Current progress, challenges and future prospects of diagnostic and therapeutic interventions in Alzheimer's disease

The amyloid hypothesis of Alzheimer's disease at 25 years

Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164

Development of Virus-Like Particle Technology from Small Highly Symmetric to Large Complex Virus-Like Particle Structures

Pushko, P., Pumpens, P., & Grens, E. (2013) · Intervirology · doi:10.1159/000346773 · Cited by 5,975

Anti-Vascular Endothelial Growth Factors Protect Retinal Pigment Epithelium Cells Against Oxidation by Modulating Nitric Oxide Release and Autophagy

Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,154

2016 Alzheimer's disease facts and figures

Alzheimer's Association (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.03.001 · Cited by 5,069

The global prevalence of dementia: a systematic review and metaanalysis.

Prince, M., Bryce, R., Albanese, E., Wimo, A., Ribeiro, W., & Ferri, C. P. (2013) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2012.11.007 · Cited by 4,941

Inflammation and Alzheimer’s disease

Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514

Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B

Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496

The Alzheimer’s disease neuroimaging initiative (ADNI): MRI methods

Jack, C. R., Bernstein, M. A., Fox, N. C., Thompson, P., Alexander, G., Harvey, D., Borowski, B., Britson, P. J., L. Whitwell, J., Ward, C., et al. (2008) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.21049 · Cited by 4,347

Autophagy: cellular and molecular mechanisms

Glick, D. R., Barth, S., & Macleod, K. F. (2010) · The Journal of Pathology · doi:10.1002/path.2697 · Cited by 3,995

Protein aggregation and neurodegenerative disease

Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454

Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease

Khan, S., Barve, K. H., & Kumar, M. S. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528142429 · Cited by 820

Biomolecules-derived biomaterials

Datta, L. P., Manchineella, S., & Govindaraju, T. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119633 · Cited by 187

Metallobiology and therapeutic chelation of biometals (copper, zinc and iron) in Alzheimer’s disease: Limitations, and current and future perspectives

Fasae, K. D., Abolaji, A. O., Faloye, T. R., Odunsi, A., Oyetayo, B. O., Enya, J. I., Rotimi, J. A., Akinyemi, R., Whitworth, A. J., & Aschner, M. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126779 · Cited by 161

Mitochondrial dysfunctions, oxidative stress and neuroinflammation as therapeutic targets for neurodegenerative diseases: An update on current advances and impediments

Rehman, M. U., Sehar, N., Dar, N. J., Khan, A., Arafah, A., Rashid, S., Rashid, S. M., & Ganaie, M. A. (2023) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104961 · Cited by 130

Antioxidant Berberine-Derivative Inhibits Multifaceted Amyloid Toxicity

Rajasekhar, K., Samanta, S., Bagoband, V., Murugan, N. A., & Govindaraju, T. (2020) · iScience · doi:10.1016/j.isci.2020.101005 · Cited by 100

Alzheimer's disease: Molecular aspects and treatment opportunities using herbal drugs

Thakral, S., Yadav, A., Singh, V., Kumar, M., Kumar, P., Narang, R., Sudhakar, K., Verma, A., Khalilullah, H., Jaremko, M., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101960 · Cited by 103

Multipronged diagnostic and therapeutic strategies for Alzheimer's disease

Ramesh, M., & Govindaraju, T. (2022) · Chemical Science · doi:10.1039/d2sc03932j · Cited by 87

Alzheimer’s Disease: Pathogenesis and Therapeutic Interventions

Ogbodo, J. O., Agbo, C. P., Njoku, U. O., Ogugofor, M. O., Egba, S. I., Ihim, S. A., Echezona, A. C., Brendan, K. C., Upaganlawar, A. B., & Upasani, C. D. (2021) · Current Aging Science · doi:10.2174/1874609814666210302085232 · Cited by 86

Role of Post‐translational Modifications in Alzheimer's Disease

Ramesh, M., Gopinath, P., & Govindaraju, T. (2019) · ChemBioChem · doi:10.1002/cbic.201900573 · Cited by 68

Hydroxylated Single-Walled Carbon Nanotubes Inhibit Aβ42 Fibrillogenesis, Disaggregate Mature Fibrils, and Protect against Aβ42-Induced Cytotoxicity

Liu, F., Wang, W., Sang, J., Jia, L., & Lu, F. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00441 · Cited by 67

Engineering Versatile Nanoparticles for Near‐Infrared Light‐Tunable Drug Release and Photothermal Degradation of Amyloid β

Lai, Y., Zhu, Y., Xu, Z., Hu, X., Saeed, M., Yu, H., Chen, X., Liu, J., & Zhang, W. (2020) · Advanced Functional Materials · doi:10.1002/adfm.201908473 · Cited by 65

Dendrimer Architectonics to Treat Cancer and Neurodegenerative Diseases with Implications in Theranostics and Personalized Medicine

Moorthy, H., & Govindaraju, T. (2021) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c01319 · Cited by 64

Molecular Cobalt(II) Complexes for Tau Polymerization in Alzheimer’s Disease

Gorantla, N. V., Landge, V. G., Nagaraju, P. G., Sunny, L. P., Nair, A., Midya, S. P., G., P. P. C., Balaraman, E., & Chinnathambi, S. (2019) · ACS Omega · doi:10.1021/acsomega.9b00692 · Cited by 66

Photothermal Conjugated Polymers and Their Biological Applications in Imaging and Therapy

Wang, Y., Zhang, H., Wang, Z., & Feng, L. (2020) · ACS Applied Polymer Materials · doi:10.1021/acsapm.0c00672 · Cited by 59

Small Molecule Inhibits Metal-Dependent and -Independent Multifaceted Toxicity of Alzheimer’s Disease

Samanta, S., Rajasekhar, K., Babagond, V., & Govindaraju, T. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00216 · Cited by 59

Unambiguous Detection of Elevated Levels of Hypochlorous Acid in Double Transgenic AD Mouse Brain

Samanta, S., & Govindaraju, T. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00554 · Cited by 57

Intranasal administration of dauricine loaded on graphene oxide: Multi-target therapy for Alzheimer’s disease

Wang, K., Wang, L., Chen, L., Peng, C., Luo, B., Mo, J., & Chen, W. (2021) · Drug Delivery · doi:10.1080/10717544.2021.1895909 · Cited by 55

Amyloid‐β Oligomer‐Targeted Gadolinium‐Based NIR/MR Dual‐Modal Theranostic Nanoprobe for Alzheimer's Disease

Wang, C., Wang, X., Chan, H., Liu, G., Wang, Z., Li, H., & Wong, M. S. (2020) · Advanced Functional Materials · doi:10.1002/adfm.201909529 · Cited by 56

Coassembled Chitosan-Hyaluronic Acid Nanoparticles as a Theranostic Agent Targeting Alzheimer’s β-Amyloid

Wang, W., Liu, M., Gao, W., Sun, Y., & Dong, X. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c17267 · Cited by 53

A multi-target theranostic nano-composite against Alzheimer's disease fabricated by conjugating carbon dots and triple-functionalized human serum albumin

Wang, W., Lin, X., Dong, X., & Sun, Y. (2022) · Acta Biomaterialia · doi:10.1016/j.actbio.2022.06.029 · Cited by 53

Molecular Tools to Detect Alloforms of Aβ and Tau: Implications for Multiplexing and Multimodal Diagnosis of Alzheimer’s Disease

Arora, H., Ramesh, M., Rajasekhar, K., & Govindaraju, T. (2020) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20190356 · Cited by 53

Perspectives for New and More Efficient Multifunctional Ligands for Alzheimer′s Disease Therapy

Zagórska, A., & Jaromin, A. (2020) · Molecules · doi:10.3390/molecules25153337 · Cited by 51

Multiple reactivities of flavonoids towards pathological elements in Alzheimer's disease: structure–activity relationship

Nam, G., Hong, M., Lee, J., Lee, H. J., Ji, Y., Kang, J., Baik, M., & Lim, M. H. (2020) · Chemical Science · doi:10.1039/d0sc02046j · Cited by 48

Exploring advancements in early detection of Alzheimer's disease with molecular assays and animal models

Sethi, P., Bhaskar, R., Singh, D. K. K., Gupta, S., Han, S. S., Avinash, D., Abomughaid, M. M., Koul, A., Rani, B., Ghosh, S., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102411 · Cited by 44

Dual Effect of the Acidic Polysaccharose Ulvan on the Inhibition of Amyloid-β Protein Fibrillation and Disintegration of Mature Fibrils

Liu, F., Zhao, W., Zhao, F., Dong, Q., Wang, Y., Wei, W., Jia, L., Li, L., & Lu, F. (2020) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.0c14292 · Cited by 45

Nanotechnology‐Based Strategies for Early Diagnosis of Central Nervous System Disorders

Hanif, S., Muhammad, P., Niu, Z., Ismail, M., Morsch, M., Zhang, X., Li, M., & Shi, B. (2021) · Advanced NanoBiomed Research · doi:10.1002/anbr.202100008 · Cited by 44

Design, synthesis and biological evaluation of naringenin carbamate derivatives as potential multifunctional agents for the treatment of Alzheimer’s disease

Wu, J., Kou, X., Ju, H., Zhang, H., Yang, A., & Shen, R. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.128316 · Cited by 42

Electrochemical aptamer-based nanobiosensors for diagnosing Alzheimer's disease: A review

Negahdary, M., & Angnes, L. (2022) · Biomaterials Advances · doi:10.1016/j.msec.2022.112689 · Cited by 42

Guanidine-based β amyloid precursor protein cleavage enzyme 1 (BACE-1) inhibitors for the Alzheimer's disease (AD): A review

Gehlot, P., Kumar, S., Vyas, V. K., Choudhary, B. S., Sharma, M., & Malik, R. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.117047 · Cited by 40

Cyanidin-3- O -glucoside inhibits Aβ40 fibrillogenesis, disintegrates preformed fibrils, and reduces amyloid cytotoxicity

Liu, F., Zhao, F., Wang, W., Sang, J., Jia, L., Li, L., & Lu, F. (2020) · Food & Function · doi:10.1039/c9fo00316a · Cited by 39

Design of an activatable NIR-II nanoprobe for the in vivo elucidation of Alzheimer's disease-related variations in methylglyoxal concentrations

Lai, Y., Dang, Y., Sun, Q., Pan, J., Yu, H., Zhang, W., & Xu, Z. (2022) · Chemical Science · doi:10.1039/d2sc05242c · Cited by 38

Hemicyanine-based fluorescent probes: Advancements in biomedical sensing and activity-based detection

Muhammad, S., Ahmad, H., Yan, Y., Chen, X., Muhammad, S., Maridevaru, M. C., Roy, S., Wang, Z., Zhang, Y., & Guo, B. (2025) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2025.216602 · Cited by 39

d -Enantiomeric RTHLVFFARK-NH2: A Potent Multifunctional Decapeptide Inhibiting Cu2+-Mediated Amyloid β-Protein Aggregation and Remodeling Cu2+-Mediated Amyloid β Aggregates

Liu, W., Dong, X., & Sun, Y. P. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00440 · Cited by 38

Regulation of Artemisinin and Its Derivatives on the Assembly Behavior and Cytotoxicity of Amyloid Polypeptides hIAPP and Aβ

Xu, J., Zhao, C., Huang, X., & Du, W. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00385 · Cited by 37

Naphthalene Monoimide Derivative Ameliorates Amyloid Burden and Cognitive Decline in a Transgenic Mouse Model of Alzheimer's Disease

Samanta, S., Rajasekhar, K., Ramesh, M., Murugan, N. A., Alam, S., Shah, D., Clement, J. P., & Govindaraju, T. (2021) · Advanced Therapeutics · doi:10.1002/adtp.202000225 · Cited by 36

Neuroprotection of Gastrodia elata polyphenols against H2O2-induced PC12 cell cytotoxicity by reducing oxidative stress

Tan, W., Zheng, Q., Feng, K., Feng, X., Zhong, W., Liao, C., Li, S., Liu, Y., & Hu, W. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1050775 · Cited by 35

Physiological and pathological effects of amyloid-β species in neural stem cell biology

Liste, I., Bernabeu-Zornoza, A., Coronel, R., Palmer, C., Monteagudo, M., & Zambrano, A. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.262571 · Cited by 40

Potential Alzheimer's disease therapeutic nano-platform: Discovery of amyloid-beta plaque disaggregating agent and brain-targeted delivery system using porous silicon nanoparticles

Kim, J., Um, H., Kim, N. H., & Kim, D. (2023) · Bioactive Materials · doi:10.1016/j.bioactmat.2023.01.006 · Cited by 33

Construction of a Highly Sensitive Thiol‐Reactive AIEgen‐Peptide Conjugate for Monitoring Protein Unfolding and Aggregation in Cells

Sabouri, S., Liu, M., Zhang, S., Yao, B., Soleimaninejad, H., Baxter, A. A., Armendáriz-Vidales, G., Subedi, P., Duan, C., Lou, X., et al. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202101300 · Cited by 33

Roles of Syzygium in Anti-Cholinesterase, Anti-Diabetic, Anti-Inflammatory, and Antioxidant: From Alzheimer’s Perspective

Rawa, M. S. A., Mazlan, M. K. N., Ahmad, R., Nogawa, T., & Wahab, H. A. (2022) · Plants · doi:10.3390/plants11111476 · Cited by 45

Small molecules and conjugates as theranostic agents

Pratihar, S., Bhagavath, K. K., & Govindaraju, T. (2023) · RSC Chemical Biology · doi:10.1039/d3cb00073g · Cited by 33

Rhodamine-Based Metal Chelator: A Potent Inhibitor of Metal-Catalyzed Amyloid Toxicity

Pradhan, K., Das, G., Kar, C., Mukherjee, N., Khan, J., Mahata, T., Barman, S., & Ghosh, S. (2020) · ACS Omega · doi:10.1021/acsomega.0c02235 · Cited by 30

Rationally Designed Molecules Synergistically Modulate Multifaceted Aβ Toxicity, Microglial Activation, and Neuroinflammation

Ramesh, M., Balachandra, C., Andhare, P., & Govindaraju, T. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00276 · Cited by 30

Design, synthesis, and biological evaluation of novel N-Benzyl piperidine derivatives as potent HDAC/AChE inhibitors for Alzheimer’s disease

Qin, P., Ran, Y., Xie, F., Liu, Y., Wei, C., Luan, X., & Wu, J. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117178 · Cited by 30

Edaravone inhibits the conformational transition of amyloid-β42: insights from molecular dynamics simulations

Liu, F., Ma, Z., Sang, J., & Lu, F. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1632225 · Cited by 29

Illustrating the Effect of Small Molecules Derived from Natural Resources on Amyloid Peptides

Roy, R., & Paul, S. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c07607 · Cited by 29

Discovery of Neuroregenerative Peptoid from Amphibian Neuropeptide That Inhibits Amyloid-β Toxicity and Crosses Blood–Brain Barrier

Pradhan, K., Das, G., Gupta, V., Mondal, P., Barman, S., Khan, J., & Ghosh, S. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00427 · Cited by 27

H 2 O 2 /HOCl-based fluorescent probes for dynamically monitoring pathophysiological processes

Zhang, D., Guo, S.-B., Li, L., & Shang, K. (2020) · The Analyst · doi:10.1039/d0an01313g · Cited by 26

Discovery of Potent Cholinesterase Inhibition-Based Multi-Target-Directed Lead Compounds for Synaptoprotection in Alzheimer’s Disease

Turgutalp, B., Bhattarai, P., Ercetin, T., Luise, C., Reis, R., Gurdal, E. E., Isaak, A., Biriken, D., Dinter, E., Sipahi, H., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01003 · Cited by 27

Aducanumab in Alzheimer’s Disease: A Critical Update

Ashique, S., Sirohi, E., Kumar, S., Rihan, M., Mishra, N., Bhatt, S., Gautam, R. K., Singh, S. K., Gupta, G., Chellappan, D. K., et al. (2023) · Current Medicinal Chemistry · doi:10.2174/0929867331666230727103553 · Cited by 27

Regulatory roles of microRNAs in modulating mitochondrial dynamics, amyloid beta fibrillation, microglial activation, and cholinergic signaling: Implications for alzheimer's disease pathogenesis

Sharma, M., Tanwar, A. K., Purohit, P. K., Pal, P., Kumar, D., Vaidya, S., Prajapati, S. K., Kumar, A., Dhama, N., Kumar, S., et al. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2024.105685 · Cited by 27

Synchronous screening of multiplexed biomarkers of Alzheimer's disease by a length-encoded aerolysin nanopore-integrated triple-helix molecular switch

Zou, Z., Yang, H., Yan, Q., Qi, P., Qing, Z., Zheng, J., Xu, X. H., Zhang, L., Feng, F., & Yang, R. (2019) · Chemical Communications · doi:10.1039/c9cc02065a · Cited by 26

Peptide–Polyphenol (KLVFF/EGCG) Binary Modulators for Inhibiting Aggregation and Neurotoxicity of Amyloid-β Peptide

Huang, Q., Zhao, Q., Peng, J., Yu, Y., Wang, C., Zou, Y., Su, Y., Zhu, L., Wang, C., & Yang, Y. (2019) · ACS Omega · doi:10.1021/acsomega.8b02797 · Cited by 25

Bio-inspired amyloid polypeptides: From self-assembly to nanostructure design and biotechnological applications

Lai, Y., Li, F., Zou, Z., Saeed, M., Xu, Z., & Yu, H. (2021) · Applied Materials Today · doi:10.1016/j.apmt.2021.100966 · Cited by 25

Potential molecular and graphene oxide chelators to dissolve amyloid-β plaques in Alzheimer's disease: a density functional theory study

Liu, C., & Luo, X. (2021) · Journal of Materials Chemistry B · doi:10.1039/d0tb02985h · Cited by 23

l -Dopa and dopamine conjugated naphthalenediimides modulate amyloid β toxicity

Ramesh, M., Makam, P., Voshavar, C., Khare, H., Rajasekhar, K., Ramakumar, S., & Govindaraju, T. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob01691g · Cited by 23

Synthesis and biological evaluation of 2′-Aminochalcone: A multi-target approach to find drug candidates to treat Alzheimer’s disease

Sakata, R. P., Antoniolli, G., Lancellotti, M., Kawano, D. F., Barbosa, E. G., & Almeida, W. P. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104201 · Cited by 22

Cerebrospinal fluid microRNAs as potential biomarkers in Alzheimer’s disease

Eddin, A. N., Hamsho, K., Adi, G., Al-Rimawi, M., Alfuwais, M., Rab, S. A., AlKattan, K. M., & Yaqinuddin, A. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1210191 · Cited by 26

Destabilization of amyloid fibrils on interaction with MoS 2 -based nanomaterials

Mudedla, S. K., Murugan, N. A., Subramanian, V., & Ågren, H. (2019) · RSC Advances · doi:10.1039/c8ra10184a · Cited by 21

Insights into the chemistry and therapeutic potential of acrylonitrile derivatives

Tan, O. Ü., & Zengin, M. (2021) · Archiv der Pharmazie · doi:10.1002/ardp.202100383 · Cited by 21

Tetracycline derivatives resist the assembly behavior of human islet amyloid polypeptide

Xu, J., Zhao, C., Huang, X., & Du, W. (2020) · Biochimie · doi:10.1016/j.biochi.2020.04.012 · Cited by 19

Navigating the Maze of Alzheimer’s disease by exploring BACE1: Discovery, current scenario, and future prospects

Iram, F., Shahid, M., Ansari, J., Ashraf, G. M., Hassan, M. I., & Islam, A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102342 · Cited by 20

Earlier Detection of Alzheimer’s Disease Based on a Novel Biomarker cis P-tau by a Label-Free Electrochemical Immunosensor

Shiravandi, A., Yari, F., Tofigh, N., Ashtiani, M. K., Shahpasand, K., Ghanian, M. H., Shekari, F., & Faridbod, F. (2022) · Biosensors · doi:10.3390/bios12100879 · Cited by 18

Thiophene‐Based Dual Modulators of Aβ and Tau Aggregation

Ramesh, M., Acharya, A., Murugan, N. A., Ila, H., & Govindaraju, T. (2021) · ChemBioChem · doi:10.1002/cbic.202100383 · Cited by 18

Early Diagnosis of Neurodegenerative Diseases: What Has Been Undertaken to Promote the Transition from PET to Fluorescence Tracers

Bisi, N., Pinzi, L., Rastelli, G., & Tonali, N. (2024) · Molecules · doi:10.3390/molecules29030722 · Cited by 17

From Hybrids to New Scaffolds: The Latest Medicinal Chemistry Goals in Multi-target Directed Ligands for Alzheimers Disease

Alarcón‐Espósito, J., Mallea, M., & Rodríguez-Lavado, J. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200914155951 · Cited by 19

Is Aducanumab for LMICs? Promises and Challenges

Gunawardena, I. P. C., Retinasamy, T., & Shaikh, M. F. (2021) · Brain Sciences · doi:10.3390/brainsci11111547 · Cited by 19

Navigating the dichotomy of reactive oxygen, nitrogen, and sulfur species: detection strategies and therapeutic interventions

Baruah, P., Padhi, D., Moorthy, H., Ramesh, M., & Govindaraju, T. (2025) · RSC Chemical Biology · doi:10.1039/d5cb00006h · Cited by 16

Recent studies of atomic‐resolution structures of tau protein and structure‐based inhibitors

Zhu, L., & Qian, Z. (2021) · Quantitative Biology · doi:10.15302/j-qb-021-0271 · Cited by 16

A matrix targeted fluorescent probe to monitor mitochondrial dynamics

Ramesh, M., Rajasekhar, K., Gupta, K., Babagond, V., Saini, D. K., & Govindaraju, T. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob02128h · Cited by 16

A Boron-Containing Compound Acting on Multiple Targets Against Alzheimer’s Disease. Insights from Ab Initio and Molecular Dynamics Simulations

Ritacca, A. G., Ritacco, I., Dabbish, E., Russo, N., Mazzone, G., & Sicilia, E. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00262 · Cited by 16

Pentoxifylline as Add-On Treatment to Donepezil in Copper Sulphate-Induced Alzheimer’s Disease-Like Neurodegeneration in Rats

Elseweidy, M. M., Mahrous, M., Ali, S. I., Shaheen, M. A., & Younis, N. N. (2023) · Neurotoxicity Research · doi:10.1007/s12640-023-00672-1 · Cited by 15

A new highly selective colorimetric Schiff base chemosensor for determining the copper content in artisanal cachaças

Onça, L. O., de Souza, J. C. P., dos Santos, I. G. N., Santos, E. D. S., Soares, S. M., & Diniz, P. H. G. D. (2020) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2020.118783 · Cited by 15

Polyampholyte-Based Synthetic Chaperone Modulate Amyloid Aggregation and Lithium Delivery

Datta, L. P., Samanta, S., & Govindaraju, T. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00369 · Cited by 15

A near-infrared fluorescent probe for amyloid-β aggregates

Lee, M., Kim, M., Tikum, A. F., Lee, H. J., Thamilarasan, V., Lim, M. H., & Kim, J. (2018) · Dyes and Pigments · doi:10.1016/j.dyepig.2018.10.013 · Cited by 15

Arsenic and Tau Phosphorylation: A Mechanistic Review

Ariafar, S., Makhdoomi, S., & Mohammadi, M. (2023) · Biological Trace Element Research · doi:10.1007/s12011-023-03634-y · Cited by 13

Human Serum Albumin-Inspired Glycopeptide-Based Multifunctional Inhibitor of Amyloid-β Toxicity

Roy, R., Pradhan, K., Khan, J., Das, G., Mukherjee, N., Das, D., & Ghosh, S. (2020) · ACS Omega · doi:10.1021/acsomega.0c01028 · Cited by 14

Resistance of nepetin and its analogs on the fibril formation of human islet amyloid polypeptide

Xu, J., Zheng, T., Zhao, C., Huang, X., & Du, W. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.10.202 · Cited by 14

Short Peptoid Evolved from the Key Hydrophobic Stretch of Amyloid-β42 Peptide Serves as a Potent Therapeutic Lead of Alzheimer’s Disease

Roy, R., Khan, J., Pradhan, K., Nayak, P., Sarkar, A. K., Nandi, S., Ghosh, S., Ram, H., & Ghosh, S. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00549 · Cited by 14

Unexpected Function of a Heptapeptide-Conjugated Zwitterionic Polymer that Coassembles into β-Amyloid Fibrils and Eliminates the Amyloid Cytotoxicity

Wang, W., Zhao, G., Dong, X., & Sun, Y. P. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c01132 · Cited by 13

Machine Learning Approaches for Speech-Based Alzheimer’s Detection: A Comprehensive Survey

Sharafeldeen, A., Keowen, J., & Shaffie, A. (2025) · Computers · doi:10.3390/computers14020036 · Cited by 19

Recent Progress in the Treatment Strategies for Alzheimer’s Disease

Kumar, V., & Roy, K. (2023) · Neuromethods · doi:10.1007/978-1-0716-3311-3_1 · Cited by 12

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Characterization and in-vitro Alzheimer’s properties of exopolysaccharide from Bacillus maritimus MSM1

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Multichromatic fluorescence towards aberrant proteinaceous aggregates utilizing benzimidazole-based ICT fluorophores

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Exploring the protective effect and molecular mechanism of betulin in Alzheimer's disease based on network pharmacology, molecular docking and experimental validation

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Exploring nanoparticular platform in delivery of repurposed drug for Alzheimer’s disease: current approaches and future perspectives

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Near‐Infrared Fluorescent Probe for the Early Diagnosis of Alzheimer's Disease

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Targeting protein misfolding in Alzheimer’s disease: The emerging role of molecular chaperones

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Precision Medicine: Role of Biomarkers in Early Prediction and Diagnosis of Alzheimer’s Disease

Shen, L., Xia, S., Zhang, H., Yao, F., Liu, X., Zhao, Y., Ying, M., Iqbal, J., & Liu, Q. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.82035 · Cited by 9

Luteoloside inhibits Aβ1–42 fibrillogenesis, disintegrates preformed fibrils, and alleviates amyloid-induced cytotoxicity

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Inhibition of Insulin Amyloid Fibrillogenesis Using Antioxidant Copolymers with Dopamine Pendants

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Identification of Multicolor Fluorescent Probes for Heterogeneous Aβ Deposits in Alzheimer’s Disease

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Synthesis and in vitro quantification of amyloid fibrils by barbituric and thiobarbituric acid-based chromene derivatives

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Glucosamine and Its Analogues as Modulators of Amyloid-β Toxicity

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Development of quantitative detection methods for four Alzheimer’s disease specific biomarker panels using electrochemical immunosensors based on enzyme immunoassay

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Exploring bacterial metabolites in microbe-human host dialogue and their therapeutic potential in Alzheimer’s diseases

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Near‐Infrared Two‐Photon J‐Aggregation‐Induced Organic Fluorescent Dots with Large Stokes‐Shift for Ratiometric Imaging of Hypochlorous Acid in Living Cells and Brains of AD Mice

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Structure–Activity and Brain Kinetics Relationships of 18F-Labeled Benzimidazopyridine Derivatives as Tau PET Tracers

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Cerium-doped carbon dots as dual-target agents against Alzheimer's β-amyloid fibrillogenesis and reactive oxygen species

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Chapter 1. Alzheimer's is a Multifactorial Disease

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The Pathophysiology of Alzheimer’s Disease

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Multipronged diagnostic and therapeutic strategies for Alzheimer's disease

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Next Generation Drugs in Alzheimer's Disease Treatment: From Benchtop to Bedside

(2013) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781608057221113010005

Advances in the treatment of Alzheimer’s disease

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