Therapeutic targeting of TEAD transcription factors in cancer

Oncogenic Signaling Pathways in The Cancer Genome Atlas

Sanchez-Vega, F., Mina, M., Armenia, J., Chatila, W. K., Luna, A., La, K. C., Dimitriadoy, S., Liu, D. L., Kantheti, H. S., Saghafinia, S., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.035 · Cited by 3,201

TEAD mediates YAP-dependent gene induction and growth control

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YAP/TAZ at the Roots of Cancer

Zanconato, F., Cordenonsi, M., & Piccolo, S. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.05.005 · Cited by 1,970

The Hippo pathway and human cancer

Harvey, K. F., Zhang, X., & Thomas, D. M. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3458 · Cited by 1,867

Regulation of the Hippo-YAP Pathway by G-Protein-Coupled Receptor Signaling

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Genetic and pharmacological disruption of the TEAD–YAP complex suppresses the oncogenic activity of YAP

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The Hippo Pathway: Biology and Pathophysiology

Ma, S., Meng, Z., Chen, R., & Guan, K.-L. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111829 · Cited by 1,387

Genome-wide association between YAP/TAZ/TEAD and AP-1 at enhancers drives oncogenic growth

Zanconato, F., Forcato, M., Battilana, G., Azzolin, L., Quaranta, E., Bodega, B., Rosato, A., Bicciato, S., Cordenonsi, M., & Piccolo, S. (2015) · Nature Cell Biology · doi:10.1038/ncb3216 · Cited by 1,219

YAP/TAZ upstream signals and downstream responses

Totaro, A., Panciera, T., & Piccolo, S. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0142-z · Cited by 1,086

Hippo–YAP/TAZ signalling in organ regeneration and regenerative medicine

Moya, I. M., & Halder, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0086-y · Cited by 981

Comprehensive genomic analysis of malignant pleural mesothelioma identifies recurrent mutations, gene fusions and splicing alterations

Bueno, R., Stawiski, E. W., Goldstein, L. D., Durinck, S., Rienzo, A. D., Modrusan, Z. D., Gnad, F., Nguyen, T. T., Jaiswal, B. S., Chirieac, L. R., et al. (2016) · Nature Genetics · doi:10.1038/ng.3520 · Cited by 937

The Hippo Signaling Pathway in Development and Disease

Zheng, Y., & Pan, D. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.06.003 · Cited by 867

Targeting the Hippo pathway in cancer, fibrosis, wound healing and regenerative medicine

Dey, A., Varelas, X., & Guan, K.-L. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0070-z · Cited by 860

TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm

Vassilev, A., Kaneko, K. J., Shu, H., Zhao, Y., & DePamphilis, M. L. (2001) · Genes & Development · doi:10.1101/gad.888601 · Cited by 719

E-cadherin mediates contact inhibition of proliferation through Hippo signaling-pathway components

Kim, N.-G., Koh, E., Chen, X., & Gumbiner, B. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103345108 · Cited by 698

The TEAD/TEF Family Protein Scalloped Mediates Transcriptional Output of the Hippo Growth-Regulatory Pathway

Wu, S., Liu, Y., Zheng, Y., Dong, J., & Pan, D. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.01.007 · Cited by 640

Hippo-Independent Activation of YAP by the GNAQ Uveal Melanoma Oncogene through a Trio-Regulated Rho GTPase Signaling Circuitry

Feng, X., Degese, M. S., Iglesias‐Bartolomé, R., Vaque, J. P., Molinolo, A., Rodrigues, M. W., Zaidi, M. R., Ksander, B. R., Merlino, G. T., Sodhi, A., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.016 · Cited by 577

The Hippo effector YAP promotes resistance to RAF- and MEK-targeted cancer therapies

Lin, L., Sabnis, A. J., Chan, E., Olivas, V., Cade, L., Pazarentzos, E., Asthana, S., Neel, D., Yan, J. J., Lu, X., et al. (2015) · Nature Genetics · doi:10.1038/ng.3218 · Cited by 551

Comprehensive Molecular Characterization of the Hippo Signaling Pathway in Cancer

Wang, Y., Xu, X., Maglic, D., Dill, M. T., Mojumdar, K., Ng, P. K.-S., Jeong, K. J., Tsang, Y. H., Moreno, D., Bhavana, V. H., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.10.001 · Cited by 500

Mutant Gq/11 Promote Uveal Melanoma Tumorigenesis by Activating YAP

Yu, F., Luo, J., Mo, J., Liu, G., Kim, Y. C., Meng, Z., Zhao, L., Peyman, G. A., Ouyang, H., Jiang, W., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.017 · Cited by 478

Treatment-Induced Tumor Dormancy through YAP-Mediated Transcriptional Reprogramming of the Apoptotic Pathway

Kurppa, K. J., Liu, Y., To, C., Zhang, T., Fan, M., Vajdi, A., Knelson, E. H., Xie, Y., Lim, K., Cejas, P., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2019.12.006 · Cited by 475

Role of Merlin/NF2 inactivation in tumor biology

Petrilli, A. M., & Fernández‐Valle, C. (2015) · Oncogene · doi:10.1038/onc.2015.125 · Cited by 469

SCALLOPED Interacts with YORKIE, the Nuclear Effector of the Hippo Tumor-Suppressor Pathway in Drosophila

Goulev, Y., Fauny, J., Gonzalez-Marti, B., Flagiello, D., Silber, J., & Zider, A. (2008) · Current Biology · doi:10.1016/j.cub.2008.02.034 · Cited by 456

YAP/TAZ Signaling and Resistance to Cancer Therapy

Nguyen, C. D. K., & Yi, C. (2019) · Trends in Cancer · doi:10.1016/j.trecan.2019.02.010 · Cited by 437

Hippo Pathway in Cancer: Aberrant Regulation and Therapeutic Opportunities

Calses, P. C., Crawford, J. J., Lill, J. R., & Dey, A. (2019) · Trends in cancer · doi:10.1016/j.trecan.2019.04.001 · Cited by 433

Structural insights into the YAP and TEAD complexPreprint

Li, Z., Zhao, B., Wang, P., Chen, F., Dong, Z., Yang, H., Guan, K., & Xu, Y. (2010) · Genes & Development · doi:10.1101/gad.1865810 · Cited by 415

Identification of a Disease-Defining Gene Fusion in Epithelioid Hemangioendothelioma

Tanas, M. R., Sboner, A., Oliveira, A. M., Erickson‐Johnson, M. R., Hespelt, J., Hanwright, P. J., Flanagan, J., Luo, Y., Fenwick, K., Natrajan, R., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002409 · Cited by 405

The Hippo pathway in cancer: YAP/TAZ and TEAD as therapeutic targets in cancer

Cunningham, R., & Hansen, C. G. (2022) · Clinical Science · doi:10.1042/cs20201474 · Cited by 355

Transcriptional enhancer factor 1 disruption by a retroviral gene trap leads to heart defects and embryonic lethality in mice.Preprint

Chen, Z., Friedrich, G., & Soriano, P. M. (1994) · Genes & Development · doi:10.1101/gad.8.19.2293 · Cited by 336

Rescue of Hippo coactivator YAP1 triggers DNA damage–induced apoptosis in hematological cancers

Cottini, F., Hideshima, T., Xu, C., Sattler, M., Dori, M., Agnelli, L., ten Hacken, E., Bertilaccio, M. T. S., Antonini, E., Neri, A., et al. (2014) · Nature Medicine · doi:10.1038/nm.3562 · Cited by 318

Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway

Chan, P., Han, X., Zheng, B., DeRan, M., Yu, J., Jarugumilli, G. K., Deng, H., Pan, D., Luo, X., & Wu, X. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2036 · Cited by 313

Emerging roles of TEAD transcription factors and its coactivators in cancers

Pobbati, A. V., & Hong, W. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.23788 · Cited by 271

Actin remodeling confers BRAF inhibitor resistance to melanoma cells through YAP/TAZ activation

Kim, M. H., Kim, J., Hong, H., Lee, J. J.-K., Lee, J., Jung, E., & Kim, J. (2015) · The EMBO Journal · doi:10.15252/embj.201592081 · Cited by 270

YAP/TAZ: Drivers of Tumor Growth, Metastasis, and Resistance to Therapy

Thompson, B. J. (2020) · BioEssays · doi:10.1002/bies.201900162 · Cited by 261

Regulation of TEAD Transcription Factors in Cancer Biology

Huh, H., Kim, D., Jeong, H.-S., & Park, H. (2019) · Cells · doi:10.3390/cells8060600 · Cited by 259

Structural basis of YAP recognition by TEAD4 in the Hippo pathwayPreprint

Chen, L., Chan, S. W., Zhang, X., Walsh, M. A., Lim, C. J., Hong, W., & Song, H. (2010) · Genes & Development · doi:10.1101/gad.1865310 · Cited by 256

A combat with the YAP/TAZ-TEAD oncoproteins for cancer therapy

Pobbati, A. V., & Hong, W. (2020) · Theranostics · doi:10.7150/thno.40889 · Cited by 230

Targeting the Central Pocket in Human Transcription Factor TEAD as a Potential Cancer Therapeutic Strategy

Pobbati, A. V., Han, X. Y., Hung, A. W., Seetoh, W.-G., Huda, N., Chen, G.-Y., Kang, C., Chia, C. S. B., Luo, X., Hong, W., et al. (2015) · Structure · doi:10.1016/j.str.2015.09.009 · Cited by 219

Regulation of Hippo pathway transcription factor TEAD by p38 MAPK-induced cytoplasmic translocation

Lin, K. C., Moroishi, T., Meng, Z., Jeong, H.-S., Plouffe, S. W., Sekido, Y., Han, J., Park, H. W., & Guan, K. (2017) · Nature Cell Biology · doi:10.1038/ncb3581 · Cited by 206

Tumor-selective proteotoxicity of verteporfin inhibits colon cancer progression independently of YAP1

Zhang, H., Ramakrishnan, S. K., Triner, D., Centofanti, B., Maitra, D., Győrffy, B., Sebolt-Leopold, J. S., Dame, M. K., Varani, J., Brenner, D. E., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aac5418 · Cited by 196

Binary pan-cancer classes with distinct vulnerabilities defined by pro- or anti-cancer YAP/TEAD activity

Pearson, J. D., Huang, K., Pacal, M., McCurdy, S. R., Lü, S., Aubry, A., Yu, T., Wadosky, K. M., Zhang, L., Wang, T., et al. (2021) · Cancer Cell · doi:10.1016/j.ccell.2021.06.016 · Cited by 178

Structural and Functional Similarity between the Vgll1-TEAD and the YAP-TEAD Complexes

Pobbati, A. V., Chan, S. W., Lee, I., Song, H., & Hong, W. (2012) · Structure · doi:10.1016/j.str.2012.04.004 · Cited by 177

VGLL4 targets a TCF4–TEAD4 complex to coregulate Wnt and Hippo signalling in colorectal cancer

Jiao, S., Li, C., Qian, H., Miao, H., Zhang, L., Li, L., & Zhou, Z. (2017) · Nature Communications · doi:10.1038/ncomms14058 · Cited by 161

Crumbs3-Mediated Polarity Directs Airway Epithelial Cell Fate through the Hippo Pathway Effector Yap

Szymaniak, A. D., Mahoney, J. E., Cardoso, W. V., & Varelas, X. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.06.020 · Cited by 157

YAP1 and its fusion proteins in cancer initiation, progression and therapeutic resistance

Szulzewsky, F., Holland, E. C., & Vasioukhin, V. I. (2021) · Developmental Biology · doi:10.1016/j.ydbio.2020.12.018 · Cited by 155

Transcriptional repression of estrogen receptor alpha by YAP reveals the Hippo pathway as therapeutic target for ER+ breast cancer

Ma, S., Tang, T. T.-L., Probst, G. D., Konradi, A. W., Jin, C., Li, F., Gutkind, J. S., Fu, X., & Guan, K. (2022) · Nature Communications · doi:10.1038/s41467-022-28691-0 · Cited by 154

TEAD4 ensures postimplantation development by promoting trophoblast self-renewal: An implication in early human pregnancy loss

Saha, B., Ganguly, A., Home, P., Bhattacharya, B., Ray, S. S., Ghosh, A., Rumi, M. A. K., Marsh, C. A., French, V. A., Gunewardena, S., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002449117 · Cited by 154

Pharmacological blockade of TEAD–YAP reveals its therapeutic limitation in cancer cells

Sun, Y., Hu, L., Tao, Z., Jarugumilli, G. K., Erb, H., Singh, A., Li, Q., Cotton, J. L., Greninger, P., Egan, R. K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34559-0 · Cited by 145

Epiblast Formation by TEAD-YAP-Dependent Expression of Pluripotency Factors and Competitive Elimination of Unspecified Cells

Hashimoto, M., & Sasaki, H. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.05.024 · Cited by 140

The novel potent TEAD inhibitor, K-975, inhibits YAP1/TAZ-TEAD protein-protein interactions and exerts an anti-tumor effect on malignant pleural mesothelioma.

Kaneda, A., Seike, T., Danjo, T., Nakajima, T., Otsubo, N., Yamaguchi, D., Tsuji, Y., Hamaguchi, K., Yasunaga, M., Nishiya, Y., et al. (2020) · PubMed Central · Cited by 139

Targeting intrinsically disordered proteins at the edge of chaos

Ruan, H., Sun, Q., Zhang, W., Liu, Y., & Lai, L. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2018.09.017 · Cited by 133

One cell‐specific and three ubiquitous nuclear proteins bind in vitro to overlapping motifs in the domain B1 of the SV40 enhancer.

Xiao, J. H., Davidson, I., Ferrandon, D., Rosales, R., Vigneron, M., Macchi, M., Ruffenach, F., & Chambon, P. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02606.x · Cited by 122

TEAD family transcription factors in development and disease

Currey, L., Thor, S., & Piper, M. (2021) · Development · doi:10.1242/dev.196675 · Cited by 120

Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex

Kaan, H. Y. K., Chan, S. W., Tan, S. K. J., Guo, F., Lim, C. J., Hong, W., & Song, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-02219-9 · Cited by 118

Mechanism of action of a WWTR1(TAZ)-CAMTA1 fusion oncoprotein

Tanas, M. R., Ma, S., Jadaan, F. O., Ng, C. K. Y., Weigelt, B., Reis-Filho, J. S., & Rubin, B. P. (2015) · Oncogene · doi:10.1038/onc.2015.148 · Cited by 113

MCAT Elements and the TEF-1 Family of Transcription Factors in Muscle Development and Disease

Yoshida, T. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.155788 · Cited by 109

Verteporfin exhibits YAP-independent anti-proliferative and cytotoxic effects in endometrial cancer cells

Dasari, V. R., Mazack, V., Feng, W., Nash, J. D., Carey, D. J., & Gogoi, R. P. (2017) · Oncotarget · doi:10.18632/oncotarget.15614 · Cited by 108

Focal adhesion kinase-YAP signaling axis drives drug-tolerant persister cells and residual disease in lung cancer

Haderk, F., Chou, Y., Čech, L., Fernández-Méndez, C., Yu, J. X., Olivas, V. R., Meraz, I. M., Rabago, D. B., Kerr, D. L., Gómez, C. F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47423-0 · Cited by 108

Glucocorticoid Receptor Signaling Activates TEAD4 to Promote Breast Cancer Progression

He, L., Yuan, L., Sun, Y., Wang, P., Zhang, H., Feng, X., Wang, Z., Zhang, W., Yang, C., Zeng, Y. A., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0012 · Cited by 107

YAP induces an oncogenic transcriptional program through TET1-mediated epigenetic remodeling in liver growth and tumorigenesis

Wu, B.-K., Mei, S.-C., Chen, E. H., Zheng, Y., & Pan, D. (2022) · Nature Genetics · doi:10.1038/s41588-022-01119-7 · Cited by 91

Discovery of drugs that directly target the intrinsically disordered region of the androgen receptor

Sadar, M. D. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1732920 · Cited by 83

Comparison of tumor-associated YAP1 fusions identifies a recurrent set of functions critical for oncogenesisPreprint

Szulzewsky, F., Arora, S., Hoellerbauer, P., King, C., Nathan, E., Chan, M., Cimino, P. J., Ozawa, T., Kawauchi, D., Pajtler, K. W., et al. (2020) · Genes & Development · doi:10.1101/gad.338681.120 · Cited by 82

The Hippo Pathway as a Driver of Select Human Cancers

Kulkarni, A., Chang, M. T., Vissers, J. H. A., Dey, A., & Harvey, K. F. (2020) · Trends in cancer · doi:10.1016/j.trecan.2020.04.004 · Cited by 77

YAP inhibits ERα and ER+ breast cancer growth by disrupting a TEAD-ERα signaling axis

Li, X., Zhuo, S., Zhuang, T., Cho, Y. S., Wu, G., Liu, Y., Mu, K., Zhang, K., Su, P., Yang, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30831-5 · Cited by 77

Mammalian display screening of diverse cystine-dense peptides for difficult to drug targets

Crook, Z. R., Sevilla, G. P., Friend, D. J., Brusniak, M., Bandaranayake, A. D., Clarke, M., Gewe, M. M., Mhyre, A. J., Baker, D. A., Strong, R. K., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02098-8 · Cited by 77

Yes‐associated protein/TEA domain family member and hepatocyte nuclear factor 4‐alpha (HNF4α) repress reciprocally to regulate hepatocarcinogenesis in rats and mice

Cai, W., Lin, L., Hao, H., Zhang, S., Ma, F., Hong, X., Zhang, H., Liu, Q., Ye, G., Sun, G., et al. (2016) · Hepatology · doi:10.1002/hep.28911 · Cited by 76

Update on biology and management of mesothelioma

Asciak, R., George, V., & Rahman, N. M. (2021) · European Respiratory Review · doi:10.1183/16000617.0226-2020 · Cited by 75

Recent Therapeutic Approaches to Modulate the Hippo Pathway in Oncology and Regenerative Medicine

Barry, E., Simov, V., Valtingojer, I., & Venier, O. (2021) · Cells · doi:10.3390/cells10102715 · Cited by 73

Effect of the acylation of TEAD4 on its interaction with co‐activators YAP and TAZ

Mesrouze, Y., Meyerhofer, M., Bokhovchuk, F. M., Fontana, P., Zimmermann, C., Martin, T., Delaunay, C., Izaac, A., Kallen, J. A., Schmelzle, T., et al. (2017) · Protein Science · doi:10.1002/pro.3312 · Cited by 71

Covalent disruptor of YAP-TEAD association suppresses defective Hippo signaling

Fan, M., Lu, W., Che, J., Kwiatkowski, N. P., Gao, Y., Seo, H.-S., Ficarro, S. B., Gokhale, P. C., Liu, Y., Geffken, E. A., et al. (2022) · eLife · doi:10.7554/elife.78810 · Cited by 68

WWTR1(TAZ)-CAMTA1 gene fusion is sufficient to dysregulate YAP/TAZ signaling and drive epithelioid hemangioendothelioma tumorigenesisPreprint

Seavey, C. N., Pobbati, A. V., Hallett, A., Ma, S., REYNOLDS, J. P., Kanai, R., Lamar, J. M., & Rubin, B. P. (2021) · Genes & Development · doi:10.1101/gad.348220.120 · Cited by 68

YAP1 Mediates Resistance to MEK1/2 Inhibition in Neuroblastomas with Hyperactivated RAS Signaling

Coggins, G. E., Farrel, A., Rathi, K. S., Hayes, C. M., Scolaro, L., Rokita, J. L., & Maris, J. M. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1415 · Cited by 66

Machine-Learning and Chemicogenomics Approach Defines and Predicts Cross-Talk of Hippo and MAPK Pathways

Pham, T. H., Hagenbeek, T. J., Lee, H.-J., Li, J., Rose, C. M., Lin, E., Yu, M., Martin, S. E., Piskol, R., Lacap, J. A., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0706 · Cited by 64

Inhibition of YAP/TAZ-driven TEAD activity prevents growth of NF2-null schwannoma and meningioma

Laraba, L., Hillson, L., de Guibert, J. G., Hewitt, A., Jaques, M. R., Tang, T. T.-L., Post, L. E., Ercolano, E., Rai, G., Yang, S., et al. (2022) · Brain · doi:10.1093/brain/awac342 · Cited by 63

TEAD4 overexpression promotes epithelial-mesenchymal transition and associates with aggressiveness and adverse prognosis in head neck squamous cell carcinoma

Zhang, W., Li, J., Wu, Y., Ge, H., Song, Y., Wang, D., Yuan, H., Jiang, H., Wang, Y., & Cheng, J. (2018) · Cancer Cell International · doi:10.1186/s12935-018-0675-z · Cited by 55

Protein-Protein Interaction Disruptors of the YAP/TAZ-TEAD Transcriptional Complex

Pobbati, A. V., & Rubin, B. P. (2020) · Molecules · doi:10.3390/molecules25246001 · Cited by 55

CRB3 regulates contact inhibition by activating the Hippo pathway in mammary epithelial cells

Mao, X., Li, P., Wang, Y., Liang, Z., Liu, J., Li, J., Jiang, Y., Bao, G., Li, L., Zhu, B., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2016.478 · Cited by 52

Regulatory enhancer profiling of mesenchymal-type gastric cancer reveals subtype-specific epigenomic landscapes and targetable vulnerabilities

Ho, S. W. T., Sheng, T., Xing, M., Ooi, W. F., Xu, C., Sundar, R., Huang, K. K., Li, Z., Kumar, V., Ramnarayanan, K., et al. (2022) · Gut · doi:10.1136/gutjnl-2021-326483 · Cited by 51

Progress with YAP/TAZ-TEAD inhibitors: a patent review (2018-present)

Zagiel, B., Melnyk, P., & Cotelle, P. (2022) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2022.2096436 · Cited by 50

Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence

Furet, P., Salem, B., Mesrouze, Y., Schmelzle, T., Lewis, I., Kallen, J. A., & Chêne, P. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.06.022 · Cited by 49

Both YAP1-MAML2 and constitutively active YAP1 drive the formation of tumors that resemble NF2 mutant meningiomas in micePreprint

Szulzewsky, F., Arora, S., Arakaki, A. K. S., Sievers, P., Bonnin, D. A. A., Paddison, P. J., Sahm, F., Cimino, P. J., Gujral, T. S., & Holland, E. C. (2022) · Genes & Development · doi:10.1101/gad.349876.122 · Cited by 46

Discovery of a cryptic site at the interface 2 of TEAD – Towards a new family of YAP/TAZ-TEAD inhibitors

Sturbaut, M., Bailly, F., Coevoet, M., Sileo, P., Pugnière, M., Liberelle, M., Magnez, R., Thuru, X., Chartier‐Harlin, M., Melnyk, P., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113835 · Cited by 45

The First Class of Small Molecules Potently Disrupting the YAP‐TEAD Interaction by Direct Competition

Furet, P., Bordas, V., Douget, M. L., Salem, B., Mesrouze, Y., Imbach, P. A., Sellner, H., Voegtle, M., Soldermann, N., Chapeau, E. A., et al. (2022) · ChemMedChem · doi:10.1002/cmdc.202200303 · Cited by 45

Structural and ligand-binding analysis of the YAP-binding domain of transcription factor TEAD4

Li, Y., Liu, S., Ng, E. Y., Li, R., Poulsen, A., Hill, J., Pobbati, A. V., Hung, A. W., Hong, W., Keller, T. H., et al. (2018) · Biochemical Journal · doi:10.1042/bcj20180225 · Cited by 43

The TEA domain family transcription factor TEAD4 represses murine adipogenesis by recruiting the cofactors VGLL4 and CtBP2 into a transcriptional complex

Zhang, W., Xu, J., Li, J., Guo, T., Jiang, D., Feng, X., Ma, X., He, L., Wu, W., Yin, M.-X., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003608 · Cited by 43

TEAD4 promotes colorectal tumorigenesis via transcriptionally targeting YAP1

Tang, J., Yu, C.-Y., Bao, Y.-J., Lu, C., Chen, J., Yang, S.-L., Chen, H., Hong, J., & Fang, J. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1403687 · Cited by 41

Identification of FAM181A and FAM181B as new interactors with the TEAD transcription factors

Bokhovchuk, F. M., Mesrouze, Y., Delaunay, C., Martin, T., Villard, F., Meyerhofer, M., Fontana, P., Zimmermann, C., Erdmann, D., Furet, P., et al. (2019) · Protein Science · doi:10.1002/pro.3775 · Cited by 38

Hot Spot Analysis of YAP-TEAD Protein-Protein Interaction Using the Fragment Molecular Orbital Method and Its Application for Inhibitor Discovery

Kim, J., Lim, H., Moon, S., Cho, S. Y., Kim, M., Park, J. H., Park, H. W., & No, K. T. (2021) · Cancers · doi:10.3390/cancers13164246 · Cited by 38

Cell adhesion molecule KIRREL1 is a feedback regulator of Hippo signaling recruiting SAV1 to cell-cell contact sites

Paul, A., Annunziato, S., Lu, B., Sun, T., Evrova, O., Planas‐Paz, L., Orsini, V., Terracciano, L., Charlat, O., Yang, Z., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28567-3 · Cited by 36

Inhibitors of the Hippo Pathway Kinases STK3/MST2 and STK4/MST1 Have Utility for the Treatment of Acute Myeloid Leukemia

Bata, N., Chaikuad, A., Bakas, N. A., Limpert, A. S., Lambert, L. J., Sheffler, D. J., Berger, L. M., Liu, G., Yuan, C., Wang, L., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00804 · Cited by 36

Common Secondary Genomic Variants Associated With Advanced Epithelioid Hemangioendothelioma

Seligson, N. D., Awasthi, A., Millis, S. Z., Turpin, B. K., Meyer, C. F., Grand’Maison, A., Liebner, D. A., Hays, J. L., & Chen, J. L. (2019) · JAMA Network Open · doi:10.1001/jamanetworkopen.2019.12416 · Cited by 32

The Surprising Features of the TEAD4‐Vgll1 Protein–Protein Interaction

Mesrouze, Y., Hau, J. C., Erdmann, D., Zimmermann, C., Fontana, P., Schmelzle, T., & Chêne, P. (2014) · ChemBioChem · doi:10.1002/cbic.201300715 · Cited by 30

Homeobox A4 suppresses vascular remodeling by repressing YAP/TEAD transcriptional activity

Kimura, M., Horie, T., Baba, O., Ide, Y., Tsuji, S., Rodriguez, R. R., Watanabe, T., Yamasaki, T., Otani, C., Xu, S., et al. (2020) · EMBO Reports · doi:10.15252/embr.201948389 · Cited by 29

TEA Domain Transcription Factor 4 Is the Major Mediator of Yes-Associated Protein Oncogenic Activity in Mouse and Human Hepatoblastoma

Zhang, J., Pin, L., Tao, J., Wang, P., Zhang, Y., Song, X., Che, L., Sumazin, P., Ribback, S., Kiss, A., et al. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.01.016 · Cited by 28

Nerfin-1 represses transcriptional output of Hippo signaling in cell competition

Guo, P., Lee, C.-H., Lei, H., Zheng, Y., Prieto, K. D. P., & Pan, D. (2019) · eLife · doi:10.7554/elife.38843 · Cited by 28

Toward the Design of Ligands Selective for the C-Terminal Domain of TEADs

Liberelle, M., Toulotte, F., Renault, N., Gelin, M., Allemand, F., Melnyk, P., Guichou, J., & Cotelle, P. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00075 · Cited by 24

Pan-cancer analysis, cell and animal experiments revealing TEAD4 as a tumor promoter in ccRCC

Li, F., Feng, Y., Jiang, Q., Zhang, J., Wu, F., Li, Q., Jing, X., Wang, X., & Huang, C. Y. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120327 · Cited by 23

Loss of CDKN2A Cooperates with WWTR1(TAZ)–CAMTA1 Gene Fusion to Promote Tumor Progression in Epithelioid Hemangioendothelioma

Seavey, C. N., Hallett, A., Li, S., Che, K., Pobbati, A. V., Ma, S., Burtscher, A., Kanai, R., Lamar, J. M., & Rubin, B. P. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-22-2497 · Cited by 23

An Early Association between the α-Helix of the TEAD Binding Domain of YAP and TEAD Drives the Formation of the YAP:TEAD Complex

Bokhovchuk, F. M., Mesrouze, Y., Meyerhofer, M., Zimmermann, C., Fontana, P., Erdmann, D., Jemth, P., & Chêne, P. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00217 · Cited by 22

Association of subcellular localization of TEAD transcription factors with outcome and progression in pancreatic ductal adenocarcinoma

Drexler, R., Fahy, R., Küchler, M., Wagner, K. C., Reese, T., Ehmke, M., Feyerabend, B., Kleine, M., & Oldhafer, K. J. (2020) · Pancreatology · doi:10.1016/j.pan.2020.12.003 · Cited by 22

Abstract 5364: The TEAD autopalmitoylation inhibitor VT3989 improves efficacy and increases durability of efficacy of osimertinib in preclinical EGFR mutant tumor models

Tang, T. T., & Post, L. E. (2022) · Cancer Research · doi:10.1158/1538-7445.am2022-5364 · Cited by 21

YAP1 is essential for malignant mesothelioma tumor maintenance

Calvet, L., Dos-Santos, O., Spanakis, E., Jean‐Baptiste, V., Bail, J.-C. L., Buzy, A., Paul, P., Henry, C., Valence, S., Dib, C., et al. (2022) · BMC Cancer · doi:10.1186/s12885-022-09686-y · Cited by 20

A focal adhesion kinase-YAP signaling axis drives drug tolerant persister cells and residual disease in lung cancerPreprint

Haderk, F., Fernández-Méndez, C., Čech, L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.23.465573 · Cited by 18

Abstract 2156: IK-930 is a novel TEAD inhibitor for the treatment of cancers harboring mutations in the Hippo signal transduction pathway

Amidon, B., Sánchez-Martín, M., Bartolini, W. P., Syed, S., McGovern, K., Xu, L., Ecsedy, J., Zhang, X. M., Constan, A., & Castro, A. C. (2022) · Cancer Research · doi:10.1158/1538-7445.am2022-2156 · Cited by 18

The role of lysine palmitoylation/myristoylation in the function of the TEAD transcription factors

Mesrouze, Y., Aguilar, G., Meyerhofer, M., Bokhovchuk, F. M., Zimmermann, C., Fontana, P., Vissières, A., Voshol, H., Erdmann, D., Affolter, M., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-09127-7 · Cited by 15

TEADs serve as potential prognostic biomarkers and targets for human gastric cancer

Wang, M.-H., Li, B., Chen, Y., & Wang, J. (2022) · BMC Gastroenterology · doi:10.1186/s12876-022-02386-8 · Cited by 12

Aurintricarboxylic acid is a canonical disruptor of the TAZ-TEAD transcriptional complex

Che, K., Pobbati, A. V., Seavey, C. N., Federov, Y., Komar, A. A., Burtscher, A., Ma, S., & Rubin, B. P. (2022) · PLoS ONE · doi:10.1371/journal.pone.0266143 · Cited by 7

Direct and selective pharmacological disruption of the YAP–TEAD interface by IAG933 inhibits Hippo-dependent and RAS–MAPK-altered cancers

Chapeau, E. A., Sansregret, L., Galli, G. G., Chêne, P., Wartmann, M., Mourikis, T. P., Jaaks, P., Baltschukat, S., Barbosa, I. A. M., Bauer, D., et al. (2024) · Nature Cancer · doi:10.1038/s43018-024-00754-9 · Cited by 168

Genome-Wide CRISPR Screens Identify Multiple Synthetic Lethal Targets That Enhance KRASG12C Inhibitor Efficacy

Mukhopadhyay, S., Huang, H.-Y., Lin, Z., Ranieri, M., Li, S., Sahu, S., Liu, Y., Ban, Y., Guidry, K., Hu, H., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-2729 · Cited by 105

Expected and unexpected effects after systemic inhibition of Hippo transcriptional output in cancer

Baroja, I., Kyriakidis, N. C., Halder, G. A., & Moya, I. M. (2024) · Nature Communications · doi:10.1038/s41467-024-46531-1 · Cited by 96

TEAD Inhibition Overcomes YAP1/TAZ-Driven Primary and Acquired Resistance to KRASG12C Inhibitors

Edwards, A. C., Stalnecker, C. A., Jean Morales, A., Taylor, K. E., Klomp, J. E., Klomp, J. A., Waters, A. M., Sudhakar, N., Hallin, J., Tang, T. T., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-2994 · Cited by 91

New insights into the ambivalent role of YAP/TAZ in human cancers

Luo, J., Deng, L., Zou, H., Guo, Y., Tong, T., Huang, M., Ling, G., & Li, P. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02704-2 · Cited by 89

Targeting TEAD in cancer

Battina, R., Rahhal, R., Wellstein, A., Riegel, A. T., & Sharif, G. M. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1692512 · Cited by 18

Targeting the Hippo Pathway and Cancer through the TEAD Family of Transcription Factors

Holden, J. K., & Cunningham, C. N. (2018) · Cancers · doi:10.3390/cancers10030081 · Cited by 181

A chemical perspective on the modulation of TEAD transcriptional activities: Recent progress, challenges, and opportunities

Lou, J., Lu, Y., Cheng, J., Zhou, F., Yan, Z., Zhang, D., Meng, X., & Zhao, Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114684 · Cited by 39

Abstract 2474: Potent small molecule TEAD inhibitors targeting the Hippo pathway exhibit antiproliferation in vitro and anti-tumor effect in vivo

Amidon, B., Syed, S., Cavanaugh, J., Frosch, H., Natarajan, P., Ecsedy, J., McGovern, K., & Castro, A. C. (2020) · Cancer Research · doi:10.1158/1538-7445.am2020-2474

Abstract 4516: Inhibiting YAP activity in cancers by targeted degradation of TEAD

Chen, H., Gridnev, A., Schlamowitz, N. S., Zheng, G., & Misra, J. R. (2024) · Cancer Research · doi:10.1158/1538-7445.am2024-4516