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  18. ↑ Raman, Arvind; Pablo, Pedro J. de; Carrascosa, José L.; Hernando-Pérez, Mercedes; Cartagena, Alexander «Mapping in vitro local material properties of intact and disrupted virions at high resolution using multi-harmonic atomic force microscopy» (en anglès). Nanoscale, 5, 11, 16-05-2013, pàg. 4729–4736. DOI: 10.1039/C3NR34088K. ISSN: 2040-3372.
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  26. ↑ MG, Krukemeyer; V, Krenn; F, Huebner «History and Possible Uses of Nanomedicine Based on Nanoparticles and Nanotechnological Progress» (en anglès). Journal of Nanomedicine & Nanotechnology, 06, 06, 2015. DOI: 10.4172/2157-7439.1000336. ISSN: 2157-7439.
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  30. ↑ Wu, Li; Wu, I-Che; DuFort, Christopher C.; Carlson, Markus A.; Wu, Xu «Photostable Ratiometric Pdot Probe for in Vitro and in Vivo Imaging of Hypochlorous Acid» (en anglès). Journal of the American Chemical Society, 139, 20, 11-05-2017, pàg. 6911–6918. DOI: 10.1021/jacs.7b01545. ISSN: 0002-7863. PMC: PMC5695557. PMID: 28459559.
  31. ↑ Berthelot, Karine; Cullin, Christophe; Lecomte, Sophie «What does make an amyloid toxic: Morphology, structure or interaction with membrane?». Biochimie, 95, 1, 2013-01, pàg. 12–19. DOI: 10.1016/j.biochi.2012.07.011. ISSN: 0300-9084.
  32. ↑ Chakraborty, Mainak; Jain, Surangna; Rani, Vibha «Nanotechnology: Emerging Tool for Diagnostics and Therapeutics» (en anglès). Applied Biochemistry and Biotechnology, 165, 5-6, 17-08-2011, pàg. 1178–1187. DOI: 10.1007/s12010-011-9336-6. ISSN: 0273-2289.
  33. ↑ Berthelot, Karine; Cullin, Christophe; Lecomte, Sophie «What does make an amyloid toxic: Morphology, structure or interaction with membrane?». Biochimie, 95, 1, 2013-01, pàg. 12–19. DOI: 10.1016/j.biochi.2012.07.011. ISSN: 0300-9084.
  34. ↑ Stefani, Massimo; Dobson, Christopher M. «Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution». Journal of Molecular Medicine, 81, 11, 01-11-2003, pàg. 678–699. DOI: 10.1007/s00109-003-0464-5. ISSN: 0946-2716.
  35. ↑ Chiti, Fabrizio; Dobson, Christopher M. «Protein Misfolding, Functional Amyloid, and Human Disease». Annual Review of Biochemistry, 75, 1, 2006-06, pàg. 333–366. DOI: 10.1146/annurev.biochem.75.101304.123901. ISSN: 0066-4154.
  36. ↑ Engel, M. F. M.; Khemtemourian, L.; Kleijer, C. C.; Meeldijk, H. J. D.; Jacobs, J. «Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane». Proceedings of the National Academy of Sciences, 105, 16, 11-04-2008, pàg. 6033–6038. DOI: 10.1073/pnas.0708354105. ISSN: 0027-8424.
  37. ↑ Friedrich, Ralf P.; Tepper, Katharina; Rönicke, Raik; Soom, Malle; Westermann, Martin «Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity» (en anglès). Proceedings of the National Academy of Sciences, 107, 5, 02-02-2010, pàg. 1942–1947. DOI: 10.1073/pnas.0904532106. ISSN: 0027-8424. PMC: PMC2836607. PMID: 20133839.
  38. ↑ Terry, Robert D.; Masliah, Eliezer; Salmon, David P.; Butters, Nelson; DeTeresa, Richard «Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment» (en anglès). Annals of Neurology, 30, 4, 1991-10, pàg. 572–580. DOI: 10.1002/ana.410300410. ISSN: 0364-5134.
  39. ↑ Benilova, Iryna; Karran, Eric; De Strooper, Bart «The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes». Nature Neuroscience, 15, 3, 29-01-2012, pàg. 349–357. DOI: 10.1038/nn.3028. ISSN: 1097-6256.
  40. ↑ Karran, Eric; Mercken, Marc; Strooper, Bart De «The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics». Nature Reviews Drug Discovery, 10, 9, 19-08-2011, pàg. 698–712. DOI: 10.1038/nrd3505. ISSN: 1474-1776.
  41. ↑ Montoliu-Gaya, Laia; Villegas, Sandra «Aβ-Immunotherapeutic strategies: a wide range of approaches for Alzheimer's disease treatment». Expert Reviews in Molecular Medicine, 18, 2016. DOI: 10.1017/erm.2016.11. ISSN: 1462-3994.
  42. ↑ Rakhit, Rishi; Chakrabartty, Avijit «Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis». Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1762, 11-12, 2006-11, pàg. 1025–1037. DOI: 10.1016/j.bbadis.2006.05.004. ISSN: 0925-4439.
  43. ↑ Choi, Inhee; Lee, Elizabeth; Lee, Luke P. «Current nano/biotechnological approaches in amyotrophic lateral sclerosis» (en anglès). Biomedical Engineering Letters, 3, 4, 01-12-2013, pàg. 209–222. DOI: 10.1007/s13534-013-0114-y. ISSN: 2093-9868.
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  45. ↑ Yim, M. B.; Kang, J. H.; Yim, H. S.; Kwak, H. S.; Chock, P. B. «A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide.». Proceedings of the National Academy of Sciences, 93, 12, 11-06-1996, pàg. 5709–5714. DOI: 10.1073/pnas.93.12.5709. ISSN: 0027-8424.
  46. ↑ Perlmutter, J. S.; Kilbourn, M. R.; Raichle, M. E.; Welch, M. J. «MPTP-induced up-regulation of in vivo dopaminergic radioligand-receptor binding in humans». Neurology, 37, 10, 01-10-1987, pàg. 1575–1575. DOI: 10.1212/wnl.37.10.1575. ISSN: 0028-3878.
  47. ↑ Ono, Masahiro; Saji, Hideo «Recent advances in molecular imaging probes for β-amyloid plaques». MedChemComm, 6, 3, 2015, pàg. 391–402. DOI: 10.1039/c4md00365a. ISSN: 2040-2503.
  48. ↑ Ortiz-Teran, Laura; MR, Juan; Nieves Cabrera Martin, Maria de las; Ortiz, Tomas. Currently Available Neuroimaging Approaches in Alzheimer Disease (AD) Early Diagnosis. InTech, 2011-09-06. ISBN 9789533079936. 
  49. ↑ Engler, Henry; Klunk, William; Nordberg, Agneta; Blomqvist, Gunnar; Holt, Daniel. First PET Study with a Benzothiazol Amyloidimaging Agent (PIB) in Alzheimer’s Disease Patients and Healthy Volunteers. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004, p. 123–137. ISBN 9783642639272. 
  50. ↑ Zhang, Wei; Kung, Mei-Ping; Oya, Shunichi; Hou, Catherine; Kung, Hank F. «18F-labeled styrylpyridines as PET agents for amyloid plaque imaging». Nuclear Medicine and Biology, 34, 1, 2007-01, pàg. 89–97. DOI: 10.1016/j.nucmedbio.2006.10.003. ISSN: 0969-8051.
  51. ↑ Choi, S. R.; Golding, G.; Zhuang, Z.; Zhang, W.; Lim, N. «Preclinical Properties of 18F-AV-45: A PET Agent for A  Plaques in the Brain». Journal of Nuclear Medicine, 50, 11, 16-10-2009, pàg. 1887–1894. DOI: 10.2967/jnumed.109.065284. ISSN: 0161-5505.
  52. ↑ Vandenberghe, Rik; Van Laere, Koen; Ivanoiu, Adrian; Salmon, Eric; Bastin, Christine «18F-flutemetamol amyloid imaging in Alzheimer disease and mild cognitive impairment: A phase 2 trial». Annals of Neurology, 68, 3, 04-08-2010, pàg. 319–329. DOI: 10.1002/ana.22068. ISSN: 0364-5134.
  53. ↑ Rowe, Christopher C; Ackerman, Uwe; Browne, William; Mulligan, Rachel; Pike, Kerryn L «Imaging of amyloid β in Alzheimer's disease with 18F-BAY94-9172, a novel PET tracer: proof of mechanism». The Lancet Neurology, 7, 2, 2008-02, pàg. 129–135. DOI: 10.1016/s1474-4422(08)70001-2. ISSN: 1474-4422.
  54. ↑ Cui, Mengchao; Ono, Masahiro; Watanabe, Hiroyuki; Kimura, Hiroyuki; Liu, Boli «Smart Near-Infrared Fluorescence Probes with Donor–Acceptor Structure for in Vivo Detection of β-Amyloid Deposits». Journal of the American Chemical Society, 136, 9, 20-02-2014, pàg. 3388–3394. DOI: 10.1021/ja4052922. ISSN: 0002-7863.
  55. ↑ Cui, Mengchao; Ono, Masahiro; Watanabe, Hiroyuki; Kimura, Hiroyuki; Liu, Boli «Smart Near-Infrared Fluorescence Probes with Donor–Acceptor Structure for in Vivo Detection of β-Amyloid Deposits». Journal of the American Chemical Society, 136, 9, 20-02-2014, pàg. 3388–3394. DOI: 10.1021/ja4052922. ISSN: 0002-7863.
  56. ↑ Ono, Masahiro; Watanabe, Hiroyuki; Kimura, Hiroyuki; Saji, Hideo «BODIPY-Based Molecular Probe for Imaging of Cerebral β-Amyloid Plaques». ACS Chemical Neuroscience, 3, 4, 17-02-2012, pàg. 319–324. DOI: 10.1021/cn3000058. ISSN: 1948-7193.
  57. ↑ Hajipour, Mohammad Javad; Santoso, Michelle R.; Rezaee, Farhad; Aghaverdi, Haniyeh; Mahmoudi, Morteza «Advances in Alzheimer’s Diagnosis and Therapy: The Implications of Nanotechnology». Trends in Biotechnology, 35, 10, 2017-10, pàg. 937–953. DOI: 10.1016/j.tibtech.2017.06.002. ISSN: 0167-7799.
  58. ↑ Choi, Inhee; Yang, Young In; Jeong, Eunhye; Kim, Kihoon; Hong, Surin «Colorimetric tracking of protein structural evolution based on the distance-dependent light scattering of embedded gold nanoparticles». Chemical Communications, 48, 17, 2012, pàg. 2286. DOI: 10.1039/c2cc17174k. ISSN: 1359-7345.
  59. ↑ Marini, Alberto; Muñoz-Losa, Aurora; Biancardi, Alessandro; Mennucci, Benedetta «What is Solvatochromism?». The Journal of Physical Chemistry B, 114, 51, 03-12-2010, pàg. 17128–17135. DOI: 10.1021/jp1097487. ISSN: 1520-6106.
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