Registro:

Referencias:

• Bellacosa, A., Kumar, C.C., Di Cristofano, A., Testa, J.R., Activation of AKT kinases in cancer: implications for therapeutic targeting (2005) Adv Cancer Res, 94, pp. 29-86
• Hay, N., Sonenberg, N., Upstream and downstream of mTOR (2004) Genes Dev, 18, pp. 1926-1945
• Doble, B.W., Woodgett, J.R., GSK-3: tricks of the trade for a multi-tasking kinase (2003) J Cell Sci, 116, pp. 1175-1186
• Alessi, D.R., James, S.R., Downes, C.P., Holmes, A.B., Gaffney, P.R., Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha (1997) Curr Biol, 7, pp. 261-269
• Sarbassov, D.D., Guertin, D.A., Ali, S.M., Sabatini, D.M., Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex (2005) Science, 307, pp. 1098-1101
• Conus, N.M., Hannan, K.M., Cristiano, B.E., Hemmings, B.A., Pearson, R.B., Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase (2002) J Biol Chem, 277, pp. 38021-38028
• Mahajan, K., Coppola, D., Challa, S., Fang, B., Chen, Y.A., Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates its activation (2010) PLoS One, 5, pp. e9646
• Hosoi, T., Hyoda, K., Okuma, Y., Nomura, Y., Ozawa, K., Akt up- and down-regulation in response to endoplasmic reticulum stress (2007) Brain Res, 1152, pp. 27-31
• Santi, S.A., Lee, H., The Akt isoforms are present at distinct subcellular locations (2010) Am J Physiol Cell Physiol, 298, pp. C580-C591
• Altomare, D.A., Testa, J.R., Perturbations of the AKT signaling pathway in human cancer (2005) Oncogene, 24, pp. 7455-7464
• Fayard, E., Tintignac, L.A., Baudry, A., Hemmings, B.A., Protein kinase B/Akt at a glance (2005) J Cell Sci, 118, pp. 5675-5678
• Toker, A., Yoeli-Lerner, M., Akt signaling and cancer: surviving but not moving on (2006) Cancer Res, 66, pp. 3963-3966
• Berndt, N., Yang, H., Trinczek, B., Betzi, S., Zhang, Z., The Akt activation inhibitor TCN-P inhibits Akt phosphorylation by binding to the PH domain of Akt and blocking its recruitment to the plasma membrane (2010) Cell Death Differ, 17, pp. 1795-1804
• Gaitonde, S., De, S.K., Tcherpakov, M., Dewing, A., Yuan, H., BI-69A11-mediated inhibition of AKT leads to effective regression of xenograft melanoma (2009) Pigment Cell Melanoma Res, 22, pp. 187-195
• Okuzumi, T., Ducker, G.S., Zhang, C., Aizenstein, B., Hoffman, R., Synthesis and evaluation of indazole based analog sensitive Akt inhibitors (2010) Mol Biosyst, 6, pp. 1389-1402
• Okuzumi, T., Fiedler, D., Zhang, C., Gray, D.C., Aizenstein, B., Inhibitor hijacking of Akt activation (2009) Nat Chem Biol, 5, pp. 484-493
• Kau, T.R., Schroeder, F., Ramaswamy, S., Wojciechowski, C.L., Zhao, J.J., A chemical genetic screen identifies inhibitors of regulated nuclear export of a Forkhead transcription factor in PTEN-deficient tumor cells (2003) Cancer Cell, 4, pp. 463-476
• Koomoa, D.L., Yco, L.P., Borsics, T., Wallick, C.J., Bachmann, A.S., Ornithine decarboxylase inhibition by alpha-difluoromethylornithine activates opposing signaling pathways via phosphorylation of both Akt/protein kinase B and p27Kip1 in neuroblastoma (2008) Cancer Res, 68, pp. 9825-9831
• Margalit, D.N., Romberg, L., Mets, R.B., Hebert, A.M., Mitchison, T.J., Targeting cell division: small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality (2004) Proc Natl Acad Sci U S A, 101, pp. 11821-11826
• Dunn, E.F., Fearns, R., Connor, J.H., Akt inhibitor Akt-IV blocks virus replication through an Akt-independent mechanism (2009) J Virol, 83, pp. 11665-11672
• Rutkowski, D.T., Hegde, R.S., Regulation of basal cellular physiology by the homeostatic unfolded protein response (2010) J Cell Biol, 189, pp. 783-794
• Ron, D., Walter, P., Signal integration in the endoplasmic reticulum unfolded protein response (2007) Nat Rev Mol Cell Biol, 8, pp. 519-529
• So, A.Y., de la Fuente, E., Walter, P., Shuman, M., Bernales, S., The unfolded protein response during prostate cancer development (2009) Cancer Metastasis Rev, 28, pp. 219-223
• Wouters, B.G., Koritzinsky, M., Hypoxia signalling through mTOR and the unfolded protein response in cancer (2008) Nat Rev Cancer, 8, pp. 851-864
• Bernales, S., McDonald, K.L., Walter, P., Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response (2006) PLoS Biol, 4, pp. e423
• Schroder, M., Kaufman, R.J., The mammalian unfolded protein response (2005) Annu Rev Biochem, 74, pp. 739-789
• Ni, M., Zhou, H., Wey, S., Baumeister, P., Lee, A.S., Regulation of PERK signaling and leukemic cell survival by a novel cytosolic isoform of the UPR regulator GRP78/BiP (2009) PLoS One, 4, pp. e6868
• van Huizen, R., Martindale, J.L., Gorospe, M., Holbrook, N.J., P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling (2003) J Biol Chem, 278, pp. 15558-15564
• Zhang, Y., Liu, R., Ni, M., Gill, P., Lee, A.S., Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP (2010) J Biol Chem, 285, pp. 15065-15075
• Hu, M.C., Gong, H.Y., Lin, G.H., Hu, S.Y., Chen, M.H., XBP-1, a key regulator of unfolded protein response, activates transcription of IGF1 and Akt phosphorylation in zebrafish embryonic cell line (2007) Biochem Biophys Res Commun, 359, pp. 778-783
• Ishigaki, S., Fonseca, S.G., Oslowski, C.M., Jurczyk, A., Shearstone, J.R., AATF mediates an antiapoptotic effect of the unfolded protein response through transcriptional regulation of AKT1 (2010) Cell Death Differ, 17, pp. 774-786
• Kato, H., Nakajima, S., Saito, Y., Takahashi, S., Katoh, R., mTORC1 serves ER stress-triggered apoptosis via selective activation of the IRE1-JNK pathway (2012) Cell Death Differ, 19, pp. 310-320
• Dong, L., Jiang, C.C., Thorne, R.F., Croft, A., Yang, F., Ets-1 mediates upregulation of Mcl-1 downstream of XBP-1 in human melanoma cells upon ER stress (2011) Oncogene, 30, pp. 3716-3726
• Jiang, C.C., Yang, F., Thorne, R.F., Zhu, B.K., Hersey, P., Human melanoma cells under endoplasmic reticulum stress acquire resistance to microtubule-targeting drugs through XBP-1-mediated activation of Akt (2009) Neoplasia, 11, pp. 436-447
• Hu, P., Han, Z., Couvillon, A.D., Exton, J.H., Critical role of endogenous Akt/IAPs and MEK1/ERK pathways in counteracting endoplasmic reticulum stress-induced cell death (2004) J Biol Chem, 279, pp. 49420-49429
• Deldicque, L., Bertrand, L., Patton, A., Francaux, M., Baar, K., ER stress induces anabolic resistance in muscle cells through PKB-induced blockade of mTORC1 (2011) PLoS One, 6, pp. e20993
• Qin, L., Wang, Z., Tao, L., Wang, Y., ER stress negatively regulates AKT/TSC/mTOR pathway to enhance autophagy (2010) Autophagy, 6, pp. 239-247
• Mao, W., Iwai, C., Keng, P.C., Vulapalli, R., Liang, C.S., Norepinephrine-induced oxidative stress causes PC-12 cell apoptosis by both endoplasmic reticulum stress and mitochondrial intrinsic pathway: inhibition of phosphatidylinositol 3-kinase survival pathway (2006) Am J Physiol Cell Physiol, 290, pp. C1373-C1384
• Mounir, Z., Krishnamoorthy, J.L., Wang, S., Papadopoulou, B., Campbell, S., Akt determines cell fate through inhibition of the PERK-eIF2alpha phosphorylation pathway (2011) Sci Signal, 4, pp. ra62
• Vlahos, C.J., Matter, W.F., Hui, K.Y., Brown, R.F., A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002) (1994) J Biol Chem, 269, pp. 5241-5248
• Lindsley, C.W., Zhao, Z., Leister, W.H., Robinson, R.G., Barnett, S.F., Allosteric Akt (PKB) inhibitors: discovery and SAR of isozyme selective inhibitors (2005) Bioorg Med Chem Lett, 15, pp. 761-764
• Dudek, H., Datta, S.R., Franke, T.F., Birnbaum, M.J., Yao, R., Regulation of neuronal survival by the serine-threonine protein kinase Akt (1997) Science, 275, pp. 661-665
• Wek, R.C., Jiang, H.Y., Anthony, T.G., Coping with stress: eIF2 kinases and translational control (2006) Biochem Soc Trans, 34, pp. 7-11
• Hamanaka, R.B., Bennett, B.S., Cullinan, S.B., Diehl, J.A., PERK and GCN2 contribute to eIF2alpha phosphorylation and cell cycle arrest after activation of the unfolded protein response pathway (2005) Mol Biol Cell, 16, pp. 5493-5501
• Alessi, D.R., Caudwell, F.B., Andjelkovic, M., Hemmings, B.A., Cohen, P., Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase (1996) FEBS Lett, 399, pp. 333-338
• Moritz, A., Li, Y., Guo, A., Villen, J., Wang, Y., Akt-RSK-S6 kinase signaling networks activated by oncogenic receptor tyrosine kinases (2010) Sci Signal, 3, pp. ra64
• Kane, S., Sano, H., Liu, S.C., Asara, J.M., Lane, W.S., A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain (2002) J Biol Chem, 277, pp. 22115-22118
• Karyala, P., Namsa, N.D., Chilakalapudi, D.R., Translational up-regulation and high-level protein expression from plasmid vectors by mTOR activation via different pathways in PC3 and 293T cells (2010) PLoS One, 5, pp. e14408
• Mahajan, K., Coppola, D., Rawal, B., Chen, Y.A., Lawrence, H.R., Ack1 mediated androgen receptor phosphorylation modulates radiation resistance in castration resistant prostate cancer (2012) J Biol Chem
• Sun, Q., Wu, R., Cai, S., Lin, Y., Sellers, L., Synthesis and biological evaluation of analogues of AKT (protein kinase B) inhibitor-IV (2011) J Med Chem, 54, pp. 1126-1139
• Mahajan, K., Coppola, D., Chen, Y.A., Zhu, W., Lawrence, H.R., Ack1 tyrosine kinase activation correlates with pancreatic cancer progression (2012) Am J Pathol, 180, pp. 1386-1393
• Mahajan, K., Mahajan, N.P., PI3K-independent AKT activation in cancers: A treasure trove for novel therapeutics (2012) J Cell Physiol
• Barros, L.F., Kanaseki, T., Sabirov, R., Morishima, S., Castro, J., Apoptotic and necrotic blebs in epithelial cells display similar neck diameters but different kinase dependency (2003) Cell Death Differ, 10, pp. 687-697
• Dewhirst, M.W., Cao, Y., Moeller, B., Cycling hypoxia and free radicals regulate angiogenesis and radiotherapy response (2008) Nat Rev Cancer, 8, pp. 425-437
• Kanichai, M., Ferguson, D., Prendergast, P.J., Campbell, V.A., Hypoxia promotes chondrogenesis in rat mesenchymal stem cells: a role for AKT and hypoxia-inducible factor (HIF)-1alpha (2008) J Cell Physiol, 216, pp. 708-715
• Kim, S.Y., Jeong, E., Joung, S.M., Lee, J.Y., PI3K/Akt contributes to increased expression of Toll-like receptor 4 in macrophages exposed to hypoxic stress (2012) Biochem Biophys Res Commun, 419, pp. 466-471
• Koumenis, C., Naczki, C., Koritzinsky, M., Rastani, S., Diehl, A., Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha (2002) Mol Cell Biol, 22, pp. 7405-7416
• Lemasters, J.J., DiGuiseppi, J., Nieminen, A.L., Herman, B., Blebbing, free Ca2+ and mitochondrial membrane potential preceding cell death in hepatocytes (1987) Nature, 325, pp. 78-81
• Liu, X., Shi, Y., Birnbaum, M.J., Ye, K., De Jong, R., Quantitative analysis of anti-apoptotic function of Akt in Akt1 and Akt2 double knock-out mouse embryonic fibroblast cells under normal and stressed conditions (2006) J Biol Chem, 281, pp. 31380-31388
• Nogueira, V., Park, Y., Chen, C.C., Xu, P.Z., Chen, M.L., Akt determines replicative senescence and oxidative or oncogenic premature senescence and sensitizes cells to oxidative apoptosis (2008) Cancer Cell, 14, pp. 458-470
• Huttlin, E.L., Jedrychowski, M.P., Elias, J.E., Goswami, T., Rad, R., A tissue-specific atlas of mouse protein phosphorylation and expression (2010) Cell, 143, pp. 1174-1189
• Jo, H., Lo, P.K., Li, Y., Loison, F., Green, S., Deactivation of Akt by a small molecule inhibitor targeting pleckstrin homology domain and facilitating Akt ubiquitination (2011) Proc Natl Acad Sci U S A, 108, pp. 6486-6491
• Pinner, S., Sahai, E., PDK1 regulates cancer cell motility by antagonising inhibition of ROCK1 by RhoE (2008) Nat Cell Biol, 10, pp. 127-137
• Pyrko, P., Kardosh, A., Liu, Y.T., Soriano, N., Xiong, W., Calcium-activated endoplasmic reticulum stress as a major component of tumor cell death induced by 2,5-dimethyl-celecoxib, a non-coxib analogue of celecoxib (2007) Mol Cancer Ther, 6, pp. 1262-1275
• Yacoub, A., Park, M.A., Hanna, D., Hong, Y., Mitchell, C., OSU-03012 promotes caspase-independent but PERK-, cathepsin B-, BID-, and AIF-dependent killing of transformed cells (2006) Mol Pharmacol, 70, pp. 589-603
• Zhu, J., Huang, J.W., Tseng, P.H., Yang, Y.T., Fowble, J., From the cyclooxygenase-2 inhibitor celecoxib to a novel class of 3-phosphoinositide-dependent protein kinase-1 inhibitors (2004) Cancer Res, 64, pp. 4309-4318
• Brami-Cherrier, K., Valjent, E., Garcia, M., Pages, C., Hipskind, R.A., Dopamine induces a PI3-kinase-independent activation of Akt in striatal neurons: a new route to cAMP response element-binding protein phosphorylation (2002) J Neurosci, 22, pp. 8911-8921
• Liao, Y., Hung, M.C., Physiological regulation of Akt activity and stability (2010) Am J Transl Res, 2, pp. 19-42
• Shaw, J., Kirshenbaum, L.A., Prime time for JNK-mediated Akt reactivation in hypoxia-reoxygenation (2006) Circ Res, 98, pp. 7-9
• Wei, J., Wang, W., Chopra, I., Li, H.F., Dougherty, C.J., c-Jun N-terminal kinase (JNK-1) confers protection against brief but not extended ischemia during acute myocardial infarction (2011) J Biol Chem, 286, pp. 13995-14006
• Yang, W.L., Wang, J., Chan, C.H., Lee, S.W., Campos, A.D., The E3 ligase TRAF6 regulates Akt ubiquitination and activation (2009) Science, 325, pp. 1134-1138
• Luo, H.R., Hattori, H., Hossain, M.A., Hester, L., Huang, Y., Akt as a mediator of cell death (2003) Proc Natl Acad Sci U S A, 100, pp. 11712-11717
• Matheny Jr., R.W., Adamo, M.L., Current perspectives on Akt Akt-ivation and Akt-ions (2009) Exp Biol Med (Maywood), 234, pp. 1264-1270
• Yang, W.L., Wu, C.Y., Wu, J., Lin, H.K., Regulation of Akt signaling activation by ubiquitination (2010) Cell Cycle, 9, pp. 487-497
• Hassan, I.H., Zhang, M.S., Powers, L.S., Shao, J.Q., Baltrusaitis, J., Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway (2012) J Biol Chem, 287, pp. 4679-4689
• Trujillo-Alonso, V., Maruri-Avidal, L., Arias, C.F., Lopez, S., Rotavirus infection induces the unfolded protein response of the cell and controls it through the nonstructural protein NSP3 (2011) J Virol, 85, pp. 12594-12604
• Buchkovich, N.J., Maguire, T.G., Yu, Y., Paton, A.W., Paton, J.C., Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly (2008) J Virol, 82, pp. 31-39
• Yung, H.W., Korolchuk, S., Tolkovsky, A.M., Charnock-Jones, D.S., Burton, G.J., Endoplasmic reticulum stress exacerbates ischemia-reperfusion-induced apoptosis through attenuation of Akt protein synthesis in human choriocarcinoma cells (2007) FASEB J, 21, pp. 872-884
• Yung, H.W., Charnock-Jones, D.S., Burton, G.J., Regulation of AKT phosphorylation at Ser473 and Thr308 by endoplasmic reticulum stress modulates substrate specificity in a severity dependent manner (2011) PLoS One, 6, pp. e17894
• Appenzeller-Herzog, C., Hall, M.N., Bidirectional crosstalk between endoplasmic reticulum stress and mTOR signaling (2012) Trends Cell Biol, 22, pp. 274-282
• Harding, H.P., Zhang, Y., Bertolotti, A., Zeng, H., Ron, D., Perk is essential for translational regulation and cell survival during the unfolded protein response (2000) Mol Cell, 5, pp. 897-904
• Mak, B.C., Wang, Q., Laschinger, C., Lee, W., Ron, D., Novel function of PERK as a mediator of force-induced apoptosis (2008) J Biol Chem, 283, pp. 23462-23472
• Lin, J.H., Li, H., Yasumura, D., Cohen, H.R., Zhang, C., IRE1 signaling affects cell fate during the unfolded protein response (2007) Science, 318, pp. 944-949
• Ahmed, N.N., Grimes, H.L., Bellacosa, A., Chan, T.O., Tsichlis, P.N., Transduction of interleukin-2 antiapoptotic and proliferative signals via Akt protein kinase (1997) Proc Natl Acad Sci U S A, 94, pp. 3627-3632
• Blaustein, M., Quadrana, L., Risso, G., Mata Mde, L., Pelisch, F., SF2/ASF regulates proteomic diversity by affecting the balance between translation initiation mechanisms (2009) J Cell Biochem, 107, pp. 826-833
• Blaustein, M., Pelisch, F., Tanos, T., Munoz, M.J., Wengier, D., Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT (2005) Nat Struct Mol Biol, 12, pp. 1037-1044

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------