Akt Phosphorylates the Yes-Associated Protein, YAP, to Induce Interaction with 14-3-3 and Attenuation of p73-Mediated Apoptosis

Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells

Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., & Tuschl, T. (2001) · Nature · doi:10.1038/35078107 · Cited by 9,456

Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., & Greenberg, M. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80405-5 · Cited by 5,689

Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor

Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594

Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244

Extension of Life-Span by Introduction of Telomerase into Normal Human Cells

Bodnar, A. G., Ouellette, M., Frolkis, M., Holt, S. E., Chiu, C.-P., Morin, G. B., Harley, C. B., Shay, J. W., Lichtsteiner, S., & Wright, W. E. (1998) · Science · doi:10.1126/science.279.5349.349 · Cited by 4,975

Cellular survival: a play in three Akts

Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216

A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002).

Vlahos, C. J., Matter, W. F., Hui, K. Y., & Brown, R. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37680-9 · Cited by 3,248

A generic protein purification method for protein complex characterization and proteome exploration

Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., & Séraphin, B. (1999) · Nature Biotechnology · doi:10.1038/13732 · Cited by 2,707

Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt

Peso, L. D., González-Garcı́a, M., Page, C., Herrera, R., & Nuñez, G. (1997) · Science · doi:10.1126/science.278.5338.687 · Cited by 1,797

The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity

Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H. C. B., Gamblin, S. J., Smerdon, S. J., & Cantley, L. C. (1997) · Cell · doi:10.1016/s0092-8674(00)80487-0 · Cited by 1,604

YAP-mediated trophoblast dysfunction: the common pathway underlying pregnancy complications

Lin, Q., Cao, J., Yu, J., Zhu, Y., Shen, Y., Wang, S., Wang, Y., Liu, Z., & Chang, Y. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01371-2 · Cited by 23

TRIM15 drives chondrocyte senescence and osteoarthritis progression

Li, Z., Zhang, W., Xiao, W., Hu, J. Z., Hu, X., Liu, H., Lü, J., Shen, S., & Ji, M.-L. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adq1735 · Cited by 26

IFN-γ-response mediator GBP-1 represses human cell proliferation by inhibiting the Hippo signaling transcription factor TEAD

Unterer, B., Wiesmann, V., Gunasekaran, M., Sticht, H., Tenkerian, C., Behrens, J., Leone, M., Engel, F. B., Britzen‐Laurent, N., Naschberger, E., et al. (2018) · Biochemical Journal · doi:10.1042/bcj20180123 · Cited by 23

Proteomic Profiling of Stem Cell Tissues during Regeneration of Deer Antler: A Model of Mammalian Organ Regeneration

Dong, Z., Haines, S. R., & Coates, D. E. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00026 · Cited by 23

VGLL1 phosphorylation and activation promotes gastric cancer malignancy via TGF-β/ERK/RSK2 signaling

Im, J., Kim, D.-M., Park, H., Kang, M., Kim, D.-Y., Chang, K. Y., Kim, B., & Won, M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118892 · Cited by 23

Hippo pathway effectors YAP and TAZ and their association with skeletal muscle ageing

Setiawan, I., Sanjaya, A., Lesmana, R., Yen, P. M., & Goenawan, H. (2021) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-021-00787-z · Cited by 25

Metabolic control of progenitor cell propagation during Drosophila tracheal remodeling

Li, Y., Dong, P., Yang, Y., Guo, T., Zhao, Q., Miao, D., Li, H., Lu, T., Xia, F., Lyu, J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30492-4 · Cited by 22

Chromatin signaling in muscle stem cells: interpreting the regenerative microenvironment

Brancaccio, A., & Palacios, D. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00036 · Cited by 24

Polyomavirus Small t Antigen Interacts with Yes-Associated Protein To Regulate Cell Survival and Differentiation

Hwang, J. H., Pores‐Fernando, A. T., Faure, N., Andrabi, S., Hahn, W. C., Schaffhausen, B. S., & Roberts, T. M. (2014) · Journal of Virology · doi:10.1128/jvi.01399-14 · Cited by 26

Insulin-response Element-binding Protein 1

Villafuerte, B. C., Phillips, L. S., Rane, M. J., & Zhao, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404349200 · Cited by 23

Polystyrene nanoplastics promote muscle cell senescence through microtubule hyper-stabilization-mediated mitophagy dysfunction and cGAS-Sting activation

Cui, J., Yue, X., Zhang, Y., Wang, B., Mu, A., Ren, S., Shao, L., Zhu, S., Zhang, N., Lu, Y., et al. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.139232 · Cited by 22

Modeling mesothelioma utilizing human mesothelial cells reveals involvement of phospholipase-C beta 4 in YAP-active mesothelioma cell proliferation

kakiuchi., T., Takahara, T., Kasugai, Y., Arita, K., Yoshida, N., Karube, K., Suguro, M., Matsuo, K., Nakanishi, H., Kiyono, T., et al. (2016) · Carcinogenesis · doi:10.1093/carcin/bgw084 · Cited by 22

Initiation of human mammary cell tumorigenesis by mutant KRAS requires YAP inactivation

Lefort, S., Tan, S., Balani, S., Rafn, B., Pellacani, D., Hirst, M., Sorensen, P. H. B., & Eaves, C. J. (2019) · Oncogene · doi:10.1038/s41388-019-1111-0 · Cited by 24

TEAD Proteins Associate With DNA Repair Proteins to Facilitate Cellular Recovery From DNA Damage

Calses, P. C., Pham, V. C., Guarnaccia, A. D., Choi, M., Verschueren, E., Bakker, S. T., Pham, T. H., Hinkle, T., Liu, C., Chang, M. T., et al. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100496 · Cited by 22

CD248 ‐expressing cancer‐associated fibroblasts induce non‐small cell lung cancer metastasis via Hippo pathway‐mediated extracellular matrix stiffness

Wu, J., Zhang, Q., Yang, Z., Xu, Y., Liu, X., Wang, X., Peng, J., Xiao, J., Wang, Y., Shang, Z., et al. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.70025 · Cited by 22

Protein Kinase C-Dependent Phosphorylation Regulates the Cell Cycle-Inhibitory Function of the p73 Carboxy Terminus Transactivation Domain

Nyman, U., Engskog‐Vlachos, P., Cascante, A., Hermanson, O., Zhivotovsky, B., & Joseph, B. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00585-08 · Cited by 22

Metaplastic carcinoma show different expression pattern of YAP compared to triple-negative breast cancer

Kim, H. M., Kim, S. K., Jung, W. H., & Koo, J. S. (2014) · Tumor Biology · doi:10.1007/s13277-014-2735-x · Cited by 22

Hippo signaling in epithelial stem cells

Yin, M.-X., & Zhang, L. (2014) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmu111 · Cited by 23

Hippo vs. Crab: tissue‐specific functions of the mammalian Hippo pathway

Nishio, M., Maehama, T., Goto, H., Nakatani, K., Kato, W., Omori, H., Miyachi, Y., Togashi, H., Shimono, Y., & Suzuki, A. (2017) · Genes to Cells · doi:10.1111/gtc.12461 · Cited by 22

c-Yes response to growth factor activation

Clump, D. A., Clump, D. A., Qazi, I. H., Clump, D. A., Qazi, I. H., Sudol, M., & Flynn, D. C. (2005) · Growth Factors · doi:10.1080/08977190500199360 · Cited by 22

Targeting 14-3-3θ-mediated TDP-43 pathology in amyotrophic lateral sclerosis and frontotemporal dementia mice

Ke, Y. D., van Hummel, A., Au, C. G., Chan, G., Lee, W. S., van der Hoven, J., Przybyla, M., Deng, Y., Sabale, M., Morey, N., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.01.022 · Cited by 21

Akt1-dependent expression of angiopoietin 1 and 2 in vascular smooth muscle cells leads to vascular stabilization

Ha, J. M., Jin, S. Y., Lee, H. S., Kum, H. J., Vafaeinik, F., Ha, H. K., Song, S. H., Kim, C. D., & Bae, S. S. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00819-8 · Cited by 21

Convergence of YAP/TAZ, TEAD and TP63 activity is associated with bronchial premalignant severity and progression

Ning, B., Tilston-Lünel, A., Simonetti, J., Hicks‐Berthet, J., Matschulat, A. M., Pfefferkorn, R., Spira, A. E., Edwards, M., Mazzilli, S. A., Lenburg, M. E., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02674-5 · Cited by 22

SRY-Box transcription factor 9 triggers YAP nuclear entry via direct interaction in tumors

Qian, H., Ding, C., Liu, F., Chen, S., Huang, C., Xiao, M., Hong, X.-L., Wang, M., Yan, F., Ding, K., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01805-4 · Cited by 21

Yap1 plays a protective role in suppressing free fatty acid-induced apoptosis and promoting beta-cell survival

Deng, Y., Matsui, Y., Pan, W., Li, Q., & Lai, Z.-C. (2016) · Protein & Cell · doi:10.1007/s13238-016-0258-5 · Cited by 22

Inhibition of isoprenylation synergizes with MAPK blockade to prevent growth in treatment‐resistant melanoma, colorectal, and lung cancer

Theodosakis, N., Langdon, C. G., Micevic, G., Krykbaeva, I., Means, R. E., Stern, D. F., & Bosenberg, M. (2018) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12742 · Cited by 21

Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction

Verma, A., Fan, J., Finch‐Edmondson, M., Velázquez‐Campoy, A., Balasegaran, S., Sudol, M., & Sivaraman, J. (2018) · Oncotarget · doi:10.18632/oncotarget.23909 · Cited by 19

Evidence for discrete modes of YAP1 signaling via mRNA splice isoforms in development and diseases

Vrbský, J., Vinarský, V., Perestrelo, A. R., Cruz, J. O. L., Martino, F. D., Pompeiano, A., Izzi, V., Hlinomaz, O., Rotrekl, V., Sudol, M., et al. (2021) · Genomics · doi:10.1016/j.ygeno.2021.03.009 · Cited by 19

Cellular feedback dynamics and multilevel regulation driven by the hippo pathway

Park, J., & Hansen, C. G. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200253 · Cited by 19

The effect of AKT in extracellular matrix stiffness induced osteogenic differentiation of hBMSCs

Shen, Y., Jing, D., & Zhao, Z. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110404 · Cited by 20

Roles of Hippo signaling in lung cancer

Zhang, H.-X., Wang, Y., Ding, W., Chen, C., Niu, Z., & Pan, M. (2015) · Indian Journal of Cancer · doi:10.4103/0019-509x.168949 · Cited by 20

p53 Family: Therapeutic Targets in Neuroblastoma

Wolter, J. K., Angelini, P., & Irwin, M. S. (2010) · Future Oncology · doi:10.2217/fon.09.176 · Cited by 22

Docking Analysis of Verteporfin with WW Domain of YAP

Laboratoire de Biotechnologie (MedBiotech), F. D. M. E. D. P. D. R., Kandoussi, I., Lakhlili, W., Laboratoire de Biotechnologie (MedBiotech), F. D. M. E. D. P. D. R., Taoufik, J., Laboratoire de Chimie thérapeutique Faculté de Médecine et de Pharmacie de Rabat, U. M. V. R., Ibrahimi, A., & Laboratoire de Biotechnologie (MedBiotech), F. D. M. E. D. P. D. R. (2017) · Bioinformation · doi:10.6026/97320630013237 · Cited by 20

Nestin expression is dynamically regulated in cardiomyocytes during embryogenesis

Hertig, V., Matos‐Nieves, A., Garg, V., Villeneuve, L. R., Mamarbachi, M., Caland, L., & Calderone, A. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26165 · Cited by 20

Overexpression of YAP1 induces immortalization of normal human keratinocytes by blocking clonal evolution

D’Addario, I., Abbruzzese, C., Iacono, M. L., Teson, M., Golisano, O., & Barone, V. (2010) · Histochemistry and Cell Biology · doi:10.1007/s00418-010-0728-4 · Cited by 20

Involvement of 14-3-3 protein post-translational modifications in Giardia duodenalis encystation

Lalle, M., Bavassano, C., Fratini, F., Cecchetti, S., Boisguérin, P., Crescenzi, M., & Pozio, E. (2009) · International Journal for Parasitology · doi:10.1016/j.ijpara.2009.07.010 · Cited by 20

RNA-binding protein Dnd1 inhibits epithelial–mesenchymal transition and cancer stem cell-related traits on hepatocellular carcinoma cells

Xu, W., Gong, F., Zhang, T., Chi, B., & Wang, J. (2017) · Biotechnology Letters · doi:10.1007/s10529-017-2375-5 · Cited by 20

P2RY2 Alleviates Cerebral Ischemia–Reperfusion Injury by Inhibiting YAP Phosphorylation and Reducing Mitochondrial Fission

Xue, L.-X., Chen, S., Xue, S.-X., Zhang, X., & Lian, Y. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.11.013 · Cited by 19

Yes-associated protein promotes endothelial-to-mesenchymal transition of endothelial cells in choroidal neovascularization fibrosis

Zou, R., Xu, Y., Shen, M.-Q., Zhang, X., & Yuan, Y. (2022) · International Journal of Ophthalmology · doi:10.18240/ijo.2022.05.03 · Cited by 18

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

Production of Polyclonal Antibodies in Rabbits

Hancock, D. C., & O’Reilly, N. (2005) · Humana Press eBooks · doi:10.1385/1-59259-873-0:027 · Cited by 19

The tuberous sclerosis complex subunit TBC1D7 is stabilized by Akt phosphorylation–mediated 14-3-3 binding

Madigan, J. P., Hou, F., Ye, L., Hu, J., Dong, A., Tempel, W., Yohe, M. E., Randazzo, P. A., Jenkins, L. M. M., Gottesman, M. M., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003525 · Cited by 19

The Power of Drosophila Genetics: The Discovery of the Hippo Pathway

Gokhale, R. H., & Pfleger, C. M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8910-2_1 · Cited by 21

Emerging roles for the YAP/TAZ transcriptional regulators in brain tumour pathology and targeting options

Strepkos, D., Markouli, M., Papavassiliou, K. A., Papavassiliou, A. G., & Piperi, C. (2021) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12762 · Cited by 21

Arsenic trioxide activates yes-associated protein by lysophosphatidic acid metabolism to selectively induce apoptosis of vascular smooth muscle cells

Yu, H., Hou, Z., Xiang, M., Yang, F., Ma, J., Yang, L., Ma, X., Zhou, L., He, F., Miao, M. Z., et al. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119211 · Cited by 19

Deletion of Irs2 causes reduced kidney size in mice: role for inhibition of GSK3β?

Carew, R. M., Sadagurski, M., Goldschmeding, R., Martin, F., White, M. F., & Brazil, D. P. (2010) · BMC Developmental Biology · doi:10.1186/1471-213x-10-73 · Cited by 18

YAP/TAZ: An epitome of tumorigenesis

Mukherjee, S., Warden, E. A., & Zhang, J. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217806 · Cited by 21

Synergistic effects of fluid shear stress and adhesion morphology on the apoptosis and osteogenesis of mesenchymal stem cells

Jiao, F., Xu, J., Zhao, Y., Ye, C., Sun, Q., Liu, C., & Huo, B. (2022) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.37413 · Cited by 18

Self-Sustained Regulation or Self-Perpetuating Dysregulation: ROS-dependent HIF-YAP-Notch Signaling as a Double-Edged Sword on Stem Cell Physiology and Tumorigenesis

Guo, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.862791 · Cited by 19

The Hippo pathway regulates axis formation and morphogenesis in Hydra

Brooun, M., Salvenmoser, W., Dana, C. E., Sudol, M., Steele, R. E., Hobmayer, B., & McNeill, H. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2203257119 · Cited by 17

Allosteric Modulation of the YAP/TAZ-TEAD Interaction by Palmitoylation and Small-Molecule Inhibitors

Mills, K. R., Misra, J. R., & Torabifard, H. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c07073 · Cited by 18

Functional phosphoproteomic analysis reveals cold-shock domain protein A to be a Bcr-Abl effector-regulating proliferation and transformation in chronic myeloid leukemia

Sears, D., Luong, P., Yuan, M., Nteliopoulos, G., Man, Y. K. S., Melo, J. V., & Basu, S. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.72 · Cited by 18

Stiehopus japonieus acidic mucopolysaccharide inhibits the proliferation of pancreatic cancer SW1990 cells through Hippo-YAP pathway

Li, X., Liu, Y., Zhang, C., Niu, Q., Wang, H., Che, C., Xie, M., Zhou, B., Xu, Y., Zhang, Q., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.14633 · Cited by 18

The expression of S100A8/S100A9 is inducible and regulated by the Hippo/YAP pathway in squamous cell carcinomas

Li, Y., Kong, F., Jin, C., Hu, E.-Z., Shao, Q., Liu, J., He, D., & Xiao, X. (2019) · BMC Cancer · doi:10.1186/s12885-019-5784-0 · Cited by 17

Activation of the Ca2+sensing receptor and the PKC/WNK4 downstream signaling cascade induces incorporation of ZO-2 to tight junctions and its separation from 14-3-3

Amaya, E., Alarcón, L., Martín-Tapia, D., Cuellar-Pérez, F., Cano-Cortina, M., Ortega-Olvera, J. M., Cisneros, B., Rodriguez, A. J., Gamba, G., & González‐Mariscal, L. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-09-0591 · Cited by 18

S100A7 promotes lung adenocarcinoma to squamous carcinoma transdifferentiation, and its expression is differentially regulated by the Hippo-YAP pathway in lung cancer cells

Wang, R., Li, Y., Hu, E.-Z., Kong, F., Wang, J., Liu, J., Shao, Q., Hao, Y., He, D., & Xiao, X. (2017) · Oncotarget · doi:10.18632/oncotarget.15063 · Cited by 19

Hippo in Gastric Cancer: From Signalling to Therapy

Seeneevassen, L., Dubus, P. R., Gronnier, C., & Varon, C. (2022) · Cancers · doi:10.3390/cancers14092282 · Cited by 18

The effects of dietary myo-inositol on growth and physiological, biochemical, and molecular responses in the Pacific white shrimp Litopenaeus vannamei

Yu, Q., Han, F., Huang, M., Wang, X., Qin, J. G., Chen, L., & Li, E. (2023) · Aquaculture · doi:10.1016/j.aquaculture.2023.739323 · Cited by 20

Phosphorylation‐linked complex profiling identifies assemblies required for Hippo signal integration

Uliana, F., Ciuffa, R., Mishra, R., Fossati, A., Frommelt, F., Keller, S., Mehnert, M., Birkeland, E. S., van Drogen, F., Srejić, N., et al. (2023) · Molecular Systems Biology · doi:10.15252/msb.202211024 · Cited by 21

CD43 Promotes Cells Transformation by Preventing Merlin-Mediated Contact Inhibition of Growth

Camacho‐Concha, N., Olivos-Ortiz, A., Núñez-Rivera, A., Pedroza-Saavedra, A., Gutiérrez‐Xicoténcatl, L., Rosenstein, Y., & Pedraza‐Alva, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080806 · Cited by 18

Introducing STRaNDs: shuttling transcriptional regulators that are non-DNA binding

Lu, M. M., Muers, M. R., & Lü, X. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.41 · Cited by 18

How vitamin E and its derivatives regulate tumour cells via the MAPK signalling pathway?'

Yu, Z.-Q., Wang, L.-M., & Yang, W. (2021) · Gene · doi:10.1016/j.gene.2021.145998 · Cited by 17

The pro-apoptotic protein Prostate Apoptosis Response Protein-4 (Par-4) can be activated in colon cancer cells by treatment with Src inhibitor and 5-FU

Kline, C. L. B., & Irby, R. (2011) · APOPTOSIS · doi:10.1007/s10495-011-0648-3 · Cited by 17

Increased Expression of Mcl-1 Is Required for Protection against Serum Starvation in Phosphatase and Tensin Homologue on Chromosome 10 Null Mouse Embryonic Fibroblasts, but Repression of Bim Is Favored in Human Glioblastomas

Austin, M. J., & Cook, S. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508187200 · Cited by 16

YAP1 Meets Tumor Suppression

Strano, S., & Blandino, G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.004 · Cited by 17

RASSF Signalling and DNA Damage: Monitoring the Integrity of the Genome?

Scrace, S., & O’Neill, E. E. (2012) · Molecular Biology International · doi:10.1155/2012/141732 · Cited by 18

Extrinsic induction of apoptosis and tumor suppression via the p53–Reprimo–Hippo–YAP/TAZ–p73 pathway

Takikawa, M., Nakano, A., Krishnaraj, J., Tabata, Y., Watanabe, Y., Okabe, A., Sakaguchi, Y., Fujiki, R., Mochizuki, A., Tajima, T., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2413126122 · Cited by 16

YAP increases response to Trastuzumab in HER2-positive Breast Cancer by enhancing P73-induced apoptosis

Cao, L., Yao, M., Sasano, H., Sun, P.-L., & Gao, H. (2020) · Journal of Cancer · doi:10.7150/jca.48535 · Cited by 16

YAP mediates apoptosis through failed integrin adhesion reinforcement

Shi, L., Nadjar-Boger, E., Jafarinia, H., Carlier, A., & Wolfenson, H. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113811 · Cited by 16

Cellular mechanotransduction of human osteoblasts in microgravity

Wubshet, N. H., Cai, G., Chen, S. J., Sullivan, M., Reeves, M., Mays, D., Harrison, M., Varnado, P., Yang, B. A., Arreguin-Martinez, E., et al. (2024) · npj Microgravity · doi:10.1038/s41526-024-00386-4 · Cited by 17

Transcriptome- and proteome-oriented identification of dysregulated eIF4G, STAT3, and Hippo pathways altered by PIK3CA H1047R in HER2/ER-positive breast cancer

Cheng, F., Zhao, J., Hanker, A. B., Brewer, M. R., Arteaga, C. L., & Zhao, Z. (2016) · Breast Cancer Research and Treatment · doi:10.1007/s10549-016-4011-9 · Cited by 16

The Hippo-YAP Pathway Regulates 3D Organ Formation and Homeostasis

Ishihara, E., & Nishina, H. (2018) · Cancers · doi:10.3390/cancers10040122 · Cited by 17

The role of Hippo signaling pathway in physiological cardiac hypertrophy

Gholipour, M., & Tabrizi, A. (2019) · Bioimpacts · doi:10.34172/bi.2020.32 · Cited by 15

The ε Isoform of 14-3-3 Protein Is a Component of the Prion Protein Amyloid Deposits of Gerstmann-Sträussler-Scheinker Disease

Fede, G. D., Giaccone, G., Limido, L., Mangieri, M., Suardi, S., Puoti, G., Morbin, M., Mazzoleni, G., Ghetti, B. F., & Tagliavini, F. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3180302060 · Cited by 16

Prenatal Exposure to Dietary Fat Induces Changes in the Transcriptional Factors,TEF and YAP, Which May Stimulate Differentiation of Peptide Neurons in Rat Hypothalamus

Poon, K., Mandava, S., Chen, K. S., Barson, J. R., Büschlen, S., & LEIBOWITZ, S. F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077668 · Cited by 16

Cytoplasmic YAP Expression is Associated with Prolonged Survival in Patients with Lung Adenocarcinomas and Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor Treatment

Sun, P.-L., Kim, J. E., Yoo, S. B., Kim, H., Jin, Y., Jheon, S., Kim, K., Lee, C. T., & Chung, J. H. (2014) · Annals of Surgical Oncology · doi:10.1245/s10434-014-3715-5 · Cited by 16

Variations of the 3′ Protruding Ends in Synthetic Short Interfering RNA (siRNA) Tested by Microinjection in Drosophila Embryos

Boutla, A., Delidakis, C., Livadaras, I., & Tabler, M. (2003) · Oligonucleotides · doi:10.1089/154545703322616970 · Cited by 16

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Chen, J., Lockett, A. D., Zhao, S., Huang, L., Wang, Y., Wu, W., Tang, M., Haider, S., Vélez‐Rendón, D., Khan, R., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314516 · Cited by 15

Zyxin regulates embryonic stem cell fate by modulating mechanical and biochemical signaling interface

Zhang, S., Chong, L. H., Woon, J. Y. X., Chua, T. X., Cheruba, E., Yip, A. K., Li, H., Chiam, K., & Koh, C.-G. (2023) · Communications Biology · doi:10.1038/s42003-023-04421-0 · Cited by 15

Musculoskeletal defects associated with myosin heavy chain‐embryonic loss of function are mediated by the YAP signaling pathway

Bharadwaj, A., Sharma, J., Singh, J., Kumari, M., Dargar, T., Kalita, B., & Mathew, S. J. (2023) · EMBO Molecular Medicine · doi:10.15252/emmm.202217187 · Cited by 16

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Yang, H., Yang, J., Zheng, X., Chen, T., Zhang, R., Chen, R., Cao, T., Zeng, F., & Liu, Q. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312868 · Cited by 17

Hippo circuitry and the redox modulation of hippo components in cancer cell fate decisions

Ashraf, A., & Pervaiz, S. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.10.001 · Cited by 16

Anti-Cancer Potential of Some Commonly Used Drugs

Kumari, P., & Dang, S. (2021) · Current Pharmaceutical Design · doi:10.2174/1381612827666210622104821 · Cited by 15

Ibrutinib Blocks YAP1 Activation and Reverses BRAF Inhibitor Resistance in Melanoma Cells

Misek, S. A., Newbury, P. A., Chekalin, E., Paithankar, S., Doseff, A. I., Chen, B., Gallo, K. A., & Neubig, R. R. (2021) · Molecular Pharmacology · doi:10.1124/molpharm.121.000331 · Cited by 14

Mu‐KRAS attenuates Hippo signaling pathway through PKCι to sustain the growth of pancreatic cancer

Wang, P., Zhang, H., Yang, J., Li, Z., Wang, Y., Leng, X., Ganapathy, S., Isakson, P., Chen, C., & Zhu, T. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28981 · Cited by 15

Targeting the Hippo/YAP Pathway: A Promising Approach for Cancer Therapy and Beyond

Bala, R., Madaan, R., Bedi, O., Singh, A., Taneja, A., Dwivedi, R., Figueroa‐González, G., Reyes‐Hernández, O. D., Granados, L. I. Q., Cortés, H., et al. (2025) · MedComm · doi:10.1002/mco2.70338 · Cited by 20

Spatial modeling reveals nuclear phosphorylation and subcellular shuttling of YAP upon drug-induced liver injury

Wehling, L., Keegan, L., Fernández‐Palanca, P., Hassan, R. A. R. A., Ghallab, A., Schmitt, J., Tang, Y., Marois, M. L., Roessler, S. K., Schirmacher, P., et al. (2022) · eLife · doi:10.7554/elife.78540 · Cited by 14

Yap1 promotes proliferation of transiently amplifying stress erythroid progenitors during erythroid regeneration

Hao, S., Matsui, Y., Lai, Z.-C., & Paulson, R. F. (2019) · Experimental Hematology · doi:10.1016/j.exphem.2019.11.002 · Cited by 14

PPIP5K2 promotes colorectal carcinoma pathogenesis through facilitating DNA homologous recombination repair

Cao, C., Ling, H., Han, K., Lu, X., Cai, M., Cao, J., Zhou, J., Xiang, Z., Chen, J., Li, S., et al. (2021) · Oncogene · doi:10.1038/s41388-021-02052-5 · Cited by 14

PML Surfs into HIPPO Tumor Suppressor Pathway

Strano, S., Fausti, F., Agostino, S. D., Sudol, M., & Blandino, G. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00036 · Cited by 14

The cyclin-dependent kinase 11 interacts with 14-3-3 proteins

Feng, Y., Qi, W., Martinez, J. D., & Nelson, M. A. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.078 · Cited by 14

WW-Domain Containing Protein Roles in Breast Tumorigenesis

Jamous, A., & Salah, Z. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00580 · Cited by 14

Genotype based Risk Predictors for Polycystic Ovary Syndrome in Western Saudi Arabia

Bakhashab, S. (2019) · Bioinformation · doi:10.6026/97320630015812 · Cited by 14

Gene-expression changes induced by Feline immunodeficiency virus infection differ in epithelial cells and lymphocytes

Dowling, R. J. O., & Bienzle, D. (2005) · Journal of General Virology · doi:10.1099/vir.0.80735-0 · Cited by 14

The TP53 signaling network in mammals and worms

Jolliffe, A. K., & Derry, W. B. (2012) · Briefings in Functional Genomics · doi:10.1093/bfgp/els047 · Cited by 14

Targeting YAP/TAZ–TEAD and their protein-protein interaction for precision cancer therapy

Chen, F., Su, J., Liu, Y., Zhang, Z., Li, S., Yuan, Y., & Lai, J. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118330 · Cited by 15

Genetic Alterations and Deregulation of Hippo Pathway as a Pathogenetic Mechanism in Bone and Soft Tissue Sarcoma

Salguero‐Aranda, C., Olmedo-Pelayo, J., de Álava, E., Amaral, A. T., & Díaz‐Martín, J. (2022) · Cancers · doi:10.3390/cancers14246211 · Cited by 12

WW domain binding protein 2 (WBP2) as an oncogene in breast cancer: mechanisms and therapeutic prospects—a narrative review

Liu, Y., He, E., Zhang, Y., Liu, Y., Wang, Y., Chen, S., Wu, X., Zeng, Y., & Leng, P. (2022) · Gland Surgery · doi:10.21037/gs-22-716 · Cited by 12

Sub-Cellular Localisation Studies May Spuriously Detect the Yes-Associated Protein, YAP, in Nucleoli Leading to Potentially Invalid Conclusions of Its Function

Finch‐Edmondson, M., Passman, A. M., Strauss, R. P., Yeoh, G. C., & Callus, B. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0114813 · Cited by 14

Mst1/2 Is Necessary for Satellite Cell Differentiation to Promote Muscle Regeneration

Yang, J., Wang, K., An, Y., Wu, R., Li, J., Wang, H., & Dong, Y. (2021) · Stem Cells · doi:10.1093/stmcls/sxab010 · Cited by 13

The Transcriptional Coactivator Yes-Associated Protein Drives p73 Gene-Target Specificity in Response to DNA Damage

Strano, S., Monti, O., Pediconi, N., Baccarini, A., Fontemaggi, G., Lapi, E., Mantovani, F., Damalas, A., Citro, G., Sacchi, A., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.008 · Cited by 366

Akt Inhibits DNA damage by Suppressing p73, p53, Forkhead or all Three?

Basu, S. (2003) · Cell Cycle · doi:10.4161/cc.2.2.303 · Cited by 4

Molecular Cell Article PML, YAP, and p73 Are Components of a Proapoptotic

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Yap1 Phosphorylation by c-Abl Is a Critical Step in Selective Activation of Proapoptotic Genes in Response to DNA Damage

Levy, D., Adamovich, Y., Reuven, N. B., & Shaul, Y. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.022 · Cited by 363

Identification of a mechanism that couples multisite phosphorylation of Yes-associated protein (YAP) with transcriptional coactivation and regulation of apoptosis.

Lee, K.-K., & Yonehara, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.a111.296954 · Cited by 2