, C., Hill, S., de Matos Granja-Ingram, N., González-Angulo, A. M., Mills, G. B., Dave, B., Chang, J. C., Liebler, D. C., et al. (2011) · Oncogene · doi:10.1038/onc.2011.130 · Cited by 139 · see citing works
Dasatinib sensitizes KRAS mutant colorectal tumors to cetuximab
Dunn, E. F., Iida, M., Myers, R. A., Campbell, D. A., Hintz, K. A., Armstrong, E. A., Li, C., & Wheeler, D. L. (2011) · Oncogene · doi:10.1038/onc.2010.430 · Cited by 133 · see citing works
Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations
Littlefield, P., Liu, L., Mysore, V., Shan, Y., Shaw, D. E., & Jura, N. (2014) · Science Signaling · doi:10.1126/scisignal.2005786 · Cited by 126 · see citing works
Mechanisms of resistance to anti-epidermal growth factor receptor inhibitors in metastatic colorectal cancer
Sforza, V., Martinelli, E., Ciardiello, F., Gambardella, V., Napolitano, S., Martini, G., della Corte, C., Cardone, C., Ferrara, M. L., Reginelli, A., et al. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i28.6345 · Cited by 123 · see citing works
Isomerization of a Single Aspartyl Residue of Anti-Epidermal Growth Factor Receptor Immunoglobulin γ2 Antibody Highlights the Role Avidity Plays in Antibody Activity
Rehder, D. S., Chelius, D., McAuley, A., Dillon, T. M., Xiao, G., Crouse-Zeineddini, J., Vardanyan, L., Perico, N., Mukku, V., Brems, D. N., et al. (2008) · Biochemistry · doi:10.1021/bi7018223 · Cited by 110 · see citing works
Differential Content of Proteins, mRNAs, and miRNAs Suggests that MDSC and Their Exosomes May Mediate Distinct Immune Suppressive Functions
Geis-Asteggiante, L., Belew, A. T., Clements, V. K., Edwards, N. J., Ostrand-Rosenberg, S., El-Sayed, N. M., & Fenselau, C. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00646 · Cited by 104 · see citing works
Chemotherapy-induced activation of ADAM-17: a novel mechanism of drug resistance in colorectal cancer
Kyula, J. N., Van Schaeybroeck, S., Doherty, J., Fenning, C. S., Longley, D. B., & Johnston, P. G. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0014 · Cited by 99 · see citing works
H1047R phosphatidylinositol 3-kinase mutant enhances HER2-mediated transformation by heregulin production and activation of HER3
Chakrabarty, A., Rexer, B. N., Wang, S. E., Cook, R. S., Engelman, J. A., & Arteaga, C. L. (2010) · Oncogene · doi:10.1038/onc.2010.257 · Cited by 102 · see citing works
Aryl Hydrocarbon Receptor Is an Ozone Sensor in Human Skin
Afaq, F., Zaid, M. A., Pelle, E., Khan, N., Syed, D. N., Matsui, M. S., Maes, D., & Mukhtar, H. (2009) · Journal of Investigative Dermatology · doi:10.1038/jid.2009.85 · Cited by 99 · see citing works
Concerted Activation of ETS Protein ER81 by p160 Coactivators, the Acetyltransferase p300 and the Receptor Tyrosine Kinase HER2/Neu
Goel, A., & Janknecht, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400036200 · Cited by 95 · see citing works
MEK1/2 Inhibitors AS703026 and AZD6244 May Be Potential Therapies for KRAS Mutated Colorectal Cancer That Is Resistant to EGFR Monoclonal Antibody Therapy
Yoon, J., Koo, K.-H., & Choi, K.-Y. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3058 · Cited by 92 · see citing works
Induction of immunogenic apoptosis by blockade of epidermal growth factor receptor activation with a specific antibody
Garrido, G., Rabasa, A., Sánchez, B., López, M. V., Blanco, R., López, A., Hernández, D. R., Pérez, R., & Fernández, L. E. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003477 · Cited by 91 · see citing works
Current targeted therapies in the treatment of advanced colorectal cancer: a review
Moriarity, A., O’Sullivan, J., Kennedy, J., Mehigan, B., & McCormick, P. (2016) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758834016646734 · Cited by 87 · see citing works
Primary and acquired resistance to EGFR-targeted therapies in colorectal cancer: impact on future treatment strategies
Leto, S. M., & Trusolino, L. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1161-2 · Cited by 87 · see citing works
Stimulus Design for Model Selection and Validation in Cell Signaling
Apgar, J. F., Toettcher, J. E., Endy, D., White, F. M., & Tidor, B. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0040030 · Cited by 79 · see citing works
Modulation of HER2 expression by ferulic acid on human breast cancer MCF7 cells
Chang, C. J., Chiu, J. H., Tseng, L. M., Chang, C. H., Chien, T. M., Wu, C. W., & Lui, W. Y. (2006) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2006.01676.x · Cited by 80 · see citing works
Targeting CLDN18.2 in cancers of the gastrointestinal tract: new drugs and new indications
Chen, J., Xu, Z., Hu, C., Zhang, S., Zi, M., Yuan, L., & Cheng, X. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1132319 · Cited by 78 · see citing works
NSCLC and HER2: between lights and shadows
Ricciardi, G. R. R., Russo, A., Franchina, T., Ferraro, G., Zanghì, M., Picone, A., Scimone, A., & Adamo, V. (2014) · Journal of Thoracic Oncology · doi:10.1097/jto.0000000000000379 · Cited by 78 · see citing works
Inhibitory effects of fucoidan on activation of epidermal growth factor receptor and cell transformation in JB6 Cl41 cells
Lee, N. Y., Ermakova, S. P., Zvyagintseva, T. N., Kang, K. W., Dong, Z., & Choi, H. S. (2008) · Food and Chemical Toxicology · doi:10.1016/j.fct.2008.01.025 · Cited by 75 · see citing works
The Yin and Yang of ERBB4: Tumor Suppressor and Oncoprotein
Lucas, L. M., Dwivedi, V., Senfeld, J. I., Cullum, R. L., Mill, C. P., Piazza, J. T., Bryant, I. N., Cook, L. J., Miller, S. T., Lott, J. H., et al. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000381 · Cited by 70 · see citing works
Inhibition of zebrafish epidermal growth factor receptor activity results in cardiovascular defects
Goishi, K., Lee, P., Davidson, A. J., Nishi, E., Zon, L. I., & Klagsbrun, M. (2003) · Mechanisms of Development · doi:10.1016/s0925-4773(03)00068-6 · Cited by 70 · see citing works
HER3 Is an Actionable Target in Advanced Prostate Cancer
Gil, V., Miranda, S., Riisnaes, R., Gurel, B., D’Ambrosio, M., Vasciaveo, A., Crespo, M., Ferreira, A., Brina, D., Troiani, M., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-3360 · Cited by 68 · see citing works
HER-2/neu gene copy number quantified by real-time PCR: comparison of gene amplification, heterozygosity, and immunohistochemical status in breast cancer tissue
Königshoff, M., Wilhelm, J., Bohle, R. M., Pingoud, A., & Hahn, M. (2003) · Clinical Chemistry · doi:10.1373/49.2.219 · Cited by 63 · see citing works
Extracellular Vesicle–Mediated In Vitro Transcribed mRNA Delivery for Treatment of HER2+ Breast Cancer Xenografts in Mice by Prodrug CB1954 without General Toxicity
Forterre, A. V., Wang, J.-H., Delcayre, A., Kim, K., Green, C., Pegram, M. D., Jeffrey, S. S., & Matin, A. C. (2020) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0928 · Cited by 62 · see citing works
Down-regulation of programmed cell death 4 (PDCD4) is associated with aromatase inhibitor resistance and a poor prognosis in estrogen receptor-positive breast cancer
Chen, Z., Yuan, Y.-C., Wang, Y., Liu, Z., Chan, H. J., & Chen, S. (2015) · Breast Cancer Research and Treatment · doi:10.1007/s10549-015-3446-8 · Cited by 59 · see citing works
The intestinal epithelium compensates for p53-mediated cell death and guarantees organismal survival
Valentin-Vega, Y. A., Okano, H., & Lozano, G. (2008) · Cell Death & Differentiation · doi:10.1038/cdd.2008.109 · Cited by 58 · see citing works
Metalloproteinase-mediated, context-dependent function of amphiregulin and HB-EGF in human keratinocytes and skin
Stoll, S. W., Johnson, J. L., Bhasin, A., Johnston, A., Gudjonsson, J. E., Rittié, L., & Elder, J. T. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2009.211 · Cited by 50 · see citing works
Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence
Duran-Frigola, M., Cigler, M., & Winter, G. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c11098 · Cited by 50 · see citing works
Molecular pathways: sensitivity and resistance to anti-EGFR antibodies
Bertotti, A., & Sassi, F. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-0848 · Cited by 45 · see citing works
NRF2 inhibition represses ErbB2 signaling in ovarian carcinoma cells: Implications for tumor growth retardation and docetaxel sensitivity
Manandhar, S., Choi, B.-H., Jung, K.-A., Ryoo, I.-G., Song, M., Kang, S. J., Choi, H.-G., Kim, J.-A., Park, P.-H., & Kwak, M.-K. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.031 · Cited by 45 · see citing works
EGFR-targeted therapy results in dramatic early lung tumor regression accompanied by imaging response and immune infiltration in EGFR mutant transgenic mouse models
Venugopalan, A., Lee, M.-J., Niu, G., Medina-Echeverz, J., Tomita, Y., Lizak, M. J., Cultraro, C. M., Simpson, R. M., Chen, X., Trepel, J. B., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.11021 · Cited by 40 · see citing works
Fucoidan from Laminaria cichorioides inhibits AP‐1 transactivation and cell transformation in the mouse epidermal JB6 cells
Lee, N. Y., Ermakova, S. P., Choi, H., Kusaykin, M. I., Shevchenko, N. M., Zvyagintseva, T. N., & Choi, H. S. (2008) · Molecular Carcinogenesis · doi:10.1002/mc.20428 · Cited by 40 · see citing works
A phase I study of AST1306, a novel irreversible EGFR and HER2 kinase inhibitor, in patients with advanced solid tumors
Zhang, J., Cao, J., Li, J., Zhang, Y., Chen, Z., Peng, W., Sun, S., Zhao, N., Wang, J., Zhong, D., et al. (2014) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-7-22 · Cited by 40 · see citing works
Contrasting effects of the cytotoxic anticancer drug gemcitabine and the EGFR tyrosine kinase inhibitor gefitinib on NK cell-mediated cytotoxicity via regulation of NKG2D ligand in non-small-cell lung cancer cells
Okita, R., Wolf, D., Yasuda, K., Maeda, A., Yukawa, T., Saisho, S., Shimizu, K., Yamaguchi, Y., Oka, M., Nakayama, E., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139809 · Cited by 39 · see citing works
Degradation of HER2 by Cbl-Based Chimeric Ubiquitin Ligases
Li, X., Shen, L., Zhang, J., Su, J., Shen, L., Liu, X., Han, H., Han, W., & Yao, L. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3731 · Cited by 37 · see citing works
Inhibition of ErbB kinase signalling promotes resolution of neutrophilic inflammation
Rahman, A., Henry, K. M., Herman, K. D., Thompson, A. A., Isles, H. M., Tulotta, C., Sammut, D., Rougeot, J. J., Khoshaein, N., Reese, A. E., et al. (2019) · eLife · doi:10.7554/elife.50990 · Cited by 38 · see citing works
Fibroblast growth factor receptor 4 increases epidermal growth factor receptor (EGFR) signaling by inducing amphiregulin expression and attenuates response to EGFR inhibitors in colon cancer
Hong, C., Sun, E., Choi, J., Kim, D., Kim, J., Ryu, K., Shim, H., Hwang, J., Bae, W., Kim, H., et al. (2020) · Cancer Science · doi:10.1111/cas.14526 · Cited by 35 · see citing works
The novel long noncoding RNA CRART16 confers cetuximab resistance in colorectal cancer cells by enhancing ERBB3 expression via miR-371a-5p
Zhang, X., Wen, L., Chen, S., Zhang, J., Ma, Y., Hu, J., Yue, T., Wang, J., Zhu, J., Bu, D., et al. (2020) · Cancer Cell International · doi:10.1186/s12935-020-1155-9 · Cited by 35 · see citing works
The EGFR inhibitor gefitinib suppresses recruitment of pericytes and bone marrow-derived perivascular cells into tumor vessels
Iivanainen, E., Lauttia, S., Zhang, N., Tvorogov, D., Kulmala, J., Grenman, R., Salven, P., & Elenius, K. (2009) · Microvascular Research · doi:10.1016/j.mvr.2009.06.010 · Cited by 34 · see citing works
Revealing the Potency of Growth Factors in Bovine Colostrum
Yalçıntaş, Y. M., Duman, H., López, J. M. M., Portocarrero, A. C. M., Lombardo, M., Khallouki, F., Koch, W., Bordiga, M., El-Seedi, H., Raposo, A., et al. (2024) · Nutrients · doi:10.3390/nu16142359 · Cited by 31 · see citing works
Exome Sequencing Identified NRG3 as a Novel Susceptible Gene of Hirschsprung’s Disease in a Chinese Population
Yang, J., Duan, S., Zhong, R., Yin, J., Pu, J., Ke, J., Lu, X., Zou, L., Zhang, H., Zhu, Z., et al. (2013) · Molecular Neurobiology · doi:10.1007/s12035-012-8392-4 · Cited by 31 · see citing works
Lung injury in axolotl salamanders induces an organ‐wide proliferation response
Jensen, T. B., Giunta, P., Schultz, N. G., Griffiths, J. M., Duerr, T. J., Kyeremateng, Y., Wong, H., Adesina, A., & Monaghan, J. R. (2021) · Developmental Dynamics · doi:10.1002/dvdy.315 · Cited by 25 · see citing works
The pan-ErbB receptor tyrosine kinase inhibitor canertinib promotes apoptosis of malignant melanoma in vitro and displays anti-tumor activity in vivo
Djerf Severinsson, E. A., Trinks, C., Gréen, H., Abdiu, A., Hallbeck, A.-L., Stål, O., & Walz, T. M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.09.118 · Cited by 24 · see citing works
Panitumumab interaction with<scp>TAS</scp>‐102 leads to combinational anticancer effects via blocking of<scp>EGFR</scp>‐mediated tumor response to trifluridine
Baba, Y., Tamura, T., Satoh, Y., Gotou, M., Sawada, H., Ebara, S., Shibuya, K., Soeda, J., & Nakamura, K. (2017) · Molecular Oncology · doi:10.1002/1878-0261.12074 · Cited by 23 · see citing works
Dynamic Protein Allosteric Regulation and Disease
Nussinov, R., Tsai, C.-J., & Jang, H. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-13-8719-7_2 · Cited by 18 · see citing works
Unleashing the power of anti-HER2 therapies in metastatic colorectal cancer: paving the way for a brighter future
Babkoff, A., Zick, A., Hubert, A., Tarantino, P., & Grinshpun, A. (2024) · ESMO Gastrointestinal Oncology · doi:10.1016/j.esmogo.2023.100032 · Cited by 14 · see citing works

Referentialism and the Objects of Credence: A Reply to Braun
Chalmers, D. J. (2016) · Mind · doi:10.1093/mind/fzv111 · Cited by 3 · see citing works
Is there any cumulative dose for trastuzumab?
Mutlu, H., & Çoşkun, H. Ş. (2014) · Journal of Oncology Pharmacy Practice · doi:10.1177/1078155214538686 · Cited by 3 · see citing works
Mechanisms of Trastuzumab Resistance and Their Clinical Implications
Lan, K., Lu, C., & Yu, D. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1339.026 · Cited by 75 · see citing works
Cardiac toxicity of trastuzumab in elderly patients with breast cancer
Andrea, A., Denegri, Tiziano, et al. (2016) · 老年心脏病学杂志：英文版
Cytotoxic Effects of Seleno-Trastuzumab, Trastuzumab (Herceptin) and T-DM-1 (Kadcyla) on Trastuzumab Resistant JIMT-1 Breast Cancer Cells
Bapat, P., Boylan, M., Cobos, E., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.213

Authors: Yarden, Y., & Sliwkowski, M. X.
Affiliations: Weizmann Institute of Science (IL)
Genentech (US)
ORCID: Sliwkowski, Mark X.
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2001-02
Volume: 2
Issue: 2
Pages: 127-137
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/35052073
OpenAlex: W1964321121
Cited by: 6,974
References: 111
Citations by year: 2026: 203 · 2025: 185 · 2024: 212 · 2023: 261 · 2022: 257 · 2021: 260 · 2020: 230 · 2019: 215 · 2018: 258 · 2017: 259 · 2016: 279 · 2015: 319 · 2014: 322 · 2013: 418 · 2012: 377
FWCI: 18.85
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Lung Cancer Treatments and Mutations
Keywords: ErbB receptors, epidermal growth factor, receptor tyrosine kinase signaling, signaling networks, breast cancer, trastuzumab, ERBB2, EGF receptor, monoclonal antibodies, small-molecule kinase inhibitors
MeSH terms: Animals, Neoplasms, Signal Transduction, Erb-b2 Receptor Tyrosine Kinases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Untangling the ErbB signalling network

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks