Crystal Structure of Glycogen Synthase Kinase 3β

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

Wnt signaling and cancer

Polakis, P. (2000) · Genes & Development · doi:10.1101/gad.14.15.1837 · Cited by 3,183

Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization

Diehl, J. A., Cheng, M., Roussel, M. F., & Sherr, C. J. (1998) · Genes & Development · doi:10.1101/gad.12.22.3499 · Cited by 2,130

Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells

Stambolic, V., Ruel, L., & Woodgett, J. R. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70790-2 · Cited by 1,321

Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592

AKT/PKB Signaling: Navigating the Network

Manning, B. D., & Toker, A. (2017) · Cell · doi:10.1016/j.cell.2017.04.001 · Cited by 3,772

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

The Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation

Mendoza, M. C., Er, E. E., & Blenis, J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.03.006 · Cited by 1,817

Mechanisms of specificity in protein phosphorylation

Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451

Probing sporadic and familial Alzheimer’s disease using induced pluripotent stem cells

Israel, M. A., Yuan, S. H., Bardy, C., Reyna, S. M., Mu, Y., Herrera, C., Hefferan, M. P., Van Gorp, S., Nazor, K. L., Boscolo, F. S., et al. (2012) · Nature · doi:10.1038/nature10821 · Cited by 1,253

GSK3 takes centre stage more than 20 years after its discovery

FRAME, S., & COHEN, P. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590001 · Cited by 1,433

Flexible nets: The roles of intrinsic disorder in protein interaction networks

Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122

Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837

Tau protein kinases: Involvement in Alzheimer's disease

Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631

The evolution of signalling pathways in animal development

Pires-daSilva, A., & Sommer, R. J. (2003) · Nature Reviews Genetics · doi:10.1038/nrg977 · Cited by 466

Phosphorylation by p38 MAPK as an Alternative Pathway for GSK3β Inactivation

Thornton, T. M., Pedraza-Alva, G., Deng, B., Wood, C. D., Aronshtam, A., Clements, J. L., Sabio, G., Davis, R. J., Matthews, D. E., Doble, B., et al. (2008) · Science · doi:10.1126/science.1156037 · Cited by 484

Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau

Green, K. N., Steffan, J. S., Martinez-Coria, H., Sun, X., Schreiber, S. S., Thompson, L. M., & LaFerla, F. M. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3203-08.2008 · Cited by 404

Sustained interleukin-1β overexpression exacerbates tau pathology despite reduced amyloid burden in an alzheimer’s mouse model

Ghosh, S., Wu, M. D., Shaftel, S. S., Kyrkanides, S., LaFerla, F. M., Olschowka, J. A., & O'Banion, M. K. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.4361-12.2013 · Cited by 390

Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions

BIONDI, R. M., & NEBREDA, A. R. (2003) · Biochemical Journal · doi:10.1042/bj20021641 · Cited by 334

The Roles of Cyclin-dependent Kinase 5 and Glycogen Synthase Kinase 3 in Tau Hyperphosphorylation

Plattner, F., Angelo, M., & Giese, K. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603469200 · Cited by 340

Deciphering the Phosphorylation “Code” of the Glucocorticoid Receptor in Vivo

Wang, Z., Frederick, J., & Garabedian, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110530200 · Cited by 321

Structural basis for recruitment of glycogen synthase kinase 3β to the axin—APC scaffold complex

Dajani, R., Fraser, E., Roe, S. M., Yeo, M., Good, V. M., Thompson, V., Dale, T. C., & Pearl, L. H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg068 · Cited by 315

Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3β (GSK3β) plays a critical role in regulating tau's ability to bind and stabilize microtubules

Cho, J., & Johnson, G. V. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02155.x · Cited by 282

Glycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites

Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266

Neurons derived from sporadic Alzheimer’s disease iPSCs reveal elevated TAU hyperphosphorylation, increased amyloid levels, and GSK3B activation

Ochalek, A., Mihalik, B., Avci, H. X., Chandrasekaran, A., Téglási, A., Bock, I., Giudice, M. L., Táncos, Z., Molnár, K., László, L., et al. (2017) · Alzheimer's Research & Therapy · doi:10.1186/s13195-017-0317-z · Cited by 225

Docking interactions in protein kinase and phosphatase networks

Reményi, A., Good, M. C., & Lim, W. A. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.10.008 · Cited by 188

GSK‐3 in Neurodegenerative Diseases

Lei, P., Ayton, S., Bush, A. I., & Adlard, P. A. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/189246 · Cited by 177

Substrate and Docking Interactions in Serine/Threonine Protein Kinases

Goldsmith, E. J., Akella, R., Min, X., Zhou, T., & Humphreys, J. M. (2007) · Chemical Reviews · doi:10.1021/cr068221w · Cited by 143

β-Catenin is critical for early postnatal liver growth

Apte, U., Zeng, G., Thompson, M. D., Muller, P., Micsenyi, A., Cieply, B., Kaestner, K. H., & Monga, S. P. S. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00359.2006 · Cited by 119

GSK-3 Is Activated by the Tyrosine Kinase Pyk2 during LPA1-mediated Neurite Retraction

Sayas, C. L., Ariaens, A., Ponsioen, B., & Moolenaar, W. H. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0688 · Cited by 115

Wnt/β-Catenin Signaling in Alzheimer’s Disease

Ferrari, G., Avila, M., Medina, M., Perez-Palma, E., Bustos, B., & Alarcon, M. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527312666131223113900 · Cited by 95

Glycogen Synthase Kinase-3β Is Involved in the Phosphorylation and Suppression of Androgen Receptor Activity

Salas, T. R., Kim, J., Vakar-Lopez, F., Sabichi, A. L., Troncoso, P., Jenster, G., Kikuchi, A., Chen, S.-Y., Shemshedini, L., Suraokar, M., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309560200 · Cited by 81

Role of GSK-3β Inhibitors: New Promises and Opportunities for Alzheimer’s Disease

Shri, S. R., Manandhar, S., Nayak, Y., & Pai, K. S. R. (2023) · Advanced Pharmaceutical Bulletin · doi:10.34172/apb.2023.071 · Cited by 71

Tau, where are we now?

Johnson, G. V. W., & Bailey, C. D. C. (2002) · Journal of Alzheimer's Disease · doi:10.3233/jad-2002-4505 · Cited by 61

Protein S -Nitrosylation Controls Glycogen Synthase Kinase 3β Function Independent of Its Phosphorylation State

Wang, S.-B., Venkatraman, V., Crowgey, E. L., Liu, T., Fu, Z., Holewinski, R., Ranek, M., Kass, D. A., O’Rourke, B., & Van Eyk, J. E. (2018) · Circulation Research · doi:10.1161/circresaha.118.312789 · Cited by 54

Control of neuronal excitability by GSK-3beta: epilepsy and beyond.

Jaworski, T. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118745 · Cited by 43

Development of inhibitors targeting glycogen synthase kinase-3β for human diseases: Strategies to improve selectivity

Wei, J., Wang, J., Zhang, J., Yang, J., Wang, G., & Wang, Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114301 · Cited by 42

Protein kinase A enhances, whereas glycogen synthase kinase-3β inhibits, the activity of the exon 2-encoded transactivator domain of heterogeneous nuclear ribonucleoprotein D in a hierarchical fashion

TOLNAY, M., JUANG, Y.-T., & TSOKOS, G. C. (2002) · Biochemical Journal · doi:10.1042/bj3630127 · Cited by 27

Colocalization of phosphorylated forms of WAVE1, CRMP2, and tau in Alzheimer's disease model mice: Involvement of Cdk5 phosphorylation and the effect of ATRA treatment

Watamura, N., Toba, J., Yoshii, A., Nikkuni, M., & Ohshima, T. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23674 · Cited by 25

Discovery and Design of Novel Small Molecule GSK-3 Inhibitors Targeting the Substrate Binding Site

Rippin, I., Khazanov, N., Ben Joseph, S., Kudinov, T., Berent, E., Arciniegas Ruiz, S. M., Marciano, D., Levy, L., Gruzman, A., Senderowitz, H., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228709 · Cited by 25

Elucidation of the GSK3α Structure Informs the Design of Novel, Paralog-Selective Inhibitors

Amaral, B., Capacci, A., Anderson, T., Tezer, C., Bajrami, B., Lulla, M., Lucas, B., Chodaparambil, J. V., Marcotte, D., Kumar, P. R., et al. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00476 · Cited by 22

A SWI/SNF-specific Ig-like domain, SWIFT, is a transcription factor binding platform

Jain, S. U., Williamson, K. E., Ying, A. W., Turner, A. M., Jiang, R. J., Raval, S., So, K., Allison, M. J., Sankar, A., Sáme Guerra, D. D., et al. (2026) · Science · doi:10.1126/science.aeb3627 · Cited by 11