The DOI matches its Crossref record; 100 of the 100 references it cites were found in a registry or an index.
Untangling Amyloid-β, Tau, and Metals in Alzheimer’s Disease
Abstract
Protein misfolding and metal ion dyshomeostasis are believed to underlie numerous neurodegenerative diseases, including Alzheimer's disease (AD). The pathological hallmark of AD is accumulation of misfolded amyloid-β (Aβ) peptides and hyperphosphorylated tau (ptau) proteins in the brain. Since AD etiology remains unclear, several hypotheses have emerged to elucidate its pathological pathways. The amyloid cascade hypothesis, a leading hypothesis for AD development, advocates Aβ as the principal culprit. Additionally, evidence suggests that tau may contribute to AD pathology. Aβ and tau have also been shown to impact each other's pathology either directly or indirectly. Furthermore, metal ion dyshomeostasis is associated with these misfolded proteins. Metal interactions with Aβ and tau/ptau also influence their aggregation properties and neurotoxicity. Herein, we present current understanding on the roles of Aβ, tau, and metal ions, placing equal emphasis on each of these proposed features, as well as their inter-relationships in AD pathogenesis.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedVMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,423
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
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
Metals in Neurobiology: Probing Their Chemistry and Biology with Molecular Imaging
Que, E. L., Domaille, D. W., & Chang, C. J. (2008) · Chemical Reviews · doi:10.1021/cr078203u · Cited by 2,061
Buée, L., Bussière, T., Buée-Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,015
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., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 1,996
Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892
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
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
Paravastu, A. K., Leapman, R. D., Yau, W.-M., & Tycko, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806270105 · Cited by 1,160
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111
Metals, oxidative stress and neurodegenerative disorders
Jomova, K., Vondrakova, D., Lawson, M., & Valko, M. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0563-x · Cited by 1,052
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I., & Glabe, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500997200 · Cited by 1,041
2012 Alzheimer's disease facts and figures Alzheimer's Association ∗
Thies, W., & Bleiler, L. (2012) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2012.02.001 · Cited by 982
Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J.-H., Mohan, P. S., Mercken, M., Farmery, M. R., Tjernberg, L. O., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505082 · Cited by 967
Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., Arnsdorf, M. F., & Lindquist, S. L. (2000) · Science · doi:10.1126/science.289.5483.1317 · Cited by 963
Tauopathy in Drosophila : Neurodegeneration Without Neurofibrillary Tangles
Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939
Bernstein, S. L., Dupuis, N. F., Lazo, N. D., Wyttenbach, T., Condron, M. M., Bitan, G., Teplow, D. B., Shea, J.-E., Ruotolo, B. T., Robinson, C. V., et al. (2009) · Nature Chemistry · doi:10.1038/nchem.247 · Cited by 918
The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization
Hamley, I. W. (2012) · Chemical Reviews · doi:10.1021/cr3000994 · Cited by 882
Alonso, A. D. C., Zaidi, T., Novak, M., Grundke-Iqbal, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 827
Zinc in the physiology and pathology of the CNS
Sensi, S. L., Paoletti, P., Bush, A. I., & Sekler, I. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2734 · Cited by 759
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 672
Mechanisms of tau-induced neurodegeneration
Iqbal, K., Liu, F., Gong, C.-X., Alonso, A. D. C., & Grundke-Iqbal, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0486-3 · Cited by 628
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
Brandt, R., Léger, J., & Lee, G. (1995) · The Journal of cell biology · doi:10.1083/jcb.131.5.1327 · Cited by 625
β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595
Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid
Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 579
Schweers, O., Schönbrunn-Hanebeck, E., Marx, A., & Mandelkow, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51080-8 · Cited by 567
Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559
Proline-directed and non-proline-directed phosphorylation of PHF-tau
Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Titani, K., & Ihara, Y. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.823 · Cited by 557
Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration
Wang, J., Grundke‐Iqbal, I., & Iqbal, K. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05226.x · Cited by 553
Sayre, L. M., Perry, G., Harris, P. L. R., Liu, Y., Schubert, K. A., & Smith, M. A. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0740270.x · Cited by 540
Self-citationBioinorganic 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
Copper in the brain and Alzheimer’s disease
Hung, Y. H., Bush, A. I., & Cherny, R. A. (2010) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0600-y · Cited by 498
Hoshi, M., Sato, M., Matsumoto, S., Noguchi, A., Yasutake, K., Yoshida, N., & Sato, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1237107100 · Cited by 496
Tau Reduction Prevents Aβ-Induced Defects in Axonal Transport
Vossel, K. A., Zhang, K., Brodbeck, J., Daub, A. C., Sharma, P., Finkbeiner, S., Cui, B., & Mucke, L. (2010) · Science · doi:10.1126/science.1194653 · Cited by 486
Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases
Mazanetz, M. P., & Fischer, P. M. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2111 · Cited by 459
Harper, J. D., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90303-3 · Cited by 453
Alonso, A. D. C., Grundke-Iqbal, I., Barra, H. S., & Iqbal, K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.1.298 · Cited by 437
A partially folded structure of amyloid-beta(1–40) in an aqueous environment
Vivekanandan, S., Brender, J. R., Lee, S. Y., & Ramamoorthy, A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.06.133 · Cited by 432
Self-citationLee, J.-Y., Cole, T. B., Palmiter, R. D., Suh, S. W., & Koh, J.-Y. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092034699 · Cited by 430
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
Temporal Profile of Amyloid-β (Aβ) Oligomerization in an in Vivo Model of Alzheimer Disease
Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L., & LaFerla, F. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507892200 · Cited by 379
Misfolded proteins in Alzheimer's disease and type II diabetes
DeToma, A. S., Salamekh, S., Ramamoorthy, A., & Lim, M. H. (2012) · Chem. Soc. Rev. · doi:10.1039/c1cs15112f · Cited by 361
Self-citationStructural Characterization of a Soluble Amyloid β-Peptide Oligomer
Yu, L., Edalji, R., Harlan, J. E., Holzman, T. F., Lopez, A. P., Labkovsky, B., Hillen, H., Barghorn, S., Ebert, U., Richardson, P. L., et al. (2009) · Biochemistry · doi:10.1021/bi802046n · Cited by 354
Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer
Kayed, R., Pensalfini, A., Margol, L., Sokolov, Y., Sarsoza, F., Head, E., Hall, J., & Glabe, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808591200 · Cited by 348
Paravastu, A. K., Qahwash, I., Leapman, R. D., Meredith, S. C., & Tycko, R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812033106 · Cited by 322
Role of metal dyshomeostasis in Alzheimer's disease
Bonda, D. J., Lee, H.-G., Blair, J. A., Zhu, X., Perry, G., & Smith, M. A. (2011) · Metallomics · doi:10.1039/c0mt00074d · Cited by 319
Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.t01-1-01061.x · Cited by 313
Biochemistry of Tau in Alzheimer’s disease and related neurological disorders
Sergeant, N., Bretteville, A., Hamdane, M., Caillet-Boudin, M.-L., Grognet, P., Bombois, S., Blum, D., Delacourte, A., Pasquier, F., Vanmechelen, E., et al. (2008) · Expert Review of Proteomics · doi:10.1586/14789450.5.2.207 · Cited by 300
Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease
Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 290
Berriman, J., Serpell, L. C., Oberg, K. A., Fink, A. L., Goedert, M., & Crowther, R. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1530287100 · Cited by 288
Elucidation of Primary Structure Elements Controlling Early Amyloid β-Protein Oligomerization
Bitan, G., Vollers, S. S., & Teplow, D. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300825200 · Cited by 287
Miller, Y., Ma, B., & Nussinov, R. (2010) · Chemical Reviews · doi:10.1021/cr900377t · Cited by 286
Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900321 · Cited by 285
Biological metals and Alzheimer's disease: Implications for therapeutics and diagnostics
Duce, J. A., & Bush, A. I. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.003 · Cited by 283
Increasing Cu bioavailability inhibits Aβ oligomers and tau phosphorylation
Crouch, P. J., Hung, L. W., Adlard, P. A., Cortes, M., Lal, V., Filiz, G., Perez, K. A., Nurjono, M., Caragounis, A., Du, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809057106 · Cited by 278
Guilloreau, L., Combalbert, S., Sournia‐Saquet, A., Mazarguil, H., & Faller, P. (2007) · ChemBioChem · doi:10.1002/cbic.200700111 · Cited by 270
Guo, J.-P., Arai, T., Miklossy, J., & McGeer, P. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509386103 · Cited by 261
Metal-associated amyloid-β species in Alzheimer's disease
Pithadia, A. S., & Lim, M. H. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.01.016 · Cited by 259
Self-citationYamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01061.x · Cited by 246
Aβ40-Lactam(D23/K28) Models a Conformation Highly Favorable for Nucleation of Amyloid
Sciarretta, K. L., Gordon, D. J., Petkova, A. T., Tycko, R., & Meredith, S. C. (2005) · Biochemistry · doi:10.1021/bi0474867 · Cited by 244
Dementia: A problem for our age
Abbott, A. (2011) · Nature · doi:10.1038/475s2a · Cited by 241
Soluble Amyloid Oligomers Increase Bilayer Conductance by Altering Dielectric Structure
Sokolov, Y., Kozak, J. A., Kayed, R., Chanturiya, A., Glabe, C., & Hall, J. E. (2006) · The Journal of General Physiology · doi:10.1085/jgp.200609533 · Cited by 228
Tõugu, V., Tiiman, A., & Palumaa, P. (2011) · Metallomics · doi:10.1039/c0mt00073f · Cited by 225
Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
King, M. E., Kan, H.-M., Baas, P. W., Erisir, A., Glabe, C. G., & Bloom, G. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605187 · Cited by 217
Iron(II) Binding to Amyloid-β, the Alzheimer’s Peptide
Bousejra-ElGarah, F., Bijani, C., Coppel, Y., Faller, P., & Hureau, C. (2011) · Inorganic Chemistry · doi:10.1021/ic201233b · Cited by 198
Pathways by Which Aβ Facilitates Tau Pathology
Blurton-Jones, M., & LaFerla, F. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025242 · Cited by 195
Shearer, J., & Szalai, V. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja805940m · Cited by 189
Noguchi, A., Matsumura, S., Dezawa, M., Tada, M., Yanazawa, M., Ito, A., Akioka, M., Kikuchi, S., Sato, M., Ideno, S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000208 · Cited by 173
Kitazawa, M., Cheng, D., & LaFerla, F. M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05901.x · Cited by 165
Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151
Harris, F. M., Brecht, W. J., Xu, Q., Mahley, R. W., & Huang, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408127200 · Cited by 151
Himes, R. A., Park, G. Y., Siluvai, G. S., Blackburn, N. J., & Karlin, K. D. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200803908 · Cited by 149
Binding of Zn(II), Cu(II), and Fe(II) ions to alzheimer's Aß peptide studied by fluorescence
Garzon-Rodriguez, W., Yatsimirsky, A. K., & Glabe, C. G. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00357-1 · Cited by 148
Chimon, S., & Ishii, Y. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054039l · Cited by 143
Wilson, M. R., Yerbury, J. J., & Poon, S. (2007) · Molecular BioSystems · doi:10.1039/b712728f · Cited by 142
Hureau, C., Balland, V., Coppel, Y., Solari, P. L., Fonda, E., & Faller, P. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0570-0 · Cited by 138
Kheterpal, I., Chen, M., Cook, K. D., & Wetzel, R. B. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.066 · Cited by 136
Aluminum modifies the properties of Alzheimer's disease PHF tau proteins in vivo and in vitro
Shin, R. W., Lee, V., & Trojanowski, J. Q. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-11-07221.1994 · Cited by 124
Ma, Q., Li, Y., Du, J., Liu, H., Kanazawa, K., Nemoto, T., Nakanishi, H., & Zhao, Y. (2006) · Peptides · doi:10.1016/j.peptides.2005.09.002 · Cited by 123
Iron-induced oxidative stress modify tau phosphorylation patterns in hippocampal cell cultures
Egaña, J. T., Zambrano, C. A., Núñez, M. T., González-Billault, C. E., & Maccioni, R. B. (2003) · BioMetals · doi:10.1023/a:1020727218493 · Cited by 116
Metal Binding Dictates Conformation and Function of the Amyloid Precursor Protein (APP) E2 Domain
Dahms, S. O., Könnig, I., Roeser, D., Gührs, K., Mayer, M., Kaden, D., Multhaup, G., & Than, M. E. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.057 · Cited by 112
Werner coordination chemistry and neurodegeneration
Telpoukhovskaia, M. A., & Orvig, C. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35236b · Cited by 112
The Role of Amyloid-Beta Derived Diffusible Ligands (ADDLs) in Alzheimers Disease
Catalano, S. M., Dodson, E., Henze, D. A., Joyce, J. G., Krafft, G. A., & Kinney, G. G. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606776743066 · Cited by 107
Structural Characterization of Binding of Cu(II) to Tau Protein
Soragni, A., Zambelli, B., Mukrasch, M. D., Biernat, J., Jeganathan�, S., Griesinger, C., Ciurli, S., Mandelkow�, E., & Zweckstetter, M. (2008) · Biochemistry · doi:10.1021/bi8008856 · Cited by 104
Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI‐TOF MS, CD, and NMR
Ma, Q., Li, Y., Du, J., Kanazawa, K., Nemoto, T., Nakanishi, H., & Zhao, Y. (2005) · Biopolymers · doi:10.1002/bip.20335 · Cited by 96
Tew, D. J., Bottomley, S. P., Smith, D. P., Ciccotosto, G. D., Babon, J., Hinds, M. G., Masters, C. L., Cappai, R., & Barnham, K. J. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.119909 · Cited by 93
Copper (II) modulates in vitro aggregation of a tau peptide
Zhou, L., Du, J., Zeng, Z., Wu, W., Zhao, Y., Kanazawa, K., Ishizuka, Y., Nemoto, T., Nakanishi, H., & Li, Y. (2007) · Peptides · doi:10.1016/j.peptides.2007.08.022 · Cited by 88
Innocenti, M., Salvietti, E., Guidotti, M., Casini, A., Bellandi, S., Foresti, M. L., Gabbiani, C., Pozzi, A., Zatta, P. F., & Luigi Messori, A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1338 · Cited by 87
Affinity of Cu+ for the Copper-Binding Domain of the Amyloid-β Peptide of Alzheimer’s Disease
Feaga, H. A., Maduka, R. C., Foster, M. N., & Szalai, V. A. (2011) · Inorganic Chemistry · doi:10.1021/ic100967s · Cited by 78
Hydrogen peroxide can be generated by tau in the presence of Cu(II)
Su, X., Wu, W., Huang, Z., Hu, J. N., Lei, P., Yu, C., Zhao, Y., & Li, Y. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.191 · Cited by 77
Chen, Y. R., Huang, H., Chyan, C. L., Shiao, M. S., Lin, T. H., & Chen, Y. C. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj083 · Cited by 54
Shearer, J., Callan, P. E., Tran, T., & Szalai, V. A. (2010) · Chemical Communications · doi:10.1039/c0cc02446e · Cited by 44
Ding, H., & Johnson, G. V. W. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14413 · Cited by 30
New application of β‐galactosidase complementation to monitor tau self‐association
Ding, H., & Johnson, G. V. W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05496.x · Cited by 5
Cited by
Synthetic fluorescent probes for studying copper in biological systems
Cotruvo, Jr., Aron, A. T., Ramos-Torres, K. M., & Chang, C. J. (2015) · Chemical Society Reviews · doi:10.1039/c4cs00346b · Cited by 558
Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation
Tamás, M., Sharma, S., Ibstedt, S., Jacobson, T., & Christen, P. (2014) · Biomolecules · doi:10.3390/biom4010252 · Cited by 468
Chemically diverse small molecule fluorescent chemosensors for copper ion
Sivaraman, G., Iniya, M., Anand, T., Kotla, N. G., Sunnapu, O., Singaravadivel, S., Gulyani, A., & Chellappa, D. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.11.020 · Cited by 391
The biological pathways of Alzheimer disease: a review
Calabrò, M., Department of Biomedical and Dental Sciences and Morphofunctional Imaging, U. O. M., Rinaldi, C., Santoro, G., & Crisafulli, C. (2021) · AIMS Neuroscience · doi:10.3934/neuroscience.2021005 · Cited by 265
Rajasekhar, K., & Govindaraju, T. (2018) · RSC Advances · doi:10.1039/c8ra03620a · Cited by 150
Metadata
- Authors
- Savelieff, M. G., Lee, S., Liu, Y., & Lim, M. H.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-03-18
- Volume
- 8
- Issue
- 5
- Pages
- 856-865
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W2029119021
- Cited by
- 400
- References
- 100
- FWCI
- 17.95
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.