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

Zhao, B., Ye, X., Yu, J., Li, L., Li, W., Li, S., Yu, J., Lin, J. D., Wang, C.-Y., Chinnaiyan, A. M., et al. (2008) · Genes & Development · doi:10.1101/gad.1664408 · Cited by 2,498

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

Yu, F.-X., Zhao, B., Panupinthu, N., Jewell, J. L., Lian, I., Wang, L. H., Zhao, J., Yuan, H., Tumaneng, K., Li, H., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.037 · Cited by 1,628

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

Liu-Chittenden, Y., Huang, B., Shim, J. S., Chen, Q., Lee, S.-J., Anders, R. A., Liu, J. O., & Pan, D. (2012) · Genes & Development · doi:10.1101/gad.192856.112 · Cited by 1,452

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

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 the Hippo pathway in cancer

Harvey, K. F., & Tang, T. T.-L. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01234-0 · Cited by 68

Plastic persisters: revival stem cells in colorectal cancer

Tape, C. J. (2023) · Trends in cancer · doi:10.1016/j.trecan.2023.11.003 · Cited by 60

Hippo Signaling at the Hallmarks of Cancer and Drug Resistance

Kumar, R., & Hong, W. (2024) · Cells · doi:10.3390/cells13070564 · Cited by 47

The Hippo pathway: Organ size control and beyond

Guo, P., Wan, S., & Guan, K. (2024) · Pharmacological Reviews · doi:10.1016/j.pharmr.2024.100031 · Cited by 51

Pancreatic cancer: molecular pathogenesis and emerging therapeutic strategies

Rozengurt, E., & Eibl, G. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02499-y · Cited by 49

Cell softness renders cytotoxic T lymphocytes and T leukemic cells resistant to perforin-mediated killing

Zhou, Y., Wang, D., Zhou, L., Zhou, N., Wang, Z., Chen, J., Pang, R., Fu, H., Huang, Q., Dong, F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45750-w · Cited by 42

Complex roles of Hippo-YAP/TAZ signaling in hepatocellular carcinoma

Shi, H., Zou, Y., Zhong, W., Li, Z., Wang, X., Yin, Y., Li, D., Liu, Y., & Li, M. (2023) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-023-05272-2 · Cited by 38

Cooperation between the Hippo and MAPK pathway activation drives acquired resistance to TEAD inhibition

Paul, S., Hagenbeek, T. J., Tremblay, J., Kameswaran, V., Ong, C. C., Liu, C., Guarnaccia, A. D., Mondo, J. A., Hsu, P., Kljavin, N. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56634-y · Cited by 34

Nuclear Import and Export of YAP and TAZ

Kofler, M., & Kapùs, A. (2023) · Cancers · doi:10.3390/cancers15204956 · Cited by 30

Targeting the Hippo pathway in cancer: kidney toxicity as a class effect of TEAD inhibitors?

Paul, S., Sims, J., Pham, T., & Dey, A. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.10.004 · Cited by 30

It’s all downstream from here: RTK/Raf/MEK/ERK pathway resistance mechanisms in glioblastoma

Yakubov, R., Kaloti, R., Persaud, P., McCracken, A., Zadeh, G. M., & Bunda, S. (2025) · Journal of Neuro-Oncology · doi:10.1007/s11060-024-04930-w · Cited by 29

Leveraging Hot Spots of TEAD–Coregulator Interactions in the Design of Direct Small Molecule Protein-Protein Interaction Disruptors Targeting Hippo Pathway Signaling

Zhao, B., Pobbati, A. V., Rubin, B. P., & Stauffer, S. R. (2023) · Pharmaceuticals · doi:10.3390/ph16040583 · Cited by 26

Mechanical Properties of Glioblastoma: Perspectives for YAP/TAZ Signaling Pathway and Beyond

Pontes, B., & Mendes, F. A. (2023) · Diseases · doi:10.3390/diseases11020086 · Cited by 27

A Single-Arm Phase 2 Trial of Trametinib in Patients with Locally Advanced or Metastatic Epithelioid Hemangioendothelioma

Schuetze, S. M., Ballman, K. V., Heise, R. S., Ganjoo, K. N., Davis, E. J., George, S., Burgess, M. A., Choy, E., Shepard, D. R., Tinoco, G., et al. (2024) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-3817 · Cited by 24

Palmitoylation: an emerging therapeutic target bridging physiology and disease

Li, W., Shen, J. M., Zhuang, A., Wang, R., Li, Q., Rabata, A., Zhang, Y., & Cao, D. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00776-w · Cited by 31

Tyrosine phosphorylation-mediated YAP1-TFAP2A interactions coordinate transcription and trastuzumab resistance in HER2+ breast cancer

Zou, H., Luo, J., Guo, Y., Deng, L., Zeng, L., Pan, Y., & Li, P. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101051 · Cited by 27

Design, Synthesis, and Bioevaluation of Transcriptional Enhanced Assocciated Domain (TEAD) PROTAC Degraders

Li, H., Ge, Z., Lin, K., He, W., Chu, Q., Zheng, M., Zhang, S., & Xu, T. (2024) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.4c00029 · Cited by 23

Pharmacological regulators of Hippo pathway: Advances and challenges of drug development

Lao, Z., Chen, X., Pan, B., Fang, B., Yang, W., & Qian, Y. (2025) · The FASEB Journal · doi:10.1096/fj.202401895rr · Cited by 25

Estrogen receptor activation remodels TEAD1 gene expression to alleviate hepatic steatosis

Sommerauer, C., Gallardo-Dodd, C. J., Savva, C., Hases, L., Birgersson, M., Indukuri, R., Shen, J. X., Carravilla, P., Geng, K., Søndergaard, J. N., et al. (2024) · Molecular Systems Biology · doi:10.1038/s44320-024-00024-x · Cited by 25

Hippo signaling in acute kidney injury to chronic kidney disease transition: Current understandings and future targets

Habshi, T., Shelke, V., Kale, A., Lech, M., & Gaikwad, A. B. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103649 · Cited by 20

Nuclear deformation regulates YAP dynamics in cancer associated fibroblasts

Emon, B., Joy, M. S. H., Lalonde, L., Ghrayeb, A., Doha, U., Ladehoff, L. C., Brockstein, R., Saengow, C., Ewoldt, R. H., & Saif, M. T. A. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.11.015 · Cited by 22

Deoxynivalenol regulates intestinal and stem cell regeneration via the Hippo pathway and clinical intervention strategies

Liao, P. (2025) · Toxicon · doi:10.1016/j.toxicon.2025.108553 · Cited by 18

TEAD-targeting small molecules induce a cofactor switch to regulate the Hippo pathway

Guarnaccia, A. D., Hagenbeek, T. J., Lee, W., Kljavin, N. M., Choi, M., Tombling, B. J., Peukert, C., Ulas, G., Kameswaran, V., Le, D., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2425984122 · Cited by 17

Endogenous YAP/TAZ partitioning in TEAD condensates orchestrates the Hippo response

Zhu, T., Li, H., Mao, S., Zhu, Y., Cao, H., Zhang, Q., Zhen, N., Zhang, H., Tian, Y., Guo, Y., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.014 · Cited by 15

Allosteric PROTACs: Expanding the Horizon of Targeted Protein Degradation

Frost, A. B., O’Connor, S., & Ciulli, A. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c14840 · Cited by 21

Development of HC-258, a Covalent Acrylamide TEAD Inhibitor That Reduces Gene Expression and Cell Migration

Fnaiche, A., Chan, H., Paquin, A., Suárez, N. G., Vu, V., Li, F., Allali‐Hassani, A., Cao, M. A., Szewczyk, M. M., Bolotokova, A., et al. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00386 · Cited by 16

Identification of a Gene Signature That Predicts Dependence upon YAP/TAZ-TEAD

Kanai, R., Norton, E., Stern, P., Hynes, R. O., & Lamar, J. M. (2024) · Cancers · doi:10.3390/cancers16050852 · Cited by 16

Identification of resistance mechanisms to small-molecule inhibition of TEAD-regulated transcription

Kulkarni, A., Mohan, V., Tang, T. T.-L., Post, L. E., Chan, Y.-C., Manning, M., Thio, N., Parker, B. L., Dawson, M. A., Rosenbluh, J., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00217-3 · Cited by 17

The recent advances and implications in cancer therapy for the hippo pathway

Chan, S. W., Ong, C., & Hong, W. (2025) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2025.102476 · Cited by 13

Development of LM-41 and AF-2112, two flufenamic acid-derived TEAD inhibitors obtained through the replacement of the trifluoromethyl group by aryl rings

Fnaiche, A., Mélin, L., Suárez, N. G., Paquin, A., Vu, V., Li, F., Allali‐Hassani, A., Bolotokova, A., Allemand, F., Gelin, M., et al. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129488 · Cited by 13

The Hippo pathway in endometrial cancer: a potential therapeutic target?

Shen, X., Li, Q., Sun, Y., Chen, L., Xue, F., Tian, W., & Wang, Y. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1273345 · Cited by 12

VGLL2 and TEAD1 fusion proteins identified in human sarcoma drive YAP/TAZ-independent tumorigenesis by engaging EP300

Guo, S., Hu, X., Cotton, J. L., Ma, L., Li, Q., Cui, J., Wang, Y., Thakare, R., Tao, Z., Ip, Y. T., et al. (2024) · eLife · doi:10.7554/elife.98386 · Cited by 14

Reactivating Hippo by drug compounds to suppress gastric cancer and enhance chemotherapy sensitivity

Cao, Z., Hou, Y., Zhao, Z., Zhang, H., Tian, L., Zhang, Y., Dong, C., Guo, F., Tan, L., Han, Y., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107311 · Cited by 12

Direct Inhibition of the YAP : TEAD Interaction: An Unprecedented Drug Discovery Challenge

Chêne, P. (2024) · ChemMedChem · doi:10.1002/cmdc.202400361 · Cited by 12

ATXN3 deubiquitinates YAP1 to promote tumor growth.

Wang, S., Liu, K., Han, X., Cheng, Y., Zhao, E., Brat, D. J., Sun, Z., & Fang, D. (2023) · PubMed Central · Cited by 11

Exploring RNF213 in Ischemic Stroke and Moyamoya Disease: From Cellular Models to Clinical Insights

Tan, B. Y., Kok, C. H. P., Ng, M. B. J., Loong, S. S. E., Jou, E., Yeo, L. L. L., Han, W., Anderson, C. D., Khor, C. C., & Lai, P. S. (2024) · Biomedicines · doi:10.3390/biomedicines13010017 · Cited by 11

Comparative Assessment and High-Throughput Drug-Combination Profiling of TEAD-Palmitoylation Inhibitors in Hippo Pathway Deficient Mesothelioma

Evsen, L., Morris, P. J., Thomas, C. J., & Ceribelli, M. (2023) · Pharmaceuticals · doi:10.3390/ph16121635 · Cited by 10

MoA Studies of the TEAD P-Site Binding Ligand MSC-4106 and Its Optimization to TEAD1-Selective Amide M3686

Heinrich, T., Schwarz, D. F., Petersson, C., Gunera, J., Garg, S., Schneider, R., Keil, M., Grimmeisen, L., Lopez, A. U., Albers, L., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01949 · Cited by 10

Noncanonical role of Golgi-associated macrophage TAZ in chronic inflammation and tumorigenesis

Park, S. Y., Ju, S., Lee, J. H., Kim, H.-R., Sub, Y., Park, D. J., Park, S., Kwon, D., Kang, H.-G., Shin, J. E., et al. (2025) · Science Advances · doi:10.1126/sciadv.adq2395 · Cited by 10

UCHL3: a crucial deubiquitinase in DNA damage repair and tumor progression

Liu, J., Hu, S., Xiao, J., & Zhou, J. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03884-x · Cited by 10

Pipeline to evaluate YAP-TEAD inhibitors indicates TEAD inhibition represses NF2 -mutant mesothelioma

Cunningham, R., Jia, S., Purohit, K. P., Nosková, M., Maniak, M. K., Lin, Y., Hui, N. S., Graham, R. E., Rossi, A. G., Cholewa-Waclaw, J., et al. (2025) · Life Science Alliance · doi:10.26508/lsa.202503241 · Cited by 12

Discovery of reversible and covalent TEAD 1 selective inhibitors MSC-1254 and MSC-5046 based on one scaffold

Carswell, E. L., Heinrich, T., Petersson, C., Gunera, J., Garg, S., Schwarz, D. F., Schlesiger, S., Fischer, F., Eichhorn, T., Calder, M., et al. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129981 · Cited by 9

An updated patent review of TEAD modulators (2022–present)

Xu, D., Zhong, J., Zeng, Y., Zhang, X., Wang, C., Luo, C., & Xiong, H. (2025) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2025.2522747 · Cited by 9

PKN2 Is a Dependency of the Mesenchymal-like Cancer Cell State

Killarney, S. T., Mesa, G., Washart, R., Mayro, B., Dillon, K. A., Wardell, S. E., Newlin, M., Lu, M., Rmaileh, A. A., Liu, N., et al. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-0928 · Cited by 9

Discovery of a Potent and Selective TEAD Degrader with Durable Degradation Activity

Cao, L., Yang, J., Liu, Y., Chen, X., Shi, Y., Zhao, Y., Zhang, Y., Chen, J., Li, B., Wen, W., et al. (2025) · Advanced Science · doi:10.1002/advs.202503277 · Cited by 8

Bidirectional relationship between cancer and depression: From shared mechanisms to integrated therapeutic strategies

Liu, Z., Wan, J., & Liu, S. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218318 · Cited by 8

Role of the YAP/TAZ-TEAD Transcriptional Complex in the Metabolic Control of TRAIL Sensitivity by the Mevalonate Pathway in Cancer Cells

Yousfi, Y. E., Mora-Molina, R., López‐Rivas, A., & Yerbes, R. (2023) · Cells · doi:10.3390/cells12192370 · Cited by 8

Gene therapy for diffuse pleural mesotheliomas in preclinical models by concurrent expression of NF2 and SuperHippo

Zhu, R., Liu, X., Zhang, X., Zhong, Z., Qi, S., Jin, R., Gu, Y., Wang, Y., Chen, L., Chen, K., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101763 · Cited by 8

CDK9 Inhibition by Dinaciclib Is a Therapeutic Vulnerability in Epithelioid Hemangioendothelioma

Pobbati, A. V., Burtscher, A., Siva, N. R., Hallett, A., Romigh, T., Che, K., Zhao, B., Coker, J. A., Wang, N., Stauffer, S. R., et al. (2024) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-24-1097 · Cited by 7

Oncogenic YAP sensitizes cells to CHK1 inhibition via CDK4/6 driven G1 acceleration

Gertzmann, D., Presek, C., Mattes, A. L., Sänger, M., Zoller, M., Schülein‐Völk, C., Ade, C. P., Eilers, M., & Gaubatz, S. (2025) · EMBO Reports · doi:10.1038/s44319-025-00514-5 · Cited by 8

Synergistic effect of PAK and Hippo pathway inhibitor combination in NF2-deficient Schwannoma

Benton, D., Chow, H. Y., Karchugina, S., & Chernoff, J. (2024) · PLoS ONE · doi:10.1371/journal.pone.0305121 · Cited by 7

Transcription factor TCF7L1 targeting HSPB6 is involved in EMT and PI3K/AKT/mTOR pathways in bladder cancer

Li, Z., Li, J., Cao, Q., Shen, T., Wang, Y., He, H., & Tong, M. H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108024 · Cited by 7

The Hippo pathway as an antitumor target: time to focus on

Koroleva, O. A., Kurkin, A. V., & Shtil, A. A. (2024) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2024.2432395 · Cited by 7

ELK4 induced upregulation of HOMER3 promotes the proliferation and metastasis in glioma via Wnt/β-catenin/EMT signaling pathway

Wang, F., Zhou, H., Tian, Y., Wang, X., Huang, Y., Tu, Y., Li, L., & Zhen, H. (2025) · Biology Direct · doi:10.1186/s13062-025-00643-w · Cited by 6

Transcription factor TFAP2A drives the growth and metastasis and blocks ferroptosis of triple-negative breast cancer by activating PRAME transcription

Pei, B., Sun, H., & Xu, L.-Y. (2025) · Naunyn-Schmiedeberg's Archives of Pharmacology · doi:10.1007/s00210-025-04359-6 · Cited by 7

γδ T cell-stromal networks modulate matrix composition and vascularity in foreign body response

Ruta, A., Krishnan, K., Woo, J., Mejías, J. C., Gray-Gaillard, E. F., Maestas, D. R., Nguyen, H. H., Rindone, A. N., Cherry, C., Patatanian, M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71540-7 · Cited by 5

Single-cell multi-omics analysis reveals cancer regulatory elements of transcriptional programs and clinical implications

Tang, X., Zhang, Q., Shen, Z., Xiao, J., Li, M., Meng, X., Wang, C., Zhang, G., Liu, A., & Yin, Y. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08060-7 · Cited by 5

Translating molecular mechanisms of epithelioid hemangioendothelioma to improve patient outcome

Beretta, A., Stacchiotti, S., Tam, Y. B., Jones, R. L., Giani, C., Zaffaroni, N., Huang, P. H., & Pasquali, S. (2025) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2025.105021 · Cited by 6

Discovery of Clinical Candidate IAG933, a Potent YAP-TEAD PPI Disrupter

Vögtle, M., Sellner, H., Chapeau, E. A., Furet, P., Salem, B., Douget, M. L., Bordas, V., Groell, J., Goff, A.-L. L., Rouzet, C., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03009 · Cited by 5

NSUN2 promoted tumor growth and metastatic via m5C-regulation of YAP through ALYREF/YBX1 axis in NSCLC

Li, R., Jin, D., Shao, S., & Guo, J. (2026) · Cell Death and Disease · doi:10.1038/s41419-025-08353-x · Cited by 5

RHOA drivers take alternate routes in gastric cancer

Benton, D., & Chernoff, J. (2023) · Science Signaling · doi:10.1126/scisignal.adk9171 · Cited by 5

Regulation of Hippo–YAP signaling axis by Isoalantolactone suppresses tumor progression in cholangiocarcinoma

Kim, C.-L., Lim, S.-B., Kim, D. H., Sim, Y. E., Kang, L., Park, S. J., Kim, H., Roh, T. H., Mo, J., & Jeong, H.-S. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.101971 · Cited by 5

Identification of pyrazolo-piperidinone derivatives targeting YAP-TEAD interface 3 as anticancer agents through integrated virtual screening and mass spectrometry proteomics

Scalvini, L., Tagliazucchi, L., Elisi, G. M., Zappaterra, D., Moschella, M. G., Fantini, S., Aiello, D., Guerrini, R., Albanese, V., Pacifico, S., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118056 · Cited by 5

TRIMming away colon cancer: TRIM21-mediated ubiquitination as an activator of the Hippo tumor suppressor pathway

Benton, D., & Chernoff, J. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.06.023 · Cited by 5

Novel Indazole Compounds as TEAD Inhibitors for Treating Cancer

Sabnis, R. W. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00392 · Cited by 5

SARS-CoV-2 NSP13 interacts with TEAD to suppress Hippo-YAP signaling

Meng, F., Kim, J.-H., Tsai, C.-R., Steimle, J. D., Wang, J., Shi, Y., Li, R. G., Xie, B., Deshmukh, V., Liu, S., et al. (2024) · eLife · doi:10.7554/elife.100248.3 · Cited by 6

Covalent pan-TEAD inhibitors block YAP activity and demonstrate brain penetrance in a Hippo-dependent cancer model

Hagenbeek, T. J., Zbieg, J. R., Smith, R., Paul, S., Gerosa, L., Torrini, C., Guarnaccia, A. D., Ong, C. C., Lacap, J. A., Ning, M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74722-5 · Cited by 4

Discovery and biological evaluation of carborane-containing derivatives as TEAD auto palmitoylation inhibitors

Li, C., Zhang, Y., Zhang, Z., Zhang, Y., Song, Y., Wang, L., Yuan, C., Hao, G., Sun, N., Li, H., et al. (2025) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2025.130155 · Cited by 4

Mechanism study of serum extracellular nano-vesicles miR-412-3p targeting regulation of TEAD1 in promoting malignant biological behavior of sub-centimeter lung nodules

Deng, Y., Patel, N. D., Ding, S., & Zhang, H. (2024) · Cancer Biomarkers · doi:10.3233/cbm-240137 · Cited by 3

Hippo pathway effectors are associated with glioma patient survival, control cell proliferation and sterol metabolism through TEAD3

Masliantsev, K., Desette, A., Gonzalez, A., Garrouche, I., Noblanc, A., Soulard, M., Triquard, M., Milin, S., Wager, M., Karayan, L., et al. (2025) · Brain Pathology · doi:10.1111/bpa.70021 · Cited by 3

TFAP4/DLGAP5 promotes tumor progression and macrophage M2 polarization in prostate cancer by activating the JAK2/STAT3 signaling

Li, S., Dong, Q., Ren, W., Yi, S., Wang, Z., & Pan, L. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114753 · Cited by 3

PARP1-mediated PARylation of TEAD4 stabilizes the YAP1-TEAD4 complex and promotes growth and immune evasion in breast cancer cells

Guo, Y., Song, G., Zou, H., Lu, L., Dai, X., Sun, C., Huangen, C. H. E. N., Tong, T., Huang, M., Zhu, M., et al. (2025) · Science Signaling · doi:10.1126/scisignal.adx2532 · Cited by 4

FRA1 drives melanoma metastasis through an actionable transcriptional network

Xu, X., Jarajapu, V., Chadourne, M., Soto-Vargas, Z., Ochoa-Rios, S. L., Jasani, N., Wang, K., Mecozzi, N., Yao, J., Yu, X., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03632-5 · Cited by 4

Expanding the toolbox to develop IAP-based degraders of TEAD transcription factors

Gupta, N., Trainor, N. B., Radwan, M., Nguyen, S., Duncan, L. J., Tang, A. X., Beveridge, J. G., Silke, N., Yousef, J. M., Bilgilier, C., et al. (2026) · Communications Chemistry · doi:10.1038/s42004-025-01871-x · Cited by 3

Discovery of Pan-TEAD Inhibitors That Disrupt YAP-TEAD Interaction as a Potential Therapy for Gastric Cancers and Mutant KRAS and EGFR Lung Cancers

Kumar, R., Thian, J., Toh, J. D. W., Mohideen, N. F., Sun, J., Kang, C., Low, S. M. C., Wee, S., Lim, Z., Gunaratne, J., et al. (2026) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5c00590 · Cited by 3

The Hippo Pathway Is Dysregulated in Cancer-Associated Fibroblasts in Anti–PD-L1–Resistant Cancer

Roels, J., Ghaedi, H., Kancherla, J., Yang, Y., Ganesan, R., Babu, P., Williams, K., Yao, X., Pradhan, R., Guan, X., et al. (2026) · Cancer Research · doi:10.1158/0008-5472.can-24-3954 · Cited by 5

EDNRA Forms a Positive Feedback Loop with the Hippo/YAP Axis to Drive Triple‐Negative Breast Cancer Progression

Hong, Z., Li, B., Xu, J., Lin, R., Pan, J., Fang, C., Zhang, B., Lau, L. Y., Aldridge, R. J., Whitmore, E. A., et al. (2026) · Advanced Science · doi:10.1002/advs.76784 · Cited by 3

Drug targets regulate systemic metabolism and provide new horizons to treat nonalcoholic steatohepatitis

Wang, Y., Yu, H., Cen, Z., Zhu, Y., & Wu, W. (2023) · Metabolism Open · doi:10.1016/j.metop.2023.100267 · Cited by 3

Key roles of ubiquitination in regulating critical regulators of cancer stem cell functionality

Guo, Q., Qin, H., Chen, Z., Zhang, W., Zheng, L., & Qin, T. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101311 · Cited by 3

The YAP1-MAML2 fusion drives tumorigenesis and sustains tumor growth

Ni, W., Yu, M., Yang, R., Li, J. W., Zhou, X., Calbay, O., Pi, L., Lu, J., Huang, S., & Wu, L. (2024) · Molecular Therapy Oncology · doi:10.1016/j.omton.2024.200900 · Cited by 3

An oncoembryology approach uncovers SoxC-driven regulation of colon development and cancerPreprint

Dalessi, T., Valenta, T., Moro, G., Brügger, M. D., Meijs, A., Szczerba, B. M., Brunner, T., Lampart, S., Nater, M., Platt, R. J., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.08.617191 · Cited by 3

Structural and functional basis of PU.1-BAF interaction enables targeting of lineage-specific transcription

Sadalge, D., Clasman, J. R., Topal, S., Musser, D., Von der Porten, L., Wu, S., Schultz, S. E., Austin, W., Huang, D., Gao, Y.-D., et al. (2025) · doi:10.1101/2025.08.01.667454 · Cited by 2

Phase II study of axitinib in patients with NF2-related schwannomatosis and progressive vestibular schwannomas

Garcia, M. R., Hagiwara, M., Yaffe, A., Mitchell, C., Akshintala, S., Nicolaides, T. P., Phadnis, S., Yohay, K. H., Feng, Y., Goldberg, J. D., et al. (2025) · Neuro-Oncology Advances · doi:10.1093/noajnl/vdaf083 · Cited by 2

Alexidine is a TAZ-specific small-molecule inhibitor that suppresses breast cancer invasion and metastasis

Ge, A., Niu, L., Rubino, R., Seaman, K., Song, X., Hao, Y., Klupt, K. A., Iaboni, N., Jia, Z., You, L., et al. (2025) · iScience · doi:10.1016/j.isci.2025.114116 · Cited by 3

CD155 reprograms glycolysis via the YAP/TEAD1-GLUT1 axis to promote lung adenocarcinoma progression and M2 macrophage polarization: a metabolic-immune target visualized by 18F-FDG PET/CT

Cheng, Z., Wang, S., Xu, S., Wang, Y., Diao, Y., Du, B., Li, X., & Li, Y. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07551-7 · Cited by 2

CNS penetrant TEAD1,2,4 inhibitor MSC-4070 derived from phenotypic screening hit optimization

Heinrich, T., Petersson, C., Gunera, J., Gambardella, A., Schwarz, D., Garg, S., Schilke, H., Weitzel, T., Kolb, C., Anlauf, U., et al. (2026) · RSC Medicinal Chemistry · doi:10.1039/d5md00928f · Cited by 2

TEAD1::NCOA2 fusion driver in primary central nervous system malignancy: case report

Панферова, А. В., Сенченко, М. А., Zaytseva, M., Rasskazova, Y., Abasov, R. K., Tarakanova, A. V., Usman, N. Y., Papusha, L. I., & Druy, A. E. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02851-0 · Cited by 2

PPP1CA promotes hepatocellular carcinoma progression in a YAP1-dependent way

Liu, X., Xu, G., Luo, W., Wang, K., & Wang, F. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111938 · Cited by 2

Current Model Systems for Investigating Epithelioid Haemangioendothelioma

Neil, E., & Kouskoff, V. (2023) · Cancers · doi:10.3390/cancers15113005 · Cited by 2

Novel Compounds as TEAD Inhibitors for Treating Cancer

Sabnis, R. W. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00346 · Cited by 2

OTUD6A orchestrates complex modulation of TEAD4 ‐mediated transcriptional programs

Kim, H. J., Choi, Y.-S., Lee, Y., Hwangbo, M. H., & Kim, J. (2024) · FEBS Letters · doi:10.1002/1873-3468.14861 · Cited by 1

Decoy oligodeoxynucleotides targeting STATs in non-cancer gene therapy

Mahjoubin‐Tehran, M., Rezaei, S., Kesharwani, P., Karav, S., & Sahebkar, A. (2025) · Gene · doi:10.1016/j.gene.2025.149482 · Cited by 1

Integrative High-Throughput RNAi Screening Identifies BRSK1, STK32C and STK40 as Novel Activators of YAP/TAZ

Gill, M. K., Song, S., Christova, T. Y., & Attisano, L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167810 · Cited by 1

Hippo signaling as a therapeutic switch for T cell functions and tumor immunity

Fan, J., Riaz, F., & Riaz, F. (2026) · Molecular Immunology · doi:10.1016/j.molimm.2025.12.013 · Cited by 1

Subtype-Dependent Expression Patterns of Core Hippo Pathway Components in Thymic Epithelial Tumors (TETs): An RT-qPCR Study

Elm, L., Gerlitz, N., Neumann, J. H. L., & Levidou, G. (2026) · Biomedicines · doi:10.3390/biomedicines14020305 · Cited by 1

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