The DOI matches its Crossref record; 40 of the 41 references it cites were found in a registry or an index.
Akt Phosphorylates the Yes-Associated Protein, YAP, to Induce Interaction with 14-3-3 and Attenuation of p73-Mediated Apoptosis
Open accessAbstract
We have used an affinity purification method to identify substrates of protein kinase B/Akt. One protein that associates with 14-3-3 in an Akt-dependent manner is shown here to be the Yes-associated protein (YAP), which is phosphorylated by Akt at serine 127, leading to binding to 14-3-3. Akt promotes YAP localization to the cytoplasm, resulting in loss from the nucleus where it functions as a coactivator of transcription factors including p73. p73-mediated induction of Bax expression following DNA damage requires YAP function and is attenuated by Akt phosphorylation of YAP. YAP overexpression increases, while YAP depletion decreases, p73-mediated apoptosis following DNA damage, in an Akt inhibitable manner. Akt phosphorylation of YAP may thus suppress the induction of the proapoptotic gene expression response following cellular damage.
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 cited source says what the claim attributes to it.
In the citing paper
“Akt was initially shown to phosphorylate Yap on Ser127 (13) but this finding was not confirmed by subsequent studies.”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [13]
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
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
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
Cited by
Sorted by citations
Items 701–800 of 845
Identification and functional comparison of novel alternatively spliced isoforms of human YAP
Liu, L., Zhang, J., Wang, J., Tian, Y., Wang, J., Xu, Y., Cheng, Y., Yu, M., Wang, J., Yang, Y., et al. (2023) · FEBS Open Bio · doi:10.1002/2211-5463.13618 · Cited by 2
Liang, F., Zhang, S., Zhou, W., Bi, G., Yang, X., Wang, P., Fan, S., Hu, S., Wu, C., Jiang, X., et al. (2025) · Toxicology Letters · doi:10.1016/j.toxlet.2025.111728 · Cited by 2
The molecular intersections of pulmonary fibrosis and lung cancer
Luo, B., Liu, X., Wang, S., Tong, Z., Han, Y., Tan, K., & Cao, P. (2025) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2025.105042 · Cited by 2
The Biology and Therapeutic Potential of the Src-YAP Axis in Non-Small Cell Lung Cancer (NSCLC)
Papavassiliou, K. A., & Papavassiliou, A. G. (2022) · Cancers · doi:10.3390/cancers14246178 · Cited by 2
Tolfenamic acid negatively regulates YAP and TAZ expression in human cancer cells
Kim, I., Lertpatipanpong, P., Yoon, Y., Lee, J., Hong, Y., Boonruang, K., Ryu, J., & Baek, S. J. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119556 · Cited by 2
The PI3K-AKT-mTOR Signaling Network in AML
Beagle, B. R., & Fruman, D. A. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1393-0_17 · Cited by 2
The c-Abl/YAP/p73 Apoptotic Module and the HIPPO Pathway
Reuven, N. B., & Shaul, Y. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6220-0_9 · Cited by 2
Zhang, J., Zhu, J.-S., Yang, Y.-C., Zhou, Z., Chen, W.-X., & Chen, N.-W. (2013) · European Journal of Inflammation · doi:10.1177/1721727x1301100112 · Cited by 2
Molecular Genetics of Meningioma
Smith, M. J. (2016) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0026645 · Cited by 2
Wu, Y., Ko, B., & Liou, J. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101693 · Cited by 2
Piezo1–Yap1 signalling translates tissue mechanics into regenerative cell statesPreprint
Ferreira, F., Espina, J. A., Korovesi, A. G., Ferreira, I., Tirel, Q., & Barriga, E. H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.20.677431 · Cited by 2
Zhang, S., Hong, H. I., Mak, V. C. Y., Zhou, Y., Lu, Y., Zhuang, G., & Cheung, L. W. T. (2024) · Molecular Oncology · doi:10.1002/1878-0261.13761 · Cited by 1
Parshina, E. A., Оrlov, E. E., Voronezhskaya, E. E., Martynova, N. Y., & Zaraisky, A. G. (2025) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162025601727 · Cited by 1
Silvano, S., Rick-Lenze, V. A. Z., Bagnall, J., Saravanakumar, M., Yang, X., Lea, R., Birchall, L., Jones, J. R., Davis, J. M., Sampson, J., et al. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168231 · Cited by 1
Hughes, L., Baio, J., Hasaniya, N. W. M. A., Bailey, L. L., Kim, J., Yanez, D., Austin, E., Vega, R., Rivera-Morales, P., Camberos, V., et al. (2026) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2025.1671367 · Cited by 1
Ma, P., Guo, Y. Z., Wang, L. L., & Ou, Y. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.117696 · Cited by 1
Targeting the UFL1-AKT cascade suppresses triple-negative breast cancer progression
Yang, X., Wen, Y., Ma, X., Qin, S.-Y., Liu, Y., Chen, J., Zhang, H., Goding, C. R., Cui, R., & Liu, T. (2026) · Nature Communications · doi:10.1038/s41467-026-68493-2 · Cited by 2
PRIP/PLCL deficiency activates PI3K–AKT–YAP signaling and promotes organ fibrosis
Yuan, M., Sano, T., Gao, J., Mizokami, A., & Kanematsu, T. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02717-2 · Cited by 1
Li, J., Zeng, X., Hu, E., Zhou, H., & Huang, W. (2026) · Molecular Cancer · doi:10.1186/s12943-026-02649-y · Cited by 1
YAP1 (Yes-associated protein 1, 65kDa)
Agostino, S. D., Strano, S., & Blandino, G. (2011) · Atlas of Genetics and Cytogenetics in Oncology and Haematology · doi:10.4267/2042/44893 · Cited by 1
AKT1 (v-akt murine thymoma viral oncogene homolog 1)
Etro, D., Missiroli, S., Buontempo, F., Neri, L., & Capitani, S. (2011) · Atlas of Genetics and Cytogenetics in Oncology and Haematology · doi:10.4267/2042/44725 · Cited by 1
Potential Role of Hippo-Signaling Pathway in Gastric Cancer
Ali, N., Asim, M., Asghar, R., Amin, A., & Rahman, M. S. U. (2016) · OALib · doi:10.4236/oalib.1102481 · Cited by 1
The Instructive Role of Biomaterials in Cell-Based Therapy and Tissue Engineering
Jones, R. R., Hamley, I. W., & Connon, C. J. (2014) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622055-00073 · Cited by 1
Inhibition of ULK2 Autophagic Activity by Its Association with YAP
Shin, S. H., Lee, E. J., Hyun, S. H., Park, D., & Kang, S. S. (2016) · Journal of Biology and Life Science · doi:10.5296/jbls.v8i1.10214 · Cited by 1
Retinoic acid induced specific changes in the phosphoproteome of C17 .2 neural stem cells
Zhang, C., Ge, L., Xie, H., Liu, X., Xun, C., Chen, Y., Chen, H., Lü, M., & Chen, P. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.18205
TAZ interactome analysis using nanotrap-based affinity purification–mass spectrometry
Kelebeev, J., MacKeracher, A., Miyake, T., & McDermott, J. C. (2025) · Journal of Cell Science · doi:10.1242/jcs.263527 · Cited by 1
p53, p63 and p73 Network in Breast Cancers
Leong, C. (2011) · InTech eBooks · doi:10.5772/20337 · Cited by 1
Daszczuk, P., & Prószyński, T. J. (2016) · Matters · doi:10.19185/matters.201602000035 · Cited by 1
Differentiation and Development of the Bovine Blastocyst
Negrón‐Pérez, V. M. (2017) · PhDT · Cited by 1
Hemodynamic Control of Endothelial Cell Fates in Development
Peacock, H. M., Daems, M., & Jones, E. A. V. (2021) · Cardiac and vascular biology · doi:10.1007/978-3-030-63164-2_6 · Cited by 1
Sun, Y., Chen, H., Chen, S., Xu, X., Zhang, W., & Li, Y. (2023) · Journal of Ovarian Research · doi:10.1186/s13048-023-01249-4 · Cited by 1
Irinotecano ativa a via PI3-quinase/AKT/mTOR em linhagem de adenocarcinoma de colon
Souza, K. K. (2007) · doi:10.47749/t/unicamp.2007.413273 · Cited by 1
Nguyen, V. H. (2010) · Digital Commons-TMC (Texas Medical Center) · Cited by 1
Bezuidenhout, N. (2011) · SUNScholar (Stellenbosch University) · Cited by 1
Reply: YAP is a Key Factor to Improve the Management of Cancer Treatments
Sun, P.-L., Jin, Y., & Chung, J.-H. (2017) · Annals of Surgical Oncology · doi:10.1245/s10434-017-6205-8 · Cited by 1
Amot regulates neuronal dendritic tree through Yap1Preprint
Rojek, K. O., Krzemień, J., Doleżyczek, H., Boguszewski, P. M., Kaczmarek, L., Konopka, W., Rylski, M., Jaworski, J., Holmgren, L., & Prószyński, T. J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/345264 · Cited by 1
Vasko Popa a diez años de su muerte
Prenz, J. O. (2001) · Cuadernos hispanoamericanos · Cited by 1
An ancient role for the Hippo pathway in axis formation and morphogenesisPreprint
Brooun, M., Salvenmoser, W., Dana, C. E., Sudol, M., Steele, R. E., Hobmayer, B., & McNeill, H. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.19.476962 · Cited by 1
Self-citationUliana, F., Ciuffa, R., Mishra, R. K., Fossati, A., Frommelt, F., Mehnert, M., Birkeland, E. S., Peter, M., Tapon, N., Aebersold, R. H., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.13.484137 · Cited by 1
Button, R. W., Harwood, C. A., & O’Shaughnessy, R. F. L. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.03.510591 · Cited by 1
Chow, S., Hsu, C., Yang, C., & Meir, Y. J. (2022) · Research Square · doi:10.21203/rs.3.rs-2051118/v1 · Cited by 1
Roh, J.-L., & Koch, W. M. (2014) · Springer eBooks · doi:10.1007/978-1-4614-8815-6_12
The Role of Activating Transcription Factor 3 (ATF3) in Chemotherapeutic Induced Cytotoxicity
Germain, C. S. (2011) · uO Research (University of Ottawa) · doi:10.20381/ruor-4610
Chiarini, F. (2010) · AMS Dottorato Institutional Doctoral Theses Repository (University of Bologna) · doi:10.6092/unibo/amsdottorato/2273
Role of the PY Motif Containing Protein, WBP-2 in ER, PR Signaling and Breast Tumorigenesis
Dhananjayan, S. C., & Nawaz, Z. (2007) · doi:10.21236/ada469779
On the structure-function relationship of p73
Nyman, U. (2009) · Figshare
The design and synthesis of peptidomimetic serine-based prodrugs as 14-3-3 inhibitors
Jones, E. D. (2013) · Purdue e-Pubs (Purdue University System)
Xu, J. (2012) · Digital Commons-TMC (Texas Medical Center)
p73 Affects Cell Fate and Tumorigenesis
Ramadan, S. M., Sayan, E., Oberst, A., Chikh, A., Pietroni, V., Rufini, A., Melino, G., & Bernassola, F. (2006) · Wiley eBooks · doi:10.1002/9783527619665.ch20
Cell Survival Signaling through Phosphoinositide 3‐kinase and Protein Kinase B
Scheid, M. P., & Woodgett, J. R. (2006) · Wiley eBooks · doi:10.1002/9783527619665.ch17
YAP1 and the Hippo Signaling Pathway Regulate Progenitor Proliferation
Schlegelmilch, K. (2013) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-13853
Biological Pathways in B-cell Non-Hodgkin's Lymphoma
Aggarwal, M. (2009) · Figshare
Transcriptional regulation of cell life and death decisions by p73
Muppani, N. R. (2013) · Figshare
Yes-Associated Protein (YAP) Promotes the Nuclear Import of p73
Zhang, H., & Wu, S. (2011) · Journal of Physics Conference Series · doi:10.1088/1742-6596/277/1/012050
The p53 homolog p63 modulates acute and chronic damage in irradiated salivary glands
Mitchell, G. C. (2010) · UA Campus Repository (The University of Arizona)
[The evolution of medical research: from trials to tailored therapy].
Pasini, E., Pirelli, S., Lenarda, A. D., Dioguardi, F. S., & Maseri, A. (2010) · PubMed
Castiglioni, I. (2014) · Unitn-eprints PhD (University of Trento) · doi:10.15168/11572_368889
Modulation of the Mdm2 signaling axis sensitizes triple-negative breast cancer cells to carboplatin
Tonsing-Carter, E. Y. (2014) · ProQuest Demo Repository · doi:10.7912/c2/308
Identification of novel and direct target genes of p73
Lapi, E. (2008) · Cineca Institutional Research Information System (Tor Vergata University)
Cloning and Bioinformatics Analysis of Full-Length cDNA Sequence of YAP1 Gene in Sheep
Zhou, H. (2013) · Zhongguo nongye Kexue
Hondermarck, H. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00169-8 · Cited by 1
Defining mechanisms directing YAP/TAZ-mediated tumorigenesis
Hiemer, S. E. (2016) · OpenBU (Boston University)
Regulation of FoxO Transcription Factors in Breast Cancer
Pomeranz, K. M. (2008) · Spiral (Imperial College London) · doi:10.25560/4253
TRIAD (Transcriptional Repression‐Induced Atypical Death)
Tamura, T., & Okazawa, H. (2018) · Wiley eBooks · doi:10.1002/9781119432463.ch20
The role of POPX2 in the regulation of hippo pathway
Muhammad, B. R. (2018) · doi:10.32657/10220/46579
Modulation of Endothelial Cytoskeletal Dynamics and YAP Localization by Angiogenic Factors
Tang, L. K. (2017) · OakTrust (Texas A&M University Libraries)
Expressão das moléculas da via Hippo em neoplasias mieloproliferativas
Cacemiro, M. D. C. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.60.2019.tde-23052019-090023
New Approaches for the Treatment of Triple Negative Breast Cancer
Sulaiman, A. (2019) · uO Research (University of Ottawa) · doi:10.20381/ruor-23348
Therapeutic options for progressive Meningiomas
Ming, L.-S. (2017) · Psychology and Mental Health Care · doi:10.31579/2637-8892/012
Molecular determinants of phenotype of orbital fibroblasts in thyroid eye disease
Yang, I.-H. (2019) · UCL Discovery (University College London)
Thompson, M. G., Zargar, A., Cruz‐Morales, P., de Rond, T., Chang, S., Pearson, A. N., Goyal, G., Barajas, J. F., Blake-Hedges, J. M., Phelan, R. M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.30.927608
Молекулярная биология менингиом головного мозга
Byvaltsev, V. A., Stepanov, I. A., Belykh, E. G., & Исмагиловна, Я. А. (2017) · Zhurnal «Patologicheskaia fiziologiia i eksperimental`naia terapiia» · doi:10.25557/0031-2991.2017.02.82-91
Optogenetic manipulation of YAP cellular localisation and functionPreprint
Toh, P. J. Y., Lai, J. K. H., Hermann, A., Destaing, O., Sheetz, M. P., Sudol, M., & Saunders, T. E. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.19.436118
Self-citationThe mechanobiology of the nucleus
Damato, M., & Maffia, M. (2020) · Università del Salento · doi:10.1285/i25327518v4i2p7
SPINT2 Suppresses Hippo Effector YAP and Limits Cellular Tolerance for Aneuploidy
Zhang, H. (2017) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
BAD Phosphorylation: A Novel Link between Apoptosis and Cancer
Polzien, L. (2011)
Effect of Fluid Shear Stress on Apoptosis and Osteogenesis of Mesenchymal Stem CellsPreprint
Jiao, F., Zhang, X., Ye, C., Sun, Q., Gao, Y., Liu, C., & Huo, B. (2022) · Research Square · doi:10.21203/rs.3.rs-1535410/v1
Cha, Y. J., Bae, S. J., Kim, D., Ahn, S. G., Jeong, J., Koo, J. S., Yoo, T.-K. R., Park, W. C., Lee, A., & Yoon, C. I. (2020) · doi:10.21203/rs.3.rs-77394/v1
Oren, M., & Aylon, Y. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6220-0_1
Robinson, D. N. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.726192080.793553227
Wu, Y., Ko, B., & Liou, J. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101693-1
Pan, Z. (2008) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1092090.559724
Gordon, M., El‐Kalla, M., Zhao, Y., Fiteih, Y., Law, J., Volodko, N. V., Anwar‐Mohamed, A., El‐Kadi, A. O. S., Liu, L., Odenbach, J., et al. (2014) · PLoS ONE · doi:10.1371/annotation/0ed852a0-eb39-4a28-986f-81f28d870747
Sanz‐Moreno, V. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727192580.793567342
TEAD is required for DNA repair independent of its transcriptional functionPreprint
Calses, P. C., Pham, V. C., Verschueren, E., Bakker, S. T., Haley, B., Liu, C., Chang, M. T., Kljavin, N. M., Hinkle, T. B., Zou, J., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1498950/v1
The Hippo pathway terminal effector TAZ/WWTR1 mediates oxaliplatin sensitivity in colon cancer cellsPreprint
Slaninová, V., Héron‐Milhavet, L., Robin, M., Jeanson, L., Kantar, D., Tosi, D., Bréhélin, L., Gongora, C., & Djiane, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.17.533075
Data from Proapoptotic Kinase MST2 Coordinates Signaling Crosstalk between RASSF1A, Raf-1, and Akt
Romano, D., Matallanas, D., Weitsman, G. E., Preisinger, C., Ng, T., & Kölch, W. (2023) · doi:10.1158/0008-5472.c.6501189.v1
Metadata
- Authors
- Basu, S., Totty, N. F., Irwin, M. S., Sudol, M., & Downward, J.
- Affiliations
- Cancer Research UK (GB)
- Hospital for Sick Children (CA)
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Downward, Julian
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2003-01
- Volume
- 11
- Issue
- 1
- Pages
- 11-23
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2011818472
- Cited by
- 843
- References
- 41
- Citations by year
- 2026: 19 · 2025: 26 · 2024: 41 · 2023: 43 · 2022: 43 · 2021: 51 · 2020: 46 · 2019: 33 · 2018: 47 · 2017: 48 · 2016: 58 · 2015: 41 · 2014: 47 · 2013: 41 · 2012: 26
- FWCI
- 9.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Cancer Research UK
- 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 › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
- Keywords
- Akt, YAP, protein phosphorylation, p73, apoptosis, DNA damage response, Bax expression, nuclear localization, transcriptional coactivation
- MeSH terms
- Tumor Protein p73, YAP-Signaling Proteins, Animals, Antibodies, Carrier Proteins, Cell Line, DNA-Binding Proteins, Fluorescent Dyes, Humans, Luminescent Proteins, Nuclear Proteins, Phosphoproteins, Phosphorylation, Protein Binding, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Serine, Transcription Factors, Transcription, Genetic, Tyrosine 3-Monooxygenase, Genes, Tumor Suppressor, Apoptosis, Protein Serine-Threonine Kinases, Genes, Reporter, Amino Acid Motifs, Tumor Suppressor Proteins, RNA Interference, Adaptor Proteins, Signal Transducing, 14-3-3 Proteins, Green Fluorescent Proteins, Proto-Oncogene Proteins c-akt
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