RETRACTED ARTICLE: Fuzhisan, a Chinese Herbal Medicine, Inhibits Beta-Amyloid-Induced Neurotoxicity and Tau Phosphorylation Through Calpain/Cdk5 Pathway in Cultured Cortical Neurons

Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration

Patrick, G. N., Zukerberg, L. R., Nikolić, M., de la Monte, S. M., Dikkes, P., & Tsai, L. (1999) · Nature · doi:10.1038/45159 · Cited by 1,541 · see citing works

A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · cited 2× · see citing works

Neurotoxicity induces cleavage of p35 to p25 by calpain

Lee, M.-S., Kwon, Y. T., Li, M., Peng, J., Friedlander, R. M., & Tsai, L. (2000) · Nature · doi:10.1038/35012636 · Cited by 1,057 · see citing works

A decade of CDK5

Dhavan, R., & Tsai, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096019 · Cited by 1,052 · see citing works

Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease

Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998 · see citing works

Tau is essential to β-amyloid-induced neurotoxicity

Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807 · see citing works

Alzheimer's Disease: A Central Role for Amyloid

Selkoe, D. J. (1994) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199409000-00003 · Cited by 752 · see citing works

Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles

Cruz, J. C., Tseng, H.-C., Goldman, J. A., Shih, H., & Tsai, L.-H. (2003) · Neuron · doi:10.1016/s0896-6273(03)00627-5 · Cited by 609 · see citing works

β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595 · see citing works

Cdk5 Is a Key Factor in Tau Aggregation and Tangle Formation In Vivo

Noble, W. J., Olm, V., Takata, K., Casey, E., Mary, O., Meyerson, J. L., Gaynor, K., LaFrancois, J. J., Wang, L., Kondo, T., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00259-9 · Cited by 511 · see citing works

The car☐yl third of tau is tightly bound to paired helical filaments

Kondo, J., Honda, T., Mori, H., Hamada, Y., Miura, R., OGAWARA, M., & Ihara, Y. (1988) · Neuron · doi:10.1016/0896-6273(88)90130-4 · Cited by 355 · see citing works

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 · see citing works

Inhibition of tau phosphorylating protein kinase cdk5 prevents β‐amyloid‐induced neuronal death

Alvarez, A. R., Toro, R., Cáceres, A., & Maccioni, R. B. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01279-x · Cited by 228 · see citing works

Interaction of Tau with the Neural Membrane Cortex Is Regulated by Phosphorylation at Sites That Are Modified in Paired Helical Filaments

Maas, T., Eidenmüller, J., & Brandt, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000389200 · Cited by 226 · see citing works

Calcium dysregulation in Alzheimer's disease

Bojarski, Ł., Herms, J. W., & Kuźnicki, J. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.10.002 · Cited by 202 · see citing works

A Cdk5 inhibitory peptide reduces tau hyperphosphorylation and apoptosis in neurons

Zheng, Y., Kesavapany, S., Gravell, M., Hamilton, R. S., Schubert, M., Amin, N. D., Albers, W., Grant, P. G., & Pant, H. C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600441 · Cited by 190 · see citing works

An Unusual Member of the Cdk Family: Cdk5

Dhariwala, F. A., & Rajadhyaksha, M. S. (2008) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-007-9242-1 · Cited by 173 · see citing works

A Jekyll and Hyde kinase: roles for Cdk5 in brain development and disease

Cruz, J. C., & Tsai, L. (2004) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2004.05.002 · Cited by 170 · see citing works

Elevated neuronal Cdc2-like kinase activity in the Alzheimer disease brain

Lee, K., Clark, A. W., Rosales, J. L., Chapman, K. R., Fung, T. S., & Johnston, R. N. (1999) · Neuroscience Research · doi:10.1016/s0168-0102(99)00026-7 · Cited by 168 · see citing works

Protective effect of caffeic acid against beta-amyloid-induced neurotoxicity by the inhibition of calcium influx and tau phosphorylation

Sul, D., Kim, H.-S., Lee, D., Joo, S. S., Hwang, K. W., & Park, S. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.12.001 · Cited by 158 · see citing works

Amyloid-beta-induced neurotoxicity is reduced by inhibition of glycogen synthase kinase-3

Koh, S., Noh, M., & Kim, S. H. (2007) · Brain Research · doi:10.1016/j.brainres.2007.10.064 · Cited by 126 · see citing works

A Cdk5–p35 Stable Complex Is Involved in the β-Amyloid-Induced Deregulation of Cdk5 Activity in Hippocampal Neurons

Alvarez, A. R., Muñoz, J. P., & Maccioni, R. B. (2001) · Experimental Cell Research · doi:10.1006/excr.2001.5152 · Cited by 125 · see citing works

Neurofibrillary Pathology in Transgenic Mice Overexpressing V717F β-Amyloid Precursor Protein

Masliah, E., Sisk, A., Mallory, M. E., & Games, D. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.4.357 · Cited by 117 · see citing works

Neurodegeneration in an Aβ‐induced model of Alzheimer’s disease: the role of Cdk5

Lopes, J. P., Oliveira, C. R., & Agostinho, P. M. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00536.x · Cited by 86 · see citing works

Cdk5: mediator of neuronal death and survival

Cheung, Z. H., & Ip, N. Y. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2003.12.117 · Cited by 85 · see citing works

Stabilization of the cyclin‐dependent kinase 5 activator, p35, by paclitaxel decreases β‐amyloid toxicity in cortical neurons

Li, G., Faibushevich, A. A., Turunen, B. J., Yoon, S. O., Georg, G. I., Michaelis, M. L., & Dobrowsky, R. T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01526.x · Cited by 71 · see citing works

Inverse and distinct modulation of tau‐dependent neurodegeneration by presenilin 1 and amyloid‐β in cultured cortical neurons: evidence that tau phosphorylation is the limiting factor in amyloid‐β‐induced cell death

Leschik, J., Welzel, A. T., Weissmann, C., Eckert, A., & Brandt, R. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04435.x · Cited by 56 · see citing works

Microtubule‐associated Protein Tau, Paired Helical Filaments, and Phosphorylationa

Mandelkow, E., BIERNAT, J., DREWES, G., STEINER, B., LICHTENBERG‐KRAAG, B., WILLE, H., GUSTKE, N., & MANDELKOW, E. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23054.x · Cited by 53 · see citing works

Involvement of calpain and p25 of CDK5 pathway in ginsenoside Rb1's attenuation of β-amyloid peptide25–35-induced tau hyperphosphorylation in cortical neurons

Chen, X., Huang, T., Zhang, J., Song, J., Chen, L., & Zhu, Y. (2008) · Brain Research · doi:10.1016/j.brainres.2007.12.029 · Cited by 49 · see citing works

β‐Amyloid‐Induced Neurotoxicity of a Hybrid Septal Cell Line Associated with Increased Tau Phosphorylation and Expression of β‐Amyloid Precursor Protein

Le, W., Xie, W., Kong, R., & Appel, S. H. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69030978.x · Cited by 48 · see citing works

Evidence of calpain/cdk5 pathway inhibition by lithium in 3-nitropropionic acid toxicity in vivo and in vitro

Crespo‐Biel, N., Camins, A., Pallàs, M., & Canudas, A. M. (2008) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.09.012 · Cited by 37 · see citing works

Cleavage of the cyclin-dependent kinase 5 activator p35 to p25 does not induce tau hyperphosphorylation

Kerokoski, P., Suuronen, T., Salminen, A., Soininen, H. S., & Pirttilä, T. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02543-3 · Cited by 37 · see citing works

Cyclin-dependent kinase 5 activator p35 over-expression and amyloid beta synergism increase apoptosis in cultured neuronal cells

Utreras, E., Maccioni, R. B., & González-Billault, C. E. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.04.002 · Cited by 30 · see citing works

Effects of Chinese herbal medicine fuzhisan on aged rats

Li, X. L., Wang, D. S., Zhao, B. Q., Li, Q., Qu, H. Y., Zhang, T., Zhou, J. P., & Sun, M. J. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.05.018 · Cited by 29 · see citing works

Increased expression of cdk5/p25 in N2a cells leads to hyperphosphorylation and impaired axonal transport of neurofilament proteins

Zhou, J. H. S., Wang, H., Feng, Y., & Chen, J. (2010) · Life Sciences · doi:10.1016/j.lfs.2010.02.009 · Cited by 27 · see citing works

N ‐acetylcysteine prevents β‐amyloid toxicity by a stimulatory effect on p35/cyclin‐dependent kinase 5 activity in cultured cortical neurons

Hsiao, Y., Chen, P. S., Yeh, S.-H., Lin, C., & Gean, P. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21710 · Cited by 24 · see citing works

Analysis of Fuzhisan and quantitation of baicalin and ginsenoside Rb1 by HPLC-DAD-ELSD

Zhao, J., Wang, D., Duan, S., Wang, J., Bai, J., & Li, W. (2009) · Archives of Pharmacal Research · doi:10.1007/s12272-009-1703-2 · Cited by 23 · see citing works

The efficacy of fuzhisan in patients with Alzheimer's disease

Wang, C. (2005) · Journal of Apoplexy and Nervous Diseases · Cited by 11 · see citing works

Indian Medicinal Herbs and Formulations for Alzheimer’s Disease, from Traditional Knowledge to Scientific Assessment

Mehla, J., Gupta, P., Pahuja, M., Diwan, D., & Diksha, D. (2020) · Brain Sciences · doi:10.3390/brainsci10120964 · Cited by 108 · see citing works

Cdk5-Mediated Phosphorylation of Sirt1 Contributes to Podocyte Mitochondrial Dysfunction in Diabetic Nephropathy

Wang, S., Yang, Y., He, X., Yang, L., Wang, J., Xia, S., Liu, D., Liu, S., Li, Y., Liu, W., et al. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8038 · Cited by 41 · see citing works

Changes in cerebral glucose metabolism in patients with mild-to-moderate Alzheimer's disease: A pilot study with the Chinese herbal medicine fuzhisan

Bi, M., Tong, S., Zhang, Z., Ma, Q., Zhang, S., Luo, Z., Zhang, Y., Li, X., & Wang, D. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.06.036 · Cited by 30 · see citing works

Ginsenoside Rg1 attenuates tau phosphorylation in SK-N-SH induced by Aβ‐stimulated THP-1 supernatant and the involvement of p38 pathway activation

Li, W., Chu, Y., Zhang, L., Yin, L., & Li, L. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.08.028 · Cited by 28 · see citing works

Phytomedicines as potential inhibitors of β amyloid aggregation: significance to Alzheimer's disease

Satheeshkumar, N., & Nisha, N. (2014) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(14)60122-9 · Cited by 24 · see citing works

Experimental Inhibition of Fibrillogenesis and Neurotoxicity by amyloid-beta (Aβ) and Other Disease-Related Peptides/Proteins by Plant Extracts and Herbal Compounds

Kumar, S., Okello, E. J., & Harris, J. R. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5416-4_13 · Cited by 22 · see citing works

Flavonoids from the fruits of Nepalese sumac (Rhus parviflora) attenuate glutamate-induced neurotoxicity in HT22 cells

Shrestha, S., Lee, D., Park, J., Cho, J., Lee, D., Li, B., Kim, Y., Jeon, Y.-J., Yeon, S.-W., & Baek, N. (2013) · Food Science and Biotechnology · doi:10.1007/s10068-013-0161-2 · Cited by 22 · see citing works

Fuzhisan ameliorates Aβ production and tau phosphorylation in hippocampal of 11 month old APP/PS1 transgenic mice: A Western blot study

Zhang, Z.-X., Zhao, R., Wang, D., & Wang, A.-N. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.09.003 · Cited by 20 · see citing works

Flavonoid glycosides from the fruit of Rhus parviflora and inhibition of cyclin dependent kinases by hyperin

Shrestha, S., Lee, D., Park, J., Cho, J., Seo, W. D., Kang, H. C., Jeon, Y.-J., Yeon, S.-W., Bang, M., & Baek, N. (2012) · Journal of the Korean Society for Applied Biological Chemistry · doi:10.1007/s13765-012-2133-2 · Cited by 17 · see citing works

The Use of Natural Products for Preventing Cognitive Decline/Providing Neuroprotection

Tabatabaei‐Malazy, O., Azizi, B., & Abdollahi, M. R. (2024) · Handbook of experimental pharmacology · doi:10.1007/164_2024_732 · Cited by 3 · see citing works

WITHDRAWN: Effects of traditional Chinese medicine Fuzhisan on PP1 expression in the hippocampus of SAMP8 mice

Zhang, G., Lin, L., Yang, H., Wang, T., Li, X., Li, G., Wen, S., & Wang, D. (2011) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2011.08.061 · Cited by 1 · see citing works

Fuzhisan Ameliorates the Memory Deficits in Aged SAMP8 Mice via Decreasing Aβ Production and Tau Hyperphosphorylation of the Hippocampus

Zhang, Z.-X., Zhao, R., Wang, D., & Li, Y.-B. (2016) · Neurochemical Research · doi:10.1007/s11064-016-2028-4 · Cited by 7 · see citing works

Study of Fuzhisan against Aβ25-35 toxicity to nerve cells

Zhang, J. (2003) · Journal of Apoplexy and Nervous Diseases · Cited by 1 · see citing works

Fuzhisan ameliorates Aβ production and tau phosphorylation in hippocampal of 11 month old APP/PS1 transgenic mice: A Western blot study

Zhang, Z.-X., Zhao, R., Wang, D., & Wang, A.-N. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.09.003 · Cited by 20 · see citing works

The protective effects of tanshinone IIA on neurotoxicity induced by β-amyloid protein through calpain and the p35/Cdk5 pathway in primary cortical neurons

Shi, L., Yang, W., Chen, X., Zhang, J.-S., Yang, P., Hu, X., Han, H., Qian, Y., & Liu, Y. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.04.019 · Cited by 64 · see citing works

Fuzhisan, a chinese herbal medicine, suppresses beta-secretase gene transcription via upregulation of SIRT1 expression in N2a-APP695 cells.

Gao, R., Wang, Y., Pan, Q., Huang, G., Li, N., Mou, J., & Wang, D. (2015) · Europe PMC (PubMed Central) · Cited by 13 · see citing works