Grundke-Iqbal I, Iqbal Okay, Quinlan M, Tung YC, Zaidi MS, Wisniewski HM. Microtubule-associated protein tau. A part of Alzheimer paired helical filaments. J Biol Chem. 1986;261:6084–9.
Wang JZ, Xia YY, Grundke-Iqbal I, Iqbal Okay. Abnormal hyperphosphorylation of tau: websites, regulation, and molecular mechanism of neurofibrillary degeneration. J Alzheimer’s Dis. 2013;33:S123–139.
Iqbal Okay, Grundke-Iqbal I, Zaidi T, Merz PA, Wen GY, Shaikh SS, et al. Defective mind microtubule meeting in Alzheimer’s illness. Lancet. 1986;2:421–6.
Iqbal Okay, Grundke-Iqbal I, Smith AJ, George L, Tung YC, Zaidi T. Identification and localization of a tau peptide to paired helical filaments of Alzheimer illness. Proc Natl Acad Sci USA. 1989;86:5646–50.
Lee VM, Balin BJ, Otvos L Jr, Trojanowski JQ. A68: a serious subunit of paired helical filaments and derivatized types of regular Tau. Science. 1991;251:675–8.
Novak M, Kabat J, Wischik CM. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer’s illness paired helical filament. EMBO J. 1993;12:365–70.
Grundke-Iqbal I, Iqbal Okay, Tung YC, Quinlan M, Wisniewski HM, Binder LI. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci USA. 1986;83:4913–7.
Nelson PT, Alafuzoff I, Bigio EH, Bouras C, Braak H, Cairns NJ, et al. Correlation of Alzheimer illness neuropathologic modifications with cognitive standing: a overview of the literature. J Neuropathol Exp Neurol. 2012;71:362–81.
Braak H, Braak E. Neuropathological stageing of Alzheimer-related modifications. Acta Neuropathol. 1991;82:239–59.
Alafuzoff I, Iqbal Okay, Friden H, Adolfsson R, Winblad B. Histopathological standards for progressive dementia problems: clinical-pathological correlation and classification by multivariate knowledge evaluation. Acta Neuropathol. 1987;74:209–25.
Arriagada PV, Growdon JH, Hedley-Whyte ET, Hyman BT. Neurofibrillary tangles however not senile plaques parallel period and severity of Alzheimer’s illness. Neurology. 1992;42:631–9.
Elahi FM, Miller BL. A clinicopathological strategy to the analysis of dementia. Nat Rev Neurol. 2017;13:457–76.
Therriault J, Zimmer ER, Benedet AL, Pascoal TA, Gauthier S, Rosa-Neto P. Staging of Alzheimer’s illness: previous, current, and future views. Trends Mol Med. 2022;28:726–741.
Ossenkoppele R, Hansson O. Towards medical utility of tau PET tracers for diagnosing dementia as a result of Alzheimer’s illness. Alzheimers Dement. 2021;17:1998–2008.
Wolters EE, Ossenkoppele R, Verfaillie SCJ, Coomans EM, Timmers T, Visser D, et al. Regional [(18)F]flortaucipir PET is extra intently related to illness severity than CSF p-tau in Alzheimer’s illness. Eur J Nucl Med Mol Imaging. 2020;47:2866–78.
La Joie R, Bejanin A, Fagan AM, Ayakta N, Baker SL, Bourakova V, et al. Associations between [(18)F]AV1451 tau PET and CSF measures of tau pathology in a medical pattern. Neurology. 2018;90:e282–e290.
Cho H, Choi JY, Hwang MS, Kim YJ, Lee HM, Lee HS, et al. In vivo cortical spreading sample of tau and amyloid within the Alzheimer illness spectrum. Ann Neurol. 2016;80:247–58.
Scholl M, Lockhart SN, Schonhaut DR, O’Neil JP, Janabi M, Ossenkoppele R, et al. PET Imaging of Tau Deposition within the Aging Human Brain. Neuron. 2016;89:971–82.
Qiang L, Sun X, Austin TO, Muralidharan H, Jean DC, Liu M, et al. Tau Does Not Stabilize Axonal Microtubules however Rather Enables Them to Have Long Labile Domains. Curr Biol. 2018;28:2181–2189.e2184.
Dehmelt L, Halpain S. The MAP2/Tau household of microtubule-associated proteins. Genome Biol. 2005;6:204.
Meier S, Bell M, Lyons DN, Rodriguez-Rivera J, Ingram A, Fontaine SN, et al. Pathological Tau Promotes Neuronal Damage by Impairing Ribosomal Function and Decreasing Protein Synthesis. J Neurosci. 2016;36:1001–7.
Hamdane M, Bretteville A, Sambo AV, Schindowski Okay, Begard S, Delacourte A, et al. p25/Cdk5-mediated retinoblastoma phosphorylation is an early occasion in neuronal cell demise. J Cell Sci. 2005;118:1291–8.
Qu MH, Li H, Tian R, Nie CL, Liu Y, Han BS, et al. Neuronal tau induces DNA conformational modifications noticed by atomic power microscopy. Neuroreport. 2004;15:2723–7.
Qi H, Cantrelle FX, Benhelli-Mokrani H, Smet-Nocca C, Buee L, Lippens G, et al. Nuclear magnetic resonance spectroscopy characterization of interplay of Tau with DNA and its regulation by phosphorylation. Biochemistry. 2015;54:1525–33.
Frost B, Hemberg M, Lewis J, Feany MB. Tau promotes neurodegeneration by means of international chromatin rest. Nat Neurosci. 2014;17:357–66.
Camero S, Benitez MJ, Barrantes A, Ayuso JM, Cuadros R, Avila J, et al. Tau protein gives DNA with thermodynamic and structural options that are just like these present in histone-DNA advanced. J Alzheimer’s Dis. 2014;39:649–60.
Brandt R. The tau proteins in neuronal progress and growth. Front Biosci. 1996;1:d118–130.
DeVos SL, Hyman BT. Tau on the Crossroads between Neurotoxicity and Neuroprotection. Neuron. 2017;94:703–4.
Pevalova M, Filipcik P, Novak M, Avila J, Iqbal Okay. Post-translational modifications of tau protein. Bratisl Lek Listy. 2006;107:346–53.
Gorantla NV, Chinnathambi S. Tau Protein Squired by Molecular Chaperones During Alzheimer’s Disease. J Mol Neurosci. 2018;66:356–68.
Jiang S, Bhaskar Okay. Degradation and Transmission of Tau by Autophagic-Endolysosomal Networks and Potential Therapeutic Targets for Tauopathy. Front Mol Neurosci. 2020;13:586731.
Ahmadi S, Zhu S, Sharma R, Wilson DJ, Kraatz HB. Interaction of steel ions with tau protein. The case for a metal-mediated tau aggregation. J Inorg Biochem. 2019;194:44–51.
Chiti F, Dobson CM. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Annu Rev Biochem. 2017;86:27–68.
Mamun AA, Uddin MS, Mathew B, Ashraf GM. Toxic tau: structural origins of tau aggregation in Alzheimer’s illness. Neural Regen Res. 2020;15:1417–20.
Iqbal Okay, Liu F, Gong CX. Tau and neurodegenerative illness: the story to this point. Nat Rev Neurol. 2016;12:15–27.
Iqbal Okay, Liu F, Gong CX. Recent developments with tau-based drug discovery. Expert Opin Drug Disco. 2018;13:399–410.
Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer’s illness. Neuron. 1989;3:519–26.
Morishima-Kawashima M, Hasegawa M, Takio Okay, Suzuki M, Yoshida H, Titani Okay, et al. Proline-directed and non-proline-directed phosphorylation of PHF-tau. J Biol Chem. 1995;270:823–9.
Hanger DP, Byers HL, Wray S, Leung KY, Saxton MJ, Seereeram A, et al. Novel phosphorylation websites in tau from Alzheimer mind assist a task for casein kinase 1 in illness pathogenesis. J Biol Chem. 2007;282:23645–54.
Hasegawa M, Morishima-Kawashima M, Takio Okay, Suzuki M, Titani Okay, Ihara Y. Protein sequence and mass spectrometric analyses of tau within the Alzheimer’s illness mind. J Biol Chem. 1992;267:17047–54.
Alonso AC, Zaidi T, Grundke-Iqbal I, Iqbal Okay. Role of abnormally phosphorylated tau within the breakdown of microtubules in Alzheimer illness. Proc Natl Acad Sci USA. 1994;91:5562–6.
Kopke E, Tung YC, Shaikh S, Alonso AC, Iqbal Okay, Grundke-Iqbal I. Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer illness. J Biol Chem. 1993;268:24374–84.
Despres C, Di J, Cantrelle FX, Li Z, Huvent I, Chambraud B, et al. Major Differences between the Self-Assembly and Seeding Behavior of Heparin-Induced and in Vitro Phosphorylated Tau and Their Modulation by Potential Inhibitors. ACS Chem Biol. 2019;14:1363–79.
Shi Y, Zhang W, Yang Y, Murzin AG, Falcon B, Kotecha A, et al. Structure-based classification of tauopathies. Nature. 2021;598:359–63.
Scheres SH, Zhang W, Falcon B, Goedert M. Cryo-EM buildings of tau filaments. Curr Opin Struct Biol. 2020;64:17–25.
Samimi N, Sharma G, Kimura T, Matsubara T, Huo A, Chiba Okay, et al. Distinct phosphorylation profiles of tau in brains of sufferers with totally different tauopathies. Neurobiol Aging. 2021;108:72–79.
Rawat P, Sehar U, Bisht J, Selman A, Culberson J, Reddy PH. Phosphorylated Tau in Alzheimer’s Disease and Other Tauopathies. Int J Mol Sci. 2022;23:12841.
Kitoka Okay, Skrabana R, Gasparik N, Hritz J, Jaudzems Okay. NMR Studies of Tau Protein in Tauopathies. Front Mol Biosci. 2021;8:761227.
Jadhav S, Avila J, Scholl M, Kovacs GG, Kovari E, Skrabana R, et al. A walk by means of tau therapeutic methods. Acta Neuropathol Commun. 2019;7:22.
Chang CW, Shao E, Mucke L. Tau: Enabler of numerous mind problems and goal of quickly evolving therapeutic methods. Science. 2021;371:eabb8255.
Guo Y, Li S, Zeng L-H, Tan J. Tau-targeting remedy in Alzheimer’s illness: essential advances and future alternatives. Ageing Neurodegener Dis. 2022;2:11.
Sutherland C. What Are the bona fide GSK3 Substrates? Int J Alzheimers Dis. 2011;2011:505607.
Boyle WJ, Smeal T, Defize LH, Angel P, Woodgett JR, Karin M, et al. Activation of protein kinase C decreases phosphorylation of c-Jun at websites that negatively regulate its DNA-binding exercise. Cell. 1991;64:573–84.
Beals CR, Sheridan CM, Turck CW, Gardner P, Crabtree GR. Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3. Science. 1997;275:1930–4.
Cho JH, Johnson GV. Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) performs a essential function in regulating tau’s skill to bind and stabilize microtubules. J Neurochem. 2004;88:349–58.
Zaoui Okay, Benseddik Okay, Daou P, Salaun D, Badache A. ErbB2 receptor controls microtubule seize by recruiting ACF7 to the plasma membrane of migrating cells. Proc Natl Acad Sci USA. 2010;107:18517–22.
Dajani R, Fraser E, Roe SM, Yeo M, Good VM, Thompson V, et al. Structural foundation for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold advanced. EMBO J. 2003;22:494–501.
Frame S, Cohen P, Biondi RM. A standard phosphate binding web site explains the distinctive substrate specificity of GSK3 and its inactivation by phosphorylation. Mol Cell. 2001;7:1321–7.
Yin L, Wang J, Klein PS, Lazar MA. Nuclear receptor Rev-erbalpha is a essential lithium-sensitive part of the circadian clock. Science. 2006;311:1002–5.
Woodgett JR. Molecular cloning and expression of glycogen synthase kinase-3/issue A. EMBO J. 1990;9:2431–8.
Zhang F, Phiel CJ, Spece L, Gurvich N, Klein PS. Inhibitory phosphorylation of glycogen synthase kinase-3 (GSK-3) in response to lithium. Evidence for autoregulation of GSK-3. J Biol Chem. 2003;278:33067–77.
Singh TJ, Haque N, Grundke-Iqbal I, Iqbal Okay. Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinases and GSK-3. FEBS Lett. 1995;358:267–72.
Polakis P. Casein kinase 1: a Wnt’er of disconnect. Curr Biol. 2002;12:R499–R501.
Lovestone S, Reynolds CH, Latimer D, Davis DR, Anderton BH, Gallo JM, et al. Alzheimer’s disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells. Curr Biol. 1994;4:1077–86.
Wagner U, Utton M, Gallo JM, Miller CC. Cellular phosphorylation of tau by GSK-3 beta influences tau binding to microtubules and microtubule organisation. J Cell Sci. 1996;109:1537–43.
Sang H, Lu Z, Li Y, Ru B, Wang W, Chen J. Phosphorylation of tau by glycogen synthase kinase 3beta in intact mammalian cells influences the soundness of microtubules. Neurosci Lett. 2001;312:141–4.
Sperbera BR, Leight S, Goedert M, Lee V-Y. Glycogen synthase kinase-3β phosphorylates tau protein at a number of websites in intact cells. Neurosci Lett. 1995;197:149–53.
Lovestone S, Hartley CL, Pearce J, Anderton BH. Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the results on the organization and stability of microtubules. Neuroscience. 1996;73:1145–57.
Cruz JC, Tseng HC, Goldman JA, Shih H, Tsai LH. Aberrant Cdk5 activation by p25 triggers pathological occasions resulting in neurodegeneration and neurofibrillary tangles. Neuron. 2003;40:471–83.
Lopes JP, Agostinho P. Cdk5: multitasking between physiological and pathological situations. Prog Neurobiol. 2011;94:49–63.
Zhang J, Li H, Yabut O, Fitzpatrick H, D’Arcangelo G, Herrup Okay. Cdk5 suppresses the neuronal cell cycle by disrupting the E2F1-DP1 advanced. J Neurosci. 2010;30:5219–28.
Kim D, Frank CL, Dobbin MM, Tsunemoto RK, Tu W, Peng PL, et al. Deregulation of HDAC1 by p25/Cdk5 in neurotoxicity. Neuron. 2008;60:803–17.
Chang KH, Vincent F, Shah Okay. Deregulated Cdk5 triggers aberrant activation of cell cycle kinases and phosphatases inducing neuronal demise. J Cell Sci. 2012;125:5124–37.
Dhavan R, Tsai LH. A decade of CDK5. Nat Rev Mol Cell Biol. 2001;2:749–59.
Lee MS, Kwon YT, Li M, Peng J, Friedlander RM, Tsai LH. Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature. 2000;405:360–4.
Kusakawa G, Saito T, Onuki R, Ishiguro Okay, Kishimoto T, Hisanaga S. Calpain-dependent proteolytic cleavage of the p35 cyclin-dependent kinase 5 activator to p25. J Biol Chem. 2000;275:17166–72.
Engmann O, Giese KP. Crosstalk between Cdk5 and GSK3beta: Implications for Alzheimer’s Disease. Front Mol Neurosci. 2009;2:2.
Origlia N, Arancio O, Domenici L, Yan SS. MAPK, beta-amyloid and synaptic dysfunction: the function of RAGE. Expert Rev Neurother. 2009;9:1635–45.
Cuadrado A, Nebreda AR. Mechanisms and capabilities of p38 MAPK signalling. Biochem J. 2010;429:403–17.
Falcicchia C, Tozzi F, Arancio O, Watterson DM, Origlia N. Involvement of p38 MAPK in Synaptic Function and Dysfunction. Int J Mol Sci. 2020;21:5624.
Goedert M, Hasegawa M, Jakes R, Lawler S, Cuenda A, Cohen P. Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases. FEBS Lett. 1997;409:57–62.
Zhu X, Rottkamp CA, Boux H, Takeda A, Perry G, Smith MA. Activation of p38 kinase hyperlinks tau phosphorylation, oxidative stress, and cell cycle-related occasions in Alzheimer illness. J Neuropathol Exp Neurol. 2000;59:880–8.
Becker W, Weber Y, Wetzel Okay, Eirmbter Okay, Tejedor FJ, Joost HG. Sequence traits, subcellular localization, and substrate specificity of DYRK-related kinases, a novel household of twin specificity protein kinases. J Biol Chem. 1998;273:25893–902.
Liu F, Liang Z, Wegiel J, Hwang YW, Iqbal Okay, Grundke-Iqbal I, et al. Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome. FASEB J. 2008;22:3224–33.
Ryoo SR, Jeong HK, Radnaabazar C, Yoo JJ, Cho HJ, Lee HW, et al. DYRK1A-mediated hyperphosphorylation of Tau. A practical hyperlink between Down syndrome and Alzheimer illness. J Biol Chem. 2007;282:34850–7.
Trinczek B, Brajenovic M, Ebneth A, Drewes G. MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the mobile microtubule community and to centrosomes. J Biol Chem. 2004;279:5915–23.
Gu GJ, Lund H, Wu D, Blokzijl A, Classon C, von Euler G, et al. Role of particular person MARK isoforms in phosphorylation of tau at Ser(2)(6)(2) in Alzheimer’s illness. Neuromol Med. 2013;15:458–69.
Drubin DG, Nelson WJ. Origins of cell polarity. Cell. 1996;84:335–44.
Tournebize R, Heald R, Hyman A. Role of chromosomes in meeting of meiotic and mitotic spindles. Prog Cell Cycle Res. 1997;3:271–84.
Oba T, Saito T, Asada A, Shimizu S, Iijima KM, Ando Okay. Microtubule affinity-regulating kinase 4 with an Alzheimer’s disease-related mutation promotes tau accumulation and exacerbates neurodegeneration. J Biol Chem. 2020;295:17138–47.
Naz F, Islam A, Ahmad F, Hassan MI. Atypical PKC phosphorylates microtubule affinity-regulating kinase 4 in vitro. Mol Cell Biochem. 2015;410:223–8.
Saito T, Oba T, Shimizu S, Asada A, Iijima KM, Ando Okay. Cdk5 will increase MARK4 exercise and augments pathological tau accumulation and toxicity by means of tau phosphorylation at Ser262. Hum Mol Genet. 2019;28:3062–71.
Le Beau MM, Westbrook CA, Diaz MO, Rowley JD. Evidence for 2 distinct c-src loci on human chromosomes 1 and 20. Nature. 1984;312:70–71.
Parsons SJ, Parsons JT. Src household kinases, key regulators of sign transduction. Oncogene. 2004;23:7906–9.
Lee G, Newman ST, Gard DL, Band H, Panchamoorthy G. Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci. 1998;111:3167–77.
Williamson R, Scales T, Clark BR, Gibb G, Reynolds CH, Kellie S, et al. Rapid tyrosine phosphorylation of neuronal proteins together with tau and focal adhesion kinase in response to amyloid-beta peptide publicity: involvement of Src household protein kinases. J Neurosci. 2002;22:10–20.
Lee G, Thangavel R, Sharma VM, Litersky JM, Bhaskar Okay, Fang SM, et al. Phosphorylation of tau by fyn: implications for Alzheimer’s illness. J Neurosci. 2004;24:2304–12.
Wang JY, Ledley F, Goff S, Lee R, Groner Y, Baltimore D. The mouse c-abl locus: molecular cloning and characterization. Cell. 1984;36:349–56.
Heisterkamp N, Groffen J, Stephenson JR, Spurr NK, Goodfellow PN, Solomon E, et al. Chromosomal localization of human mobile homologues of two viral oncogenes. Nature. 1982;299:747–9.
Jhanwar SC, Neel BG, Hayward WS, Chaganti RS. Localization of the mobile oncogenes ABL, SIS, and FES on human germ-line chromosomes. Cytogenet Cell Genet. 1984;38:73–5.
Van Etten RA, Jackson P, Baltimore D. The mouse kind IV c-abl gene product is a nuclear protein, and activation of remodeling skill is related to cytoplasmic localization. Cell. 1989;58:669–78.
Hantschel O, Superti-Furga G. Regulation of the c-Abl and Bcr-Abl tyrosine kinases. Nat Rev Mol Cell Biol. 2004;5:33–44.
Derkinderen P, Scales TM, Hanger DP, Leung Okay-Y, Byers HL, Ward MA, et al. Tyrosine 394 is phosphorylated in Alzheimer’s paired helical filament tau and in fetal tau with c-Abl because the candidate tyrosine kinase. J Neurosci. 2005;25:6584–93.
Cancino GI, Perez de Arce Okay, Castro PU, Toledo EM, von Bernhardi R, Alvarez AR. c-Abl tyrosine kinase modulates tau pathology and Cdk5 phosphorylation in AD transgenic mice. Neurobiol Aging. 2011;32:1249–61.
Zukerberg LR, Patrick GN, Nikolic M, Humbert S, Wu CL, Lanier LM, et al. Cables hyperlinks Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth. Neuron. 2000;26:633–46.
Ho GJ, Hashimoto M, Adame A, Izu M, Alford MF, Thal LJ, et al. Altered p59Fyn kinase expression accompanies illness development in Alzheimer’s illness: implications for its practical function. Neurobiol Aging. 2005;26:625–35.
Bhaskar Okay, Yen SH, Lee G. Disease-related modifications in tau have an effect on the interplay between Fyn and Tau. J Biol Chem. 2005;280:35119–25.
Amano M, Fukata Y, Kaibuchi Okay. Regulation and capabilities of Rho-associated kinase. Exp Cell Res. 2000;261:44–51.
Chen J, Sun Z, Jin M, Tu Y, Wang S, Yang X, et al. Inhibition of AGEs/RAGE/Rho/ROCK pathway suppresses non-specific neuroinflammation by regulating BV2 microglial M1/M2 polarization by means of the NF-kappaB pathway. J Neuroimmunol. 2017;305:108–14.
Mueller BK, Mack H, Teusch N. Rho kinase, a promising drug goal for neurological problems. Nat Rev Drug Disco. 2005;4:387–98.
Koch JC, Tatenhorst L, Roser AE, Saal KA, Tonges L, Lingor P. ROCK inhibition in fashions of neurodegeneration and its potential for medical translation. Pharm Ther. 2018;189:1–21.
Gao Y, Yan Y, Fang Q, Zhang N, Kumar G, Zhang J, et al. The Rho kinase inhibitor fasudil attenuates Abeta(1-42)-induced apoptosis through the ASK1/JNK sign pathway in main cultures of hippocampal neurons. Metab Brain Dis. 2019;34:1787–801.
Amano M, Kaneko T, Maeda A, Nakayama M, Ito M, Yamauchi T, et al. Identification of Tau and MAP2 as novel substrates of Rho-kinase and myosin phosphatase. J Neurochem. 2003;87:780–90.
Hennequin LF, Allen J, Breed J, Curwen J, Fennell M, Green TP, et al. N-(5-chloro-1,3-benzodioxol-4-yl)-7-[2-(4-methylpiperazin-1-yl)ethoxy]-5- (tetrahydro-2H-pyran-4-yloxy)quinazolin-4-amine, a novel, extremely selective, orally out there, dual-specific c-Src/Abl kinase inhibitor. J Med Chem. 2006;49:6465–88.
Green TP, Fennell M, Whittaker R, Curwen J, Jacobs V, Allen J, et al. Preclinical anticancer exercise of the potent, oral Src inhibitor AZD0530. Mol Oncol. 2009;3:248–61.
Jakobsson E, Arguello-Miranda O, Chiu SW, Fazal Z, Kruczek J, Nunez-Corrales S, et al. Towards a Unified Understanding of Lithium Action in Basic Biology and its Significance for Applied Biology. J Membr Biol. 2017;250:587–604.
Ryves WJ, Harwood AJ. Lithium inhibits glycogen synthase kinase-3 by competitors for magnesium. Biochem Biophys Res Commun. 2001;280:720–5.
Freland L, Beaulieu JM. Inhibition of GSK3 by lithium, from single molecules to signaling networks. Front Mol Neurosci. 2012;5:14.
De-Paula VJ, Forlenza OV. Lithium modulates a number of tau kinases with distinct results in cortical and hippocampal neurons in keeping with focus ranges. Naunyn-Schmiedeberg’s Arch Pharmacol. 2022;395:105–13.
Salomoni P, Calabretta B. Targeted therapies and autophagy: new insights from persistent myeloid leukemia. Autophagy. 2009;5:1050–1.
Weisberg E, Manley P, Mestan J, Cowan-Jacob S, Ray A, Griffin JD. AMN107 (nilotinib): a novel and selective inhibitor of BCR-ABL. Br J Cancer. 2006;94:1765–9.
Pagan FL, Hebron ML, Wilmarth B, Torres-Yaghi Y, Lawler A, Mundel EE, et al. Pharmacokinetics and pharmacodynamics of a single dose Nilotinib in people with Parkinson’s illness. Pharm Res Perspect. 2019;7:e00470.
Pagan FL, Hebron ML, Wilmarth B, Torres-Yaghi Y, Lawler A, Mundel EE, et al. Nilotinib Effects on Safety, Tolerability, and Potential Biomarkers in Parkinson Disease: A Phase 2 Randomized Clinical Trial. JAMA Neurol. 2020;77:309–17.
Nishioka H, Tooi N, Isobe T, Nakatsuji N, Aiba Okay. BMS-708163 and Nilotinib restore synaptic dysfunction in human embryonic stem cell-derived Alzheimer’s illness fashions. Sci Rep. 2016;6:33427.
Wu J, Xu X, Zheng L, Mo J, Jin X, Bao Y. Nilotinib inhibits microglia-mediated neuroinflammation to guard towards dopaminergic neuronal demise in Parkinson’s illness fashions. Int Immunopharmacol. 2021;99:108025.
Fowler AJ, Hebron M, Balaraman Okay, Shi W, Missner AA, Greenzaid JD, et al. Discoidin Domain Receptor 1 is a therapeutic goal for neurodegenerative ailments. Hum Mol Genet. 2020;29:2882–98.
Martinez A, Alonso M, Castro A, Pérez C, Moreno FJ. First non-ATP aggressive glycogen synthase kinase 3 beta (GSK-3beta) inhibitors: thiadiazolidinones (TDZD) as potential medicine for the therapy of Alzheimer’s illness. J Med Chem. 2002;45:1292–9.
Domínguez JM, Fuertes A, Orozco L, del Monte-Millán M, Delgado E, Medina M. Evidence for irreversible inhibition of glycogen synthase kinase-3β by tideglusib. J Biol Chem. 2012;287:893–904.
Noori MS, Bhatt PM, Courreges MC, Ghazanfari D, Cuckler C, Orac CM, et al. Identification of a novel selective and potent inhibitor of glycogen synthase kinase-3. Am J Physiol Cell Physiol. 2019;317:C1289–C1303.
Sereno L, Coma M, Rodriguez M, Sanchez-Ferrer P, Sanchez MB, Gich I, et al. A novel GSK-3beta inhibitor reduces Alzheimer’s pathology and rescues neuronal loss in vivo. Neurobiol Dis. 2009;35:359–67.
Luna-Medina R, Cortes-Canteli M, Sanchez-Galiano S, Morales-Garcia JA, Martinez A, Santos A, et al. NP031112, a thiadiazolidinone compound, prevents irritation and neurodegeneration below excitotoxic situations: potential therapeutic function in mind problems. J Neurosci. 2007;27:5766–76.
Griebel G, Stemmelin J, Lopez-Grancha M, Boulay D, Boquet G, Slowinski F, et al. The selective GSK3 inhibitor, SAR502250, shows neuroprotective exercise and attenuates behavioral impairments in fashions of neuropsychiatric signs of Alzheimer’s illness in rodents. Sci Rep. 2019;9:18045.
Noble W, Planel E, Zehr C, Olm V, Meyerson J, Suleman F, et al. Inhibition of glycogen synthase kinase-3 by lithium correlates with lowered tauopathy and degeneration in vivo. Proc Natl Acad Sci USA. 2005;102:6990–5.
Bhat R, Xue Y, Berg S, Hellberg S, Ormo M, Nilsson Y, et al. Structural insights and organic results of glycogen synthase kinase 3-specific inhibitor AR-A014418. J Biol Chem. 2003;278:45937–45.
Onishi T, Iwashita H, Uno Y, Kunitomo J, Saitoh M, Kimura E, et al. A novel glycogen synthase kinase-3 inhibitor 2-methyl-5-(3-{4-[(S)-methylsulfinyl]phenyl}-1-benzofuran-5-yl)-1,3,4-oxadiazole decreases tau phosphorylation and ameliorates cognitive deficits in a transgenic mannequin of Alzheimer’s illness. J Neurochem. 2011;119:1330–40.
Kitazawa M, Oddo S, Yamasaki TR, Green KN, LaFerla FM. Lipopolysaccharide-induced irritation exacerbates tau pathology by a cyclin-dependent kinase 5-mediated pathway in a transgenic mannequin of Alzheimer’s illness. J Neurosci. 2005;25:8843–53.
Maphis N, Jiang S, Xu G, Kokiko-Cochran ON, Roy SM, Van Eldik LJ, et al. Selective suppression of the alpha isoform of p38 MAPK rescues late-stage tau pathology. Alzheimers Res Ther. 2016;8:54.
Hebron ML, Javidnia M, Moussa CE-H. Tau clearance improves astrocytic operate and mind glutamate-glutamine cycle. J Neurol Sci. 2018;391:90–99.
Melchior B, Mittapalli GK, Lai C, Duong-Polk Okay, Stewart J, Guner B, et al. Tau pathology discount with SM07883, a novel, potent, and selective oral DYRK1A inhibitor: A possible therapeutic for Alzheimer’s illness. Aging Cell. 2019;18:e13000.
Branca C, Shaw DM, Belfiore R, Gokhale V, Shaw AY, Foley C, et al. Dyrk1 inhibition improves Alzheimer’s disease-like pathology. Aging Cell. 2017;16:1146–54.
Velazquez R, Meechoovet B, Ow A, Foley C, Shaw A, Smith B, et al. Chronic Dyrk1 Inhibition Delays the Onset of AD-Like Pathology in 3xTg-AD Mice. Mol Neurobiol. 2019;56:8364–75.
Schweig JE, Yao H, Coppola Okay, Jin C, Crawford F, Mullan M, et al. Spleen tyrosine kinase (SYK) blocks autophagic Tau degradation in vitro and in vivo. J Biol Chem. 2019;294:13378–95.
Hamano T, Shirafuji N, Yen SH, Yoshida H, Kanaan NM, Hayashi Okay, et al. Rho-kinase ROCK inhibitors cut back oligomeric tau protein. Neurobiol Aging. 2020;89:41–54.
Liu F, Liang Z, Gong CX. Hyperphosphorylation of tau and protein phosphatases in Alzheimer illness. Panminerva Med. 2006;48:97–108.
Liu F, Grundke-Iqbal I, Iqbal Okay, Gong CX. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur J Neurosci. 2005;22:1942–50.
Goedert M, Jakes R, Qi Z, Wang JH, Cohen P. Protein phosphatase 2A is the main enzyme in mind that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase. J Neurochem. 1995;65:2804–7.
Gong CX, Singh TJ, Grundke-Iqbal I, Iqbal Okay. Phosphoprotein phosphatase actions in Alzheimer illness mind. J Neurochem. 1993;61:921–7.
Gong CX, Shaikh S, Wang JZ, Zaidi T, Grundke-Iqbal I, Iqbal Okay. Phosphatase exercise towards abnormally phosphorylated tau: lower in Alzheimer illness mind. J Neurochem. 1995;65:732–8.
Liu F, Iqbal Okay, Grundke-Iqbal I, Rossie S, Gong CX. Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer’s illness. J Biol Chem. 2005;280:1790–6.
Sontag E, Luangpirom A, Hladik C, Mudrak I, Ogris E, Speciale S, et al. Altered expression ranges of the protein phosphatase 2A ABalphaC enzyme are related to Alzheimer illness pathology. J Neuropathol Exp Neurol. 2004;63:287–301.
Liu F, Grundke-Iqbal I, Iqbal Okay, Oda Y, Tomizawa Okay, Gong CX. Truncation and activation of calcineurin A by calpain I in Alzheimer illness mind. J Biol Chem. 2005;280:37755–62.
Janssens V, Goris J. Protein phosphatase 2A: a extremely regulated household of serine/threonine phosphatases implicated in cell progress and signalling. Biochem J. 2001;353:417–39.
Shi Y. Serine/threonine phosphatases: mechanism by means of construction. Cell. 2009;139:468–84.
Tanimukai H, Grundke-Iqbal I, Iqbal Okay. Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer’s illness. Am J Pathol. 2005;166:1761–71.
Shentu YP, Huo Y, Feng XL, Gilbert J, Zhang Q, Liuyang ZY, et al. CIP2A Causes Tau/APP Phosphorylation, Synaptopathy, and Memory Deficits in Alzheimer’s Disease. Cell Rep. 2018;24:713–23.
Qian W, Shi J, Yin X, Iqbal Okay, Grundke-Iqbal I, Gong CX, et al. PP2A regulates tau phosphorylation straight and in addition not directly through activating GSK-3beta. J Alzheimer’s Dis: JAD. 2010;19:1221–9.
Wang Y, Yang R, Gu J, Yin X, Jin N, Xie S, et al. Cross discuss between PI3K-AKT-GSK-3beta and PP2A pathways determines tau hyperphosphorylation. Neurobiol Aging. 2015;36:188–200.
Corcoran NM, Martin D, Hutter-Paier B, Windisch M, Nguyen T, Nheu L, et al. Sodium selenate particularly prompts PP2A phosphatase, dephosphorylates tau and reverses reminiscence deficits in an Alzheimer’s illness mannequin. J Clin Neurosci. 2010;17:1025–33.
Ahmed T, Van der Jeugd A, Caillierez R, Buee L, Blum D, D’Hooge R, et al. Chronic Sodium Selenate Treatment Restores Deficits in Cognition and Synaptic Plasticity in a Murine Model of Tauopathy. Front Mol Neurosci. 2020;13:570223.
Jin N, Zhu H, Liang X, Huang W, Xie Q, Xiao P, et al. Sodium selenate activated Wnt/beta-catenin signaling and repressed amyloid-beta formation in a triple transgenic mouse mannequin of Alzheimer’s illness. Exp Neurol. 2017;297:36–49.
van Eersel J, Ke YD, Liu X, Delerue F, Kril JJ, Gotz J, et al. Sodium selenate mitigates tau pathology, neurodegeneration, and practical deficits in Alzheimer’s illness fashions. Proc Natl Acad Sci USA. 2010;107:13888–93.
Zaki MO, El-Desouky S, Elsherbiny DA, Salama M, Azab SS. Glimepiride mitigates tauopathy and neuroinflammation in P301S transgenic mice: function of AKT/GSK3beta signaling. Inflammopharmacology. 2022;30:1871–90.
Zhao S, Fan Z, Zhang X, Li Z, Shen T, Li Okay, et al. Metformin Attenuates Tau Pathology in Tau-Seeded PS19 Mice. Neurotherapeutics. 2023;20:452–63.
Barini E, Antico O, Zhao Y, Asta F, Tucci V, Catelani T, et al. Metformin promotes tau aggregation and exacerbates irregular habits in a mouse mannequin of tauopathy. Mol Neurodegener. 2016;11:16.
Kickstein E, Krauss S, Thornhill P, Rutschow D, Zeller R, Sharkey J, et al. Biguanide metformin acts on tau phosphorylation through mTOR/protein phosphatase 2A (PP2A) signaling. Proc Natl Acad Sci USA. 2010;107:21830–5.
Sedjahtera A, Gunawan L, Bray L, Hung LW, Parsons J, Okamura N, et al. Targeting metals rescues the phenotype in an animal mannequin of tauopathy. Metallomics. 2018;10:1339–47.
Beauchamp LC, Liu XM, Sedjahtera A, Bogeski M, Vella LJ, Bush AI, et al. S-Adenosylmethionine Rescues Cognitive Deficits within the rTg4510 Animal Model by Stabilizing Protein Phosphatase 2A and Reducing Phosphorylated Tau. J Alzheimer’s Dis: JAD. 2020;77:1705–15.
Sontag E, Nunbhakdi-Craig V, Sontag JM, Diaz-Arrastia R, Ogris E, Dayal S, et al. Protein phosphatase 2A methyltransferase hyperlinks homocysteine metabolism with tau and amyloid precursor protein regulation. J Neurosci. 2007;27:2751–9.
Wei W, Liu YH, Zhang CE, Wang Q, Wei Z, Mousseau DD, et al. Folate/vitamin-B12 prevents persistent hyperhomocysteinemia-induced tau hyperphosphorylation and reminiscence deficits in aged rats. J Alzheimer’s Dis: JAD. 2011;27:639–50.
Xiong Y, Jing XP, Zhou XW, Wang XL, Yang Y, Sun XY, et al. Zinc induces protein phosphatase 2A inactivation and tau hyperphosphorylation by means of Src dependent PP2A (tyrosine 307) phosphorylation. Neurobiol Aging. 2013;34:745–56.
Fagan SG, Bechet S, Dev KK. Fingolimod Rescues Memory and Improves Pathological Hallmarks within the 3xTg-AD Model of Alzheimer’s Disease. Mol Neurobiol. 2022;59:1882–95.
Laurent C, Eddarkaoui S, Derisbourg M, Leboucher A, Demeyer D, Carrier S, et al. Beneficial results of caffeine in a transgenic mannequin of Alzheimer’s disease-like tau pathology. Neurobiol Aging. 2014;35:2079–90.
Tan X, Liang Z, Li Y, Zhi Y, Yi L, Bai S, et al. Isoorientin, a GSK-3beta inhibitor, rescues synaptic dysfunction, spatial reminiscence deficits and attenuates pathological development in APP/PS1 mannequin mice. Behav Brain Res. 2021;398:112968.
Chen Q, Tu Y, Mak S, Chen J, Lu J, Chen C, et al. Discovery of a novel small molecule PT109 with multi-targeted results towards Alzheimer’s illness in vitro and in vivo. Eur J Pharm. 2020;883:173361.
Halkina T, Henderson JL, Lin EY, Himmelbauer MK, Jones JH, Nevalainen M, et al. Discovery of Potent and Brain-Penetrant Tau Tubulin Kinase 1 (TTBK1) Inhibitors that Lower Tau Phosphorylation In Vivo. J Med Chem. 2021;64:6358–80.
Dillon GM, Henderson JL, Bao C, Joyce JA, Calhoun M, Amaral B, et al. Acute inhibition of the CNS-specific kinase TTBK1 considerably lowers tau phosphorylation at a number of illness related websites. PLoS One. 2020;15:e0228771.
Ashour NH, El-Tanbouly DM, El Sayed NS, Khattab MM. Roflumilast ameliorates cognitive deficits in a mouse mannequin of amyloidogenesis and tauopathy: Involvement of nitric oxide standing, Abeta extrusion transporter ABCB1, and reversal by PKA inhibitor H89. Prog Neuropsychopharmacol Biol Psychiatry. 2021;111:110366.
Yoneyama M, Shiba T, Hasebe S, Umeda Okay, Yamaguchi T, Ogita Okay. Lithium promotes neuronal restore and ameliorates depression-like habits following trimethyltin-induced neuronal loss within the dentate gyrus. PLoS One. 2014;9:e87953.
Caccamo A, Oddo S, Tran LX, LaFerla FM. Lithium reduces tau phosphorylation however not A beta or working reminiscence deficits in a transgenic mannequin with each plaques and tangles. Am J Pathol. 2007;170:1669–75.
Nakashima H, Ishihara T, Suguimoto P, Yokota O, Oshima E, Kugo A, et al. Chronic lithium therapy decreases tau lesions by selling ubiquitination in a mouse mannequin of tauopathies. Acta Neuropathol. 2005;110:547–56.
Kaufman AC, Salazar SV, Haas LT, Yang J, Kostylev MA, Jeng AT, et al. Fyn inhibition rescues established reminiscence and synapse loss in Alzheimer mice. Ann Neurol. 2015;77:953–71.
Chang Y, Yao Y, Ma R, Wang Z, Hu J, Wu Y, et al. Dl-3-n-Butylphthalide Reduces Cognitive Deficits and Alleviates Neuropathology in P301S Tau Transgenic Mice. Front Neurosci. 2021;15:620176.
Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, Kayed R, et al. Triple-transgenic mannequin of Alzheimer’s illness with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron. 2003;39:409–21.
Lewis J, Dickson DW, Lin WL, Chisholm L, Corral A, Jones G, et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science. 2001;293:1487–91.
Terwel D, Lasrado R, Snauwaert J, Vandeweert E, Van Haesendonck C, Borghgraef P, et al. Changed conformation of mutant Tau-P301L underlies the moribund tauopathy, absent in progressive, nonlethal axonopathy of Tau-4R/2N transgenic mice. J Biol Chem. 2005;280:3963–73.
Yoshiyama Y, Higuchi M, Zhang B, Huang SM, Iwata N, Saido TC, et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse mannequin. Neuron. 2007;53:337–51.
Ramsden M, Kotilinek L, Forster C, Paulson J, McGowan E, SantaCruz Okay, et al. Age-dependent neurofibrillary tangle formation, neuron loss, and reminiscence impairment in a mouse mannequin of human tauopathy (P301L). J Neurosci. 2005;25:10637–47.
Santacruz Okay, Lewis J, Spires T, Paulson J, Kotilinek L, Ingelsson M, et al. Tau suppression in a neurodegenerative mouse mannequin improves reminiscence operate. Science. 2005;309:476–81.
Ishihara T, Hong M, Zhang B, Nakagawa Y, Lee MK, Trojanowski JQ, et al. Age-dependent emergence and development of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron. 1999;24:751–62.
Andorfer C, Kress Y, Espinoza M, de Silva R, Tucker KL, Barde YA, et al. Hyperphosphorylation and aggregation of tau in mice expressing regular human tau isoforms. J Neurochem. 2003;86:582–90.
Zilka N, Korenova M, Novak M. Misfolded tau protein and illness modifying pathways in transgenic rodent fashions of human tauopathies. Acta Neuropathol. 2009;118:71–86.
Perez DI, Gil C, Martinez A. Protein kinases CK1 and CK2 as new targets for neurodegenerative ailments. Med Res Rev. 2011;31:924–54.
Ribe EM, Perez M, Puig B, Gich I, Lim F, Cuadrado M, et al. Accelerated amyloid deposition, neurofibrillary degeneration and neuronal loss in double mutant APP/tau transgenic mice. Neurobiol Dis. 2005;20:814–22.
Huang W, Percie du Sert N, Vollert J, Rice ASC. General Principles of Preclinical Study Design. Handb Exp Pharm. 2020;257:55–69.
del Ser T, Steinwachs KC, Gertz HJ, Andres MV, Gomez-Carrillo B, Medina M, et al. Treatment of Alzheimer’s illness with the GSK-3 inhibitor tideglusib: a pilot research. J Alzheimer’s Dis. 2013;33:205–15.
Lovestone S, Boada M, Dubois B, Hull M, Rinne JO, Huppertz HJ, et al. A part II trial of tideglusib in Alzheimer’s illness. J Alzheimer’s Dis. 2015;45:75–88.
Tolosa E, Litvan I, Hoglinger GU, Burn D, Lees A, Andres MV, et al. A part 2 trial of the GSK-3 inhibitor tideglusib in progressive supranuclear palsy. Mov Disord. 2014;29:470–8.
Hampel H, Ewers M, Burger Okay, Annas P, Mortberg A, Bogstedt A, et al. Lithium trial in Alzheimer’s illness: a randomized, single-blind, placebo-controlled, multicenter 10-week research. J Clin Psychiatry. 2009;70:922–31.
Macdonald A, Briggs Okay, Poppe M, Higgins A, Velayudhan L, Lovestone S. A feasibility and tolerability research of lithium in Alzheimer’s illness. Int J Geriatr Psychiatry. 2008;23:704–11.
Forlenza OV, Diniz BS, Radanovic M, Santos FS, Talib LL, Gattaz WF. Disease-modifying properties of long-term lithium therapy for amnestic gentle cognitive impairment: randomised managed trial. Br J Psychiatry. 2011;198:351–6.
Devanand DP, Strickler JG, Huey ED, Crocco E, Forester BP, Husain MM, et al. Lithium Treatment for Agitation in Alzheimer’s illness (Lit-AD): Clinical rationale and research design. Contemp Clin Trials. 2018;71:33–39.
Devanand DP, Crocco E, Forester BP, Husain MM, Lee S, Vahia IV, et al. Low Dose Lithium Treatment of Behavioral Complications in Alzheimer’s Disease: Lit-AD Randomized Clinical Trial. Am J Geriatr Psychiatry. 2022;30:32–42.
van Dyck CH, Nygaard HB, Chen Okay, Donohue MC, Raman R, Rissman RA, et al. Effect of AZD0530 on Cerebral Metabolic Decline in Alzheimer Disease: A Randomized Clinical Trial. JAMA Neurol. 2019;76:1219–29.
Nygaard HB, Wagner AF, Bowen GS, Good SP, MacAvoy MG, Strittmatter KA, et al. A part Ib a number of ascending dose research of the security, tolerability, and central nervous system availability of AZD0530 (saracatinib) in Alzheimer’s illness. Alzheimers Res Ther. 2015;7:35.
Turner RS, Hebron ML, Lawler A, Mundel EE, Yusuf N, Starr JN, et al. Nilotinib Effects on Safety, Tolerability, and Biomarkers in Alzheimer’s Disease. Ann Neurol. 2020;88:183–94.
Malpas CB, Vivash L, Genc S, Saling MM, Desmond P, Steward C, et al. A Phase IIa Randomized Control Trial of VEL015 (Sodium Selenate) in Mild-Moderate Alzheimer’s Disease. J Alzheimer’s Dis. 2016;54:223–32.
Cardoso BR, Roberts BR, Malpas CB, Vivash L, Genc S, Saling MM, et al. Supranutritional Sodium Selenate Supplementation Delivers Selenium to the Central Nervous System: Results from a Randomized Controlled Pilot Trial in Alzheimer’s Disease. Neurotherapeutics. 2019;16:192–202.
Vivash L, Malpas CB, Churilov L, Walterfang M, Brodtmann A, Piguet O, et al. A research protocol for a part II randomised, double-blind, placebo-controlled trial of sodium selenate as a disease-modifying therapy for behavioural variant frontotemporal dementia. BMJ Open. 2020;10:e040100.
Vivash L, Bertram KL, Malpas CB, Marotta C, Harding IH, Kolbe S, et al. Sodium selenate as a disease-modifying therapy for progressive supranuclear palsy: protocol for a part 2, randomised, double-blind, placebo-controlled trial. BMJ Open. 2021;11:e055019.
Jack CR Jr, Bennett DA, Blennow Okay, Carrillo MC, Dunn B, Haeberlein SB, et al. NIA-AA Research Framework: Toward a organic definition of Alzheimer’s illness. Alzheimers Dement. 2018;14:535–62.
Novak P, Kovacech B, Katina S, Schmidt R, Scheltens P, Kontsekova E, et al. ADAMANT: a placebo-controlled randomized part 2 research of AADvac1, an lively immunotherapy towards pathological tau in Alzheimer’s illness. Nat Aging. 2021;1:521–34.
Cummings J, Lee G, Zhong Okay, Fonseca J, Taghva Okay. Alzheimer’s illness drug growth pipeline: 2021. Alzheimer’s Dement. 2021;7:e12179.
Holland D, McEvoy LK, Desikan RS, Dale AM. Alzheimer’s Disease Neuroimaging I. Enrichment and stratification for predementia Alzheimer illness medical trials. PLoS One. 2012;7:e47739.
Nelson PT, Dickson DW, Trojanowski JQ, Jack CR, Boyle PA, Arfanakis Okay, et al. Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report. Brain. 2019;142:1503–27.
Jellinger KA, Attems J. Challenges of multimorbidity of the growing old mind: a essential update. J Neural Transm (Vienna). 2015;122:505–21.
Lim YY, Jaeger J, Harrington Okay, Ashwood T, Ellis KA, Stoffler A, et al. Three-month stability of the CogState temporary battery in wholesome older adults, gentle cognitive impairment, and Alzheimer’s illness: outcomes from the Australian Imaging, Biomarkers, and Lifestyle-rate of change substudy (AIBL-ROCS). Arch Clin Neuropsychol. 2013;28:320–30.
Hobart J, Cano S, Posner H, Selnes O, Stern Y, Thomas R, et al. Putting the Alzheimer’s cognitive check to the check I: conventional psychometric strategies. Alzheimers Dement. 2013;9:S4–9.
Holland D, Desikan RS, Dale AM, McEvoy LK. Rates of decline in Alzheimer illness lower with age. PLoS One. 2012;7:e42325.
Cummings J, Lee G, Nahed P, Kambar M, Zhong Okay, Fonseca J, et al. Alzheimer’s illness drug growth pipeline: 2022. Alzheimers Dement. 2022;8:e12295.
He Q, Liu J, Liang J, Liu X, Li W, Liu Z, et al. Towards Improvements for Penetrating the Blood-Brain Barrier-Recent Progress from a Material and Pharmaceutical Perspective. Cells. 2018;7:24.
Serenó L, Coma M, Rodriguez M, Sanchez-Ferrer P, Sánchez MB, Gich I, et al. A novel GSK-3β inhibitor reduces Alzheimer’s pathology and rescues neuronal loss in vivo. Neurobiol Dis. 2009;35:359–67.