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1

Masters, C. L., K. Beyreuther, M. Trillet, and Y. Christen, eds. Amyloid Protein Precursor in Development, Aging and Alzheimer’s Disease. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-01135-5.

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2

The structure and function of Alzheimer's amyloid beta proteins. Austin: R.G. Landes, 1994.

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3

1924-, Kameyama Masakuni, ed. [Beta]-amyloid precursor proteins and neurotransmitter function: Proeedings of the eighth Workshop on Neurotransmitters and Diseases, Tokyo, June 1, 1991. Amsterdam, The Netherlands: Excerpta Medica, 1991.

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4

Page, Deaglan. Spatial learning deficits in rats carrying the Swedish mutation for amyloid precursor protein overexpression as a model for Alzheimer's disease. (s.l: The Author), 2001.

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5

Dowler, Brynn C. Endocytosis: Structural components, functions, and pathways. New York: Nova Biomedical Books, 2010.

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6

Tanzi, Rudolph E. Decoding darkness: The search for the genetic causes of Alzheimer's disease. Cambridge, Mass: Perseus Publishing, 2000.

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7

Tanzi, Rudolph E. Decoding darkness: The search for the genetic causes of Alzheimer's disease. Cambridge, Mass: Perseus Pub., 2000.

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8

B, Parson Ann, ed. Decoding darkness: The search for the genetic causes of Alzheimer's disease. Cambridge, Mass: Perseus Publ., 2000.

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9

L, Masters Colin, and Colloque médecine et recherche (9th : 1993 : Lyon, France), eds. Amyloid protein precursor in development, aging, and Alzheimer's disease. Berlin: Springer-Verlag, 1994.

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10

Sekoulidis, Joannis. Transgenic analysis of the Alzheimer's disease amyloid precursor protein (APP). 2004.

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11

M, Nitsch Roger, and International Study Group on the Pharmacology of Memory Disorders Associated with Aging. Meeting, eds. Alzheimer's disease: Amyloid precursor proteins, signal transduction, and neuronal transplantation. New York, N.Y: New York Academy of Sciences, 1993.

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12

1936-, Wurtman Richard J., and Study Group on the Pharmacology of Memory Disorders Associated with Aging. Meeting, eds. The Neurobiology of Alzheimer's disease. New York, N.Y: New York Academy of Sciences, 1996.

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13

BACE: Lead target for orchestrated therapy of Alzheimer's disease. Hoboken, N.J: John Wiley & Sons, 2010.

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14

(Editor), K. Beyreuther, Y. Christen (Editor), and C. L. Masters (Editor), eds. Neurodegenerative Disorders: Loss of Function Through Gain of Function (Research and Perspectives in Alzheimer's Disease). Springer, 2001.

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15

Christian, Haass, ed. Molecular biology of Alzheimer's disease: Genes and mechanisms involved in amyloid generation. Amsterdam: Harwood Academic Publishers, 1998.

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16

A, Nixon Ralph, Banner Carl D. B, and New York Academy of Sciences., eds. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York: NewYork Academy of Sciences, 1992.

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17

1936-, Wurtman Richard J., and New York Academy of Sciences., eds. The neurobiology of Alzheimer's disease: Edited by Richard J. Wurtman ... [et al.]. New York: New York Academy of Sciences, 1996.

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18

B, Banner Carl D., and Nixon Ralph A, eds. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York, N.Y: New York Academy of Sciences, 1992.

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19

Growdon, John H., and Roger M. Nitsch. Alzheimer's Disease: Amyloid Precursor Proteins, Signal Transduction, and Neuronal Transplantation (Annals of the New York Academy of Sciences). New York Academy of Sciences, 1993.

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20

Growdon, John H., and Roger M. Nitsch. Alzheimer's Disease: Amyloid Precursor Proteins, Signal Transduction, and Neuronal Transplantation (Annals of the New York Academy of Sciences, Vol). New York Academy of Sciences, 1993.

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21

M, Hooper N., ed. Alzheimer's disease: Methods and protocols. Totowa, N.J: Humana Press, 2000.

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22

(Editor), D. J. Selkoe, and Y. Christen (Editor), eds. Immunization Against Alzheimer's Disease and Other Neurodegenerative Disorders (Research and Perspectives in Alzheimer's Disease). Springer, 2004.

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23

Chen, Shiouh-Yi. Neuropathology of beta-amyloid peptide (25-35). 1995.

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24

Abeta Peptide and Alzheimer's Disease: Celebrating a Century of Research. Springer, 2006.

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25

(Editor), Robin Harris, and Falk Fahrenholz (Editor), eds. Alzheimer's Disease: Cellular and Molecular Aspects of Amyloid beta (Subcellular Biochemistry). Springer, 2004.

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26

V.M.-Y. Lee (Editor), J. Q. Trojanowski (Editor), L. Buee (Editor), and Y. Christen (Editor), eds. Fatal Attractions: Protein Aggregates in Neurodegenerative Disorders (Research and Perspectives in Alzheimer's Disease). Springer, 2000.

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27

Saido, Takaomi. A-Beta Metabolism and Alzheimer's Disease. Landes Bioscience, 2003.

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28

Alzheimers Disease Insights Into Low Molecular Weight And Cytotoxic Aggregates From In Vitro And Computer Experiments Molecular Basis Of Amyloidbeta Protein Aggregation And Fibril Formation. Imperial College Press, 2011.

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29

Alzheimer's Disease: A Compendium of Current Theories (Annals of the New York Academy of Sciences). New York Academy of Sciences, 2001.

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30

C, Dowler Brynn, ed. Endocytosis: Structural components, functions, and pathways. Hauppauge, N.Y: Nova Science Publishers, 2010.

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31

Tanzi, Rudolph E., Rudolph Tanzi, and Ann B. Parson. Decoding Darkness: The Search for the Genetic Causes of Alzheimer's Disease. Basic Books, 2001.

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32

Lachmann, Helen J., and Giampaolo Merlini. The patient with amyloidosis. Edited by Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0152.

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Abstract:
Amyloidosis is a disorder of protein folding in which normally soluble plasma proteins are deposited in the extracellular space in an abnormal insoluble fibrillar form. The process of amyloid formation and deposition causes cytotoxicity and progressive organ dysfunction. Amyloid is remarkably diverse and can be hereditary or acquired, localized or systemic, and lethal or merely an incidental finding. The most important numerically are AL amyloidosis, in which the fibrils are composed of monoclonal immunoglobulin light chains, and AA amyloidosis, in which the acute phase reactant Serum Amyloid A component forms the fibrils.The kidney is involved in 75% of patients with systemic amyloidosis. Heavy proteinuria or nephrotic syndrome is characteristic of most amyloid variants.Without treatment, systemic disease is usually fatal but measures that reduce the supply of amyloid fibril precursor proteins can result in regression of amyloid deposits, prevention of organ failure, and improved quality of life and survival. Early diagnosis, before irreversible organ damage has occurred, is the key to effective treatment. Recent advances in diagnosis and therapy have much improved the outlook of patients with AL amyloidosis, but agents with broader promise are under investigation.
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