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2000
Volume 32, Issue 8
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Introduction

Neurodegenerative disorders such as Alzheimer's, Parkinson's, and ALS are characterized by progressive neuronal dysfunction with limited therapeutic options. Recent advances in molecular biology and drug development have highlighted the therapeutic promise of precision enzyme targeting, offering novel strategies for disease modulation and symptom management.

Methods

A comprehensive literature review spanning recent/current was conducted using PubMed, Scopus, and ScienceDirect. Studies focusing on enzyme-based targets, high-throughput screening, and molecular docking in neurodegeneration were included. Thematic synthesis was employed to categorize findings based on enzyme class, disease relevance, and therapeutic outcomes.

Results

Key enzyme families such as kinases, proteases, and oxidoreductases were identified as pivotal modulators in disease progression. Emerging enzyme-targeted compounds demonstrated enhanced bioavailability, blood-brain barrier permeability, and disease-specific efficacy. Novel screening platforms and computational modeling enabled the precise selection of inhibitors, significantly improving the therapeutic index and reducing off-target effects.

Discussion

Targeting enzymes implicated in neuroinflammation, oxidative stress, and protein misfolding has shown disease-modifying potential. Integrating precision drug discovery tools, such as AI-assisted modeling and enzyme kinetics, supports rational drug design. However, translational challenges persist due to variability in enzyme expression and disease heterogeneity.

Conclusion

Future research should focus on refining enzyme inhibitors and integrating biomarkers to facilitate personalized treatment strategies for neurodegenerative disorders. As the understanding of enzymatic roles in neurodegeneration deepens, precision enzyme-targeted drug discovery holds significant promise in transforming neurotherapeutic approaches.

© 2025 Bentham Science Publishers
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References

  1. KovacsG.G. Concepts and classification of neurodegenerative diseases.Handbook of Clinical Neurology.Elsevier201814530130710.1016/B978‑0‑12‑802395‑2.00021‑3
     [Google Scholar]
  2. LampteyR.N.L. ChaulagainB. TrivediR. GothwalA. LayekB. SinghJ. A review of the common neurodegenerative disorders: Current therapeutic approaches and the potential role of nanotherapeutics.Int. J. Mol. Sci.2022233185110.3390/ijms2303185135163773
     [Google Scholar]
  3. KoroshetzW. MuckeL. Neurodegenerative diseases: Where are we not looking for answers?Translational Neuroscience: Toward New TherapiesMIT PressCambridge (MA)2015533886206
     [Google Scholar]
  4. Spires-JonesT.L. AttemsJ. ThalD.R. Interactions of pathological proteins in neurodegenerative diseases.Acta Neuropathol.2017134218720510.1007/s00401‑017‑1709‑728401333
     [Google Scholar]
  5. Over 1 in 3 people affected by neurological conditions, the leading cause of illness and disability worldwide.2024Available from: https://www.who.int/news/item/14-03-2024-over-1-in-3-people-affected-by-neurological-conditions--the-leading-cause-of-illness-and-disability-worldwide
  6. PasseriE. ElkhouryK. MorsinkM. BroersenK. LinderM. TamayolA. MalaplateC. YenF.T. Arab-TehranyE. Alzheimer’s disease: Treatment strategies and their limitations.Int. J. Mol. Sci.202223221395410.3390/ijms23221395436430432
     [Google Scholar]
  7. YiannopoulouK.G. PapageorgiouS.G. Current and future treatments in Alzheimer disease: An update.J. Cent. Nerv. Syst. Dis.202012p.117957352090739710.1177/117957352090739732165850
     [Google Scholar]
  8. EbrahimiZ. TalaeiS. AghamiriS. GoradelN.H. JafarpourA. NegahdariB. Overcoming the blood–brain barrier in neurodegenerative disorders and brain tumours.IET Nanobiotechnol.202014644144810.1049/iet‑nbt.2019.035132755952
     [Google Scholar]
  9. YoungA.L. MarinescuR.V. OxtobyN.P. BocchettaM. YongK. FirthN.C. CashD.M. ThomasD.L. DickK.M. CardosoJ. van SwietenJ. BorroniB. GalimbertiD. MasellisM. TartagliaM.C. RoweJ.B. GraffC. TagliaviniF. FrisoniG.B. LaforceR.Jr FingerE. de MendonçaA. SorbiS. WarrenJ.D. CrutchS. FoxN.C. OurselinS. SchottJ.M. RohrerJ.D. AlexanderD.C. AnderssonC. ArchettiS. ArighiA. BenussiL. BinettiG. BlackS. CossedduM. FallströmM. FerreiraC. FenoglioC. FreedmanM. FumagalliG.G. GazzinaS. GhidoniR. GrisoliM. JelicV. JiskootL. KerenR. LombardiG. MarutaC. MeeterL. MeadS. van MinkelenR. NacmiasB. ÖijerstedtL. PadovaniA. PanmanJ. PievaniM. PolitoC. PremiE. PrioniS. RademakersR. RedaelliV. RogaevaE. RossiG. RossorM. ScarpiniE. Tang-WaiD. ThonbergH. TiraboschiP. VerdelhoA. WeinerM.W. AisenP. PetersenR. JackC.R. JagustW. TrojanowkiJ.Q. TogaA.W. BeckettL. GreenR.C. SaykinA.J. MorrisJ. ShawL.M. KhachaturianZ. SorensenG. KullerL. RaichleM. PaulS. DaviesP. FillitH. HeftiF. HoltzmanD. MesulamM.M. PotterW. SnyderP. SchwartzA. MontineT. ThomasR.G. DonohueM. WalterS. GessertD. SatherT. JiminezG. HarveyD. BernsteinM. ThompsonP. SchuffN. BorowskiB. GunterJ. SenjemM. VemuriP. JonesD. KantarciK. WardC. KoeppeR.A. FosterN. ReimanE.M. ChenK. MathisC. LandauS. CairnsN.J. HouseholderE. Taylor-ReinwaldL. LeeV. KoreckaM. FigurskiM. CrawfordK. NeuS. ForoudT.M. PotkinS. ShenL. FaberK. KimS. NhoK. ThalL. BuckholtzN. AlbertM. FrankR. HsiaoJ. KayeJ. QuinnJ. LindB. CarterR. DolenS. SchneiderL.S. PawluczykS. BecceraM. TeodoroL. SpannB.M. BrewerJ. VanderswagH. FleisherA. HeidebrinkJ.L. LordJ.L. MasonS.S. AlbersC.S. KnopmanD. JohnsonK. DoodyR.S. Villanueva-MeyerJ. ChowdhuryM. RountreeS. DangM. SternY. HonigL.S. BellK.L. AncesB. CarrollM. LeonS. MintunM.A. SchneiderS. OliverA. MarsonD. GriffithR. ClarkD. GeldmacherD. BrockingtonJ. RobersonE. GrossmanH. MitsisE. de Toledo-MorrellL. ShahR.C. DuaraR. VaronD. GreigM.T. RobertsP. AlbertM. OnyikeC. D’AgostinoD. KielbS. GalvinJ.E. CerboneB. MichelC.A. RusinekH. de LeonM.J. GlodzikL. De SantiS. DoraiswamyP.M. PetrellaJ.R. WongT.Z. ArnoldS.E. KarlawishJ.H. WolkD. SmithC.D. JichaG. HardyP. SinhaP. OatesE. ConradG. LopezO.L. OakleyM.A. SimpsonD.M. PorsteinssonA.P. GoldsteinB.S. MartinK. MakinoK.M. IsmailM.S. BrandC. MulnardR.A. ThaiG. Mc-Adams-OrtizC. WomackK. MathewsD. QuicenoM. Diaz-ArrastiaR. KingR. WeinerM. Martin-CookK. DeVousM. LeveyA.I. LahJ.J. CellarJ.S. BurnsJ.M. AndersonH.S. SwerdlowR.H. ApostolovaL. TingusK. WooE. SilvermanD.H. LuP.H. BartzokisG. Graff-RadfordN.R. ParfittF. KendallT. JohnsonH. FarlowM.R. HakeA.M. MatthewsB.R. HerringS. HuntC. van DyckC.H. CarsonR.E. MacAvoyM.G. ChertkowH. BergmanH. HoseinC. StefanovicB. CaldwellC. HsiungG-Y.R. FeldmanH. MudgeB. AssalyM. KerteszA. RogersJ. BernickC. MunicD. KerwinD. MesulamM-M. LipowskiK. WuC-K. JohnsonN. SadowskyC. MartinezW. VillenaT. TurnerR.S. JohnsonK. ReynoldsB. SperlingR.A. JohnsonK.A. MarshallG. FreyM. LaneB. RosenA. TinklenbergJ. SabbaghM.N. BeldenC.M. JacobsonS.A. SirrelS.A. KowallN. KillianyR. BudsonA.E. NorbashA. JohnsonP.L. AllardJ. LernerA. OgrockiP. HudsonL. FletcherE. CarmichaelO. OlichneyJ. DeCarliC. KitturS. BorrieM. LeeT-Y. BarthaR. JohnsonS. AsthanaS. CarlssonC.M. PotkinS.G. PredaA. NguyenD. TariotP. ReederS. BatesV. CapoteH. RainkaM. ScharreD.W. KatakiM. AdeliA. ZimmermanE.A. CelminsD. BrownA.D. PearlsonG.D. BlankK. AndersonK. SantulliR.B. KitzmillerT.J. SchwartzE.S. SinkK.M. WilliamsonJ.D. GargP. WatkinsF. OttB.R. QuerfurthH. TremontG. SallowayS. MalloyP. CorreiaS. RosenH.J. MillerB.L. MintzerJ. SpicerK. BachmanD. PasternakS. RachinskyI. DrostD. PomaraN. HernandoR. SarraelA. SchultzS.K. PontoL.L.B. ShimH. SmithK.E. RelkinN. ChaingG. RaudinL. SmithA. FargherK. RajB.A. NeylanT. GrafmanJ. DavisM. MorrisonR. HayesJ. FinleyS. FriedlK. FleischmanD. ArfanakisK. JamesO. MassogliaD. FruehlingJ.J. HardingS. PeskindE.R. PetrieE.C. LiG. YesavageJ.A. TaylorJ.L. FurstA.J. Uncovering the heterogeneity and temporal complexity of neurodegenerative diseases with subtype and stage inference.Nat. Commun.201891427310.1038/s41467‑018‑05892‑030323170
     [Google Scholar]
  10. StrafellaC. CaputoV. GalotaM.R. ZampattiS. MarellaG. MaurielloS. CascellaR. GiardinaE. Application of precision medicine in neurodegenerative diseases.Front. Neurol.2018970110.3389/fneur.2018.0070130190701
     [Google Scholar]
  11. ToaderC. DobrinN. BreharF.M. PopaC. Covache-BusuiocR.A. GlavanL.A. CostinH.P. BratuB.G. CorlatescuA.D. PopaA.A. CiureaA.V. From recognition to remedy: The significance of biomarkers in neurodegenerative disease pathology.Int. J. Mol. Sci.202324221611910.3390/ijms24221611938003309
     [Google Scholar]
  12. LiuN. LinM.M. WangY. The emerging roles of E3 ligases and DUBs in neurodegenerative diseases.Mol. Neurobiol.202360124726310.1007/s12035‑022‑03063‑336260224
     [Google Scholar]
  13. ShuklaS. TekwaniB.L. Histone deacetylases inhibitors in neurodegenerative diseases, neuroprotection and neuronal differentiation.Front. Pharmacol.20201153710.3389/fphar.2020.0053732390854
     [Google Scholar]
  14. PanC. MaoS. XiongZ. ChenZ. XuN. Glutamate dehydrogenase: Potential therapeutic targets for neurodegenerative disease.Eur. J. Pharmacol.202395017573310.1016/j.ejphar.2023.17573337116563
     [Google Scholar]
  15. KimN. LeeH.J. Target enzymes considered for the treatment of Alzheimer’s disease and Parkinson’s disease.BioMed. Res. Int.202020201201072810.1155/2020/201072833224974
     [Google Scholar]
  16. LeiP. AytonS. BushA.I. AdlardP.A. GSK-3 in neurodegenerative diseases.Int. J. Alzheimers Dis.20112011118924610.4061/2011/18924621629738
     [Google Scholar]
  17. YuanX.Z. SunS. TanC.C. YuJ.T. TanL. The role of ADAM10 in Alzheimer’s disease.J. Alzheimers Dis.201758230332210.3233/JAD‑17006128409746
     [Google Scholar]
  18. KimM. SuhJ. RomanoD. TruongM.H. MullinK. HooliB. NortonD. TescoG. ElliottK. WagnerS.L. MoirR.D. BeckerK.D. TanziR.E. Potential late-onset Alzheimer’s disease-associated mutations in the ADAM10 gene attenuate α-secretase activity.Hum. Mol. Genet.200918203987399610.1093/hmg/ddp32319608551
     [Google Scholar]
  19. ZhouM. LinY. LuL. ZhangZ. GuoW. PengG. ZhangW. ZhuZ. WuZ. MoM. YangX. ZhuX. ChenC. ChenX. XuP. Association of ADAM10 gene variants with sporadic Parkinson’s disease in Chinese Han population.J. Gene Med.2021233e331910.1002/jgm.331933527480
     [Google Scholar]
  20. CozzolinoF. VezzoliE. CheroniC. BesussoD. ConfortiP. ValenzaM. IacobucciI. MonacoV. BiroliniG. BombaciM. FalquiA. SaftigP. RossiR.L. MontiM. CattaneoE. ZuccatoC. ADAM10 hyperactivation acts on piccolo to deplete synaptic vesicle stores in Huntington’s disease.Hum. Mol. Genet.202130131175118710.1093/hmg/ddab04733601422
     [Google Scholar]
  21. FirdoshN. YadavB.S. RahmanS. KumarH. PDE-5 restore cognitive and metabolic function in patients with Alzheimer’s disease (AD).Int. J. Pharm. Sci. Med.202497112310.47760/ijpsm.2024.v09i07.002
     [Google Scholar]
  22. RussellD.S. BarretO. JenningsD.L. FriedmanJ.H. TamagnanG.D. ThomaeD. AlagilleD. MorleyT.J. PapinC. PapapetropoulosS. WaterhouseR.N. SeibylJ.P. MarekK.L. The phosphodiesterase 10 positron emission tomography tracer, [18F]MNI-659, as a novel biomarker for early Huntington disease.JAMA Neurol.201471121520152810.1001/jamaneurol.2014.195425322077
     [Google Scholar]
  23. ObergasteigerJ. FrapportiG. LamonacaG. PizziS. PicardA. PischeddaF. Kinase inhibition of G2019S-LRRK2 restores autolysosome formation and function to reduce endogenous alpha-synuclein intracellular inclusions.bioRix201910.1101/707273
     [Google Scholar]
  24. StegerM. TonelliF. ItoG. DaviesP. TrostM. VetterM. WachterS. LorentzenE. DuddyG. WilsonS. BaptistaM.A.S. FiskeB.K. FellM.J. MorrowJ.A. ReithA.D. AlessiD.R. MannM. Phosphoproteomics reveals that Parkinson’s disease kinase LRRK2 regulates a subset of Rab GTPases.eLife20165e1281310.7554/eLife.1281326824392
     [Google Scholar]
  25. ZhangQ. HuC. HuangJ. LiuW. LaiW. LengF. TangQ. LiuY. WangQ. ZhouM. ShengF. LiG. ZhangR. ROCK1 induces dopaminergic nerve cell apoptosis via the activation of Drp1-mediated aberrant mitochondrial fission in Parkinson’s disease.Exp. Mol. Med.2019511011310.1038/s12276‑019‑0318‑z31578315
     [Google Scholar]
  26. WangG. HuangY. WangL.L. ZhangY.F. XuJ. ZhouY. LourencoG.F. ZhangB. WangY. RenR.J. HallidayG.M. ChenS.D. MicroRNA-146a suppresses ROCK1 allowing hyperphosphorylation of tau in Alzheimer’s disease.Sci. Rep.2016612669710.1038/srep2669727221467
     [Google Scholar]
  27. ThapaK. KhanH. SharmaU. GrewalA.K. SinghT.G. Poly (ADP-ribose) polymerase-1 as a promising drug target for neurodegenerative diseases.Life Sci.202126711897510.1016/j.lfs.2020.11897533387580
     [Google Scholar]
  28. MaoK. ZhangG. The role of PARP1 in neurodegenerative diseases and aging.FEBS J.202228982013202410.1111/febs.1571633460497
     [Google Scholar]
  29. TristB.G. GenoudS. RoudeauS. RookyardA. AbdeenA. CottamV. HareD.J. WhiteM. AltvaterJ. FifitaJ.A. HoganA. GrimaN. BlairI.P. KyseniusK. CrouchP.J. CarmonaA. RufinY. ClaverolS. Van MalderenS. FalkenbergG. PatersonD.J. SmithB. TroakesC. VanceC. ShawC.E. Al-SarrajS. CordwellS. HallidayG. OrtegaR. DoubleK.L. Altered SOD1 maturation and post-translational modification in amyotrophic lateral sclerosis spinal cord.Brain202214593108313010.1093/brain/awac16535512359
     [Google Scholar]
  30. MielkeJ.K. KlingebornM. SchultzE.P. MarkhamE.L. ReeseE.D. AlamP. MackenzieI.R. LyC.V. CaugheyB. CashmanN.R. LeavensM.J. Seeding activity of human superoxide dismutase 1 aggregates in familial and sporadic amyotrophic lateral sclerosis postmortem neural tissues by real-time quaking-induced conversion.Acta Neuropathol.2024147110010.1007/s00401‑024‑02752‑838884646
     [Google Scholar]
  31. NorambuenaA. SunX. WallrabeH. CaoR. SunN. PardoE. SOD1 mediates lysosome-to-mitochondria communication and its dysregulation by amyloid-β oligomers.bioRix202110.1101/2021.06.14.448281
     [Google Scholar]
  32. BellingerF.P. BellingerM.T. SealeL.A. TakemotoA.S. RamanA.V. MikiT. Manning-BoğA.B. BerryM.J. WhiteL.R. RossG. Glutathione peroxidase 4 is associated with neuromelanin in substantia nigra and dystrophic axons in putamen of Parkinson’s brain.Mol. Neurodegener.201161810.1186/1750‑1326‑6‑821255396
     [Google Scholar]
  33. BarkatsM. MillecampsS. AbriouxP. GeoffroyM.C. MalletJ. Overexpression of glutathione peroxidase increases the resistance of neuronal cells to Abeta-mediated neurotoxicity.J. Neurochem.20007541438144610.1046/j.1471‑4159.2000.0751438.x10987823
     [Google Scholar]
  34. JiangW. YanYu YaoD. FeiX. AiL. DiY. ZhangJ. YueX. ZhaoS. HeR. LyuJ. TongZ. Single point mutation from E22-to-K in A β initiates early-onset Alzheimer’s Disease by binding with catalase.Oxid. Med. Cell. Longev.2020202012110.1155/2020/498120433425208
     [Google Scholar]
  35. NandiA. YanL.J. JanaC.K. DasN. Role of catalase in oxidative stress- and age-associated degenerative diseases.Oxid. Med. Cell. Longev.2019201911910.1155/2019/961309031827713
     [Google Scholar]
  36. BelliaF. LanzaV. García-ViñualesS. AhmedI.M.M. PietropaoloA. IacobucciC. MalgieriG. D’AbroscaG. FattorussoR. NicolettiV.G. SbardellaD. TundoG.R. ColettaM. PironeL. PedoneE. CalcagnoD. GrassoG. MilardiD. Ubiquitin binds the amyloid β peptide and interferes with its clearance pathways.Chem. Sci.20191092732274210.1039/C8SC03394C30996991
     [Google Scholar]
  37. LimK.L. TanJ.M.M. Role of the ubiquitin proteasome system in Parkinson’s disease.BMC Biochem.20078Suppl 1S1310.1186/1471‑2091‑8‑S1‑S1318047737
     [Google Scholar]
  38. Thi Phuong ThaoD. Ubiquitin carboxyl-terminal hydrolase L1 in Parkinson’s disease.IntechOpen201910.5772/intechopen.85273
     [Google Scholar]
  39. SapK.A. GeijtenbeekK.W. Schipper-KromS. GulerA.T. ReitsE.A. Ubiquitin-modifying enzymes in Huntington’s disease.Front. Mol. Biosci.202310110732310.3389/fmolb.2023.110732336926679
     [Google Scholar]
  40. RastegarS. NouriA. MasoudiR. TavakoliR. Role of cathepsins in Alzheimer’s disease: A systematic review.J. Med. Biomed. Sci.20187111010.4314/jmbs.v7i1.1
     [Google Scholar]
  41. XieZ. MengJ. KongW. WuZ. LanF. Narengaowa HayashiY. YangQ. BaiZ. NakanishiH. QingH. NiJ. Microglial cathepsin E plays a role in neuroinflammation and amyloid β production in Alzheimer’s disease.Aging Cell2022213e1356510.1111/acel.1356535181976
     [Google Scholar]
  42. YusufujiangA. ZengS. LiH. Cathepsins and Parkinson’s disease: Insights from Mendelian randomization analyses.Front. Aging Neurosci.202416138048310.3389/fnagi.2024.138048338903897
     [Google Scholar]
  43. LinL. WuZ. LuoH. HuangY. Cathepsin-mediated regulation of alpha-synuclein in Parkinson’s disease: A Mendelian randomization study.Front. Aging Neurosci.202416139480710.3389/fnagi.2024.139480738872630
     [Google Scholar]
  44. WangP. GuanP.P. WangT. YuX. GuoJ.J. WangZ.Y. Aggravation of A lzheimer’s disease due to the COX -2-mediated reciprocal regulation of IL -1β and A β between glial and neuron cells.Aging Cell201413460561510.1111/acel.1220924621265
     [Google Scholar]
  45. HsiehY.C. MounseyR.B. TeismannP. MPP+-induced toxicity in the presence of dopamine is mediated by COX-2 through oxidative stress.Naunyn Schmiedebergs Arch. Pharmacol.2011384215716710.1007/s00210‑011‑0660‑821667279
     [Google Scholar]
  46. DootR.K. YoungA.J. NasrallahI.M. WetherillR.R. SiderowfA. MachR.H. DubroffJ.G. [18F]NOS PET brain imaging suggests elevated neuroinflammation in idiopathic Parkinson’s disease.Cells20221119308110.3390/cells1119308136231041
     [Google Scholar]
  47. NathanC. CalingasanN. NezezonJ. DingA. LuciaM.S. La PerleK. FuortesM. LinM. EhrtS. KwonN.S. ChenJ. VodovotzY. KipianiK. BealM.F. Protection from Alzheimer’s-like disease in the mouse by genetic ablation of inducible nitric oxide synthase.J. Exp. Med.200520291163116910.1084/jem.2005152916260491
     [Google Scholar]
  48. BerndtN. HolzhütterH.G. BulikS. Implications of enzyme deficiencies on mitochondrial energy metabolism and reactive oxygen species formation of neurons involved in rotenone-induced Parkinson’s disease: A model-based analysis.FEBS J.2013280205080509310.1111/febs.1248023937586
     [Google Scholar]
  49. González-MingotC. Miana-MenaF.J. IñarreaP.J. IñiguezC. CapabloJ.L. OstaR. Gil-SánchezA. BrievaL. LarrodéP. Mitochondrial aconitase enzymatic activity: A potential long-term survival biomarker in the blood of ALS patients.J. Clin. Med.20231210356010.3390/jcm1210356037240666
     [Google Scholar]
  50. LanznasterD. BrunoC. BourgeaisJ. EmondP. ZemmouraI. LefèvreA. ReynierP. EymieuxS. BlanchardE. Vourc’hP. AndresC.R. BakkoucheS.E. HeraultO. FavardL. CorciaP. BlascoH. Metabolic profile and pathological alterations in the muscle of patients with early-stage amyotrophic lateral sclerosis.Biomedicines2022106130710.3390/biomedicines1006130735740329
     [Google Scholar]
  51. NunanJ. SmallD.H. Regulation of APP cleavage by α-, β- and γ-secretases.FEBS Lett.2000483161010.1016/S0014‑5793(00)02076‑711033346
     [Google Scholar]
  52. ZhangY. ThompsonR. ZhangH. XuH. APP processing in Alzheimer’s disease.Mol. Brain201141310.1186/1756‑6606‑4‑321214928
     [Google Scholar]
  53. García-GonzálezL. PilatD. BarangerK. RiveraS. Emerging alternative proteinases in APP metabolism and Alzheimer’s disease pathogenesis: A focus on MT1-MMP and MT5-MMP.Front. Aging Neurosci.20191124410.3389/fnagi.2019.0024431607898
     [Google Scholar]
  54. Becker-PaulyC. PietrzikC.U. The metalloprotease meprin β Is an Alternative β-secretase of APP.Front. Mol. Neurosci.2017915910.3389/fnmol.2016.0015928105004
     [Google Scholar]
  55. SongM. The asparaginyl endopeptidase legumain: An emerging therapeutic target and potential biomarker for Alzheimer’s disease.Int. J. Mol. Sci.202223181022310.3390/ijms23181022336142134
     [Google Scholar]
  56. TroyC.M. AkpanN. JeanY.Y. Regulation of caspases in the nervous system: Implications for functions in health and disease.Progress in Molecular Biology and Translational Science.Elsevier201126530510.1016/B978‑0‑12‑385504‑6.00007‑5
     [Google Scholar]
  57. GuoT. ZhangD. ZengY. HuangT.Y. XuH. ZhaoY. Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease.Mol. Neurodegener.20201514010.1186/s13024‑020‑00391‑732677986
     [Google Scholar]
  58. JiawenY. Sen-FangS. ZhengL. Brain structure and structural basis of neurodegenerative diseases.Biophys. Rep.20228317018110.52601/bpr.2022.22001337288246
     [Google Scholar]
  59. MehraS. SahayS. MajiS.K. α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis.Biochim. Biophys. Acta. Proteins Proteomics201918671089090810.1016/j.bbapap.2019.03.00130853581
     [Google Scholar]
  60. HanD. ZhengW. WangX. ChenZ. Proteostasis of α-synuclein and its role in the pathogenesis of Parkinson’s disease.Front. Cell. Neurosci.2020144510.3389/fncel.2020.0004532210767
     [Google Scholar]
  61. SchulteJ. LittletonJ.T. The biological function of the Huntingtin protein and its relevance to Huntington’s Disease pathology.Curr. Trends Neurol.20115657822180703
     [Google Scholar]
  62. ZuccatoC. CattaneoE. Role of brain-derived neurotrophic factor in Huntington’s disease.Prog. Neurobiol.2007815-629433010.1016/j.pneurobio.2007.01.00317379385
     [Google Scholar]
  63. LiW. SerpellL.C. CarterW.J. RubinszteinD.C. HuntingtonJ.A. Expression and characterization of full-length human huntingtin, an elongated HEAT repeat protein.J. Biol. Chem.200628123159161592210.1074/jbc.M51100720016595690
     [Google Scholar]
  64. GafniJ. HermelE. YoungJ.E. WellingtonC.L. HaydenM.R. EllerbyL.M. Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus.J. Biol. Chem.200427919202112022010.1074/jbc.M40126720014981075
     [Google Scholar]
  65. BarronJ.C. HurleyE.P. ParsonsM.P. Huntingtin and the Synapse.Front. Cell. Neurosci.20211568933210.3389/fncel.2021.68933234211373
     [Google Scholar]
  66. SiddiqueN. SiddiqueT. Amyotrophic lateral sclerosis overview.University of Washington.GeneReviewsSeattle2023
     [Google Scholar]
  67. DuggerB.N. DicksonD.W. Pathology of neurodegenerative diseases.Cold Spring Harb. Perspect. Biol.201797a02803510.1101/cshperspect.a02803528062563
     [Google Scholar]
  68. BlokhuisA.M. GroenE.J.N. KoppersM. van den BergL.H. PasterkampR.J. Protein aggregation in amyotrophic lateral sclerosis.Acta Neuropathol.2013125677779410.1007/s00401‑013‑1125‑623673820
     [Google Scholar]
  69. GaoC. JiangJ. TanY. ChenS. Microglia in neurodegenerative diseases: Mechanism and potential therapeutic targets.Signal Transduct. Target. Ther.20238135910.1038/s41392‑023‑01588‑037735487
     [Google Scholar]
  70. ZhuangJ. CaoY. GuoG. LiM. ZhangT. HeD. ChenJ. ZhangK. ZhangZ. Inhibition of BACE1 attenuates microglia-induced neuroinflammation after intracerebral hemorrhage by suppressing STAT3 activation.Aging202315157709772610.18632/aging.20493537552127
     [Google Scholar]
  71. RealeM. CostantiniE. Cholinergic modulation of the immune system in neuroinflammatory diseases.Diseases2021922910.3390/diseases902002933921376
     [Google Scholar]
  72. MontoyaA. ElguetaD. CamposJ. ChovarO. FalcónP. MatusS. AlfaroI. BonoM.R. PachecoR. Dopamine receptor D3 signalling in astrocytes promotes neuroinflammation.J. Neuroinflammation201916125810.1186/s12974‑019‑1652‑831810491
     [Google Scholar]
  73. HungC.C. LeeY.H. KuoY.M. HsuP.C. TsayH.J. HsuY.T. LeeC.C. LiangJ.J. ShieF.S. Soluble epoxide hydrolase modulates immune responses in activated astrocytes involving regulation of STAT3 activity.J. Neuroinflammation201916112310.1186/s12974‑019‑1508‑231176371
     [Google Scholar]
  74. TanY.Y. JennerP. ChenS.D. Monoamine oxidase-B inhibitors for the treatment of Parkinson’s disease: Past, present, and future.J. Parkinsons Dis.202212247749310.3233/JPD‑21297634957948
     [Google Scholar]
  75. NaoiM. MaruyamaW. Shamoto-NagaiM. Neuroprotective function of rasagiline and selegiline, inhibitors of type B monoamine oxidase, and role of monoamine oxidases in synucleinopathies.Int. J. Mol. Sci.202223191105910.3390/ijms23191105936232361
     [Google Scholar]
  76. SiddiquiA.J. JahanS. SiddiquiM.A. KhanA. AlshahraniM.M. BadraouiR. AdnanM. Targeting monoamine oxidase B for the treatment of Alzheimer’s and Parkinson’s diseases using novel inhibitors identified using an integrated approach of machine learning and computer-aided drug design.Mathematics2023116146410.3390/math11061464
     [Google Scholar]
  77. KumaraswamyP.M. SonalD. PrashantT. Precision medicine and antipsychotics in Parkinson’s disease: A focus on MAO-B pathway modulation.Curr. Psychopharmacol.202513E2211556034931910.2174/0122115560349319250330001147
     [Google Scholar]
  78. BorroniE. BohrmannB. GrueningerF. PrinssenE. NaveS. LoetscherH. ChintaS.J. RajagopalanS. RaneA. SiddiquiA. EllenbroekB. MesserJ. PählerA. AndersenJ.K. WylerR. CesuraA.M. Sembragiline: A novel, selective monoamine oxidase type B inhibitor for the treatment of Alzheimer’s disease.J. Pharmacol. Exp. Ther.2017362341342310.1124/jpet.117.24165328642233
     [Google Scholar]
  79. SchepetkinI.A. NurmaganbetovZ.S. FazylovS.D. NurkenovO.A. KhlebnikovA.I. SeilkhanovT.M. KishkentaevaA.S. ShultsE.E. QuinnM.T. Inhibition of acetylcholinesterase by novel lupinine derivatives.Molecules2023288335710.3390/molecules2808335737110594
     [Google Scholar]
  80. LiuY. UrasG. OnuwajeI. LiW. YaoH. XuS. LiX. LiX. PhillipsJ. AllenS. GongQ. ZhangH. ZhuZ. LiuJ. XuJ. Novel inhibitors of AChE and Aβ aggregation with neuroprotective properties as lead compounds for the treatment of Alzheimer’s disease.Eur. J. Med. Chem.202223511430510.1016/j.ejmech.2022.11430535339839
     [Google Scholar]
  81. BohnenN. YarnallA. Emerging non-invasive therapeutic approaches targeting hypocholinergic neural systems in Parkinson’s disease.Neural Regen. Res.202318480981010.4103/1673‑5374.35349036204846
     [Google Scholar]
  82. FedorovaT. KnudsenC.S. MouridsenK. NexoE. BorghammerP. Salivary acetylcholinesterase activity is increased in Parkinson’s disease: A potential marker of parasympathetic dysfunction.Parkinsons Dis.201520151710.1155/2015/15647925767737
     [Google Scholar]
  83. Ben-ShaulY. BenMoyal-SegalL. Ben-AriS. BergmanH. SoreqH. Adaptive acetylcholinesterase splicing patterns attenuate 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced Parkinsonism in mice.Eur. J. Neurosci.200623112915292210.1111/j.1460‑9568.2006.04812.x16819980
     [Google Scholar]
  84. PatelS BansoadAV SinghR KhatikGL BACE1: A key regulator in Alzheimer's disease progression and current development of its inhibitors.Curr. Neuropharmacol.20222061174119310.2174/1570159X1966621120109403134852746
     [Google Scholar]
  85. BoldinR. ZycharB.C. GonçalvesL.R.C. ScianiJ.M. Design, in silico and pharmacological evaluation of a peptide inhibitor of BACE-1.Front. Pharmacol.202314118400610.3389/fphar.2023.118400637397495
     [Google Scholar]
  86. LiY. FangJ. ZhouZ. ZhouQ. SunS. JinZ. XiZ. WeiJ. Downregulation of lncRNA BACE1-AS improves dopamine-dependent oxidative stress in rats with Parkinson’s disease by upregulating microRNA-34b-5p and downregulating BACE1.Cell Cycle202019101158117110.1080/15384101.2020.174944732308102
     [Google Scholar]
  87. IqbalJ. Emerging therapies in neurodegenerative diseases: Targeting protein aggregates.2023Available from: https://www.researchgate.net/publication/376833890_Emerging_Therapies_in_Neurodegenerative_Diseases_Targeting_Protein_Aggregates
  88. GodwaT. DubeyS. TiwariP. Enzymes and Alzheimer's disease: Pioneering drug development strategies.Curr. Psychopharmacol.20251311210.2174/0122115560340307250106065419
     [Google Scholar]
  89. HuaJ. WangF. WeiX. QinY. LianJ. WuJ. MaP. MaX. A nanoenzyme constructed from manganese and strandberg-type phosphomolybdate with versatility in antioxidant and modulating conformation of A β protein misfolding aggregates in vitro .Int. J. Mol. Sci.2023245431710.3390/ijms2405431736901748
     [Google Scholar]
  90. FerreiraL. Dos SantosR. OlivaG. AndricopuloA. Molecular docking and structure-based drug design strategies.Molecules2015207133841342110.3390/molecules20071338426205061
     [Google Scholar]
  91. DiasR. de AzevedoW.Jr Molecular docking algorithms.Curr. Drug Targets20089121040104710.2174/13894500878694943219128213
     [Google Scholar]
  92. MorrisG.M. GoodsellD.S. HueyR. OlsonA.J. Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4.J. Comput. Aided Mol. Des.199610429330410.1007/BF001244998877701
     [Google Scholar]
  93. JonesG. WillettP. GlenR.C. LeachA.R. TaylorR. Development and validation of a genetic algorithm for flexible docking.J. Mol. Biol.1997267372774810.1006/jmbi.1996.0897
     [Google Scholar]
  94. FrenkelD. SmitB. Molecular dynamics simulations.Understanding Molecular Simulation.Elsevier20239712410.1016/B978‑0‑32‑390292‑2.00012‑X
     [Google Scholar]
  95. CornellW.D. CieplakP. BaylyC.I. GouldI.R. MerzK.M. FergusonD.M. SpellmeyerD.C. FoxT. CaldwellJ.W. KollmanP.A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules.J. Am. Chem. Soc.1995117195179519710.1021/ja00124a002
     [Google Scholar]
  96. BrooksB.R. BruccoleriR.E. OlafsonB.D. StatesD.J. SwaminathanS. KarplusM. CHARMM: A program for macromolecular energy, minimization, and dynamics calculations.J. Comput. Chem.19834218721710.1002/jcc.540040211
     [Google Scholar]
  97. ChristenM. HünenbergerP.H. BakowiesD. BaronR. BürgiR. GeerkeD.P. HeinzT.N. KastenholzM.A. KräutlerV. OostenbrinkC. PeterC. TrzesniakD. van GunsterenW.F. The GROMOS software for biomolecular simulation: GROMOS05.J. Comput. Chem.200526161719175110.1002/jcc.2030316211540
     [Google Scholar]
  98. LinsleyJ.W. ReisineT. FinkbeinerS. Cell death assays for neurodegenerative disease drug discovery.Expert Opin. Drug Discov.201914990191310.1080/17460441.2019.162378431179783
     [Google Scholar]
  99. KondoT. ImamuraK. FunayamaM. TsukitaK. MiyakeM. OhtaA. WoltjenK. NakagawaM. AsadaT. AraiT. KawakatsuS. IzumiY. KajiR. IwataN. InoueH. iPSC-based compound screening and in vitro trials identify a synergistic anti-amyloid β combination for Alzheimer’s disease.Cell Rep.20172182304231210.1016/j.celrep.2017.10.10929166618
     [Google Scholar]
  100. AldewachiH. Al-ZidanR.N. ConnerM.T. SalmanM.M. High-throughput screening platforms in the discovery of novel drugs for neurodegenerative diseases.Bioengineering2021823010.3390/bioengineering802003033672148
     [Google Scholar]
  101. NeziriS. KöseoğluA.E. Deniz KöseoğluG. ÖzgültekinB. ÖzgentürkN.Ö. Animal models in neuroscience with alternative approaches: Evolutionary, biomedical, and ethical perspectives.Animal Model. Exp. Med.20247686888010.1002/ame2.1248739375824
     [Google Scholar]
  102. PatwekarM. PatwekarF. ShaikhD. FatemaS.R. AherS.J. SharmaR. Receptor-based approaches and therapeutic targets in Alzheimer’s disease along with role of AI in drug designing: Unraveling pathologies and advancing treatment strategies.Appl. Chem. Eng.20236310.24294/ace.v6i3.2338
     [Google Scholar]
  103. StefanoG.B. Artificial intelligence as a tool for the diagnosis and treatment of neurodegenerative diseases.Brain Sci.202313693810.3390/brainsci1306093837371416
     [Google Scholar]
  104. BhachawatS. ShriramE. SrinivasanK. HuY.C. Leveraging computational intelligence techniques for diagnosing degenerative nerve diseases: A comprehensive review, open challenges, and future research directions.Diagnostics202313228810.3390/diagnostics1302028836673100
     [Google Scholar]
  105. JohnsonK.B. WeiW.Q. WeeraratneD. FrisseM.E. MisulisK. RheeK. ZhaoJ. SnowdonJ.L. Precision medicine, AI, and the future of personalized health care.Clin. Transl. Sci.2021141869310.1111/cts.1288432961010
     [Google Scholar]
  106. von LinstowC.U. Gan-OrZ. BrundinP. Precision medicine in Parkinson’s disease patients with LRRK2 and GBA risk variants – Let’s get even more personal.Transl. Neurodegener.2020913910.1186/s40035‑020‑00218‑x33066808
     [Google Scholar]
  107. NeganovaM.E. AleksandrovaY.R. NebogatikovV.O. KlochkovS. UstyugovA.A. Promising molecular targets for pharmacological therapy of neurodegenerative pathologies.Acta Nat.2020123608010.32607/actanaturae.1092533173597
     [Google Scholar]
  108. ParkE. LiL.Y. HeC. AbbasiA.Z. AhmedT. FoltzW.D. O’FlahertyR. ZainM. BoninR.P. RauthA.M. FraserP.E. HendersonJ.T. WuX.Y. Brain-penetrating and disease site-targeting manganese dioxide-polymer-lipid hybrid nanoparticles remodel microenvironment of Alzheimer’s disease by regulating multiple pathological pathways.Adv. Sci.20231012220723810.1002/advs.20220723836808713
     [Google Scholar]
  109. ToupsK. HathawayA. GordonD. ChungH. RajiC. BoydA. HillB.D. Hausman-CohenS. AttarhaM. ChwaW.J. JarrettM. BredesenD.E. Precision medicine approach to Alzheimer’s disease: Successful pilot project.J. Alzheimers Dis.20228841411142110.3233/JAD‑21570735811518
     [Google Scholar]
  110. DenaroC. StephensonD. MüllerM.L.T.M. PiccoliB. AzerK. Advancing precision medicine therapeutics for Parkinson’s utilizing a shared quantitative systems pharmacology model and framework.Front. Syst. Biol.20244135155510.3389/fsysb.2024.1351555
     [Google Scholar]
  111. FergusonM.W. KennedyC.J. PalpagamaT.H. WaldvogelH.J. FaullR.L.M. KwakowskyA. Current and possible future therapeutic options for Huntington’s disease.J. Cent. Nerv. Syst. Dis.2022141179573522109251710.1177/1179573522109251735615642
     [Google Scholar]
  112. KreiserR.P. WrightA.K. BlockN.R. HollowsJ.E. NguyenL.T. LeForteK. ManniniB. VendruscoloM. LimbockerR. Therapeutic strategies to reduce the toxicity of misfolded protein oligomers.Int. J. Mol. Sci.20202122865110.3390/ijms2122865133212787
     [Google Scholar]
  113. LongoF.M. MassaS.M. Neuroprotective strategies in Alzheimer’s disease.NeuroRx20041111712710.1602/neurorx.1.1.11715717012
     [Google Scholar]
  114. SweeneyP. ParkH. BaumannM. DunlopJ. FrydmanJ. KopitoR. McCampbellA. LeblancG. VenkateswaranA. NurmiA. HodgsonR. Protein misfolding in neurodegenerative diseases: Implications and strategies.Transl. Neurodegener.201761610.1186/s40035‑017‑0077‑528293421
     [Google Scholar]
  115. ZhengH. FridkinM. YoudimM. From single target to multitarget/network therapeutics in Alzheimer’s therapy.Pharmaceuticals20147211313510.3390/ph702011324463342
     [Google Scholar]
  116. TngT.J.W. WongB.W.Y. SimE.H.Y. TanE.K. GohW.W.B. LimK.L. Systematic analysis of multi-omics data reveals component-specific blood-based biomarkers for Parkinson’s disease.Transl. Med. Commun.2024911210.1186/s41231‑024‑00169‑9
     [Google Scholar]
  117. CaiadoF.L. MoriiK.Y. AlvesM.L.B. DestefaniA.C. DestefaniV.C. Precision medicine in geriatric care: Harnessing the power of genetic profiling for personalized therapies in older adults.Ibero-Am. Mag. Humanit. Sci. Educ.20241082730274010.51891/rease.v10i8.15333
     [Google Scholar]
  118. SmiesCW BellfyL WrightDS BennettsSS UrbanMW BrunswickCA Pharmacological HDAC3 inhibition alters memory updating in young and old mice.Front. Mol. Neurosci.202417142988010.3389/fnmol.2024.142988038766057
     [Google Scholar]
  119. HecklauK. MuellerS. KochS.P. MehkaryM.H. KilicB. HarmsC. Boehm-SturmP. YildirimF. The effects of selective inhibition of histone deacetylase 1 and 3 in Huntington’s disease mice.Front. Mol. Neurosci.20211461688610.3389/fnmol.2021.61688633679321
     [Google Scholar]
  120. RossiS.L. SubramanianP. BovenkampD.E. The future is precision medicine-guided diagnoses, preventions and treatments for neurodegenerative diseases.Front. Aging Neurosci.202315112861910.3389/fnagi.2023.112861937009453
     [Google Scholar]
  121. XuK. DaiX.L. HuangH.C. JiangZ.F. Targeting HDACs: A promising therapy for Alzheimer’s disease.Oxid. Med. Cell. Longev.201120111510.1155/2011/14326921941604
     [Google Scholar]
  122. SuelvesN. Kirkham-McCarthyL. LahueR.S. GinésS. A selective inhibitor of histone deacetylase 3 prevents cognitive deficits and suppresses striatal CAG repeat expansions in Huntington’s disease mice.Sci. Rep.201771608210.1038/s41598‑017‑05125‑228729730
     [Google Scholar]
  123. AngelopoulouE. PyrgelisE.S. PiperiC. Emerging potential of the phosphodiesterase (PDE) inhibitor ibudilast for neurodegenerative diseases: An update on preclinical and clinical evidence.Molecules20222723844810.3390/molecules2723844836500540
     [Google Scholar]
  124. Walczak-NowickaŁ.J. HerbetM. Acetylcholinesterase inhibitors in the treatment of neurodegenerative diseases and the role of acetylcholinesterase in their pathogenesis.Int. J. Mol. Sci.20212217929010.3390/ijms2217929034502198
     [Google Scholar]
  125. JoubertJ. PetzerJ.P. PrinsL.H.A. RepsoldB.P. MalanS.F. Multifunctional enzyme inhibition for neuroprotection - A focus on MAO, NOS, and AChE inhibitors.Drug Design and Discovery in Alzheimer’s Disease.Elsevier201429136510.1016/B978‑0‑12‑803959‑5.50005‑2
     [Google Scholar]
  126. CuiS.Y. YangM.X. ZhangY.H. ZhengV. ZhangH.T. GurneyM.E. XuY. O’DonnellJ.M. Protection from amyloid β peptide–induced memory, biochemical, and morphological deficits by a phosphodiesterase-4D Allosteric inhibitor.J. Pharmacol. Exp. Ther.2019371225025910.1124/jpet.119.25998631488603
     [Google Scholar]
  127. KillickR. ElliottC. RibeE. BroadstockM. BallardC. AarslandD. WilliamsG. Neurodegenerative disease associated pathways in the brains of triple transgenic Alzheimer’s model mice are reversed following two weeks of peripheral administration of fasudil.Int. J. Mol. Sci.202324131121910.3390/ijms24131121937446396
     [Google Scholar]
  128. Benítez-FernándezR. GilC. GuazaC. MestreL. MartínezA. The dual PDE7-GSK3β inhibitor, VP3.15, as neuroprotective disease-modifying treatment in a model of primary progressive multiple sclerosis.Int. J. Mol. Sci.202223221437810.3390/ijms23221437836430856
     [Google Scholar]
  129. GreenK.N. SteffanJ.S. Martinez-CoriaH. SunX. SchreiberS.S. ThompsonL.M. LaFerlaF.M. Nicotinamide restores cognition in Alzheimer’s disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau.J. Neurosci.20082845115001151010.1523/JNEUROSCI.3203‑08.200818987186
     [Google Scholar]
  130. LiE. ChoiJ. SimH.R. KimJ. JunJ.H. KyungJ. HaN. KimS. RyuK.H. ChungS.S. KimH.S. LeeS. SeolW. SongJ. A novel HDAC6 inhibitor, CKD-504, is effective in treating preclinical models of huntington’s disease.BMB Rep.202356317818310.5483/BMBRep.2022‑015736593104
     [Google Scholar]
  131. LiH. ShiG. ZhaH. ZhengL. LuoZ. WangY. Inhibition of histone deacetylase promotes a neuroprotective mechanism in an experimental model of Parkinson’s disease.Arch. Med. Sci.202120266467410.5114/aoms/13028738757033
     [Google Scholar]
  132. ChenY. ShiG.W. LiangZ.M. ShengS.Y. ShiY.S. PengL. WangY.P. WangF. ZhangX.M. Resveratrol improves cognition and decreases amyloid plaque formation in Tg6799 mice.Mol. Med. Rep.20191953783379010.3892/mmr.2019.1001030864708
     [Google Scholar]
  133. MoriyamaT. FukushimaT. KokateT. AlbalaB. [P3–037]: Preclinical studies with elenbecestat, a novel BACE1 inhibitor, show no evidence of hypopigmentation.Alzheimers Dement.201713P944P94410.1016/j.jalz.2017.06.1850
     [Google Scholar]
  134. ZhangS. SakumaM. DeoraG.S. LevyC.W. KlausingA. BredaC. ReadK.D. EdlinC.D. RossB.P. Wright MuelasM. DayP.J. O’HaganS. KellD.B. SchwarczR. LeysD. HeyesD.J. GiorginiF. ScruttonN.S. A brain-permeable inhibitor of the neurodegenerative disease target kynurenine 3-monooxygenase prevents accumulation of neurotoxic metabolites.Commun. Biol.20192127110.1038/s42003‑019‑0520‑531372510
     [Google Scholar]
  135. MendesG.O. PitaS.S.R. CarvalhoP.B. SilvaM.P. TarantoA.G. LeiteF.H.A. Molecular multi-target approach for human acetylcholinesterase, butyrylcholinesterase and β -secretase 1: Next generation for Alzheimer’s disease treatment.Pharmaceuticals202316688010.3390/ph1606088037375827
     [Google Scholar]
  136. UmarT. HodaN. Selective inhibitors of phosphodiesterases: Therapeutic promise for neurodegenerative disorders.Med. Chem. Comm.20156122063208010.1039/C5MD00419E
     [Google Scholar]
  137. VermaG. BhushanB. SinghG. SinghK. KumarS. GargA. RajputP. Pharmacological strategies for enzyme inhibition in disease therapeutics: A comprehensive review.Curr. Enzym. Inhib.20242029610810.2174/0115734080273835231127045336
     [Google Scholar]
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Precision Enzyme: Targeted Drug Discovery in Neurodegenerative Disorders
PPL 32, 539 (2025); https://doi.org/10.2174/0109298665391103250825102319
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  • Article Type:     Review Article
Keyword(s): acetylcholinesterase; Alzheimer’s disease; enzyme-targeted drug discovery; monoamine oxidase-B; Neurodegenerative disorders; Parkinson’s disease

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