The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Glycogen synthase kinase 3 in MLL leukaemia maintenance and targeted therapy
Open accessAbstract
Glycogen synthase kinase 3 (GSK3) is a multifunctional serine/threonine kinase that participates in numerous signalling pathways involved in diverse physiological processes. Several of these pathways are implicated in disease pathogenesis, which has prompted efforts to develop GSK3-specific inhibitors for therapeutic applications. However, before now, there has been no strong rationale for targeting GSK3 in malignancies. Here we report pharmacological, physiological and genetic studies that demonstrate an oncogenic requirement for GSK3 in the maintenance of a specific subtype of poor prognosis human leukaemia, genetically defined by mutations of the MLL proto-oncogene. In contrast to its previously characterized roles in suppression of neoplasia-associated signalling pathways, GSK3 paradoxically supports MLL leukaemia cell proliferation and transformation by a mechanism that ultimately involves destabilization of the cyclin-dependent kinase inhibitor p27(Kip1). Inhibition of GSK3 in a preclinical murine model of MLL leukaemia provides promising evidence of efficacy and earmarks GSK3 as a candidate cancer drug target.
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
“Plethora of studies in last decade showed that active GSK3b is involved in the regulation of number of pathways that can influence leukemogenesis, leukemia cell survival (13,46), myeloid differentiation, and resistance to chemotherapy.”
From FBW7 Inhibits Myeloid Differentiation in Acute Myeloid Leukemia via GSK3-Dependent Ubiquitination of PU.1 (2021) · cites this paper as [13]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“in some of the AMLs, GSK3b was shown to act as tumor promoter by targeting tumor suppressors such as p27 (13).”
From FBW7 Inhibits Myeloid Differentiation in Acute Myeloid Leukemia via GSK3-Dependent Ubiquitination of PU.1 (2021) · 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
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
Sato, N., Meijer, L., Skaltsounis, A., Greengard, P., & Brivanlou, A. H. (2003) · Nature Medicine · doi:10.1038/nm979 · Cited by 2,139
GSK-3: tricks of the trade for a multi-tasking kinase
Doble, B. W., & Woodgett, J. R. (2003) · Journal of Cell Science · doi:10.1242/jcs.00384 · Cited by 2,084
Cohen, P., & Frame, S. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096075 · Cited by 1,493
Multiple Ras-dependent phosphorylation pathways regulate Myc protein stabilityPreprint
Sears, R. C., Nuckolls, F., Haura, E. B., Taya, Y., Tamai, K., & Nevins, J. R. (2000) · Genes & Development · doi:10.1101/gad.836800 · Cited by 1,411
Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation
Hoeflich, K. P., Luo, J., Rubie, E. A., Tsao, M., Jin, O., & Woodgett, J. R. (2000) · Nature · doi:10.1038/35017574 · Cited by 1,401
Yost, C., Torres, M., Miller, J., Huang, E., Kimelman, D., & Moon, R. T. (1996) · Genes & Development · doi:10.1101/gad.10.12.1443 · Cited by 1,167
Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells
Yilmaz, Ö. H., Valdez, R., Theisen, B. K., Guo, W., Ferguson, D. O., Wu, H., & Morrison, S. J. (2006) · Nature · doi:10.1038/nature04703 · Cited by 1,113
Martin, M., Rehani, K., Jope, R. S., & Michalek, S. M. (2005) · Nature Immunology · doi:10.1038/ni1221 · Cited by 1,099
Yokoyama, A., Somervaille, T. C. P., Smith, K. S., Rozenblatt–Rosen, O., Meyerson, M. M., & Cleary, M. L. (2005) · Cell · doi:10.1016/j.cell.2005.09.025 · Cited by 698
Self-citation
Research works printed but not linked: 1
- Miller, J. R. The Wnts. Genome Biol 3, 3001 (2002)
Cited by
Sorted by citations
Items 101–200 of 269
Glycogen synthase kinase−3β inhibitors suppress leukemia cell growth
Song, E. Y., Palladinetti, P., Klamer, G., Ko, K., Lindeman, R., O'Brien, T. A., & Dolnikov, A. (2010) · Experimental Hematology · doi:10.1016/j.exphem.2010.06.001 · Cited by 40
Targeting phosphatidylinositol 3 kinase (PI3K)-Akt beyond rapalogs
Ogita, S., & LoRusso, P. M. (2011) · Targeted Oncology · doi:10.1007/s11523-011-0176-7 · Cited by 40
Targeting the Akt, GSK-3, Bcl-2 axis in acute myeloid leukemia
Ricciardi, M. R., Mirabilii, S., Licchetta, R., Piedimonte, M., & Tafuri, A. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.05.002 · Cited by 41
GSK-3 as a novel prognostic indicator in leukemia
Ruvolo, P. P. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.05.001 · Cited by 39
Retinoid Differentiation Therapy for Common Types of Acute Myeloid Leukemia
Brown, G., & Hughes, P. (2012) · Leukemia Research and Treatment · doi:10.1155/2012/939021 · Cited by 39
Zamek‐Gliszczynski, M. J., Abraham, T. L., Alberts, J. J., Kulanthaivel, P., Jackson, K. A., Chow, K. H., McCann, D., Hu, H., Anderson, S., Furr, N. A., et al. (2013) · Drug Metabolism and Disposition · doi:10.1124/dmd.112.048488 · Cited by 39
From Tyrian Purple to Kinase Modulators: Naturally Halogenated Indirubins and Synthetic Analogues
Vougogiannopoulou, K., & Skaltsounis, A. (2012) · Planta Medica · doi:10.1055/s-0032-1315261 · Cited by 38
Hu, S., Ueda, M., Stetson, L. C., Ignatz-Hoover, J. J., Moreton, S. A., Chakrabarti, A., Xia, Z., Karan, G., Lima, M. J. G. D., Agrawal, M., et al. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0566 · Cited by 37
Mirlashari, M. R., Randen, I., & Kjeldsen‐Kragh, J. (2011) · Leukemia Research · doi:10.1016/j.leukres.2011.11.013 · Cited by 38
Increased galectin-3 facilitates leukemia cell survival from apoptotic stimuli
Cheng, Y., Huang, W., Chen, C., Tsai, C., Wang, C., Chiu, W. C., Chen, Y., Lin, Y.-S., Chang, C., & Lin, C. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.07.099 · Cited by 35
GSK-3: a multifaceted player in acute leukemias
Martelli, A. M., Evangelisti, C., Paganelli, F., Chiarini, F., & McCubrey, J. A. (2021) · Leukemia · doi:10.1038/s41375-021-01243-z · Cited by 36
Grist for the MLL: how do MLL oncogenic fusion proteins generate leukemia stem cells?
Somervaille, T. C. P., & Cleary, M. L. (2010) · International Journal of Hematology · doi:10.1007/s12185-010-0579-8 · Cited by 34
Self-citationIMPDH inhibition activates TLR‐VCAM1 pathway and suppresses the development of MLL‐fusion leukemia
Liu, X., Sato, N., Yabushita, T., Li, J., Jia, Y., Tamura, M., Asada, S., Fujino, T., Fukushima, T., Yonezawa, T., et al. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202115631 · Cited by 34
Nölting, S., Rentsch, J., Freitag, H., Detjen, K. M., Briest, F., Möbs, M., Weissmann, V., Siegmund, B., Auernhammer, C. J., Prada, E. T. A., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182852 · Cited by 34
t(4;11) leukemias display addiction to MLL-AF4 but not to AF4-MLL
Kumar, A. R., Yao, Q., Li, Q., Sam, T. N., & Kersey, J. H. (2010) · Leukemia Research · doi:10.1016/j.leukres.2010.08.011 · Cited by 33
Ching, J., Amiridis, S., Stylli, S. S., Bjorksten, A. R., Kountouri, N., Zheng, T. W., Paradiso, L., Luwor, R. B., Morokoff, A. P., O'Brien, T. J., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4019 · Cited by 33
Khan, K. A., Dô, F., Marineau, A., Doyon, P., Clément, J.-F., Woodgett, J. R., Doble, B. W., & Servant, M. J. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00344-15 · Cited by 32
Mudgapalli, N., Nallasamy, P., Chava, H., Chava, S. P., Pathania, A. S., Gunda, V., Gorantla, S., Pandey, M. K., Gupta, S. C., & Challagundla, K. B. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.10.001 · Cited by 31
miR-130b and miR-128a are essential lineage-specific codrivers of t(4;11) MLL-AF4 acute leukemia
Malouf, C., Antunes, E., O’Dwyer, M. R., Jakobczyk, H., Sahm, F., Landua, S.-L., Anderson, R. A., Soufi, A., Halsey, C., & Ottersbach, K. (2021) · Blood · doi:10.1182/blood.2020006610 · Cited by 32
Overcoming Hypoxia-Induced Apoptotic Resistance through Combinatorial Inhibition of GSK-3β and CDK1
Mayes, P. A., Dolloff, N. G., Daniel, C. J., Liu, J. J., Hart, L. S., Kuribayashi, K., Allen, J. E., Jee, D. I. H., Dorsey, J. F., Liu, Y. Y., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1383 · Cited by 32
Singh, S. K., Baumgart, S., Singh, G., König, A. O., Reutlinger, K., Hofbauer, L. C., Barth, P. J., Gress, T. M., Lomberk, G. A., Urrutia, R. A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.197533 · Cited by 32
Mishra, M., Thacker, G., Sharma, A., Singh, A. K., Upadhyay, V., Sanyal, S., Verma, S. P., Tripathi, A. K., Bhatt, M. L. B., & Trivedi, A. K. (2021) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0268 · Cited by 30
Si, J., Mueller, L., & Collins, S. J. (2011) · Leukemia · doi:10.1038/leu.2011.171 · Cited by 30
Sex differences in the GSK3β-mediated survival of adherent leukemic progenitors
Bertrand‐Michel, J., Despeaux, M., Joly, S., Bourogâa, E., Gallay, N., Demur, C., Bonnevialle, P., Louache, F., Maguer‐Satta, V., Vergnolle, N., et al. (2011) · Oncogene · doi:10.1038/onc.2011.258 · Cited by 30
Identification of glycogen synthase kinase 3α as a therapeutic target in melanoma
Madhunapantula, S. V., Sharma, A. K., Gowda, R., & Robertson, G. P. (2013) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12156 · Cited by 31
Orzechowska, B., Wróbel, G., Turlej, E., Jatczak, B., Sochocka, M., & Chaber, R. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.106114 · Cited by 30
Hernandez‐Davies, J. E., Zape, J. P., Landaw, E. M., Tan, X., Presnell, A., Griffith, D., Heinrich, M. C., Glaser, K. B., & Sakamoto, K. M. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0904 · Cited by 29
Kim, T. H., Kim, C., Lee, J., Jang, S. J., Hwang, J. J., Ro, S., & Choi, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060383 · Cited by 29
GSK3A Is Redundant with GSK3B in Modulating Drug Resistance and Chemotherapy-Induced Necroptosis
Grassilli, E., Ianzano, L., Bonomo, S., Missaglia, C., Cerrito, M. G., Giovannoni, R., Masiero, L., & Lavitrano, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100947 · Cited by 30
Vincent, E. E., Elder, D. J. E., O′Flaherty, L., Pardo, O. E., Dzien, P., Phillips, L., Morgan, C., Pawade, J., May, M., Sohail, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114725 · Cited by 28
Novetsky, A. P., Thompson, D. M., Zighelboim, I., Thaker, P. H., Powell, M. A., Mutch, D. G., & Goodfellow, P. J. (2013) · International Journal of Gynecological Cancer · doi:10.1097/igc.0b013e31827cfecb · Cited by 28
Osolodkin, D. I., Palyulin, V. A., & Zefirov, N. S. (2012) · Current Pharmaceutical Design · doi:10.2174/138161213804581972 · Cited by 27
Cyclin-dependent kinase inhibitors for the treatment of chronic lymphocytic leukemia
Blachly, J. S., Byrd, J. C., & Grever, M. R. (2016) · Seminars in Oncology · doi:10.1053/j.seminoncol.2016.02.003 · Cited by 28
Aberrant GSK3β nuclear localization promotes AML growth and drug resistance
Ignatz-Hoover, J. J., Wang, V., Mackowski, N. M., Roe, A. J., Ghansah, I. K., Ueda, M., Lazarus, H. M., de Lima, M., Paietta, E., Fernandez, H., et al. (2018) · Blood Advances · doi:10.1182/bloodadvances.2018016006 · Cited by 27
Li, T., Fan, F., Liu, Y., Li, W., Zhang, L., Ruan, J., Shen, C., Sheng, X., Zhu, Z., Wang, A., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081945 · Cited by 27
Watanabe, M., Abe, N., Oshikiri, Y., Stanbridge, E. J., & Kitagawa, T. (2012) · Oncogenesis · doi:10.1038/oncsis.2012.21 · Cited by 27
Targeting self-renewal pathways in myeloid malignancies
Sands, W. A., Copland, M., & Wheadon, H. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-33 · Cited by 28
Correction: c-FLIPL enhances anti-apoptotic Akt functions by modulation of Gsk3β activity
Quintavalle, C., Incoronato, M., Puca, L., Acunzo, M., Zanca, C., Romano, G., Garofalo, M., Iaboni, M., Croce, C. M., & Condorelli, G. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.7 · Cited by 27
RetractedAnticancer activity of VDR-coregulator inhibitor PS121912
Sidhu, P. S., Teske, K. A., Feleke, B., Yuan, N. Y., Guthrie, M. L., Fernstrum, G. B., Vyas, N. D., Han, L., Preston, J., Bogart, J. W., et al. (2014) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-014-2549-y · Cited by 26
Off-target based drug repurposing opportunities for tivantinib in acute myeloid leukemia
Kuenzi, B. M., Rix, L. L. R., Kinose, F., Kroeger, J. L., Lancet, J. E., Padron, E., & Rix, U. (2019) · Scientific Reports · doi:10.1038/s41598-018-37174-6 · Cited by 26
Roles of GSK-3 and β-Catenin in Antiviral Innate Immune Sensing of Nucleic Acids
Marineau, A., Khan, K. A., & Servant, M. J. (2020) · Cells · doi:10.3390/cells9040897 · Cited by 29
Wang, F., Wu, P., Gong, S., Chen, Y., Gao, J., Wang, S., Shen, Q., Tao, H., Hua, F., Zhou, Z., et al. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109643 · Cited by 26
Harrington, C. T., Sotillo, E., Robert, A., Hayer, K. E., Bogusz, A. M., Psathas, J. N., Yu, D., Taylor, D. M., Dang, C. V., Klein, P. S., et al. (2019) · Leukemia · doi:10.1038/s41375-019-0454-4 · Cited by 28
Pro-Oncogenic and Anti-Oncogenic Pathways: Opportunities and Challenges of Cancer Therapy
Zhang, J., Chen, Y., & Lu, Q. (2010) · Future Oncology · doi:10.2217/fon.10.15 · Cited by 29
Fung, T. K., Gandillet, A., & So, C. W. E. (2012) · Current Opinion in Hematology · doi:10.1097/moh.0b013e3283545615 · Cited by 26
Glycogen synthase kinase-3: A potential immunotherapeutic target in tumor microenvironment
Liang, J., Yu, M., Li, Y., Zhao, L., & Wei, Q. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116377 · Cited by 25
Zassadowski, F., Pokorná, K., Ferré, N., Guidez, F., Llopis, L., Chourbagi, O., Chopin, M., Poupon, J., Fenaux, P., Padua, R. A., et al. (2015) · Leukemia · doi:10.1038/leu.2015.159 · Cited by 24
HMGA2 as a potential molecular target in KMT2A-AFF1 -positive infant acute lymphoblastic leukaemia
Wu, Z., Eguchi‐Ishimae, M., Yagi, C., Iwabuki, H., Gao, W., Tauchi, H., Inukai, T., Sugita, K., Ishii, E., & Eguchi, M. (2015) · British Journal of Haematology · doi:10.1111/bjh.13763 · Cited by 25
Zhao, G., Ma, H., Shen, X., Xu, G., Zhu, Y., Chen, B., Tie, R., Qü, P., Lv, Y., Zhang, H., et al. (2013) · Journal of Surgical Research · doi:10.1016/j.jss.2013.05.004 · Cited by 25
O′Flaherty, L., Shnyder, S. D., Cooper, P. A., Cross, S., Wakefield, J. G., Pardo, O. E., Seckl, M. J., & Tavaré, J. M. (2019) · PLoS ONE · doi:10.1371/journal.pone.0214610 · Cited by 25
Signaling pathways governing the behaviors of leukemia stem cells
Azizidoost, S., Nasrolahi, A., Sheykhi-Sabzehpoush, M., Anbiyaiee, A., Khoshnam, S. E., Farzaneh, M., & Shahab Uddin, M. S. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.01.008 · Cited by 29
c-FLIPL enhances anti-apoptotic Akt functions by modulation of Gsk3β activity
Quintavalle, C., Incoronato, M., Puca, L., Acunzo, M., Zanca, C., Romano, G., Garofalo, M., Iaboni, M., Croce, C. M., & Condorelli, G. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.65 · Cited by 25
RetractedPerturbing LSD1 and WNT rewires transcription to synergistically induce AML differentiation
Hosseini, A., Dhall, A., Ikonen, N., Sikora, N., Nguyen, S., Shen, Y., Amaral, M. L. J., Jiao, A. L., Wallner, F., Sergeev, P., et al. (2025) · Nature · doi:10.1038/s41586-025-08915-1 · Cited by 25
Mutations in PIK3CA sensitize breast cancer cells to physiologic levels of aspirin
Turturro, S. B., Najor, M. S., Ruby, C. E., Cobleigh, M., & Abukhdeir, A. M. (2016) · Breast Cancer Research and Treatment · doi:10.1007/s10549-016-3729-8 · Cited by 23
Zeng, F.-Y., Cui, J., Liu, L., & Chen, T. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.04.016 · Cited by 23
How Ginsenosides Trigger Apoptosis in Human Lung Adenocarcinoma Cells
Han, X., Xue, Q., Zhang, Q., Li, C., Liu, X., Liu, J., Li, H., & Yang, J. (2019) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x19500885 · Cited by 24
Tao, F., Ruan, S., Liu, W., Wang, L., Xiong, Y., & Shen, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0168892 · Cited by 23
Yin, Y., Kizer, N. T., Thaker, P. H., Chiappinelli, K. B., Trinkaus, K. M., Goodfellow, P. J., & Ma, L. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140816617 · Cited by 22
Piplani, H., Rana, C., Vaish, V., Vaiphei, K., & Sanyal, S. N. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.011 · Cited by 21
Zhang, P., Min, Z., Gao, Y., Bian, J., Lin, X., He, J., Ye, D., Li, Y., Peng, C., Cheng, Y., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02254 · Cited by 21
Frat2 mediates the oncogenic activation of Rac by MLL fusions
Walf-Vorderwülbecke, V., de Boer, J., Horton, S. J., van Amerongen, R., Proost, N., Berns, A. J. M., & Williams, O. (2012) · Blood · doi:10.1182/blood-2012-05-432534 · Cited by 20
Essential role of PR-domain protein MDS1-EVI1 in MLL-AF9 leukemia.
Zhang, Y., Owens, K. S., Hatem, L., Glass, C., Karuppaiah, K., Camargo, F., & Perkins, A. (2013) · Blood · doi:10.1182/blood-2012-08-453662 · Cited by 21
Zhao, K., Chen, C., Shi, Q., Deng, W., Zuo, T., He, X., Liu, T., Zhao, L., & Wang, W. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2650 · Cited by 20
Crisan, L., Avram, S. I., & Pacureanu, L. M. (2017) · Molecular Diversity · doi:10.1007/s11030-016-9724-5 · Cited by 20
Barboro, P., Benelli, R., Tosetti, F., Costa, D., Capaia, M., Astigiano, S., Venè, R., Poggi, A. D., & Ferrari, N. (2020) · Carcinogenesis · doi:10.1093/carcin/bgaa053 · Cited by 20
Yang, Z., Liu, H., Pan, B., He, F., & Pan, Z. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob00642c · Cited by 20
Metformin sensitizes AML cells to venetoclax through endoplasmic reticulum stress— CHOP pathway
Hua, L., Yang, N., Li, Y., Huang, K., Jiang, X., Liu, F., Yu, Z. H., Chen, J., Lai, J., Du, J., et al. (2023) · British Journal of Haematology · doi:10.1111/bjh.18968 · Cited by 20
Wang, X., Xu, Y., Yang, G., Chen, H., & ZHANG, P. (2015) · Oncology Reports · doi:10.3892/or.2015.3860 · Cited by 19
Hu, Y., Gu, X., Li, R., Luo, Q., & Xu, Y. (2010) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-29-154 · Cited by 19
Grey, W. E., Ivey, A., Milne, T. A., Haferlach, T., Grimwade, D. J., Uhlmann, F., Voisset, E., & Yu, V. P. C. C. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.09.009 · Cited by 17
Wang, H. L., Hart, J. A. L., Fan, L., Mustafi, R., & Bissonnette, M. (2011) · Clinical Colorectal Cancer · doi:10.3816/ccc.2011.n.004 · Cited by 19
Harrington, C. T., Sotillo, E., Robert, A., Hayer, K. E., Bogusz, A. M., Psathas, J. N., Yu, D., Taylor, D. M., Dang, C. V., Klein, P. S., et al. (2019) · Leukemia · doi:10.1038/s41375-019-0650-2 · Cited by 19
Kim, H., Kim, K. H., & Kim, A. (2016) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/62540 · Cited by 18
Liu, K., Li, J., Wu, X., Chen, M., Luo, F., & Li, J. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4163 · Cited by 18
Time-Lapse Imaging of Neuroblastoma Cells to Determine Cell Fate upon Gene Knockdown
Batra, R., Harder, N., Gogolin, S., Diessl, N., Soons, Z. I. T. A., Jaeger-Schmidt, C., Lawerenz, C., Eils, R., Rohr, K., Westermann, F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050988 · Cited by 19
Shen, S., Xu, N., Klamer, G., Ko, K., Khoo, M., Ma, D. D. F., Moore, J. J., O'Brien, T. A., & Dolnikov, A. (2014) · Stem Cells and Development · doi:10.1089/scd.2014.0230 · Cited by 17
Li, B., Zhang, C., He, F., Liu, W., Yang, Y., Hu, L., Liu, X., Wang, J., Zhang, L., Deng, B., et al. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000356606 · Cited by 17
Tosello, V., Bordin, F., Yu, J., Agnusdei, V., Indraccolo, S., Basso, G., Amadori, A., & Piovan, E. (2015) · Leukemia · doi:10.1038/leu.2015.335 · Cited by 17
Ramzi, M., Khalafi‐Nezhad, A., Saadi, M. I., & Jowkar, Z. (2018) · International Journal of Hematology-Oncology and Stem Cell Research · doi:10.18502/ijhoscr.v12i4.109 · Cited by 17
The Landscape of Glycogen Synthase Kinase-3 Beta Genomic Alterations in Cancer
Borden, B. A., Baca, Y., Xiu, J., Tavora, F., Winer, I., Weinberg, B. A., Vanderwalde, A. M., Darabi, S., Korn, W. M., Mazar, A. P., et al. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-20-0497 · Cited by 15
Sidestream Smoke Exposure Increases the Susceptibility of Airway Epithelia to Adenoviral Infection
Sharma, P., Kolawole, A. O., Core, S. B., Kajon, A. E., & Excoffon, K. J. D. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049930 · Cited by 15
Wang, T., Du, J., Kong, D., Yang, G., Zhou, Q., You, F., Lin, Y., & Wang, Y. (2020) · Oncology Reports · doi:10.3892/or.2020.7726 · Cited by 15
Drug Repurposing for Targeting Acute Leukemia With KMT2A (MLL)—Gene Rearrangements
Tsakaneli, A., & Williams, O. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.741413 · Cited by 16
The Pivotal Roles of GSK3β in Glioma Biology
Nakada, M., Minamoto, T., Ilya, V. V., Hayashi, Y., & Ham, J.-I. (2011) · InTech eBooks · doi:10.5772/21458 · Cited by 14
Lee, S., Shin, D., Cho, J. M., Ro, S., & Suh, Y. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.01.065 · Cited by 14
Mechanisms of mixed-lineage leukemia
Muntean, A. G. (2013) · International Journal of Hematologic Oncology · doi:10.2217/ijh.13.20 · Cited by 14
Cardiac Hypertrophy is Positively Regulated by MicroRNA-24 in Rats
Gao, J., Zhu, M., Liu, R.-F., Zhang, J.-S., & Xu, M. (2018) · Chinese Medical Journal · doi:10.4103/0366-6999.232793 · Cited by 14
Molecular Pathology of Mixed-Lineage Leukemia
Bach, C., & Slany, R. K. (2009) · Future Oncology · doi:10.2217/fon.09.96 · Cited by 14
Creatine kinase pathway inhibition alters GSK3 and WNT signaling in EVI1-positive AML
Benajiba, L., Alexe, G., Su, A. H., Raffoux, E., Soulier, J., Hemann, M. T., Hermine, O., Itzykson, R., Stegmaier, K., & Puissant, A. (2018) · Leukemia · doi:10.1038/s41375-018-0291-x · Cited by 14
Tantray, M. A., Khan, I., Hamid, H., Alam, M. S., Dhulap, A., & Kalam, A. (2016) · New Journal of Chemistry · doi:10.1039/c5nj02896e · Cited by 13
Aalaoui-Jamali, M., Bijian, K., & Batist, G. (2011) · Europe PMC (PubMed Central) · Cited by 13
Lee, J. K., Chatterjee, A., Scarpa, M., Bailey, C. M., Niyongere, S., Singh, P., Ali, M. K. M., Kapoor, S., Wang, Y., Silvestri, G., et al. (2024) · Cancer Research Communications · doi:10.1158/2767-9764.crc-23-0379 · Cited by 12
Ueda, M., Stefan, T., Stetson, L. C., Ignatz-Hoover, J. J., Tomlinson, B. K., Creger, R. J., Cooper, B., Lazarus, H. M., Lima, M. J. G. D., Wald, D. N., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00327 · Cited by 12
Eisenlöffel, C., Schmöle, A., Pews‐Davtyan, A., Brennführer, A., Kuznetsov, S. A., Hübner, R., Frech, S., Schult, C., Junghanß, C., Beller, M., et al. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.12.013 · Cited by 12
Aberrant glycogen synthase kinase 3β in the development of pancreatic cancer
Shimasaki, T., Motoo, Y., Minamoto, T., & Kitano, A. (2012) · Journal of Carcinogenesis · doi:10.4103/1477-3163.100866 · Cited by 12
Ching, J., Amiridis, S., Stylli, S. S., Morokoff, A. P., O'Brien, T. J., & Kaye, A. H. (2014) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2014.09.001 · Cited by 12
GSK3β suppression inhibits MCL1 protein synthesis in human acute myeloid leukemia cells
Lee, Y., Shi, Y., Wang, L., Chiou, J., Huang, C., & Chang, L. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29884 · Cited by 12
Wang, S.-Y., Shih, Y.-H., Shieh, T., & Tseng, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010361 · Cited by 12
Glycogen Synthase Kinase-3 and Leukemia: Restoring the Balance
Birch, N. W., & Zeleznik‐Le, N. J. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.05.017 · Cited by 12
Gao, Y., Ye, D., Zhou, W., & Chu, Y. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.04.039 · Cited by 12
Metadata
- Authors
- Wang, Z., Smith, K. S., Murphy, M., Piloto, O., Somervaille, T. C. P., & Cleary, M. L.
- Affiliations
- Stanford Medicine (US)
- Corresponding author
- Cleary, Michael L.
- Venue
- Nature
- Published
- 2008-09-17
- Volume
- 455
- Issue
- 7217
- Pages
- 1205-1209
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC4084721
- OpenAlex
- W1964632863
- Cited by
- 265
- References
- 43
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 6 · 2023: 8 · 2022: 9 · 2021: 10 · 2020: 17 · 2019: 14 · 2018: 13 · 2017: 13 · 2016: 14 · 2015: 14 · 2014: 23 · 2013: 29 · 2012: 26
- FWCI
- 19.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- David and Lucile Packard Foundation
- Lawrence Foundation
- National Cancer Institute (CA 116606, R01CA116606, CA-55029, R01CA055029)
- Topics
- Health Sciences › Medicine › Hematology › Acute Lymphoblastic Leukemia research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
- Keywords
- glycogen synthase kinase-3, p27, cyclin-dependent kinase inhibitors, GSK-3 inhibitors, oncogenic signaling, therapeutic target
- MeSH terms
- Proto-Oncogene Mas, Animals, Cell Division, Cell Line, Transformed, Cell Transformation, Neoplastic, Disease Models, Animal, Humans, Isoenzymes, Leukemia, Lymphoid, Mice, Inbred C57BL, Histone-Lysine N-Methyltransferase, G1 Phase, Mice, SCID, Myeloid Progenitor Cells, Glycogen Synthase Kinase 3, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, Cell Proliferation, Cyclin-Dependent Kinase Inhibitor p27, Mice, Myeloid-Lymphoid Leukemia Protein, Precursor Cells, B-Lymphoid
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