Eukaryotic elongation factor 2 kinase as a drug target in cancer, and in cardiovascular and neurodegenerative diseases
Open accessAbstract
Eukaryotic elongation factor 2 kinase (eEF2K) is an unusual protein kinase that regulates the elongation stage of protein synthesis by phosphorylating and inhibiting its only known substrate, eEF2. Elongation is a highly energy-consuming process, and eEF2K activity is tightly regulated by several signaling pathways. Regulating translation elongation can modulate the cellular energy demand and may also control the expression of specific proteins. Growing evidence links eEF2K to a range of human diseases, including cardiovascular conditions (atherosclerosis, via macrophage survival) and pulmonary arterial hypertension, as well as solid tumors, where eEF2K appears to play contrasting roles depending on tumor type and stage. eEF2K is also involved in neurological disorders and may be a valuable target in treating depression and certain neurodegenerative diseases. Because eEF2K is not required for mammalian development or cell viability, inhibiting its function may not elicit serious side effects, while the fact that it is an atypical kinase and quite distinct from the vast majority of other mammalian kinases suggests the possibility to develop it into compounds that inhibit eEF2K without affecting other important protein kinases. Further research is needed to explore these possibilities and there is an urgent need to identify and characterize potent and specific small-molecule inhibitors of eEF2K. In this article we review the recent evidence concerning the role of eEF2K in human diseases as well as the progress in developing small-molecule inhibitors of this enzyme.
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
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?
eEF2K signaling intersects with excitation-inhibition balance and circuit-level plasticity, suggesting strong synergy with circuit-specific interventions.
“eEF2K signaling intersects with excitation inhibition balance and circuit level plasticity, suggesting strong synergy with circuit specific interventions [159,160,164].”
From Synaptic Plasticity—Intrinsic Excitability and Antidepressant Discovery (2026) · cites this paper as [160]
The “Neurological roles of eEF2K” section links eEF2K to synaptic plasticity, altered brain activation in mutant mice, and a neuronal response to a GABA-receptor antagonist (page unavailable in our copy). It does not establish an effect on excitation–inhibition balance or discuss synergy with circuit-specific interventions; the latter appears to be the citing authors’ inference. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAll available eEF2K compounds remain experimental, with unresolved issues in kinase selectivity, brain exposure, and chronic tolerability.
“Despite consistent neuroprotective- and plasticity-enhancing effects across preclinical disease models, all available compounds remain experimental, with unresolved issues in kinase selectivity, brain exposure, and chronic tolerability [159,160,161].”
From Synaptic Plasticity—Intrinsic Excitability and Antidepressant Discovery (2026) · cites this paper as [160]
The “Inhibitors of eEF2K” section describes selectivity and cellular-effectiveness problems, and the Conclusion calls for better inhibitors for preclinical studies. These passages support the compounds’ experimental status, but our copy does not assess brain exposure or chronic tolerability. Page numbers were not supplied. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566 · see citing works
Specificity and mechanism of action of some commonly used protein kinase inhibitors.
Davies, S., Reddy, H., Caivano, M., & Cohen, P. (2000) · Biochemical Journal · doi:10.1042/bj3510095 · Cited by 3,164 · see citing works
NMDA receptor blockade at rest triggers rapid behavioural antidepressant responses
Autry, A. E., Adachi, M., Nosyreva, E., Na, E. S., Los, M. F., Cheng, P.-F., Kavalali, E. T., & Monteggia, L. M. (2011) · Nature · doi:10.1038/nature10130 · Cited by 1,926 · see citing works
Specificity and mechanism of action of some commonly used protein kinase inhibitors
Davies, S., Reddy, H., Caivano, M., & Cohen, P. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510095 · Cited by 1,618 · see citing works
Translational control of long-lasting synaptic plasticity and memory
Costa-Mattioli, M., Sossin, W. S., Klann, E., & Sonenberg, N. (2009) · Neuron · doi:10.1016/j.neuron.2008.10.055 · Cited by 944 · see citing works
Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase
Wang, X.-M., Li, W., Williams, M. R., Terada, N., Alessi, D., & Proud, C. G. (2001) · EMBO Journal · doi:10.1093/emboj/20.16.4370 · Cited by 862 · see citing works
Self-citationSignalling to translation: How signal transduction pathways control the protein synthetic machinery
Proud, C. G. (2007) · Biochemical Journal · doi:10.1042/bj20070024 · Cited by 520 · see citing works
Park, S., Park, J. M., Kim, S., Kim, J.-A., Shepherd, J. D., Smith-Hicks, C. L., Chowdhury, S., Kaufmann, W., Kuhl, D., Ryazanov, A. G., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.05.023 · Cited by 516 · see citing works
Horman, S., Browne, G., Krause, U., Patel, J., Vertommen, D., Bertrand, L., Lavoinne, A., Hue, L., Proud, C. G., & Rider, M. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01077-1 · Cited by 440 · see citing works
Self-citationThe eEF2 Kinase Confers Resistance to Nutrient Deprivation by Blocking Translation Elongation
Leprivier, G., Remke, M., Rotblat, B., Dubuc, A. M., Mateo, A.-R. F., Kool, M., Agnihotri, S., El-Naggar, A. M., Yu, B., Somasekharan, S. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.055 · Cited by 412 · see citing works
Self-citationBrowne, G. J., Finn, S. G., & Proud, C. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309773200 · Cited by 353 · see citing works
Terai, K., Hiramoto, Y., Masaki, M., Sugiyama, S., Kuroda, T., Hori, M., Kawase, I., & Hirota, H. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9554-9575.2005 · Cited by 351 · see citing works
Making synaptic plasticity and memory last: mechanisms of translational regulationPreprint
Richter, J. D., & Klann, E. (2009) · Genes & Development · doi:10.1101/gad.1735809 · Cited by 345 · see citing works
BEUGNET, A., TEE, A. R., TAYLOR, P. M., & PROUD, C. G. (2003) · Biochemical Journal · doi:10.1042/bj20021266 · Cited by 307 · see citing works
Self-citationmTORC1-mediated translational elongation limits intestinal tumour initiation and growth
Faller, W. J., Jackson, T. J., Knight, J. R. P., Ridgway, R. A., Jamieson, T. J., Karim, S. A., Jones, C., Radulescu, S., Huels, D. J., Myant, K., et al. (2014) · Nature · doi:10.1038/nature13896 · Cited by 302 · see citing works
Functional properties of phosphorylated elongation factor 2
CARLBERG, U., NILSSON, A., & Nygârd, O. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19169.x · Cited by 287 · see citing works
AMP-activated protein kinase: maintaining energy homeostasis at the cellular and whole-body levels
Hardie, D. G. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161148 · Cited by 281 · see citing works
Yamaguchi, H. Q., Matsushita, M., Nairn, A. C., & Kuriyan, J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00256-8 · Cited by 279 · see citing works
Browne, G. J., & Proud, C. G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.2986-2997.2004 · Cited by 256 · see citing works
Self-citationmTORC1 signaling controls multiple steps in ribosome biogenesis
Iadevaia, V., Liu, R., & Proud, C. G. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.08.004 · Cited by 248 · see citing works
Self-citationConnolly, E., Braunstein, S., Formenti, S., & Schneider, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3955-3965.2006 · Cited by 233 · see citing works
Ma, T., Chen, Y., Vingtdeux, V., Zhao, H., Viollet, B., Marambaud, P., & Klann, E. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1694-14.2014 · Cited by 191 · see citing works
Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles
Kenney, J. W., Moore, C. E., Xuemin, W., & Proud, C. G. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.04.003 · Cited by 182 · see citing works
Self-citationAlpha-kinases: a new class of protein kinases with a novel catalytic domain
Ryazanov, A. G., Pavur, K. S., & Dorovkov, M. V. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80006-2 · Cited by 179 · see citing works
Alpha-kinases: analysis of the family and comparison with conventional protein kinases
Drennan, D., & Ryazanov, A. G. (2003) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(03)00060-9 · Cited by 134 · see citing works
Purification of a Hepatic S6 Kinase from Cycloheximide-treated Rats
Price, D. J., Nemenoff, R. A., & Avruch, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80075-8 · Cited by 128 · see citing works
Tekedereli, İ., Alpay, S. N., Tavares, C. D. J., Cobanoglu, Z. E., Kaoud, T. S., Şahin, İ. H., Sood, A. K., Lopez‐Berestein, G., Dalby, K. N., & Özpolat, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041171 · Cited by 117 · see citing works
Chen, Z., Gopalakrishnan, S. M., Bui, M.-H., Soni, N. B., Warrior, U., Johnson, E. F., Donnelly, J. B., & Glaser, K. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.301291 · Cited by 117 · see citing works
The alpha-kinase family: an exceptional branch on the protein kinase tree
Middelbeek, J., Clark, K., Venselaar, H., Huynen, M. A., & van Leeuwen, F. N. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0215-z · Cited by 117 · see citing works
Liu, J. C., Voisin, V., Wang, S., Wang, D., Jones, R. A., Datti, A., Uehling, D., Al‐awar, R., Egan, S. E., Bader, G. D., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201404402 · Cited by 109 · see citing works
Wang, X., da Mota, S. R., Liu, R., Moore, C. E., Xie, J., Lanucara, F., Agarwala, U., Ruys, S. P. D., Vertommen, D., Rider, M. H., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01035-14 · Cited by 100 · see citing works
Self-citationHeise, C., Gardoni, F., Culotta, L., di Luca, M., Verpelli, C., & Sala, C. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00035 · Cited by 99 · see citing works
Walden, W. E., & Thach, R. E. (1986) · Biochemistry · doi:10.1021/bi00356a030 · Cited by 96 · see citing works
Hundal, R., Salh, B. S., Schrader, J. W., et al. (2001) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)30282-0 · Cited by 95 · see citing works
Xie, C., Liu, X., Sham, K. W. Y., Lai, J. M. Y., & Cheng, C. H. K. (2014) · Autophagy · doi:10.4161/auto.29164 · Cited by 94 · see citing works
Gschwendt, M., Kittstein, W., & Marks, F. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80121-5 · Cited by 93 · see citing works
Arora, S., Yang, J., Kinzy, T. G., Utsumi, R., Okamoto, T., Kitayama, T., Ortiz, P. A., & Hait, W. N. (2003) · PubMed · Cited by 92 · see citing works
Kruiswijk, F., Yuniati, L., Magliozzi, R., Low, T. Y., Lim, R., Bolder, R., Mohammed, S., Proud, C. G., Heck, A. J. R., Pagano, M., et al. (2012) · Science Signaling · doi:10.1126/scisignal.2002718 · Cited by 90 · see citing works
Self-citationEdupuganti, R., Wang, Q., Tavares, C. D. J., Chitjian, C., Bachman, J. L., Ren, P. Y., Anslyn, E. V., & Dalby, K. N. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.06.050 · Cited by 81 · see citing works
Elongation Factor 2 Kinase Is Regulated by Proline Hydroxylation and Protects Cells during Hypoxia
Moore, C. E., Mikolajek, H., da Mota, S. R., Xuemin, W., Kenney, J. W., Werner, J. M., & Proud, C. G. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01457-14 · Cited by 66 · see citing works
Self-citationInhibition of eEF2-K by thieno[2,3-b]pyridine analogues
Lockman, J. W., Reeder, M. D., Suzuki, K., Ostanin, K., Hoff, R., Bhoite, L. T., Austin, H., Baichwal, V. R., & Willardsen, J. A. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.02.005 · Cited by 65 · see citing works
Cho, S. I., Koketsu, M., Ishihara, H., Matsushita, M., Nairn, A. C., Fukazawa, H., & Uehara, Y. (2000) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(00)00061-1 · Cited by 63 · see citing works
Impaired associative taste learning and abnormal brain activation in kinase-defective eEF2K micePreprint
Gildish, I., Manor, D., David, O., Sharma, V. K., Williams, D., Agarwala, U., Wang, X., Kenney, J. W., Proud, C. G., & Rosenblum, K. (2012) · Learning & Memory · doi:10.1101/lm.023937.111 · Cited by 62 · see citing works
Self-citationWang, N., Feng, Y., Tan, H., et al. (2015) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2015.02.025 · Cited by 62 · see citing works
Tavares, C. D. J., O’Brien, J. P., Abramczyk, O., Devkota, A. K., Shores, K. S., Ferguson, S. B., Kaoud, T. S., Warthaka, M., Marshall, K., Keller, K. M., et al. (2012) · Biochemistry · doi:10.1021/bi201788e · Cited by 61 · see citing works
Hori, H., Nagasawa, H., Ishibashi, M., Uto, Y., Hirata, A., Saijo, K., Ohkura, K., Kirk, K. L., & Uehara, Y. (2002) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(02)00160-8 · Cited by 60 · see citing works
Regulation of Elongation Factor-2 Kinase by pH
Dorovkov, M. V., Pavur, K. S., Petrov, A. N., & Ryazanov, A. G. (2002) · Biochemistry · doi:10.1021/bi026494p · Cited by 59 · see citing works
Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase
Ruys, S. P. D., Wang, X., Smith, E. M., Herinckx, G., Hussain, N., Rider, M. H., Vertommen, D., & Proud, C. G. (2012) · Biochemical Journal · doi:10.1042/bj20111530 · Cited by 59 · see citing works
Self-citationDevkota, A. K., Tavares, C. D. J., Warthaka, M., Abramczyk, O., Marshall, K., Kaoud, T. S., Görgülü, K., Özpolat, B., & Dalby, K. N. (2012) · Biochemistry · doi:10.1021/bi201787p · Cited by 58 · see citing works
Activity-Dependent Augmentation of Spontaneous Neurotransmission during Endoplasmic Reticulum Stress
Nosyreva, E. D., & Kavalali, E. T. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5358-09.2010 · Cited by 58 · see citing works
Crystal Structure of the α-Kinase Domain of Dictyostelium Myosin Heavy Chain Kinase A
Ye, Q., Crawley, S. W., Yang, Y., Côté, G. P., & Jia, Z. (2010) · Science Signaling · doi:10.1126/scisignal.2000525 · Cited by 51 · see citing works
A critical role of eEF-2K in mediating autophagy in response to multiple cellular stresses
Py, B. F., Boyce, M., & Yuan, J. (2009) · Autophagy · doi:10.4161/auto.5.3.7762 · Cited by 49 · see citing works
Usui, T., Okada, M., Hara, Y., & Yamawaki, H. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00373.2013 · Cited by 47 · see citing works
Kameshima, S., Kazama, K., Okada, M., & Yamawaki, H. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00864.2014 · Cited by 42 · see citing works
Oxidized LDL-Mediated Macrophage Survival Involves Elongation Factor-2 Kinase
Chen, J. H., Riazy, M., Smith, E. M., Proud, C. G., Steinbrecher, U. P., & Duronio, V. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.174599 · Cited by 42 · see citing works
Self-citationThe Molecular Mechanism of Eukaryotic Elongation Factor 2 Kinase Activation
Tavares, C. D. J., Ferguson, S. B., Giles, D. H., Wang, Q., Wellmann, R. M., O'Brien, J. P., Warthaka, M., Brodbelt, J. S., Ren, P., & Dalby, K. N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.577148 · Cited by 41 · see citing works
Usui, T., Niijima, R., Sakatsume, T., Otani, K., Kameshima, S., Okada, M., & Yamawaki, H. (2014) · Acta Physiologica · doi:10.1111/apha.12354 · Cited by 33 · see citing works
Kenney, J. W., Sorokina, O., Genheden, M., Sorokin, A., Armstrong, J. D., & Proud, C. G. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2866-14.2015 · Cited by 33 · see citing works
Self-citationUsui, T., Okada, M., Hara, Y., & Yamawaki, H. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.12.120 · Cited by 33 · see citing works
High-Throughput Screens for eEF-2 Kinase
Devkota, A. K., Warthaka, M., Edupuganti, R., Tavares, C. D. J., Johnson, W. H., Özpolat, B., Cho, E. J., & Dalby, K. N. (2013) · SLAS DISCOVERY · doi:10.1177/1087057113505204 · Cited by 26 · see citing works
Moore, C. E., da Mota, S. R., Mikolajek, H., & Proud, C. G. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00388-14 · Cited by 24 · see citing works
Self-citationCrawley, S. W., Gharaei, M. S., Ye, Q., Yang, Y., Raveh, B., London, N., Schueler‐Furman, O., Jia, Z., & Côté, G. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177014 · Cited by 23 · see citing works
Wang, Q., Edupuganti, R., Tavares, C. D. J., Dalby, K., & Ren, P.-Y. Y. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00009 · Cited by 20 · see citing works
Wang, X., Xie, J., da Mota, S. R., Moore, C. E., & Proud, C. G. (2015) · Biochemical Journal · doi:10.1042/bj20150089 · Cited by 20 · see citing works
Self-citationImpairing Eukaryotic Elongation Factor 2 Kinase Activity Decreases Atherosclerotic Plaque Formation
Zhang, P., Riazy, M., Gold, M., Tsai, S.-H., McNagny, K. M., Proud, C. G., & Duronio, V. (2014) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2014.09.019 · Cited by 17 · see citing works
Self-citationHow does oncogene transformation render tumor cells hypersensitive to nutrient deprivation?
Leprivier, G., & Sorensen, P. H. B. (2014) · BioEssays · doi:10.1002/bies.201400085 · Cited by 10 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Browne GJ, Proud CG. A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin. Mol Cell Biol 2004; 24: 2986-97.
Cited by
Sorted by citations
MTOR inhibitors in cancer therapy
Xie, J., Wang, X., & Proud, C. G. (2016) · F1000Research · doi:10.12688/f1000research.9207.1 · Cited by 266 · see citing works
“Inhibition of mTORC1 will also activate its downstream effector, eukaryotic elongation factor 2 kinase (eEF2K), which can promote cell survival 27 .”
BackgroundMa, T. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15541 · Cited by 55 · see citing works
Karakas, D., & Ozpolat, B. (2020) · Journal of Molecular Medicine · doi:10.1007/s00109-020-01917-8 · Cited by 54 · see citing works
Kasica, N. P., Zhou, X., Yang, Q., Wang, X., Yang, W., Zimmermann, H. R., Holland, C. E., Koscielniak, E., Wu, H., Cox, A. O., et al. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15562 · Cited by 34 · see citing works
Beretta, S., Gritti, L., Ponzoni, L., Scalmani, P., Mantegazza, M., Sala, M., Verpelli, C., & Sala, C. (2022) · Molecular Autism · doi:10.1186/s13229-021-00484-0 · Cited by 18 · see citing works
Wang, X., Yang, Q., Zhou, X., Keene, C. D., Ryazanov, A. G., & Ma, T. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13916 · Cited by 17 · see citing works
Rezabakhsh, A., Habtemariam, S., Khani, E., Ghorbani Yekta, B., Rahmani, R., Iraji, H., & Nabavi, S. M. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.178253 · Cited by 3 · see citing works
Synaptic Plasticity—Intrinsic Excitability and Antidepressant Discovery
Tanaka, M. (2026) · Biomedicines · doi:10.3390/biomedicines14061265
- Authors
- Liu, R., & Proud, C. G.
- Affiliations
- South Australian Health and Medical Research Institute (AU)
- Corresponding author
- Proud, Christopher G
- Venue
- Acta Pharmacologica Sinica
- Published
- 2016-01-25
- Volume
- 37
- Issue
- 3
- Pages
- 285-294
- ISSN
- 0253-9756 (ISSN-L)
- 1671-4083
- 1745-7254
- PMC
- PMC4775846
- OpenAlex
- W2410758979
- Cited by
- 117
- References
- 66
- Citations by year
- 2026: 11 · 2025: 22 · 2024: 10 · 2023: 14 · 2022: 12 · 2021: 16 · 2020: 11 · 2019: 6 · 2018: 5 · 2017: 5 · 2016: 5
- FWCI
- 0.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Acta Pharmacologica Sinica (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- eEF2K, eEF2 phosphorylation, translation elongation, protein kinase inhibitors, small molecule inhibitors, cancer, cardiovascular disease, atherosclerosis, pulmonary arterial hypertension, neurodegenerative diseases, depression, therapeutic target
- MeSH terms
- Animals, Cardiovascular Diseases, Humans, Neoplasms, Neurodegenerative Diseases, Protein Kinase Inhibitors, Elongation Factor 2 Kinase, Drug Discovery, Molecular Targeted Therapy
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
