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Books on the topic 'Amyloid Proteins (Amyloidosis)'

Author: Grafiati

Published: 7 September 2023

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1

Sipe, Jean D. Amyloid proteins: The beta sheet conformation and disease. Weinheim: Wiley-VCH, 2005.

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2

Thomas, Scheibel, ed. Fibrous proteins. Austin, Tex: Landes Bioscience, 2008.

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3

Marina, Ramirez-Alvarado, Kelly Jeffery W, and Dobson C. M, eds. Protein misfolding diseases: Current and emerging principles and therapies. Hoboken, N.J: Wiley, 2010.

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4

Indu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part C. Amsterdam: Elsevier/Academic, 2006.

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5

B, O'Doherty Cian, and Byrne Adam C, eds. Protein misfolding. New York: Nova Science Publishers, 2008.

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6

Indu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part B. Amsterdam: Elsevier/Academic, 2006.

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7

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

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8

Sipe, Jean D. Amyloid Proteins: The Beta Sheet Conformation and Disease. Wiley-VCH, 2005.

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9

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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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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10

Amyloid Proteins Methods And Protocols. Humana Press, 2012.

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11

Mittal, Sajjan. Amyloidosis. Edited by Patrick Davey and David Sprigings. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199568741.003.0181.

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Amyloidosis is a multisystem disease caused by the extracellular deposition of insoluble abnormal fibrils that injure tissues and organs. The fibrils are formed by the aggregation of misfolded, normally soluble proteins. Systemic amyloid light-chain (AL) amyloidosis (primary amyloidosis) is the commonest type of amyloidosis in the developed world, accounting for 80% of cases. The remainder are due to AA amyloidosis (secondary or reactive amyloidosis), familial amyloidosis, or other rare types of amyloidosis. The most common clinical features at diagnosis are nephrotic syndrome, heart failure (typically with predominant right heart failure), sensorimotor and/or autonomic peripheral neuropathy, and hepatosplenomegaly.

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12

Harris, J. Robin. Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease. Springer London, Limited, 2012.

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13

Harris, J. Robin. Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease. Springer, 2012.

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14

Protein Aggregation And Fibrillogenesis In Cerebral And Systemic Amyloid Disease. Springer, 2012.

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15

Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease. Springer Netherlands, 2015.

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16

The nature and origin of amyloid fibrils. Chichester: Wiley, 1996.

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17

The Nature and Origin of Amyloid Fibrils. John Wiley & Sons, 1996.

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18

Eliezer, David. Protein Amyloid Aggregation: Methods and Protocols. Springer New York, 2015.

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19

Eliezer, David. Protein Amyloid Aggregation: Methods and Protocols. Springer New York, 2016.

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20

Roterman-Konieczna, Irena. From Globular Proteins to Amyloids. Elsevier, 2019.

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21

Wetzel, Ronald, and Indu Kheterpal. Amyloid, Prions, and Other Protein Aggregates, Part B. Elsevier Science & Technology Books, 2006.

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22

Amyloid, Prions, and Other Protein Aggregates, Part C, Volume 413 (Methods in Enzymology). Academic Press, 2006.

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23

Biophysical inquiry into protein aggregation and amyloid diseases, 2008. Trivandrum, Kerala, India: Transworld Research Network, 2008.

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24

Wetzel, Ronald, and Indu Kheterpal. Amyloid, Prions, and Other Protein Aggregates, Part C. Elsevier Science & Technology Books, 2006.

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25

(Editor), Ronald Wetzel, and Indu Kheterpal (Editor), eds. Amyloid, Prions, and Other Protein Aggregates, Part C, Volume 413 (Methods in Enzymology). Academic Press, 2006.

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26

Abelson, John N., Ronald Wetzel, and Melvin I. Simon. Amyloid, Prions, and Other Protein Aggregates. Elsevier Science & Technology Books, 1999.

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27

(Editor), Ronald Wetzel, and Indu Kheterpal (Editor), eds. Amyloid, Prions, and Other Protein Aggregates, Part B, Volume 412 (Methods in Enzymology). Academic Press, 2006.

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28

(Editor), Ronald Wetzel, and Indu Kheterpal (Editor), eds. Amyloid, Prions, and Other Protein Aggregates, Part B, Volume 412 (Methods in Enzymology). Academic Press, 2006.

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