Metal ions, Alzheimer's disease and chelation therapy

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

Pathways towards and Away from Alzheimer’s Disease

Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052

Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120

3D structure of Alzheimer's amyloid-β(1–42) fibrils

Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001

Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids

Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731

Rapid induction of Alzheimer A beta amyloid formation by zinc

Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522

Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447

Chelation therapy for the management of diabetic complications: a hypothesis and a proposal for clinical laboratory assessment of metal ion homeostasis in plasma

Frizzell, N., & Baynes, J. (2013) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2012-0881 · Cited by 17

Enhanced osteogenic activity of Ti alloy implants by modulating strontium configuration in their surface oxide layers

Xu, Z., Lu, H., Lü, J., Lv, C., Zhao, X., & Wang, G. (2018) · RSC Advances · doi:10.1039/c7ra10807a · Cited by 17

Amyloid β25–35 induced ROS-burst through NADPH oxidase is sensitive to iron chelation in microglial Bv2 cells

Part, K., Künnis-Beres, K., Poska, H., Land, T., Shimmo, R., & Zetterström Fernaeus, S. (2015) · Brain Research · doi:10.1016/j.brainres.2015.09.034 · Cited by 16

In vitro and in silico correlation of benzoxazole-based thiazolidinone hybrids derivatives: A promising acetylcholinesterase and butyrylcholinesterase inhibitors

Ashraf, M., Hussain, R., Khan, S., Rehman, W. U., Khan, Y., Sardar, A., Aziz, T. A., & Khowdiary, M. M. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.137317 · Cited by 16

A Multipurpose Metallophore and Its Copper Complexes with Diverse Catalytic Antioxidant Properties to Deal with Metal and Oxidative Stress Disorders: A Combined Experimental, Theoretical, and In Vitro Study

Menezes, L. B., Sampaio, R. M. S. N., Meurer, L., Szpoganicz, B., Cervo, R., Cargnelutti, R., Wang, L., Yang, J., Prabhakar, R. S., Fernandes, C., et al. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c00232 · Cited by 16

Using Synbiotics as a Therapy to Protect Mental Health in Alzheimer's Disease

Ngoc, A. P. T., Zahoor, A., Kim, D., & Yang, S. H. (2024) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2403.03021 · Cited by 16

New Hydroxyquinoline‐Based Derivatives as Potent Modulators of Amyloid‐β Aggregations

Fu, C., Hsu, L., Liao, Y., & Hu, M. (2016) · Archiv der Pharmazie · doi:10.1002/ardp.201500453 · Cited by 16

Antioxidants in the Prevention and Treatment of Alzheimer’s Disease

Singh, S. K., Srikrishna, S., Castellani, R. J., & Perry, G. L. (2017) · Springer eBooks · doi:10.1007/978-3-319-67625-8_20 · Cited by 16

New amyloid beta-disaggregating agents: synthesis, pharmacological evaluation, crystal structure and molecular docking of N -(4-((7-chloroquinolin-4-yl)oxy)-3-ethoxybenzyl)amines

Umar, T., Shalini, S., Raza, M. K., Gusain, S., Kumar, J., Ahmed, W., Tiwari, M., & Hoda, N. (2018) · MedChemComm · doi:10.1039/c8md00312b · Cited by 16

The salen based chemosensors for highly selective recognition of Zn2+ ion

Zhu, W., Du, L., Li, W., Zuo, J., & Shan, J. (2018) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2018.06.008 · Cited by 16

Designing a new multifunctional peptide for metal chelation and Aβ inhibition

Shamloo, A., Asadbegi, M., Khandan, V., & Amanzadi, A. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.06.004 · Cited by 15

Tuning the Anti(myco)bacterial Activity of 3-Hydroxy-4-pyridinone Chelators through Fluorophores

Rangel, M., Moniz, T., Silva, A. M. N., & Leite, A. (2018) · Pharmaceuticals · doi:10.3390/ph11040110 · Cited by 15

A Smart Nanotherapeutic Agent for in vitro and in vivo Reversal of Heavy‐Metal‐Induced Causality: Key Information from Optical Spectroscopy

Adhikari, A., Biswas, P., Mondal, S., Das, M., Darbar, S., Hameed, A. M., Alharbi, A., Ahmed, S. A., Bhattacharya, S. S., Pal, D., et al. (2019) · ChemMedChem · doi:10.1002/cmdc.201900543 · Cited by 15

Selenoproteins: Zoom-In to Their Metal-Binding Properties in Neurodegenerative Diseases

Duţă, C., Muscurel, C., Dogaru, C. B., & Stoian, I. A.-M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031305 · Cited by 14

Identifying Cu( ii )–amyloid peptide binding intermediates in the early stages of aggregation by resonance Raman spectroscopy: a simulation study

Ren, H., Zhang, Y. A., Guo, S., Lin, N., Deng, L. P., Yue, T., & Huang, F. L. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp06206k · Cited by 14

Cadmium Neurotoxicity and Its Role in Brain Disorders

Leal, R. B., Rieger, D. K., Peres, T. V., Lopes, M. W., & Gonçalves, C. A. (2012) · Springer eBooks · doi:10.1007/978-1-4419-9663-3_34 · Cited by 13

Neuritogenic activity of bi-functional bis-tryptoline triazole

Jiaranaikulwanitch, J., Tadtong, S., Govitrapong, P., Fokin, V. V., & Vajragupta, O. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.12.027 · Cited by 13

Bio-conjugated N-(2-hydroxy-1-naphthaldehyde)-glucosamine Cu(II) complex: Bacterial sensitivity and superoxide dismutase-like activity

Mir, J. M., Rajak, D. K., & MAURYA, R. C. (2018) · Journal of Coordination Chemistry · doi:10.1080/00958972.2018.1482488 · Cited by 13

Insight into inhibition of the human amyloid beta protein precursor (APP: PDB ID 3UMI) using (E)-N-(pyridin-2-ylmethylene)arylamine (L R ) models: structure elucidation of a family of ZnX 2 -L R complexes

Baul, T. S. B., Kundu, S., Singh, P., Shaveta, S., & da Silva, M. F. C. G. (2014) · Dalton Transactions · doi:10.1039/c4dt03151b · Cited by 13

Mutants of Metal Binding Site M1 in APP E2 Show Metal Specific Differences in Binding of Heparin but Not of sorLA

Dienemann, C., Coburger, I., Mehmedbašić, A., Andersen, O. M., & Than, M. E. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00111 · Cited by 12

Physalis minima L. Fruit- A Promising Approach To Alzheimer's Disease

Joseph, L., & Ravi, C. (2021) · Pharmacological Research - Modern Chinese Medicine · doi:10.1016/j.prmcm.2021.100038 · Cited by 12

Memory restorative ability of clioquinol in copper–cholesterol-induced experimental dementia in mice

Mehra, R., Sodhi, R. K., & Aggarwal, N. (2015) · Pharmaceutical Biology · doi:10.3109/13880209.2014.974061 · Cited by 12

Understanding Alzheimer’s Disease and its Metal Chelation Therapeutics: A Narrative Review

Thakur, R., Karwasra, R., & Umar, T. (2023) · Current Pharmaceutical Design · doi:10.2174/0113816128263992231012113847 · Cited by 11

Porphyromonas Gingivalis May Seek the Alzheimer’s Disease Brain to Acquire Iron from Its Surplus

Olsen, I. (2021) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200272 · Cited by 12

The binding abilities of homodetic cyclic His-peptides toward copper ions

Kotynia, A., Pap, J. S., & Brasuń, J. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.07.028 · Cited by 10

Anticarcinogenic and metal chelation properties of novel hydroxybenzylidene-1-indanone derivatives in the U-251 glioblastoma cell line

González, M. L., Ramírez‐Apán, M. T., Nieto‐Camacho, A., Toscano, R. A., Sánchez-Sandoval, A. L., & Alvarez, C. T. (2017) · New Journal of Chemistry · doi:10.1039/c7nj04266c · Cited by 10

H4HBEDpa: Octadentate Chelate after A. E. Martell

Choudhary, N., Scheiber, H., Zhang, J., Patrick, B. O., Jaraquemada-Peláez, M. D. G., & Orvig, C. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c01175 · Cited by 10

Hybrid Bis-Histidine Phenanthroline-Based Ligands to Lessen Aβ-Bound Cu ROS Production: An Illustration of Cu(I) Significance

Drommi, M., Rulmont, C., Esmieu, C., & Hureau, C. (2021) · Molecules · doi:10.3390/molecules26247630 · Cited by 10

Preparation, anticholinesterase activity, and docking study of new 2-butenediamide and oxalamide derivatives

Yerdelen, K. Ö., Koca, M., Kasap, Z., & Anıl, B. (2014) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2014.959947 · Cited by 10

The effect of substituents on the response of 3,4-dihydro-3-(2-oxo-2-phenylethylidene)-quinoxalin-2(1H)-one derivatives toward binding of Cu2+

Korin, E., Cohen, B., Bai, Y., Zeng, C., & Becker, J. Y. (2012) · Tetrahedron · doi:10.1016/j.tet.2012.06.071 · Cited by 9

A new copper ionophore DPMQ protects cells against ultraviolet B irradiation by inhibiting the TRPV1 channel

Huang, K., Ma, K., Hung, Y., Lo, L., Lin, K., Liu, P., Hu, M., & Chueh, S. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26861 · Cited by 9

11Synthesis, crystal structures, electrochemistry and biological evaluation of tris(quinolin-8-olato) Mn(III) and Co(III) complexes methanol solvate

Shamle, N. J., Tella, A. C., Obaleye, J. A., Balogun, F. O., Ashafa, A. O. T., & Ajibade, P. A. (2020) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2020.128585 · Cited by 9

A selective and sensitive peptide-based fluorescent chemical DSH sensor for detection of zinc ions and application in vitro and in vivo

Zhang, L., Cao, J., Chen, K., Liu, Y., Ge, Y., Wu, J., & Liu, D. (2019) · New Journal of Chemistry · doi:10.1039/c8nj06552g · Cited by 9

Non-invasive neuromodulation assisted by exogenous stimuli-responsive nanoplatforms for Alzheimer’s disease and Parkinson's disease therapy

Mao, M., Komes, D., Zhao, S., Pjanović, R., Wang, D., & Wang, Y. (2025) · The Innovation Medicine · doi:10.59717/j.xinn-med.2025.100121 · Cited by 8

Dual roles of tannins as polyphenols and metal complexing agents in the prevention and treatment of Alzheimer's disease: Exploring the potential of dietary interventions

Guan, Q., Cao, Y., Zhang, Y., Zhou, B., Wang, J., Baranenko, D., Cifuentes, A., Ibañez, E., Yuan, C., & Lu, W. (2025) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2025.105177 · Cited by 9

Functional nanoassemblies for the diagnosis and therapy of Alzheimer's diseases

Zhang, L., Sun, H., Chen, Y., Wei, M., Lee, J., Li, F., & Ling, D. (2021) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1696 · Cited by 8

Synthesis and structural characterization of a 8-hydroxyquinoline derivative coordinated to Zn(II)

Freitas, L. V. D., Santos, A. L. D. S. F. D., Costa, F. C. D., Calixto, J. B., Miranda, P. V. P., Silva, T. J. J., Pereira, E. S., Rocha, W. R., Almeida, W. B. D., Souza, L. A. D., et al. (2018) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2018.05.050 · Cited by 8

Pyridine aided progression from amorphous to crystalline bis([5-(aryl)-1-diazenyl]quinolin-8-olato)zinc(II) compounds − Solution and solid-state structural characterization, nanoparticle formation and antibacterial activity

Baul, T. S. B., Nongsiej, K., Biswas, K., Joshi, S. R., & Herbert Höpfl, B. (2018) · Inorganica Chimica Acta · doi:10.1016/j.ica.2018.06.049 · Cited by 8

Ligand Design to Target and Modulate Metal–Protein Interactions in Neurodegenerative Diseases

Beck, M. W., Pithadia, A. S., DeToma, A. S., Korshavn, K. J., & Lim, M. H. (2014) · Wiley eBooks · doi:10.1002/9781118697191.ch10 · Cited by 8

Multifunctional Tacrine–Quinoline Hybrids as Cholinesterase Inhibitors, Aβ Aggregation Blockers, and Metal Chelators for Alzheimer’s Therapy

Wang, X., Ma, M., Feng, Y., Li, J., & Wang, G. (2025) · Molecules · doi:10.3390/molecules30173489 · Cited by 8

Protective Effects of G Protein-Coupled Estrogen Receptor 1 (GPER1) on β-Amyloid-Induced Neurotoxicity: Implications for Alzheimer’s Disease

Kurt, A. H., Yüksel, K. Z., Üremiş, N., Üremi̇ş, M. M., Altun, İ., Boşnak, M., Kılıçaslan, D., & Alli, B. (2019) · Neurochemical Journal · doi:10.1134/s1819712419010148 · Cited by 7

Zinc(II) Complex with 2-Hydroxy-5-ethylphenylphosponic Acid: Synthesis, Structure, Toxicity, and Accumulation in HeLa Cells

Иванова, И. С., Tsebrikova, G. S., Ilyukhin, A. B., Solov’ev, V. P., Лапшина, М. А., Rogacheva, Y. I., Pyatova, E. N., Баулин, В. Е., & Tsivadze, A. Y. (2023) · Russian Journal of Inorganic Chemistry · doi:10.1134/s0036023623601393 · Cited by 7

Microwave-Assisted Synthesis, Molecular Docking, and Cholinesterase Inhibitory Activities of New Ethanediamide and 2-Butenediamide Analogues

Koca, M., Yerdelen, K. Ö., Anıl, B., & Kasap, Z. (2015) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c14-00754 · Cited by 7

Chelation Therapy

Flora, S. J. S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097774-4.00340-5 · Cited by 7

Ginsentide-like Coffeetides Isolated from Coffee Waste Are Cell-Penetrating and Metal-Binding Microproteins

Tam, J. P., Huang, J., Loo, S., Li, Y.-M., & Kam, A. (2023) · Molecules · doi:10.3390/molecules28186556 · Cited by 6

Synthesis of pyrazolo- and [1,2,4]triazolo-[1,5-а]quinolin-9-ols by cycloaddition to 8-hydroxyquinoline N-imide

Евтушок, В. Е., & Vorob’ev, A. Y. (2019) · Chemistry of Heterocyclic Compounds · doi:10.1007/s10593-019-02446-0 · Cited by 6

Synthesis and biological evaluation of novel hydrazone derivatives for the treatment of Alzheimer's disease

Ali, S. H., Osmani̇ye, D., & Kaplancıklı, Z. A. (2025) · RSC Advances · doi:10.1039/d5ra05755h · Cited by 5

Calculation of Solubility of Oxyquinolinates

Michałowska‐Kaczmarczyk, A. M., & Michałowski, T. (2014) · Journal of Analytical Sciences Methods and Instrumentation · doi:10.4236/jasmi.2014.43010 · Cited by 5

Evaluating the Multifunctionality of a New Modulator of Zinc-Induced Aβ Aggregation Using a Novel Computational Approach

Asadbegi, M., & Shamloo, A. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01264 · Cited by 5

Molecular scaffold and biological activities of anti- Alzheimer agents

Alanazi, F. K., Radwan, A. A., & Aou-Auda, H. (2022) · Tropical Journal of Pharmaceutical Research · doi:10.4314/tjpr.v21i2.30 · Cited by 5

Square Wave Voltammetric Determination of 8-Hydroxyquinoline-2-Carboxaldehyde Isonicotinoyl Hydrazone (INHHQ), a Promising Metal-Protein Attenuating Compound for the Treatment of Alzheimer’s Disease, Using a Multiwalled Carbon Nanotube (MWCNT) Modified Glassy Carbon Electrode (GCE)

Peñafiel, M. J. P., Falco, A. D., Miranda‐Andrades, J. R., Almeida, J. M. S., Larrudé, D. G., Rey, N. A., & Aucélio, R. Q. (2020) · Analytical Letters · doi:10.1080/00032719.2020.1741603 · Cited by 5

Copper interaction with cystatin C: effects on protein structure and oligomerization

Żygowska, J., Orlikowska, M., Zhukov, I., Bal, W., & Szymańska, A. (2024) · FEBS Journal · doi:10.1111/febs.17092 · Cited by 5

Rapid and high-throughput colorimetric screening for anti-aggregation reagents of protein conformational diseases by using gold nanoplasmonic particles

Kim, H. Y., Kwon, J. A., Kang, T., & Choi, I. (2017) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2017.01.004 · Cited by 5

A Hydroxyquinoline Polymer with Excellent Amyloidosis Inhibition and Protein Delivery Ability to Combat Amyloid-β-Mediated Neurotoxicity

Chen, L., Hu, Y., Cheng, Y., & Wang, H. (2024) · Nano Letters · doi:10.1021/acs.nanolett.4c03275 · Cited by 4

Organotin(IV) derivatives containing heteroditopic pyridyl-quinolin-8-olate ligands: Synthesis and structures

Baul, T. S. B., Chaurasiya, A., Nonglait, B. L., Lyčka, A., Schollmeyer, D., & Jurkschat, K. (2021) · Journal of Organometallic Chemistry · doi:10.1016/j.jorganchem.2021.121898 · Cited by 4

Study on Multi-Target Synergistic Treatment of Alzheimer’s Disease Based on Metal Chelators

Shen, R., Kou, X., Yang, A., Wu, J., & Chen, Y. (2022) · Current Drug Targets · doi:10.2174/1389450123666220926143920 · Cited by 4

Synthesis and Characterization of a Zinc(II) Complex of Bispicen

Parajón‐Costa, B. S., Echeverría, G. A., Piro, O. E., & Baran, E. J. (2013) · Zeitschrift für Naturforschung B · doi:10.5560/znb.2013-3193 · Cited by 4

Synthesis of Some Novel Quinolinols with In-vitro Antimicrobial, and Antioxidant Activity

Shehab, M. A., El-Naggar, M. H., Ismail, R. A., Kafrawy, H. M. E., Abood, A., Ismail, S. A., Sabry, N. M., & Sayed, M. T. E. (2019) · Current Bioactive Compounds · doi:10.2174/1573407215666190131112730 · Cited by 4

Kinetics and Mechanism of Oxidation of N-acetyl-d-penicillamine in Acidified lodate and Aqueous Iodine

Iodine, A., Chipiso, K., Duc, T., & Simoyi, R. H. (2018) · South African Journal of Chemistry · doi:10.17159/0379-4350/2019/v72a1 · Cited by 4

The Chelating Abilities of Tertiary Amines with N-O-Donors Towards Cu(II) Ions and the Catalytic Properties of the Resulting Complexes

Zonzin, M., Chianese, M., Squarcina, A., Dereje, D. M., Campofelice, A., Fermo, A. D., Belluti, F., Marino, N., Dębicki, F., Kotynia, A., et al. (2025) · Molecules · doi:10.3390/molecules30163419 · Cited by 3

Functionalized Two-Dimensional Carbon Nitride Nanodots Detect and Reverse Lead Toxicity in the Physiological Milieu

Mondal, S., Bayan, S., Ghosh, R., Das, M., Adhikari, A., Mukherjee, D., Mallick, A. K., Ray, S. K., & Pal, S. K. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c02377 · Cited by 3

Various pharmacological agents in the pipeline against intractable epilepsy

Waris, A., Asim, M., Ullah, A., & Alhumaydhi, F. A. (2024) · Archiv der Pharmazie · doi:10.1002/ardp.202400229 · Cited by 3

D-Penisilamin, D-Penisilamin disülfit ve N-Asetil-D-penisilamin’in Laktoperoksidaz Enzim Aktivitesi Üzerine İnhibisyon Etkileri

Korkmaz, I. N., Kalın, R., & Özdemіr, H. (2020) · Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi · doi:10.21597/jist.669441 · Cited by 3

Potansiyel karbonik anhidraz I ve II inhibitör keşfi: D-Penisilamin türevleri

Korkmaz, I. N. (2023) · Gümüşhane Üniversitesi Fen Bilimleri Enstitüsü Dergisi · doi:10.17714/gumusfenbil.1359988 · Cited by 2

Application of Organic Complex Compounds as Drug

-, D. K. S., -, B. B. S., -, V. K. S., & -, M. N. A. (2024) · International Journal For Multidisciplinary Research · doi:10.36948/ijfmr.2024.v06i04.24900 · Cited by 2

Synthesis and bio-activities of bifunctional tetrahydrosalen Cu (II) chelators with potential efficacy in Alzheimer's disease therapy

Sun, B., & Jiang, H. (2024) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2024.112636 · Cited by 2

Mechanism of Antimicrobial Activities of Medicinal Plants Extracts, From Traditional Knowledge to Scientific Insights

Iduh, M. U., Imam, U. A., Muhammad, N. B., Enitan, S. S., & Hassan, Y. (2024) · International Journal of Pathogen Research · doi:10.9734/ijpr/2024/v13i4300 · Cited by 2

Acid-base properties of hydroxyquinolines in aqueous solution: Effect of hydroxyl group position on thermodynamic protonation parameters

Baryłka, A., Santonoceta, G. D. G., Gattuso, G., Godlewska‐Żyłkiewicz, B., Sgarlata, C., Milea, D., & Gama, S. (2024) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2024.126671 · Cited by 2

Linear Free Energy Relationship (LFER) Analysis of Dissociation Constants of 8-Hydroxyquinoline and Its Derivatives in Aqueous and Dioxane–Water Solutions

Robak, W., Apostoluk, W., Maciejewski, P., Pielka, J. A., & Kwiotek, J. N. (2013) · Journal of Chemical & Engineering Data · doi:10.1021/je3009045 · Cited by 2

Metal Ions-Mediated Oxidative Stress in Alzheimer’s Disease and Chelation Therapy

Yeo, D., Choi, T. G., & Kim, S. S. (2021) · Biochemistry · doi:10.5772/intechopen.99690 · Cited by 2

Implications of statin metabolism related gene testing in guiding individualized drug use in cardiovascular diseases

Zhang, Y., You, X., Ren, Y., & Cui, J. (2022) · Tropical Journal of Pharmaceutical Research · doi:10.4314/tjpr.v22i2.30 · Cited by 2

Fluorometric Detection of Al3+ Ion in Mixed Aqueous Solvent Based on Simple Schiff-Base Molecular Prob

Das, S. (2023) · Asian Journal of Chemistry · doi:10.14233/ajchem.2023.26944 · Cited by 1

Impedimetric Detection of Amyloid Beta (1–42) on Curcumin‐Copper Complex Electropolymerized Graphite Electrode

Sayar, P., Maral, M., Yildiz, E., & Erdem, A. (2025) · Electroanalysis · doi:10.1002/elan.12049 · Cited by 1

The binding of kojic acid dimer and its Zn(II) and Cu(II) complexes at the beta-amyloid peptide: A DFT-based computational assessment

Tolbatov, I., Marzo, T., Peana, M., Medici, S., Zoroddu, M. A., Mendola, D. L., & Marrone, A. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112979 · Cited by 1

Novel Schiff base-Pt( ii ) complexes: inhibition of Aβ aggregation via histidine interaction

İrişli, S., Doğan, U., Günnaz, S., Yurt, F., & Şahin, O. (2025) · New Journal of Chemistry · doi:10.1039/d5nj04180e · Cited by 1

Characterization of the Cu(Π) and Zn(Π) binding to the Amyloid-β short peptides by both the Extended X-ray Absorption Fine Structure and the Synchrotron Radiation Circular Dichroism spectroscopy

Zhang, Z., Sun, S. S., Xu, J., Zhang, J., Huang, Y., Zhang, B., & Tao, Y. (2013) · Journal of Physics Conference Series · doi:10.1088/1742-6596/430/1/012041 · Cited by 1

A Missing Origin of the Tau Protein Aggregation Pathway Triggered by Thermal and Biological Forces

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