The DOI matches its Crossref record; 45 of the 46 references it cites were found in a registry or an index.
Protein Kinase Bα/Akt1 Regulates Placental Development and Fetal Growth
Open accessAbstract
Protein kinase B alpha (PKB alpha/Akt1) is implicated in the regulation of metabolism, transcription, cell survival, angiogenesis, cell migration, growth, and tumorigenesis. Previously, it was reported that PKB alpha-deficient mice are small with increased neonatal mortality (Cho, H., Thorvaldsen, J. L., Chu, Q., Feng, F., and Birnbaum, M. J. (2001) J. Biol. Chem. 276, 38349-38352 and Chen, W. S., Xu, P. Z., Gottlob, K., Chen, M. L., Sokol, K., Shiyanova, T., Roninson, I., Wenig, W., Suzuki, R., Tobe, K., Kadowaki, T., and Hay, N. (2001) Genes Dev. 15, 2203-2208). Here we show that PKB alpha is widely expressed in placenta including all types of trophoblast and vascular endothelial cells. Pkb alpha-/- placentae display significant hypotrophy, with marked reduction of the decidual basalis and nearly complete loss of glycogen-containing cells in the spongiotrophoblast, and exhibit decreased vascularization. Pkb alpha-/- placentae also show significant reduction of phosphorylation of PKB and endothelial nitric-oxide synthase. These defects may cause placental insufficiency, fetal growth impairment, and neonatal mortality. These data represent the first evidence for the role of PKB alpha and endothelial nitricoxide synthase in regulating placental development and provide an animal model for intrauterine growth retardation.
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?
In the citing paper
“Disruption of just Akt1 causes placental and fetal growth restriction in the mouse, with a particularly severe effect on the development of the glycogen cells (592).”
From Placental Origins of Chronic Disease (2016) · cites this paper as [592]
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
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
Blume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591
TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083
Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
Fulton, D. J., Gratton, J., McCabe, T. J. D., Fontana, J. T., Fujio, Y., Walsh, K. X., Franke, T. F., Papapetropoulos, A., & Sessa, W. C. (1999) · Nature · doi:10.1038/21218 · Cited by 2,616
Cho, H., Mu, J., Kim, J. K., Thorvaldsen, J. L., Chu, Q., Crenshaw, E. B., Kaestner, K. H., Bartolomei, M. S., Shulman, G. I., & Birnbaum, M. J. (2001) · Science · doi:10.1126/science.292.5522.1728 · Cited by 1,860
Kureishi, Y., Luo, Z., Shiojima, I., Bialik, A., Fulton, D. J., Lefer, D. J., Sessa, W. C., & Walsh, K. X. (2000) · Nature Medicine · doi:10.1038/79510 · Cited by 1,438
Placental development: Lessons from mouse mutants
Rossant, J., & Cross, J. C. (2001) · Nature Reviews Genetics · doi:10.1038/35080570 · Cited by 1,299
Akt regulates growth by directly phosphorylating Tsc2
Potter, C. J., Pedraza, L. G., & Xu, T. (2002) · Nature Cell Biology · doi:10.1038/ncb840 · Cited by 959
Cho, H., Thorvaldsen, J. L., Chu, Q., Feng, F., & Birnbaum, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100462200 · Cited by 959
Research works printed but not linked: 6
- Prada, 1998, Eur. J. Clin. Nutr., 52, S21
- Brazil, 2001, TiBS, 26, 657
- Bellacosa, 1993, Oncogene, 8, 745
- Limbourg, 2002, J. Clin. Invest., 110, 1729, 10.1172/JCI0215481 · DOI
- Anthony, 2001, Society Transaction, 29, 42
- PerkinElmer Life Sciences (1997) ABI PRISM 7700 User Bulletin Number 2, PerkinElmer Life Sciences, Foster City, CA
Cited by
Sorted by citations
Defining the role of mTOR in cancer
Guertin, D. A., & Sabatini, D. M. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.05.008 · Cited by 2,833
Exploiting the PI3K/AKT Pathway for Cancer Drug Discovery
Hennessy, B. T., Smith, D. L., Ram, P. T., Lu, Y., & Mills, G. B. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1902 · Cited by 2,214
Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways
Wee, P., & Wang, Z. (2017) · Cancers · doi:10.3390/cancers9050052 · Cited by 2,027
Akt signalling in health and disease
Hers, I., Vincent, E. E., & Tavaré, J. M. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.004 · Cited by 1,268
Advances in protein kinase B signalling: AKTion on multiple fronts
Brazil, D. P., Yang, Z., & Hemmings, B. A. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.03.006 · Cited by 840
Self-citationRegulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816
“Akt3 is not expressed in muscle [4,116]”
Bhaskar, P. T., & Hay, N. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.03.020 · Cited by 798
Structure, regulation and function of PKB/AKT—a major therapeutic target
Hanada, M., Feng, J., & Hemmings, B. A. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.009 · Cited by 739
Self-citationPlacental Origins of Chronic Disease
Burton, G. J., Fowden, A. L., & Thornburg, K. L. (2016) · Physiological Reviews · doi:10.1152/physrev.00029.2015 · Cited by 717
Akt1 and Akt2 protein kinases differentially contribute to macrophage polarization
Arranz, A., Doxaki, C., Vergadi, E., de la Torre, Y. M., Vaporidi, K., Lagoudaki, E. D., Ieronymaki, E., Androulidaki, A., Venihaki, M., Margioris, A. N., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119038109 · Cited by 605
Distinct roles of Akt1 and Akt2 in regulating cell migration and epithelial–mesenchymal transition
Irie, H. Y., Pearline, R. V., Grueneberg, D. A., Hsia, M., Ravichandran, P., Kothari, N. H., Natesan, S., & Brugge, J. S. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505087 · Cited by 582
Chapter 2 PI3K/PTEN Signaling in Angiogenesis and Tumorigenesis
(2009) · Advances in Cancer Research · doi:10.1016/s0065-230x(09)02002-8 · Cited by 620
Development of Structures and Transport Functions in the Mouse Placenta
Watson, E. D., & Cross, J. C. (2005) · Physiology · doi:10.1152/physiol.00001.2005 · Cited by 580
Role for Akt3/Protein Kinase Bγ in Attainment of Normal Brain Size
Easton, R., Cho, H., Roovers, K., Shineman, D. W., Mizrahi, M., Forman, M. S., Lee, V. M. ‐., Szabolcs, M. J., de Jong, R., Oltersdorf, T., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.5.1869-1878.2005 · Cited by 551
PI3K/AKT, MAPK and AMPK signalling: protein kinases in glucose homeostasis
Schultze, S. M., Hemmings, B. A., Nießen, M., & Tschopp, O. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411002109 · Cited by 553
Self-citationBurton, G. J., Yung, H.-W., Cindrova-Davies, T., & Charnock-Jones, D. S. (2009) · Placenta · doi:10.1016/j.placenta.2008.11.003 · Cited by 502
Tschopp, O., Yang, Z.-Z., Brodbeck, D., Dummler, B. A., Hemmings-Mieszczak, M., Watanabe, T., Michaelis, T., Frahm, J., & Hemmings, B. A. (2005) · Development · doi:10.1242/dev.01864 · Cited by 426
Self-citationYung, H.-W., Calabrese, S., Hynx, D., Hemmings, B. A., Cetin, I., Charnock-Jones, D. S., & Burton, G. J. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.071193 · Cited by 388
Self-citationAkt1/protein kinase B is critical for ischemic and VEGF-mediated angiogenesis
Ackah, E. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24726 · Cited by 386
Determinants of trophoblast lineage and cell subtype specification in the mouse placenta
Simmons, D. G., & Cross, J. C. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.05.010 · Cited by 365
Protein kinase B/Akt at a glance
Fayard, E., Tintignac, L. A. J., Baudry, A., & Hemmings, B. A. (2005) · Journal of Cell Science · doi:10.1242/jcs.02724 · Cited by 336
Self-citationCritical growth factors and signalling pathways controlling human trophoblast invasion
Knfler, M. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082769mk · Cited by 330
Cattelino, A., Liebner, S., Gallini, R., Zanetti, A., Balconi, G., Corsi, A., Bianco, P., Wolburg, H., Moore, R. H., Boussadia, O., et al. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212157 · Cited by 323
Physiological roles of PKB/Akt isoforms in development and disease
Dummler, B., & Hemmings, B. A. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350231 · Cited by 316
Self-citationThe influence of the intrauterine environment on human placental development
Burton, G. J., Jauniaux, E., & Charnock-Jones, D. S. (2010) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082764gb · Cited by 307
Feng, J., Tamaskovic, R., Yang, Z., Brazil, D. P., Merlo, A., Hess, D., & Hemmings, B. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404936200 · Cited by 294
Self-citationAkt1 in Endothelial Cell and Angiogenesis
Somanath, P. R., Razorenova, O. V., Chen, J., & Byzova, T. V. (2006) · Cell Cycle · doi:10.4161/cc.5.5.2538 · Cited by 298
Dummler, B. A., Tschopp, O., Hynx, D., Yang, Z., Dirnhofer, S., & Hemmings, B. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00722-06 · Cited by 293
Self-citationCarnero, A. (2009) · Current Pharmaceutical Design · doi:10.2174/138161210789941865 · Cited by 273
Matsui, T., & Rosenzweig, A. (2004) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.11.005 · Cited by 264
Akt1 in Osteoblasts and Osteoclasts Controls Bone Remodeling
Kawamura, N., Kugimiya, F., Oshima, Y., Ohba, S., Ikeda, T., Saito, T., Shinoda, Y., Kawasaki, Y., Ogata, N., Hoshi, K., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0001058 · Cited by 259
Protein Kinase B (PKB/Akt), a Key Mediator of the PI3K Signaling Pathway
Fayard, E., Xue, G., Parcellier, A., Bozulic, L., & Hemmings, B. A. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_58 · Cited by 250
Self-citationRegulation of Placental Angiogenesis
Chen, D., & Zheng, J. J. (2013) · Microcirculation · doi:10.1111/micc.12093 · Cited by 256
Origin and characteristics of glycogen cells in the developing murine placenta
Coan, P. M., Conroy, N., Burton, G. J., & Ferguson‐Smith, A. C. (2006) · Developmental Dynamics · doi:10.1002/dvdy.20981 · Cited by 243
Nagoshi, T., Matsui, T., Aoyama, T., Leri, A., Anversa, P., Li, L., Ogawa, W., del Monte, F., Gwathmey, J. K., Grazette, L. P., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23073 · Cited by 229
Self-citationImprinted genes in the placenta – A review
Coan, P. M., Burton, G. J., & Ferguson‐Smith, A. C. (2005) · Placenta · doi:10.1016/j.placenta.2004.12.009 · Cited by 238
Genetic insights into the mechanisms of Fgf signalingPreprint
Brewer, J. R., Mazot, P., & Soriano, P. M. (2016) · Genes & Development · doi:10.1101/gad.277137.115 · Cited by 230
Yang, Z., Tschopp, O., Di‐Poï, N., Bruder, E., Baudry, A., Dummler, B. A., Wahli, W., & Hemmings, B. A. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.23.10407-10418.2005 · Cited by 219
Self-citationKaneshiro, S., Ebina, K., Shi, K., Higuchi, C., Hirao, M., OKAMOTO, M. T., Koizumi, K., Morimoto, T., Yoshikawa, H., & Hashimoto, J. (2013) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-013-0514-1 · Cited by 225
Role of nitric oxide in placental vascular development and function
Krause, B. J., Hanson, M. A., & Casanello, P. C. (2011) · Placenta · doi:10.1016/j.placenta.2011.06.025 · Cited by 220
The Loss of Glypican-3 Induces Alterations in Wnt Signaling
Song, H. H., Shi, W., Xiang, Y., & Filmus, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410090200 · Cited by 222
Regulation of VEGF-mediated angiogenesis by the Akt/PKB substrate Girdin
Kitamura, T., Asai, N., Enomoto, A., Maeda, K., Kato, T., Ishida, M., Jiang, P., Watanabe, T., Usukura, J., Kondo, T., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1695 · Cited by 211
Nadra, K., Anghel, S. I., Joye, E., Tan, N. S., Modak, S. B., Trono, D., Wahli, W., & Desvergne, B. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.3266-3281.2006 · Cited by 199
Cell Signaling Pathways Involved During Invasion and Syncytialization of Trophoblast Cells
Sk, G., Malhotra, S. S., Malik, A., Verma, S., & Chaudhary, P. (2015) · American Journal of Reproductive Immunology · doi:10.1111/aji.12436 · Cited by 196
Akt1 is critical for acute inflammation and histamine-mediated vascular leakage
Lorenzo, A. D., Fernandez-Hernando, C. F., Cirino, G., & Sessa, W. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904073106 · Cited by 191
Roles of PI3K/AKT/GSK3 Pathway Involved in Psychiatric Illnesses
Matsuda, S., Ikeda, Y., Murakami, M., Nakagawa, Y., Tsuji, A., & Kitagishi, Y. (2019) · Diseases · doi:10.3390/diseases7010022 · Cited by 196
Forbes, K. A., Westwood, M., Baker, P. N., & Aplin, J. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00035.2008 · Cited by 187
Placental phenotype and the insulin‐like growth factors: resource allocation to fetal growth
Sferruzzi-Perri, A. N., Sandovici, I., Constância, M., & Fowden, A. L. (2017) · The Journal of Physiology · doi:10.1113/jp273330 · Cited by 185
Only Akt1 Is Required for Proliferation, while Akt2 Promotes Cell Cycle Exit through p21 Binding
Héron‐Milhavet, L., Franckhauser, C., Rana, V., Berthenet, C., Fisher, D., Hemmings, B. A., Fernandez, A., & Lamb, N. J. C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00201-06 · Cited by 176
Self-citationEndothelial Akt1 mediates angiogenesis by phosphorylating multiple angiogenic substrates
Lee, M. Y., Luciano, A. K., Ackah, E., Rodríguez‐Vita, J., Bancroft, T. A., Eichmann, A., Simons, M., Kyriakides, T. R., Morales‐Ruiz, M., & Sessa, W. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408472111 · Cited by 174
Rosario, F. J., Jansson, N., Kanai, Y., Prasad, P. D., Powell, T. L., & Jansson, T. (2011) · Endocrinology · doi:10.1210/en.2010-1153 · Cited by 176
The PI3K/Akt pathway is present and functional in the preimplantation mouse embryo
Riley, J. K., Carayannopoulos, M. O., Wyman, A., Chi, M. M.-Y., Ratajczak, C. K., & Moley, K. H. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.05.033 · Cited by 173
Boland, E., Clayton‐Smith, J., Woo, V. G. H., McKee, S. A., Manson, F. D. C., Medne, L., Zackai, E. H., Swanson, E. A., FitzPatrick, D. R., Millen, K. J., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/519999 · Cited by 168
Regulation and Function of Protein Kinases and Phosphatases
Cheng, H., Qi, R. Z., Paudel, H. K., & Zhu, H. (2011) · Enzyme Research · doi:10.4061/2011/794089 · Cited by 179
The role of skeletal muscle Akt in the regulation of muscle mass and glucose homeostasis
Jaiswal, N., Gavin, M. G., Quinn, W. J., Luongo, T. S., Gelfer, R. G., Baur, J. A., & Titchenell, P. M. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.08.001 · Cited by 167
Cell survival and metastasis regulation by Akt signaling in colorectal cancer
Agarwal, E., Brattain, M. G., & Chowdhury, S. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.03.025 · Cited by 164
The IGF Axis and Placental Function
Forbes, K. A., & Westwood, M. (2008) · Hormone Research in Paediatrics · doi:10.1159/000112585 · Cited by 164
Yung, H. W., Atkinson, D., Campion‐Smith, T., Olovsson, M., Charnock‐Jones, D. S., & Burton, G. J. (2014) · The Journal of Pathology · doi:10.1002/path.4394 · Cited by 156
Endothelial FAK is required for tumour angiogenesis
Tavora, B., Batista, S., Reynolds, L. E., Jadeja, S., Robinson, S. D., Kostourou, V., Hart, I. R., Fruttiger, M., Parsons, M., & Hodivala‐Dilke, K. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000106 · Cited by 154
p53 stabilization in response to DNA damage requires Akt/PKB and DNA-PK
Boehme, K. A., Kulikov, R., & Blattner, C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703423105 · Cited by 152
Martin, K. A., Merenick, B. L., Ding, M., Fetalvero, K. M., Rzucidlo, E. M., Kozul, C. D., Brown, D. J., Chiu, H. Y., Shyu, M., Drapeau, B. L., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703914200 · Cited by 149
Calcineurin Signaling Regulates Human Islet β-Cell Survival
Soleimanpour, S. A., Crutchlow, M. F., Ferrari, A., Raum, J. C., Groff, D., Rankin, M. M., Liu, C., León, D. D. D., Naji, A., Kushner, J. A., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.154955 · Cited by 145
Protein kinase B: signalling roles and therapeutic targeting
Sale, E. M., & Sale, G. J. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7274-9 · Cited by 148
Maternal growth factor regulation of human placental development and fetal growth
Forbes, K. A., & Westwood, M. (2010) · Journal of Endocrinology · doi:10.1677/joe-10-0174 · Cited by 151
The ARE‐dependent mRNA‐destabilizing activity of BRF1 is regulated by protein kinase B
Schmidlin, M., Lu, M., Leuenberger, S. A., Stoecklin, G., Mallaun, M., Gross, B., Gherzi, R., Heß, D., Hemmings, B. A., & Moroni, C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600477 · Cited by 138
Self-citationCao, C., Huang, X., Han, Y., Wan, Y., Birnbaumer, L., Feng, G. S., Marshall, J. J., Jiang, M., & Chu, W. (2009) · Science Signaling · doi:10.1126/scisignal.2000118 · Cited by 137
Akt1 and Akt2 are required for αβ thymocyte survival and differentiation
Juntilla, M. M., Wofford, J. A., Birnbaum, M. J., Rathmell, J. C., & Koretzky, G. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705285104 · Cited by 146
Endoplasmic reticulum stress in the pathogenesis of early-onset pre-eclampsia
Burton, G. J., & Yung, H. W. (2010) · Pregnancy Hypertension · doi:10.1016/j.preghy.2010.12.002 · Cited by 133
Huang, Z., Huang, S., Song, T., Yin, Y., & Tan, C. (2021) · Advances in Nutrition · doi:10.1093/advances/nmab070 · Cited by 138
Bayascas, J. R., Wullschleger, S., Sakamoto, K., García‐Martínez, J. M., Clacher, C., Komander, D., van Aalten, D. M. F., Boini, K. M., Lang, F. J. W., Lipina, C., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02032-07 · Cited by 136
Kolahi, K. S., Valent, A. M., & Thornburg, K. L. R. (2017) · Scientific Reports · doi:10.1038/srep42941 · Cited by 130
Ain, R., Kent, L. N., & Soares, M. J. (2005) · Journal of Endocrinology · doi:10.1677/joe.1.06039 · Cited by 124
Adiponectin Inhibits Osteoclastogenesis and Bone Resorption via APPL1-mediated Suppression of Akt1
Tu, Q., Zhang, J., Dong, L., Saunders, E., Luo, E., Tang, J., & Chen, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.152405 · Cited by 122
Ericson, K., Gan, C. M., Cheong, I., Rago, C., Samuels, Y., Velculescu, V. E., Kinzler, K. W., Huso, D. L., Vogelstein, B., & Papadopoulos, N. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914018107 · Cited by 122
Uko, N. E., Güner, O. F., Matesic, D. F., & Bowen, J. P. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200224101808 · Cited by 125
Yung, H. W., Cox, M., van Patot, M. T., & Burton, G. J. (2012) · The FASEB Journal · doi:10.1096/fj.11-190082 · Cited by 112
Loss of Cited2 affects trophoblast formation and vascularization of the mouse placenta
Withington, S. L., Scott, A., Saunders, D. N., Floro, K. L., Preis, J. I., Michalicek, J., Maclean, K., Sparrow, D. B., Martínez-Barberá, J. P., & Dunwoodie, S. L. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.02.025 · Cited by 113
Potential role of Akt signaling in chronic kidney disease
Lan, A., & Du, J. (2014) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfu196 · Cited by 108
Suppression of survival signalling pathways by the phosphatase PHLPP
O’Neill, A., Niederst, M. J., & Newton, A. C. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08537.x · Cited by 107
Akt/Protein Kinase B Is Required for Lymphatic Network Formation, Remodeling, and Valve Development
Zhou, F., Chang, Z., Zhang, L., Hong, Y., Shen, B., Wang, B., Zhang, F., Lu, G., Tvorogov, D., Alitalo, K. K., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.091301 · Cited by 104
Self-citationTargeting the Akt Kinase to Modulate Survival, Invasiveness and Drug Resistance of Cancer Cells
Cassinelli, G., Zuco, V., Gatti, L., Lanzi, C., Zaffaroni, N., Colombo, D., & Perego, P. (2013) · Current Medicinal Chemistry · doi:10.2174/09298673113209990106 · Cited by 104
Regulation of PI3K effector signalling in cancer by the phosphoinositide phosphatases
Rodgers, S. J., Ferguson, D. T., Mitchell, C. A., & Ooms, L. M. (2017) · Bioscience Reports · doi:10.1042/bsr20160432 · Cited by 105
Higgins, J., Vaughan, O. R., de Liger, E. F., Fowden, A. L., & Sferruzzi-Perri, A. N. (2015) · The Journal of Physiology · doi:10.1113/jp271057 · Cited by 104
Cristofano, A. D. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.11.006 · Cited by 108
The role of Akt1 in terminal stages of endochondral bone formation: Angiogenesis and ossification
Ulici, V., Hoenselaar, K. D., Agoston, H., McErlain, D. D., Umoh, J. U., Chakrabarti, S., Holdsworth, D. W., & Beier, F. (2009) · Bone · doi:10.1016/j.bone.2009.08.003 · Cited by 101
Li, G., Anderson, R. E., Tomita, H., Adler, R., Liu, X., Zack, D. J., & Rajala, R. V. S. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0445-06.2007 · Cited by 100
Rao, G., Pierobon, M., Kim, I., Hsu, W., Deng, J., Moon, Y., Petricoin, E. F., Zhang, Y., Wang, Y., & Giaccone, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-06128-9 · Cited by 98
IGF signaling defects as causes of growth failure and IUGR
Klammt, J., Pfäffle, R. W., Werner, H., & Kieß, W. (2008) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2008.03.003 · Cited by 98
He, Z., Opland, D. M., Way, K. J., Ueki, K., Bodyak, N., Kang, P. M., Izumo, S., Kulkarni, R. N., Wang, B., Liao, R., et al. (2006) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000209500.15801.4e · Cited by 94
Krey, G., Frank, P., Shaikly, V., Barrientos, G., Russo, R. I. C., Ringel, F., Moschansky, P., Chernukhin, I. V., Metodiev, M. V., Fernández, N., et al. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0379-2 · Cited by 94
PKBα is required for adipose differentiation of mouse embryonic fibroblasts
Baudry, A., Yang, Z., & Hemmings, B. A. (2006) · Journal of Cell Science · doi:10.1242/jcs.02792 · Cited by 95
Self-citationStringer, T. P., Guerrieri, D., Vivar, C., & van Praag, H. (2015) · Translational Psychiatry · doi:10.1038/tp.2014.135 · Cited by 95
Yung, H. W., Hemberger, M., Watson, E. D., Senner, C. E., Jones, C. J. P., Kaufman, R. J., Jones, D. S., & Burton, G. J. (2012) · The Journal of Pathology · doi:10.1002/path.4068 · Cited by 91
Endocannabinoid signaling directs differentiation of trophoblast cell lineages and placentation
Sun, X., Xie, H., Yang, J., Wang, H., Bradshaw, H. B., & Dey, S. K. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010892107 · Cited by 91
Benjamin, D., Schmidlin, M., Lu, M., Gross, B., & Moroni, C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01099-06 · Cited by 91
Briest, F., & Grabowski, P. (2014) · Theranostics · doi:10.7150/thno.7851 · Cited by 96
Inman, K. E., & Downs, K. M. (2007) · genesis · doi:10.1002/dvg.20281 · Cited by 91
Activation of elastin transcription by transforming growth factor-β in human lung fibroblasts
Kuang, P., Zhang, X., Rich, C. B., Foster, J. A., Subramanian, M., & Goldstein, R. H. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00184.2006 · Cited by 83
Discovery of a novel class of AKT pleckstrin homology domain inhibitors
Mahadevan, D., Powis, G., Mash, E. A., George, B. L., Gokhale, V. M., Zhang, S., Shakalya, K., Du‐Cuny, L., Berggren, M. I., Ali, M. A., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2276 · Cited by 81
Promiscuous affairs of PKB/AKT isoforms in metabolism
Schultze, S. M., Jensen, J., Hemmings, B. A., Tschopp, O., & Nießen, M. (2011) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2010.539236 · Cited by 85
Self-citation
Metadata
- Authors
- Yang, Z.-Z., Tschopp, O., Hemmings-Mieszczak, M., Feng, J., Brodbeck, D., Perentes, E., & Hemmings, B. A.
- Affiliations
- Friedrich Miescher Institute (CH)
- Novartis (Switzerland) (CH)
- Corresponding author
- Hemmings, Brian A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-08
- Volume
- 278
- Issue
- 34
- Pages
- 32124-32131
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2131840335
- Cited by
- 384
- References
- 46
- Citations by year
- 2026: 5 · 2025: 14 · 2024: 10 · 2023: 9 · 2022: 11 · 2021: 14 · 2020: 12 · 2019: 14 · 2018: 10 · 2017: 26 · 2016: 14 · 2015: 23 · 2014: 22 · 2013: 22 · 2012: 20
- FWCI
- 17.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Novartis Pharma
- Topics
- Health Sciences › Medicine › Obstetrics and Gynecology › Pregnancy and preeclampsia studies
- Health Sciences › Medicine › Pediatrics, Perinatology and Child Health › Birth, Development, and Health
- Life Sciences › Immunology and Microbiology › Immunology › Reproductive System and Pregnancy
- Keywords
- AKT1, placental development, fetal growth, trophoblast, spongiotrophoblast, placental vascularization, endothelial nitric oxide synthase, endothelial cell proliferation, fetal growth restriction, neonatal mortality
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Embryonic and Fetal Development, Immunohistochemistry, Molecular Sequence Data, Placentation, Proto-Oncogene Proteins, Blotting, Western, Protein Serine-Threonine Kinases, DNA Primers, Mice, Knockout, Proto-Oncogene Proteins c-akt, Mice
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