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Metal-associated amyloid-β species in Alzheimer's disease
Abstract
Highly concentrated metals such as Cu, Zn, and Fe are found in amyloid-β (Aβ) plaques within the brain of Alzheimer's disease (AD). In vitro and in vivo studies have suggested that metal binding to Aβ could facilitate Aβ aggregation and generate reactive oxygen species (ROS), which could contribute to the neuropathogenesis of AD. The connection between metal-Aβ interaction/reactivity and AD development, however, has not been clearly revealed owing to the complexity of the disease. In this review, metal-Aβ interaction/reactivity and its relation to neurotoxicity are briefly discussed. Additionally, our review illustrates the recent progress of small molecules, capable of targeting metal-Aβ species and modulating their interaction/reactivity, which could offer a promising approach to interrogate their role in AD.
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“Recent efforts to control abnormal Aβ–metal interactions have focused on small molecules, bifunctional chelators (BFCs), that have binding affinity for both metal ions and Aβ aggregates.20,25,27−30”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [29]
Citations
Cites
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
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
Alzheimer's Disease: From Pathology to Therapeutic Approaches
Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802808 · Cited by 626
The redox chemistry of the Alzheimer's disease amyloid β peptide
Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608
Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
Alzheimer's disease, metal ions and metal homeostatic therapy
Zatta, P., Drago, D., Bolognin, S., & Sensi, S. L. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.05.002 · Cited by 369
Causes of oxidative stress in Alzheimer disease
Zhu, X., Su, B., Wang, X., Smith, M. A., & Perry, G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7218-4 · Cited by 336
Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332
Choi, J.-S., Braymer, J. J., Nanga, R. P. R., Ramamoorthy, A., & Lim, M. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006091107 · Cited by 264
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Flagged first, then by citations
Research works printed but not linked: 31
- Alzheimer's Association, 2011, Alzheimer's disease facts and figures, Alzheimers Dement, 7, 208, 10.1016/j.jalz.2011.02.004 · DOI
- Hardy, 1992, Alzheimer's disease: the amyloid cascade hypothesis, Science, 256, 184, 10.1126/science.1566067 · DOI · Paper page
- Wang, 2006, Clearance of amyloid-beta in Alzheimer's disease: progress, problems and perspectives, Drug Discov Today, 11, 931, 10.1016/j.drudis.2006.08.004 · DOI
- Kurz, 2011, Amyloid clearance as a treatment target against Alzheimer's disease, J Alzheimers Dis, 24, 61, 10.3233/JAD-2011-102139 · DOI
- Maynard, 2005, Metals and amyloid-β in Alzheimer's disease, Int J Exp Pathol, 86, 147, 10.1111/j.0959-9673.2005.00434.x · DOI
- Bonda, 2011, Role of metal dyshomeostasis in Alzheimer's disease, Metallomics, 3, 267, 10.1039/c0mt00074d · DOI
- Jomova, 2011, Advances in metal-induced oxidative stress and human diseases, Toxicology, 283, 65, 10.1016/j.tox.2011.03.001 · DOI
- DeToma, 2012, Misfolded proteins in Alzheimer's disease and type II diabetes, Chem Soc Rev, 41, 608, 10.1039/C1CS15112F · DOI
- Burdette, 2003, Meeting of the minds: metalloneurochemistry, Proc Natl Acad Sci USA, 100, 3605, 10.1073/pnas.0637711100 · DOI
- Que, 2008, Metals in neurobiology: probing their chemistry and biology with molecular imaging, Chem Rev, 108, 1517, 10.1021/cr078203u · DOI
- Bush, 2008, Therapeutics for Alzheimer's disease based on the metal hypothesis, Neurotherapeutics, 5, 421, 10.1016/j.nurt.2008.05.001 · DOI
- Frederickson, 2005, The neurobiology of zinc in health and disease, Nat Rev Neurosci, 6, 449, 10.1038/nrn1671 · DOI
- Faller, 2009, Copper and zinc binding to amyloid-β: coordination, dynamics, aggregation, reactivity and metal-ion transfer, ChemBioChem, 10, 2837, 10.1002/cbic.200900321 · DOI · Paper page
- Gaggelli, 2006, Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyothrophic lateral sclerosis), Chem Rev, 106, 1995, 10.1021/cr040410w · DOI · Paper page
- Drew, 2011, The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide, Acc Chem Res, 44, 1146, 10.1021/ar200014u · DOI
- Karr, 2008, Cu(II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer's disease amyloid-β peptide, Biochemistry, 47, 5006, 10.1021/bi702423h · DOI
- Dorlet, 2009, Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1–16 amyloid-β peptide: a key role of the first two N-terminus residues, Angew Chem Int Ed, 48, 9273, 10.1002/anie.200904567 · DOI
- Shearer, 2008, The amyloid-β peptide of Alzheimer's disease binds CuI in a linear bis-His coordination environment: insight into a possible neuroprotective mechanism for the amyloid-β peptide, J Am Chem Soc, 130, 17826, 10.1021/ja805940m · DOI
- Himes, 2008, Structural studies of copper(I) complexes of amyloid-β peptide fragments: formation of two-coordinate bis(histidine) complexes, Angew Chem Int Ed, 47, 9084, 10.1002/anie.200803908 · DOI
- Shearer, 2010, Cu K-edge X-ray absorption spectroscopy reveals differential copper coordination within amyloid-β oligomers compared to amyloid-β monomers, Chem Commun, 46, 9137, 10.1039/c0cc02446e · DOI
- Feaga, 2011, Affinity of Cu+ for the copper-binding domain of amyloid-β peptide of Alzheimer's disease, Inorg Chem, 50, 1614, 10.1021/ic100967s · DOI
- Bousejra-ElGarah, 2011, Iron(II) binding to amyloid-β, the Alzheimer's peptide, Inorg Chem, 50, 9024, 10.1021/ic201233b · DOI
- Noy, 2008, Zinc-amyloid β interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species, J Am Chem Soc, 130, 1376, 10.1021/ja076282l · DOI
- Chen, 2011, Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-β stability, oligomerization, and aggregation, J Biol Chem, 286, 9646, 10.1074/jbc.M110.177246 · DOI
- Pramanik, 2011, Active site environment of heme-bound amyloid β peptide associated with Alzheimer's disease, J Am Chem Soc, 133, 81, 10.1021/ja1084578 · DOI
- Atamna, 2006, Amyloid-β peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease, Proc Natl Acad Sci USA, 103, 3381, 10.1073/pnas.0600134103 · DOI
- Atamna, 2006, Heme binding to amyloid β peptide: mechanistic role in Alzheimer's disease, J Alzheimers Dis, 10, 255, 10.3233/JAD-2006-102-310 · DOI
- Adlard, 2008, Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Aβ, Neuron, 59, 43, 10.1016/j.neuron.2008.06.018 · DOI · Paper page
- Kung, 2001, Novel stilbenes as probes for amyloid plaques, J Am Chem Soc, 123, 12740, 10.1021/ja0167147 · DOI
- Ono, 2004, Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro, J Neurosci Res, 75, 742, 10.1002/jnr.20025 · DOI · Paper page
- Wu, 2008, Sequestration of copper from β-amyloid promotes selective lysis by cyclen-hybrid cleave agents, J Biol Chem, 283, 31657, 10.1074/jbc.M804722200 · DOI
Cited by
Sorted by citations
Items 101–200 of 237
Ghosh, U., Yau, W., Collinge, J., & Tycko, R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2111863118 · Cited by 38
Adhikari, S. S., Ghosh, A., Ghosh, M., Guria, S., & Das, D. (2017) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2017.05.135 · Cited by 38
Jones, M. R., Dyrager, C., Hoarau, M., Korshavn, K. J., Lim, M. H., Ramamoorthy, A., & Storr, T. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.04.022 · Cited by 34
Self-citationLee, H. J., Kerr, R. A., Korshavn, K. J., Lee, J., Kang, J., Ramamoorthy, A., Ruotolo, B. T., & Lim, M. H. (2016) · Inorganic Chemistry Frontiers · doi:10.1039/c5qi00219b · Cited by 36
Self-citationLiu, Y., Kochi, A., Pithadia, A. S., Lee, S., Nam, Y., Beck, M. W., He, X., Lee, D., & Lim, M. H. (2013) · Inorganic Chemistry · doi:10.1021/ic400851w · Cited by 30
Self-citationTay, W. M., da Silva, G. F. Z., & Ming, L. (2013) · Inorganic Chemistry · doi:10.1021/ic301832p · Cited by 35
Gao, Z.-Y., Kan, C., Liu, H., Zhu, J., & Bao, X. (2019) · Tetrahedron · doi:10.1016/j.tet.2019.01.029 · Cited by 29
Exploring the reactivity of flavonoid compounds with metal-associated amyloid-β species
He, X., Park, H. M., Hyung, S., DeToma, A. S., Kim, C., Ruotolo, B. T., & Lim, M. H. (2012) · Dalton Transactions · doi:10.1039/c2dt12207c · Cited by 31
Self-citationHickey, J. P., Collins, A. E., Nelson, M. L., Chen, H., & Kalisch, B. E. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46050266 · Cited by 39
“Extracellular senile plaques, composed of aggregated A β , can contain metal ions such as iron (Fe), copper (Cu), and zinc (Zn) [100–108].”
BackgroundInfluentialKhan, H. Y., Ahmad, A., Hassan, M. N., Khan, Y. H., Arjmand, F., & Khan, R. H. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215580 · Cited by 26
Drug design strategies with metal-hydroxyquinoline complexes
Savić, I., & Savic, I. M. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1702964 · Cited by 34
“In Alzheimer’s disease, metal ions promote pathogenesis by accelerating amyloid-β (Aβ) aggregation and inducing the formation of neurotoxic reactive oxygen species (ROS) [27].”
BackgroundDwivedi, S. K., Gupta, R., Ali, R., Razi, S. S., Hira, S., Manna, P., & Misra, A. (2018) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2018.03.011 · Cited by 28
Zhang, H., Dong, X., & Sun, Y. P. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00133 · Cited by 33
Nootem, J., Sattayanon, C., Daengngern, R., Kamkaew, A., Wattanathana, W., Wannapaiboon, S., Rashatasakhon, P., & Chansaenpak, K. (2021) · Chemosensors · doi:10.3390/chemosensors9070165 · Cited by 28
Dolar-Szczasny, J., Święch-Zubilewicz, A., Flieger, J., Tatarczak‐Michalewska, M., Niedzielski, P., Proch, J., Majerek, D., Kawka, J., & Mackiewicz, J. (2019) · Molecules · doi:10.3390/molecules24224127 · Cited by 31
Xu, L., Chen, Y., & Wang, X. (2014) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24669 · Cited by 27
Bacchella, C., Dell’Acqua, S., Nicolis, S., Monzani, E., & Casella, L. (2022) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2022.214756 · Cited by 27
Vijay, N., Wu, S., & Velmathi, S. (2019) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2019.112060 · Cited by 26
Maity, P., Naskar, B., Goswami, S., Prodhan, C., Chaudhuri, T., Chaudhuri, K., & Mukhopadhyay, C. (2018) · ACS Omega · doi:10.1021/acsomega.8b02110 · Cited by 25
A europium(III) metal-organic framework as ratiometric turn-on luminescent sensor for Al3+ ions
Zhou, X.-H., Cheng, J., Li, L., Chen, Q., You, Y.-J., Xiao, H.-P., & Huang, W. (2018) · Science China Materials · doi:10.1007/s40843-017-9186-3 · Cited by 25
Thiophene-based rhodamine as selectivef luorescence probe for Fe(III) and Al(III) in living cells
Wang, K., Chen, J.-P., Zhang, S., Lei, Y., Zhong, H., Chen, S.-J., Zhou, X.-H., & Hu, Z.-Q. (2017) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-017-0490-8 · Cited by 25
Zn2+ Effect on Structure and Residual Hydrophobicity of Amyloid β-Peptide Monomers
Shi, H., Kang, B., & Lee, J. Y. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp504779m · Cited by 30
A novel pyridine-pyrazole based selective "turn-off" fluorescent chemosensor for Fe(III) ions
Madhu, P., & Sivakumar, P. (2019) · Journal of Photochemistry and Photobiology A: Chemistry · doi:10.1016/j.jphotochem.2018.11.033 · Cited by 24
A dual target chemosensor for the fluorometric detection of In3+ and colorimetric detection of Fe3.
Lee, S. Y., Yang, M., & Kim, C. (2018) · Spectrochimica Acta Part A - Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2018.07.091 · Cited by 24
A new Rhodamine-based visual and fluorometric probe for selective detection of trivalent cations
Hou, S.-H., Qu, Z.-G., Zhong, K.-L., Bian, Y.-J., & Tang, L.-J. (2016) · doi:10.1016/j.tetlet.2016.04.106 · Cited by 24
Said, A. I., Georgiev, N., & Bojinov, V. (2019) · Spectrochimica Acta Part A - Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.117304 · Cited by 23
Mumtaz, A., Majeed, A., Zaib, S., Rahman, S. U., Hameed, S., Saeed, A., Rafique, H., Mughal, E. U., Maalik, A., Hussain, I., et al. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103036 · Cited by 27
Dey, N., Ali, A., Kamra, M., & Bhattacharya, S. (2018) · Journal of Materials Chemistry B · doi:10.1039/c8tb01523f · Cited by 31
Wang, H., Wang, M., Wang, B., Li, M., Chen, H., Yu, X., Yang, K., Chai, Z., Zhao, Y., & Feng, W. (2012) · Metallomics · doi:10.1039/c2mt20056b · Cited by 31
Meng, J., Zhang, H., Dong, X., Liu, F., & Sun, Y. P. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.01.012 · Cited by 26
Abnormal metal levels in the primary visual pathway of the DBA/2J mouse model of glaucoma
DeToma, A. S., Crish, S. D., Deb, A., Braymer, J. J., Penner‐Hahn, J. E., der Schyf, C. J. V., Lim, M. H., & Crish, S. D. (2014) · BioMetals · doi:10.1007/s10534-014-9790-z · Cited by 24
“Abnormal levels (both increases and decreases) of Cu, Zn, and Fe ions have been implicated in the pathogenesis and progression of a number of central nervous system neurodegenerative disorders, including Alzheimer’s disease (DeToma et al. 2012; Pithadia and Lim 2012; Kepp 2012; Savelieff et al. 2013), Parkinson’s dise…”
Self-citationMetallomics in environmental and health related research: Current status and perspectives
Hu, L., He, B., Wang, Y., Jiang, G., & Sun, H. (2012) · Chinese Science Bulletin · doi:10.1007/s11434-012-5496-1 · Cited by 26
Murugan, A., Kiruthika, M., Noelson, E. R. A., Yogapandi, P., Kumar, G. G., & Annaraj, J. (2020) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2020.11.016 · Cited by 21
Nam, G., Ji, Y., Lee, H. J., Kang, J., Yi, Y., Kim, M., Lin, Y.-X., Lee, Y.-H., & Lim, M.-H. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00232 · Cited by 21
Self-citationKv3 channel assembly, trafficking and activity are regulated by zinc through different binding sites
Gu, Y., Barry, J., & Gu, C. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.251983 · Cited by 15
“Its concentration can become even higher in some pathophysiological conditions, such as Alzheimer’s disease, epilepsy and ischaemia injury (Weiss et al. 2000; Galasso & Dyck, 2007; Hershfinkel et al. 2009; Medvedeva et al. 2009; Pithadia & Lim, 2012).”
BackgroundAlrouji, M., Alshammari, M. S., Syed, T., & Shamsi, A. (2025) · Antioxidants · doi:10.3390/antiox14070774 · Cited by 21
“It has been demonstrated that this combination produces hydrogen peroxide and superoxide, with copper forming the most stable link among these metals [87–89].”
Key roles of Arg5, Tyr10 and His residues in Aβ–heme peroxidase: Relevance to Alzheimer’s disease
Lu, N., Li, J., Tian, R., & Peng, Y. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.08.130 · Cited by 22
Tai, M.-H., Wang, J., Yu, Z., Wang, Q., Wu, Q., Guo, J.-H., Cheng, Y., Jin, D.-L., & Wang, L.-C. (2023) · Microchemical journal (Print) · doi:10.1016/j.microc.2023.109182 · Cited by 19
Therapeutic Potential of Multifunctional Derivatives of Cholinesterase Inhibitors
Przybyłowska, M., Dzierzbicka, K., Kowalski, S., Chmielewska, K., & Inkielewicz‐Stępniak, I. (2020) · Current Neuropharmacology · doi:10.2174/1570159x19666201218103434 · Cited by 31
Iniya, M., Vidya, B., Anand, T., Sivaraman, G., Jeyanthi, D., Krishnaveni, K., & Chellappa, D. (2018) · ChemistrySelect · doi:10.1002/slct.201702860 · Cited by 20
Electrochemical sensing of iron (III) by using rhodamine dimer as an electroactive material.
Kamal, A., Sharma, N., Bhalla, V., Kumar, M., & Mahajan, R. (2014) · Talanta: The International Journal of Pure and Applied Analytical Chemistry · doi:10.1016/j.talanta.2014.04.034 · Cited by 19
A rhodamine derivative as a highly sensitive chemosensor for iron(III)
Wu, K., Xiao, H., Wang, L.-L., Yin, G., Quan, Y., & Wang, R.-Y. (2014) · RSC Advances · doi:10.1039/c4ra05180g · Cited by 19
pH-dependent kinetics of copper ions binding to amyloid-β peptide
Bin, Y., Chen, S., & Xiang, J. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.10.013 · Cited by 19
Han, S., Auger, C., Castonguay, Z., Appanna, V. D., Thomas, S. C., & Appanna, V. D. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-6413-9 · Cited by 18
Zhi, J., Tang, R., Yuan, X., Zhu, H., Guo, J., Chen, Y., Yang, Y., Liang, B., Lu, S., Cao, D., et al. (2023) · Small · doi:10.1002/smll.202302176 · Cited by 20
Singh, G., Pawan, Singh, A., Shilpy, Diksha, Suman, Sharma, G., Sahoo, S., & Kaur, A. (2020) · doi:10.1016/j.molstruc.2020.129618 · Cited by 18
Mou, X., Pilozzi, A. R., Tailor, B. A., Yi, J., Cahill, C. M., Rogers, J. T., & Huang, X. (2020) · Biomedicines · doi:10.3390/biomedicines8030045 · Cited by 21
Mukherjee, S., & Talukder, S. (2016) · Journal of Fluorescence · doi:10.1007/s10895-016-1790-7 · Cited by 18
Synthesis of new fluorene compounds for highly selective sensing of picric acid, Fe3+ and l-arginine
Han, Y., Zhao, J.-X., Yang, H., Huang, X.-T., Zhou, X., Hui, T., & Yan, J. (2020) · doi:10.1016/j.molstruc.2020.128395 · Cited by 17
Petdum, A., Waraeksiri, N., Hanmeng, O., Jarutikorn, S., Chaneam, S., Sirirak, J., Charoenpanich, A., Panchan, W., Sooksimuang, T., & Wanichacheva, N. (2020) · doi:10.1016/j.jphotochem.2020.112769 · Cited by 17
An excellent example illustrating the fluorescence sensing property of cobalt-organic frameworks.
Zhang, C., Liu, Z., Xu, H., Zheng, H.-G., Ma, J., & Zhao, J. (2019) · Dalton Transactions · doi:10.1039/c9dt00005d · Cited by 17
Turner, M., Mutter, S. T., & Platts, J. A. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1555490 · Cited by 18
“…Faller & Hureau, 2012; Kepp, 2017; Kozlowski, Luczkowski, Remelli, & Valensin, 2012; Lovell, Robertson, Teesdale, Campbell, & Markesbery, 1998; Pithadia & Lim, 2012); the exact role and behaviour of these metals in relation to AD is reviewed in detail elsewhere (Duce & Bush, 2010; Greenough,…”
BackgroundXie, B., Liu, F., Dong, X., Wang, Y., Liu, M., & Sun, Y. P. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.03.009 · Cited by 18
A Sensitive Colorimetric and Ratiometric Chemosensor for Trivalent Metal Cations
Zhao, X., Yin, G., Jin, D., Yan, X., Yang, L., & Chen, L. (2015) · Journal of Fluorescence · doi:10.1007/s10895-015-1513-5 · Cited by 17
“Its deficiency or excess has been demonstrated to be associated with a various of diseases , such as anemia, low immunity [4] [5] and Alzheimer [6] [7].”
BackgroundThree selective and sensitive “off–on” probes based on rhodamine for Fe3+ imaging in living cells
Yang, M.-P., Xu, C.-L., Li, S.-N., Cheng, Z., Zhou, J., & Yang, B.-Q. (2014) · RSC Advances · doi:10.1039/c4ra00396a · Cited by 17
Lázaro-Martínez, J., Monti, G., & Chattah, A. (2013) · doi:10.1016/j.polymer.2013.07.036 · Cited by 16
Murariu, M., Habasescu, L., Ciobanu, C. I., Grădinaru, V. R., Pui, A., Drochioiu, G., & Mangalagiu, I. I. (2018) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-018-9738-1 · Cited by 15
Beck, M. W., Derrick, J. S., Suh, J., Kim, M., Korshavn, K. J., Kerr, R. A., Cho, W. J., Larsen, S. D., Ruotolo, B. T., Ramamoorthy, A., et al. (2017) · ChemMedChem · doi:10.1002/cmdc.201700456 · Cited by 15
Self-citationYang, T., Liu, Y., Zhang, C., Wang, Y., Ma, X., Wang, K., Luo, J. H., Yao, C., Wang, X., & Wang, X. (2016) · Inorganic Chemistry Frontiers · doi:10.1039/c6qi00268d · Cited by 26
Jiang, N., Wang, X., Li, Z., Li, S., Xie, S., Huang, M. Y., & Kong, L. (2015) · RSC Advances · doi:10.1039/c4ra10692j · Cited by 15
Lin, J.-B., Zhu, C.-H., Liu, X.-Q., Chen, B., Zhang, Y.-Y., Xue, J., & Liu, J.-Y. (2014) · doi:10.1002/cjoc.201400464 · Cited by 15
Gao, Y., Ma, S.-Y., Ya, X., Gao, J., Han, S., Li, T., Gao, Y., & Zhao, B. (2020) · Tetrahedron Letters · doi:10.1016/j.tetlet.2019.151452 · Cited by 14
Asadbegi, M., & Shamloo, A. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00468 · Cited by 14
Asili, E., Yarahmadian, S., Khani, H., & Sharify, M. (2019) · Bulletin of Mathematical Biology · doi:10.1007/s11538-019-00583-3 · Cited by 15
Alam, M., Ahmad, S., Mohasin, M., Salma, U., Alimuddin, Parveen, H., Mukhtar, S., & Khan, S. A. (2025) · Journal of Fluorescence · doi:10.1007/s10895-025-04327-6 · Cited by 12
“Both a deficiency and an excess of copper can lead to severe health issues such as neurological disorder and blood disease [7, 8], Alzheimer’s disease [9], anaemia, and weakened immune function [10].”
Novel Bis-pyrazoline Fluorescent Probe for Cu^2+ and Fe^3+ Detection and Application in Cell Imaging
Yang, Y.-S., Wang, F., Zhang, Y.-P., Yang, F., & Xue, J. (2023) · Journal of Fluorescence · doi:10.1007/s10895-023-03213-3 · Cited by 12
“For example: Alzheimer's syndrome [4], anemia, decreased immune function and other symptoms [5].”
Battula, H., Muduli, S., Bandi, S. P., Kapoor, S., Mishra, S., Aggarwal, H., Venuganti, V. V. K., & Jayanty, S. (2021) · Journal of Photochemistry and Photobiology A: Chemistry · doi:10.1016/j.jphotochem.2021.113748 · Cited by 12
Cobalt(III) Schiff base complexes stabilize non-fibrillar amyloid-β aggregates with reduced toxicity
Roberts, K. F., Brue, C. R., Preston, A., Baxter, D., Herzog, E., Varelas, E. A., & Meade, T. J. (2020) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2020.111265 · Cited by 12
Intertwined Pathologies of Amyloid-β and Metal Ions in Alzheimer’s Disease: Metal–Amyloid-β
Nam, G., & Lim, M. H. (2019) · Chemistry Letters · doi:10.1246/cl.190281 · Cited by 16
Self-citationBhowmick, R., Islam, A. S. M., Giri, A., Katarkar, A., & Ali, M. (2018) · New Journal of Chemistry · doi:10.1039/c7nj02446k · Cited by 12
Two macrocyclic polyamines as modulators of metal-mediated Aβ40aggregation
Yang, Y., Chen, T., Zhu, S., Gu, X., Jia, X., Lu, Y., & Zhu, L. (2015) · Integrative Biology · doi:10.1039/c5ib00064e · Cited by 25
Lupano, L. V. L., Martínez, J. M. L., Piehl, L., de Celis, E. R., Sánchez, R. M., & Campodall'Orto, V. (2014) · Langmuir · doi:10.1021/la404799t · Cited by 12
Solving the Amyloid Paradox: Unveiling the Complex Pathogenicity of Amyloid Fibrils
Sulatsky, M. I., Stepanenko, O. V., Stepanenko, O. V., & Sulatskaya, A. I. (2025) · Aggregate · doi:10.1002/agt2.70078 · Cited by 9
Plant-derived chelators and ionophores as potential therapeutics for metabolic diseases
Lee, V. J., Janisse, S. E., & Heffern, M. C. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00167a · Cited by 17
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Anwar, F., Al-Abbasi, F. A., Naqvi, S., Sheikh, R. A., Alhayyani, S., Asseri, A. H., Asar, T. O., & Kumar, V. (2023) · International Journal of Nanomedicine · doi:10.2147/ijn.s405454 · Cited by 15
“This can increase the deposition of Aβ(138) and can promote the progression of disease.(139) Zinc loaded nanoparticles in wild type (WT) and APP23 mice model alters the pathological conditions in the mice model by significant effect on proinflammatory cytokines IL-6 and IL-18 and reduction in plague size.”
BackgroundHu, C., Jiang, L., Tang, L., Zhang, M.-K., & Sheng, R. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116306 · Cited by 11
Bataglioli, J. C., Gomes, L. M., Maunoir, C., Smith, J. R., Cole, H. D., McCain, J., Sainuddin, T., Cameron, C. G., McFarland, S. A., & Storr, T. (2021) · Chemical Science · doi:10.1039/d1sc00004g · Cited by 29
Ma, S., Qiang, J., Li, L., Mo, Y., She, M., Yang, Z., Liu, P., Zhang, S., & Li, J. (2019) · Journal of Materials Chemistry B · doi:10.1039/c9tb00291j · Cited by 18
A Unified View of Assessing the Pro‐oxidant versus Antioxidant Nature of Amyloid Beta Conformers
Mitra, S., Prasad, P., & Chakraborty, S. (2018) · ChemBioChem · doi:10.1002/cbic.201800446 · Cited by 13
Márquez, M., Blancas‐Mejía, L. M., Campos, A., Rojas-Ochoa, L. F., Castañeda‐Hernández, G., & Quintanar, L. (2014) · Metallomics · doi:10.1039/c4mt00257a · Cited by 20
Khatun, M., Ghorai, P., Mandal, J., Chowdhury, S. G., Karmakar, P., Blasco, S., García‐España, E., & Saha, A. (2023) · ACS Omega · doi:10.1021/acsomega.2c06549 · Cited by 14
Jiang, Q.-W., Chuang, P.-M., & Wu, J.-Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010369 · Cited by 10
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Miller, J. J., Kwan, K., Gaiddon, C., & Storr, T. (2022) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-022-01939-2 · Cited by 14
Cendrowska‐Pinkosz, M., Krauze, M., Juśkiewicz, J., & Ognik, K. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126777 · Cited by 12
Qian, Y., Suo, J., Gao, Z., Liu, H., Hua, Q., Lu, Y., Zhang, P., Kan, C., Bao, X., & Zhu, J. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115309 · Cited by 10
Smith, K. J., Schwartz, T. M., Freire, D. M., Bowers, C. J., Dunn, S. K., Bonnell, J. F., Mekhail, M. A., Akkaraju, G. R., & Green, K. N. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c02776 · Cited by 10
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Li, Y.-J., Yu, X.-D., & Pang, X.-L. (2023) · Journal of Photochemistry and Photobiology A: Chemistry · doi:10.1016/j.jphotochem.2023.115040 · Cited by 9
Iyappan, M., Dhineshkumar, E., & Anbuselvan, C. (2020) · Chemické zvesti · doi:10.1007/s11696-020-01236-9 · Cited by 9
Ghosh, A., Mandal, S., Das, S. K., Shaw, P., Chattopadhyay, A., & Sahoo, P. (2020) · Tetrahedron Letters · doi:10.1016/j.tetlet.2019.151520 · Cited by 9
A high-efficiency and low-cost AEE polyurethane chemo-sensor for Fe3+ and explosives detection
Wang, K., Lu, H., Liu, B., & Yang, J. (2018) · Tetrahedron Letters · doi:10.1016/j.tetlet.2018.10.035 · Cited by 12
Lee, H. J., Savelieff, M. G., Kang, J., Brophy, M. B., Nakashige, T. G., Lee, S. J. C., Nolan, E. M., & Lim, M. H. (2018) · Metallomics · doi:10.1039/c8mt00091c · Cited by 12
Self-citationSafadi, M. E., Bhadbhade, M. M., Shimmon, R., Baker, A. T., & McDonagh, A. M. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.07.060 · Cited by 10
Jiang, L., Zhang, M., Tang, L., Weng, Q., Shen, Y., Hu, Y., & Sheng, R. (2016) · RSC Advances · doi:10.1039/c5ra25788c · Cited by 15
Key roles of Tyr 10 in Cu bound Aβ complexes and its relevance to Alzheimer's disease
Lu, N., Li, J., & Gao, Z. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.07.009 · Cited by 12
Guzmán, R., Campos, C., Yuguero, R., Masegù, C., Gil, P., & Moragón, Á. C. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.04.006 · Cited by 8
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Zhang, C., Gomes, L. M., Zhang, T., & Storr, T. (2017) · Canadian Journal of Chemistry · doi:10.1139/cjc-2017-0623 · Cited by 7
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Collins, A. E., Saleh, T. M., & Kalisch, B. E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010442 · Cited by 10
Kim, M., & Lim, M. H. (2021) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.12372 · Cited by 14
Self-citationMaity, P., Naskar, B., Mukhopadhyay, C. D., Goswami, S., & Mukhopadhyay, C. (2021) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2021.130280 · Cited by 8
Park, S., Yi, Y., & Lim, M. H. (2020) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.12172 · Cited by 14
Self-citation
Metadata
- Authors
- Pithadia, A. S., & Lim, M. H.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Lim, Mi Hee
- ORCID
- Lim, Mi Hee
- Venue
- Current Opinion in Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2012-04
- Volume
- 16
- Issue
- 1-2
- Pages
- 67-73
- ISSN
- 1367-5931 (ISSN-L)
- OpenAlex
- W1984223653
- Cited by
- 259
- References
- 48
- Citations by year
- 2026: 3 · 2025: 12 · 2024: 10 · 2023: 14 · 2022: 11 · 2021: 17 · 2020: 21 · 2019: 28 · 2018: 30 · 2017: 25 · 2016: 16 · 2015: 18 · 2014: 26 · 2013: 20 · 2012: 8
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Scholarworks@UNIST (Ulsan National Institute of Science and Technology) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Aluminum toxicity and tolerance in plants and animals
- Keywords
- Alzheimer's disease, amyloid-beta, metal ion binding, copper, zinc, iron, amyloid plaques, amyloid-beta aggregation, reactive oxygen species, neurotoxicity, metal chelators
- MeSH terms
- Alzheimer Disease, Amyloid, Humans, Metals, Reactive Oxygen Species
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