The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
AMPK modulates Hippo pathway activity to regulate energy homeostasis
Open accessAbstract
The Hippo pathway was discovered as a conserved tumour suppressor pathway restricting cell proliferation and apoptosis. However, the upstream signals that regulate the Hippo pathway in the context of organ size control and cancer prevention are largely unknown. Here, we report that glucose, the ubiquitous energy source used for ATP generation, regulates the Hippo pathway downstream effector YAP. We show that both the Hippo pathway and AMP-activated protein kinase (AMPK) were activated during glucose starvation, resulting in phosphorylation of YAP and contributing to its inactivation. We also identified glucose-transporter 3 (GLUT3) as a YAP-regulated gene involved in glucose metabolism. Together, these results demonstrate that glucose-mediated energy homeostasis is an upstream event involved in regulation of the Hippo pathway and, potentially, an oncogenic function of YAP in promoting glycolysis, thereby providing an exciting link between glucose metabolism and the Hippo pathway in tissue maintenance and cancer prevention.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“and the direct phosphorylation of YAP on Ser61/94, which is key for the interaction between Yap and Teads (100, 145).”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [145]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Endurance exercise-associated signals linked to YAP/TAZ”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as Wang et al Nature Cell Biol (2015)
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Both glucose starvation (36, 100, 145) and AMPK activators (26, 100, 145) inhibit Yap in different cell types.”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [145]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Also, because Hippo signalling responds to glucose and regulates the expression of glucose transporters (145)”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [145]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,996
Eng, J. K., McCormack, A. L., & Yates, J. R. (1994) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(94)80016-2 · Cited by 6,484
Role of YAP/TAZ in mechanotransduction
Dupont, S., Morsut, L., Aragona, M., Enzo, E., Giulitti, S., Cordenonsi, M., Zanconato, F., Le Digabel, J., Forcato, M., Bicciato, S., et al. (2011) · Nature · doi:10.1038/nature10137 · Cited by 5,979
Regulation of cancer cell metabolism
Cairns, R. A., Harris, I. S., & Mak, T. W. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2981 · Cited by 4,744
Zhao, B., Wei, X., Li, W., Udan, R. S., Yang, Q., Kim, J., Xie, J., Ikenoue, T., Yu, J., Li, L., et al. (2007) · Genes & Development · doi:10.1101/gad.1602907 · Cited by 3,092
Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600
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
Elucidation of a universal size-control mechanism in Drosophila and mammals
Dong, J., Feldmann, G., Huang, J., Wu, S., Zhang, N., Comerford, S. A., Gayyed, M. F., Anders, R. A., Maitra, A., & Pan, D. (2007) · Cell · doi:10.1016/j.cell.2007.07.019 · Cited by 2,370
The Hippo Signaling Pathway in Development and Cancer
Pan, D. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.09.011 · Cited by 2,317
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 401–500 of 550
Regulation of myocardial glucose metabolism by YAP/TAZ signaling
Kashihara, T., & Sadoshima, J. (2024) · Journal of Cardiology · doi:10.1016/j.jjcc.2024.01.002 · Cited by 7
Nuclear localization of YAP in pancreatic cancer: More players besides Hippo pathway
Xie, Y., Qin, C. Y., Zhang, X., Li, Z., Zhao, B., Li, T., Zhao, Y., Yan, Y., Shi, H., Huang, L., et al. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217864 · Cited by 7
Self-citationNon-hippo kinases: indispensable roles in YAP/TAZ signaling and implications in cancer therapy
Zhu, J., Wu, T., & Lin, Q. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08329-0 · Cited by 8
Qiao, Y., Xia, Q., Cao, X., Xu, J., Qiao, Z., Wu, L., Chen, Z., Yang, L., & Lu, X. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03043-5 · Cited by 7
Singh, P., Kaur, L., Ghose, S., Varshney, S., Jyothi, V., Ghosh, S., Kommineni, P., Shamsudheen, K. V., Scaria, V., Sivasubbu, S., et al. (2023) · Journal of Nutrition · doi:10.1016/j.tjnut.2023.08.032 · Cited by 7
Fan, Y., Han, W., Zhan, G., Li, S., Jiang, X., Xiang, S., Zhu, B., Yang, L., Hua, D., Luo, A., et al. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.09.018 · Cited by 7
Targeting the Hippo pathway to prevent radioresistance brain metastases from the lung (Review)
Taylor, J., Dubois, F., Bergot, E., & Levallet, G. (2024) · International Journal of Oncology · doi:10.3892/ijo.2024.5656 · Cited by 6
Regulation of Hippo-YAP1/TAZ pathway in metabolic dysfunction-associated steatotic liver disease
Xuan, W., Song, D., Hou, J., & Meng, X. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1505117 · Cited by 8
Wang, X., Sun, X., Zhang, X., Shen, N., Xia, J., Wang, L., & Ye, S. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110433 · Cited by 6
The anti-tumour role of ketogenic diet based on energy metabolism
Wu, J., Sun, X., Luo, H., Luo, X., & Sun, S. (2025) · Clinical Nutrition · doi:10.1016/j.clnu.2025.06.006 · Cited by 6
Yu, Y., Chu, C., Wang, K., Li, Y., Mao, Z., Hu, L., Wang, J., Yu, Y., Sun, H. X., & Chen, F. (2024) · Respiratory Research · doi:10.1186/s12931-024-02832-z · Cited by 6
Zhang, J., Zhu, X., Liu, Y., & Wu, X. (2024) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30621 · Cited by 6
Gao, T., Wang, Z., Zhou, J., Wang, D., Hou, X., Lin, X., Wang, Z., Chang, J., Liu, J., & Ren, C. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.155437 · Cited by 6
Albrecht, L. V., Green, K. J., & Dubash, A. D. (2016) · Springer eBooks · doi:10.1007/978-4-431-56033-3_14 · Cited by 6
Chen, P., Yang, B., Wu, Y., & Wang, J. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03846-z · Cited by 6
Li, S., Li, X., Yang, Y., & Wu, S. (2024) · APOPTOSIS · doi:10.1007/s10495-023-01935-0 · Cited by 5
Self-citationWang, Y., Ni, Y., Huang, Y., Fan, L., & Xi, J. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5c13349 · Cited by 5
Grudtsyna, V., Swaminathan, V., & Doostmohammadi, A. (2025) · Journal of The Royal Society Interface · doi:10.1098/rsif.2025.0490 · Cited by 5
Dey, S., Ghosh, M., & Dev, A. (2024) · Gene · doi:10.1016/j.gene.2024.149099 · Cited by 5
Soria-Lara, D. M., Gaitán-Vélez, B. V., Jiménez‐Islas, H., & Miranda‐López, R. (2019) · REVISTA BIOMÉDICA · doi:10.32776/revbiomed.v30i2.638 · Cited by 5
The roles of miRNAs’ clinical efficiencies in the colorectal cancer pathobiology: A review article
Eshghifar, N., Badrlou, E., & Pouresmaeili, F. (2020) · Human Antibodies · doi:10.3233/hab-200417 · Cited by 5
Activation of the Hippo Pathway in Rana sylvatica: Yapping Stops in Response to Anoxia
Gupta, A., & Storey, K. B. (2021) · Life · doi:10.3390/life11121422 · Cited by 5
Chen, C. G., Kapoor, A., Xie, C., Moss, A., Vadigepalli, R., Ricard‐Blum, S., & Iozzo, R. V. (2023) · Matrix Biology · doi:10.1016/j.matbio.2023.03.005 · Cited by 5
The molecular crosstalk of the hippo cascade in breast cancer: A potential central susceptibility
Parambil, S. T., Antony, G. R., Littleflower, A. B., & Subhadradevi, L. (2024) · Biochimie · doi:10.1016/j.biochi.2024.03.008 · Cited by 5
Targeting the Hippo Pathway to Improve Response to Chemotherapy
Zhao, Y., & Yang, X. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813753-6.00008-1 · Cited by 5
2015: Signaling Breakthroughs of the Year
Adler, E. M. (2016) · Science Signaling · doi:10.1126/scisignal.aad9795 · Cited by 5
The HIPPO-Thesis of Pulmonary HYPERtension
Boucherat, O., Bonnet, S., & Paulin, R. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201604-0741ed · Cited by 5
Kanhai, A. A., Sánchez‐López, E., Kuipers, T. B., van Klinken, J. B., Dijkstra, K. L., van der Veen, I., Baelde, H. J., Song, X., Pei, Y., Mei, H., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108278 · Cited by 4
Yes-associated protein plays oncogenic roles in human sporadic colorectal adenomas
Fan, L., Guo, X., Washington, M. K., Shi, J., Ness, R. M., Liu, Q., Wen, W., Huang, S., Liu, X., Cai, Q., et al. (2025) · Carcinogenesis · doi:10.1093/carcin/bgaf007 · Cited by 4
AMOTL2 mono-ubiquitination by WWP1 promotes contact inhibition by facilitating LATS activation
Hwang, D., Kim, M., Kim, S., Kwon, M. R., Kang, Y.-S., Kim, D., Kang, H. C., & Lim, D. (2021) · Life Science Alliance · doi:10.26508/lsa.202000953 · Cited by 5
Cai, X., Chen, F., Tang, H., Chao, D., Kang, R., Tang, D., & Liu, J. (2024) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2024.106646 · Cited by 4
CK2α-mediated phosphorylation of DUB3 promotes YAP1 stability and oncogenic functions
Huang, L., Wen, Y., Guo, Q., Zhang, C., Yang, X., Li, M., Liu, Y., Li, X., Tang, J., Zhou, X., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-024-07323-z · Cited by 5
Self-citationKodaka, M., Mao, F., Arimoto‐Matsuzaki, K., Kitamura, M., Xu, X., Yang, Z., Nakagawa, K., Maruyama, J., Ishii, K., Akazawa, C., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0231265 · Cited by 4
Aga, H., Soultoukis, G. A., Stadion, M., García‐Carrizo, F., Jähnert, M., Gottmann, P., Vogel, H., Schulz, T. J., & Schürmann, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042108 · Cited by 4
Khurana, P., Cox, A., Islam, B., Eckert, J. J., Willaime‐Morawek, S., Gould, J. M., Smyth, N. R., McHugh, P., & Fleming, T. P. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10490-1 · Cited by 4
An improved TEAD dominant-negative protein inhibitor to study Hippo YAP1/TAZ-dependent transcriptionPreprint
Branch, B., Yao Zong, Y. U. A. N., Cascone, M., Raimondi, F., & Iglesias‐Bartolomé, R. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.03.615022 · Cited by 4
Jahn, J., Ehlen, Q. T., Kaplan, L. D., Best, T. M., Meng, Z., & Huang, C.-Y. C. (2024) · Bioengineering · doi:10.3390/bioengineering11100972 · Cited by 3
Hexokinase 2-driven aerobic glycolysis modulates YAP1 in placental trophoblast development
Zhao, C., Zhou, H., Wang, P., Zhang, S., Lin, X., Pan, Y., & Zhu, H. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167872 · Cited by 3
Cellular mechanometabolism: stimuli and implications
Ortiz, I., Lopez, S., Kondapaneni, R. V., Hernández, J. A., Boone, K., & Reinhart‐King, C. A. (2026) · EMBO Reports · doi:10.1038/s44319-026-00795-4 · Cited by 3
YAP upregulates AMPKα1 to induce cancer cell senescence
Zhan, Y., Wu, G., Fan, X., Fu, Z., Ni, Y., Sun, B., Chen, H., Chen, T., & Wang, X. (2024) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2024.106559 · Cited by 3
Gerardo, H., Oliveira, P. J., Cavadas, C., Grãos, M., & Teixeira, J. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167678 · Cited by 4
Transient activation of YAP/TAZ confers resistance to morusin-induced apoptosis
Lee, H., Cho, S. W., Cha, H. S., Tae, K., & Choi, C. Y. (2025) · BMC Molecular and Cell Biology · doi:10.1186/s12860-025-00531-1 · Cited by 4
Energy crisis and the Hippo pathway
Wang, W., Li, X., & Chen, J. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1046788 · Cited by 3
Self-citationMechanisms of Hippo pathway in the pancreatic cancer
Xie, R., & Chen, R. (2020) · Journal of Pancreatology · doi:10.1097/jp9.0000000000000041 · Cited by 4
Hippo: A New Hub for Atherosclerotic Disease
Liu, X.-Y., Zhou, K., Tian, K.-J., Yan, B., Ren, Z., Zhou, Z., Xiong, W., & Jiang, Z. (2022) · Current Pharmaceutical Design · doi:10.2174/1381612828666220428090540 · Cited by 3
Krasniqi, E., Lisa, F. S. D., Benedetto, A. D., Barba, M., Pizzuti, L., Filomeno, L., Ercolani, C., Tinari, N., Grassadonia, A., Santini, D., et al. (2022) · Cancers · doi:10.3390/cancers14194835 · Cited by 3
Jia, Y.-S., Yang, L., Zhu, Y.-Q., & Ma, C. (2023) · PubMed Central · Cited by 3
LATS in cancer repression: Extracting its role in hippo pathway and beyond
Akhtar, S. (2023) · Gene Reports · doi:10.1016/j.genrep.2023.101826 · Cited by 5
Identification of BRCC3 and BRCA1 as Regulators of TAZ Stability and Activity
Sberna, S., Lopez-Hernandez, A., Biancotto, C., Motta, L., Andronache, A., Verhoef, L. G. G. C., Cagánová, M., & Campaner, S. (2023) · Cells · doi:10.3390/cells12202431 · Cited by 3
RAMP1 Protects Hepatocytes against Ischemia-reperfusion Injury by Inhibiting the ERK/YAP Pathway
Tang, Y., Yuan, Z., Lu, X., Song, Y., Zhu, S., Qiu, C., Zhang, Q., Fu, B., Jia, C., & Li, H. (2024) · Journal of Clinical and Translational Hepatology · doi:10.14218/jcth.2023.00339 · Cited by 3
The immunometabolic function of VGLL3 and female-biased autoimmunity
Kennicott, K., & Liang, Y. (2024) · Immunometabolism · doi:10.1097/in9.0000000000000041 · Cited by 2
Haripriya, E., Hemalatha, K., Matada, G. S. P., Pal, R., Das, P. K., Sk, M. D. A., Mounika, S., Viji, M. P., Aayishamma, I., & Jayashree, K. R. (2024) · Molecular Diversity · doi:10.1007/s11030-024-11009-1 · Cited by 3
Metabolic Pathways of Eukaryotes and Connection to Cell Mechanics
Mierke, C. T. (2020) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-030-58532-7_17 · Cited by 2
MST3 Regulates AMPK and YAP-Hippo Signaling in Cell Models Relevant to Renal Fibrosis
Chan, C.-H., Lu, T., Bao, B., Chu, P.-C., Chen, Y.-K., Syu, S.-L., Jeng, W. Y., & Lu, T. (2025) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2025.023 · Cited by 2
Epithelial-Mesenchymal Transition Activates YAP to Drive Malignant Progression and Immune Evasion
Huang, X., Zhang, M., Pearce, A. D., Gibbons, M. D., Jin, D., Li, L., Hu, D., Liu, R., Yu, M., Tan, M., et al. (2025) · Cancers · doi:10.3390/cancers17172767 · Cited by 2
Fu, L., Liao, W., Tan, Y., Lin, H., Ye, K., Zhou, X., Lin, M., Huang, K., Chen, M., Wei, J., et al. (2025) · Advanced Science · doi:10.1002/advs.202506367 · Cited by 3
Self-citationLi, Y., Tang, J., Wu, X., & Zhang, H. (2025) · International Journal of Cancer · doi:10.1002/ijc.70180 · Cited by 2
Glutamine synthetase modulates YAP activation by stabilizing LATS under glutamine homeostasis
Li, S., Ling, T., Wang, Y., Shi, J., Wang, Q., Lv, J., Li, J., Liu, Y., Zhang, Y., Liu, C., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116620 · Cited by 2
Self-citationFeng, R., Tuerhong, X., Cai, Y., & Aihaiti, Y. (2026) · Experimental Gerontology · doi:10.1016/j.exger.2026.113058 · Cited by 2
Hsieh, M.-Y., Yang, C.-C., Hsu, W.-J., Liu, Z., Lu, H.-Y., Chiang, M.-C., Huang, C.-J., Liao, C.-Y., Lin, C.-W., & Shueng, P. (2026) · Translational Oncology · doi:10.1016/j.tranon.2026.102700 · Cited by 2
Promotion of breast cancer by the DNPH1 enzyme
Oh, S., Sui, Y., Shin, S., & Janknecht, R. (2026) · iScience · doi:10.1016/j.isci.2026.115227 · Cited by 2
Li, S., Ma, J. G., Ma, C., Song, Y., Chang, L., & Huo, B. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1791005 · Cited by 2
Yamazaki, Y., Harada, S., & Tokuyama, S. (2018) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.17-00223-4 · Cited by 2
Aliakbarian, M., Khodashahi, R., Tavakkoli, M., Ashrafzadeh, K., Rahimi, H., Khaleghi, E., Ghayour‐Mobarhan, M., & Arjmand, M. (2023) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266253222231011102151 · Cited by 2
ImmunoMet Oncogenesis: A New Concept to Understand the Molecular Drivers of Cancer
Sirajee, R., Khatib, S. E., Dieleman, L. A., Salla, M., & Baksh, S. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14051620 · Cited by 2
Križanac, A.-M., Reimer, C., Heise, J., Liu, Z., Pryce, J. E., Bennewitz, J., Thaller, G. E., Falker‐Gieske, C., & Tetens, J. (2025) · Journal of Dairy Science · doi:10.3168/jds.2025-26328 · Cited by 2
Huang, Y., Yang, F., Zhou, T., & Xie, S. (2020) · PubMed Central · doi:10.3785/j.issn.1008-9292.2020.02.23 · Cited by 2
The Role of Hippo Signaling in Intestinal Homeostasis
Ma, X., & Shah, Y. M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00005-0 · Cited by 2
Fatoki, T. H., Ibraheem, O., Abolaji, A. O., & Sanni, D. M. (2020) · Nova Biotechnologica et Chimica · doi:10.36547/nbc.v19i1.576 · Cited by 2
Characterization of ATG8-family protein phosphorylation by Phos-tag gel for autophagy study
Seo, G., & Wang, W. (2024) · STAR Protocols · doi:10.1016/j.xpro.2024.102872 · Cited by 1
Self-citationWu, C., Zhu, H., Zhang, Y., Ding, L., & Wang, J. (2024) · PLoS ONE · doi:10.1371/journal.pone.0290753 · Cited by 1
Gill, M. K., Song, S., Christova, T. Y., & Attisano, L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167810 · Cited by 1
AMPK Signaling Regulates Epithelioid Hemangioendothelioma Cell Growth
Kanai, R., McMullan, S., Baniya, P., Dai, R. S., Norton, E., Lasher, K., Purello, C. T., Seavey, C. N., Rubin, B. P., & Lamar, J. M. (2025) · Cancers · doi:10.3390/cancers17172889 · Cited by 2
Irg1l regulates neuromast size via metabolic reprogramming to promote supporting cell proliferation
Wang, X., Shi, R., Xiang, Y., Gao, Y., Wan, G., Sun, S., & Liu, D. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202501122 · Cited by 1
Phosphatase PPP1CC Regulates the First Lineage Segregation by GAS5 in Mouse Preimplantation Embryos
Wang, J., Zhang, Y., Wu, L., Xie, H., Yang, G., Zhang, Y., Huang, C., Chou, S., Li, X., Liu, Z. H., et al. (2025) · Cell Proliferation · doi:10.1111/cpr.70155 · Cited by 1
Self-citationGuo, Z., Jiang, H., Wang, X., Xuan, K., Zhong, H., Liu, C., Zhang, M., Li, Z., Huang, W., & Sun, Y. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03013-1 · Cited by 1
Ren, X., Xie, T., Liu, L., Jin, X., & Zhang, M. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1765361 · Cited by 1
Transcriptional reprogramming in fused cells is triggered by plasma-membrane diminutionPreprint
Feliciano, D., Espinosa-Medina, I., Weigel, A. V., Milano, K. M., Tang, Z., Lee, T., Kliman, H. J., Guller, S. M., Ott, C. M., & Lippincott‐Schwartz, J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/832378 · Cited by 1
Rozycki, M. (2015) · TSpace (University of Toronto)
The Role of Hippo Pathway in Mitosis and Cancer
Chen, X. (2018) · DigitalCommons@UNMC
Mengjie, L. I., Li, C., Song, S., Xu, X., & Zhou, G. (2018) · Frontiers of Agricultural Science and Engineering · doi:10.15302/j-fase-2018206
Autophagic Regulation of Cardiomyocyte Survival and Heart Regeneration
Aki, T., Noritake, K., Unuma, K., & Uemura, K. (2018) · Stem cell biology and regenerative medicine · doi:10.1007/978-3-319-98146-8_7
The role of POPX2 in the regulation of hippo pathway
Muhammad, B. R. (2018) · doi:10.32657/10220/46579
Identification and Characterization of Novel Upstream Regulators of the Hippo Signalling Pathway
Heidaryarash, E. (2018) · TSpace (University of Toronto)
[Establishment of a mice model with liver-specific AMP-activated protein kinase gene knockout].
Tang, X., Kong, Q., Jiang, Y., & Jing, J. (2017) · PubMed Central · doi:10.7507/1001-5515.201703025
Hanumantharao, S. N. (2020) · Digital Commons - Michigan Tech (Michigan Technological University) · doi:10.37099/mtu.dc.etdr/1088
Cao, M., Zhang, W.-L., Yu, X., Wu, J., Qiao, X., Huang, M.-C., Wang, K., Wu, J., Tang, Y.-J., Jiang, J., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02112-4
RetractedLa guerra más salvaje: la invasión japonesa de China
Meseguer, X. C. I. (2010) · Clío: Revista de historia
La Universidad, institución sin edad
Lobato, E. P. (2005) · Sesenta y más
Lipoxin Alleviates Diabetic Vascular Calcification via the YAP PathwayPreprint
Han, B., Yang, M., Liu, Q., Wang, G., Ma, X., Liu, D., Huang, X., Wang, X., Zhang, R., Hou, J., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-1179483/v1
DeMali, K. A., & Campbell, H. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727215210.793538385
Cao, M., Zhang, W., Yu, X., Wu, J., Qiao, X., Huang, M.-C., Wang, K., Wu, J., Tang, Y., Jiang, J., et al. (2020) · Research Square · doi:10.21203/rs.3.rs-23980/v1
Effect of CLN3-loss-of-function on cellular metabolism and signalling
Więciorek-Płuciennik, K. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9277
Smorodina, E., Tao, F., Qing, R., et al. (2022) · QRB Discovery · doi:10.1017/qrd.2022.6.pr4
Smorodina, E., Tao, F., Qing, R., et al. (2022) · QRB Discovery · doi:10.1017/qrd.2022.6.pr2
Smorodina, E., Tao, F., Qing, R., et al. (2022) · QRB Discovery · doi:10.1017/qrd.2022.6.pr1
Smorodina, E., Tao, F., Qing, R., et al. (2022) · QRB Discovery · doi:10.1017/qrd.2022.6.pr3
Metadata
- Authors
- Wang, W., Xiao, Z.-D., Li, X., Aziz, K. E., Gan, B., Johnson, R. L., & Chen, J.
- Affiliations
- The University of Texas System (US)
- The University of Texas MD Anderson Cancer Center (US)
- Corresponding author
- Chen, Junjie
- Venue
- Nature Cell Biology
- Published
- 2015-03-09
- Volume
- 17
- Issue
- 4
- Pages
- 490-499
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC4380807
- OpenAlex
- W2020511240
- Cited by
- 549
- References
- 40
- Citations by year
- 2026: 31 · 2025: 51 · 2024: 57 · 2023: 40 · 2022: 53 · 2021: 55 · 2020: 72 · 2019: 43 · 2018: 52 · 2017: 41 · 2016: 33 · 2015: 19
- FWCI
- 25.72
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute (CA 016672, R01CA089239, R01CA092312, R01CA181196, P30CA016672)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK102611)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- AMPK, Hippo signaling pathway, YAP, energy homeostasis, glucose metabolism, glucose deprivation, GLUT3, YAP phosphorylation, organ size control, tumor suppression, glycolysis, cancer prevention
- MeSH terms
- Hippo Signaling Pathway, YAP-Signaling Proteins, Animals, Colonic Neoplasms, Energy Metabolism, Enzyme Activation, Female, Glucose, Glycolysis, HeLa Cells, Humans, Liver Neoplasms, Mice, Inbred C57BL, Phosphoproteins, Phosphorylation, Starvation, Transcription, Genetic, Protein Serine-Threonine Kinases, Cell Cycle Proteins, rho GTP-Binding Proteins, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, Glucose Transporter Type 3, Mice, AMP-Activated Protein Kinases, HEK293 Cells
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
