Книга: Нестареющий мозг
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Глава 4: Как вызвать у себя болезнь Альцгеймера: Учебное пособие
1. Kumar, D. K., et al. Amyloid-beta peptide protects against microbial infection in mouse and worm models of Alzheimer’s disease. Science Translational Medicine 8: 340ra72, doi: 10.1126/scitranslmed.aaf1059 (2016).
2. Kumar, D. K., W. A. Eimer, R. E. Tanzi, and R. D. Moir. Alzheimer’s disease: the potential therapeutic role of the natural antibiotic amyloid-beta peptide. Neurodegenerative Disease Management 6: 345–348, doi: 10.2217/nmt-2016-0035 (2016).
Глава 5: На грани отчаяния: из лаборатории в клинику и обратно
1. https://en.wikipedia.org/wiki/Dependence_receptor.
2. Lourenço, F. C., et al. Netrin-1 interacts with amyloid precursor protein and regulates amyloid-beta production. Cell Death and Differentiation 16: 655–663, doi: cdd2008191 [pii]10.1038/cdd.2008.191 (2009).
3. Galvan, V., et al. Reversal of Alzheimer’s-like pathology and behavior in human APP transgenic mice by mutation of Asp664. Proceedings of the National Academy of Science USA 103: 7130–7135, doi: 10.1073/pnas.0509695103 (2006).
4. Spilman, P., et al. The multi-functional drug tropisetron binds APP and normalizes cognition in a murine Alzheimer’s model. Brain Research 1551: 25–44, doi: 10.1016/j.brainres.2013.12.029 (2014).
5. Там же.
6. Clarkson, T. W., L. Magos, and G. J. Myers. The toxicology of mercury – current exposures and clinical manifestations. New England Journal of Medicine 349: 1731–1737, doi: 10.1056/NEJMra022471 (2003).
Глава 6: Ген Бога и три типа болезни Альцгеймера
1. Mutter, J., A. Curth, J. Naumann, R. Deth, and H. Walach. Does inorganic mercury play a role in Alzheimer’s disease? A systematic review and an integrated molecular mechanism. Journal of Alzheimer’s Disease 22: 357–374, doi:10.3233/JAD-2010-100705 (2010).
Глава 7: «Когноскопия». Что вам угрожает?
1. den Heijer, T., et al. Homocysteine and brain atrophy on MRI of non-demented elderly. Brain 126 (Pt 1): 170–175 (2003).
2. Rocca, W. A., B. R. Grossardt, L. T. Shuster, and E. A. Stewart. Hysterectomy, oophorectomy, estrogen, and the risk of dementia. Neurodegenerative Diseases 10: 175–178, doi: 10.1159/000334764 (2012).
3. Brewer, G. J. Copper excess, zinc deficiency, and cognition loss in Alzheimer’s disease. Biofactors 38: 107–113, doi: 10.1002/biof.1005 (2012).
4. Chausmer, A. B. Zinc, insulin and diabetes. Journal of the American College of Nutrition 17: 109–115 (1998).
5. Liu, G., J. G. Weinger, Z. L. Lu, F. Xue, and S. Sadeghpour. Efficacy and safety of MMFS-01, a synapse density enhancer, for treating cognitive impairment in older adults: a randomized, double-blind, placebo-controlled trial. Journal of Alzheimer’s Disease 49: 971–990, doi: 10.3233/JAD-150538 (2016).
6. Smorgon, C., et al. Trace elements and cognitive impairment: an elderly cohort study. Archives of Gerontology and Geriatrics Supplement 9: 393–402, doi: 10.1016/j.archger.2004.04.050 (2004).
7. Tyler, C. R., and A. M. Allan. The effects of arsenic exposure on neurological and cognitive dysfunction in human and rodent studies: a review. Current Environmental Health Reports 132–147, Report No. 2196-5412 (Electronic) (2014).
8. Basha, M. R., et al. The fetal basis of amyloidogenesis: exposure to lead and latent overexpression of amyloid precursor protein and beta-amyloid in the aging brain. Journal of Neuroscience 25: 823–829, doi: 10.1523/JNEUROSCI.4335-04.2005 (2005).
9. Bakulski, K. M., L. S. Rozek, D. C. Dolinoy, H. L. Paulson, and H Hu. Alzheimer’s disease and environmental exposure to lead: the epidemiologic evidence and potential role of epigenetics. Current Alzheimer Research 9: 563–573 (2012).
10. Ashok A., N. K. Rai, S. Tripathi, and S. Bandyopadhyay. Exposure to As-, Cd-, and Pb-mixture induces Aβ, amyloidogenic APP processing and cognitive impairments via oxidative stress-dependent neuroinflammation in young rats. Toxicological Sciences 143: 64–80, doi: 10.1093/toxsci/kfu208 (2015).
11. Dysken, M. W. et al. Effect of vitamin E and memantine on functional decline in Alzheimer disease: the TEAM-AD VA cooperative randomized trial. Journal of the American Medical Association 311: 33–44, doi:10.1001/jama.2013.282834 (2014).
12. Poole, S., S. K. Singhrao, L. Kesavalu, M. A. Curtis, and S. Crean. Determining the presence of periodontopathic virulence factors in short-term postmortem Alzheimer’s disease brain tissue. Journal of Alzheimer’s Disease 36: 665–677, doi: 10.3233/JAD-121918 (2013).
13. Descamps, O., Q. Zhang, V. John, and D. E. Bredesen. Induction of the C-terminal proteolytic cleavage of AβPP by statins. Journal of Alzheimer’s Disease 25: 51–57, doi: 10.3233/JAD-2011-101857 (2011).
14. Bredesen, D. E. Inhalational Alzheimer’s disease: an unrecognized – and treatable – epidemic. Aging (Albany NY) 8: 304–313 (2016).
Глава 8: Протокол ReCODE: восстановление когнитивных функций
1. Heijer, T., et al. Association between blood pressure levels over time and brain atrophy in the elderly. Neurobiology of Aging 24: 307–313 (2003).
2. http://.
3. Khan, A., M. Safdar, M. M. Ali Khan, K. N. Khattak, and R. A. Anderson. Cinnamon improves glucose and lipids of people with type 2 diabetes. Diabetes Care 26: 3215–3218 (2003).
4. .
6. learn/resources/probiotics-five-core-species.
7. Thrasher, J. D., M. R. Gray, K. H. Kilburn, D. P. Dennis, and A. Yu. A water-damaged home and health of occupants: a case study. Journal of Environmental and Public Health 2012, doi: 10.1155/2012/312836 (2012).
8. -Physicians-Shoemaker-Protocol
9. practitioner_search.aspx?id=117.
10. Shoemaker, R. C., MD. Surviving Mold: Life in the Era of Dangerous Buildings. Otter Bay Books, 2010.
Приложение D
1. Galvan, V., et al. Reversal of Alzheimer’s-like pathology and behavior in human APP transgenic mice by mutation of Asp664. Proceedings of the National Academy of Science USA 103: 7130–7135, doi:10.1073/pnas.0509695103 (2006).
2. Там же.
3. Theendakara, V., et al. Neuroprotective sirtuin ratio reversed by ApoE4. Proceedings of the National Academy of Science USA 110: 18303–18308, doi: 10.1073/pnas.1314145110 (2013).
4. Lourenзo, F. C., et al. Netrin-1 interacts with amyloid precursor protein and regulates amyloid-beta production. Cell Death and Differentiation 16: 655–663, doi: cdd2008191 [pii]10.1038/cdd.2008.191 (2009).
5. Lu, D. C., et al. A second cytotoxic proteolytic peptide derived from amyloid-beta-protein precursor. Nature Medicine 6: 397–404, doi:10.1038/74656 (2000).
6. Spilman, P., B. Jagodzinska, D. E. Bredesen, and John Varghese. Enhancement of sAPPα as a therapeutic strategy for Alzheimer’s and other neurodegenerative diseases. HSOA Journal of Alzheimer’s & Neurodegenerative Diseases 1: 1–10 (2015).
7. Spilman, P. R., et al. Netrin-1 interrupts amyloid-beta amplification, increases sAβPPα in vitro and in vivo, and improves cognition in a mouse model of Alzheimer’s disease. Journal of Alzheimer’s Disease 52: 223–242, doi: 10.3233/JAD-151046 (2016).
8. Julien, O., et al. Unraveling the mechanism of cell death induced by chemical fibrils. Nature Chemical Biology 10: 969–976, doi: 10.1038/nchembio.1639 (2014).
9. Matrone, C., et al. Activation of the amyloidogenic route by NGF deprivation induces apoptotic death in PC12 cells. Journal of Alzheimer’s Disease 13: 81–96 (2008).
10. Bredesen, D. E. Reversal of cognitive decline: A novel therapeutic program. Aging 6: 707–717, doi: 10.18632/aging.100690 (2014).
11. Bredesen, D. E., et al. Reversal of cognitive decline in Alzheimer’s disease. Aging 8: 1250–1258, doi: 10.18632/aging.100981 (2016).
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