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Physicochemical Principles of Protein Aggregation

2013
This chapter provides a theoretical framework on the quantitative description of protein aggregation. The reader is provided with an overview of the fundamental theory of linear and helical polymers, as well as an introduction on the parameters governing evolution of aggregates over time.
Bolognesi B., Tartaglia G. G.
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Protein Denaturation and Aggregation

Annals of the New York Academy of Sciences, 2006
Abstract: Protein aggregation is a prominent feature of many neurodegenerative diseases, such as Alzheimer's, Huntington's, and Parkinson's diseases, as well as spongiform encephalopathies and systemic amyloidoses. These diseases are sometimes called protein misfolding diseases, but the latter term begs the question of what is the “folded” state of ...
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Protein aggregation: An overview

In order for an ordered protein to perform its specific function, it must have a specific molecular structure. Information about this structure is encoded in the protein's amino acid sequence. The unique functional state is achieved as a result of a specific process, known as protein folding. However, as a result of partial or complete unfolding of the
Bahareh, Dabirmanesh, Khosro, Khajeh, Vladimir N, Uversky   +2 more
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Aggregate Formation and the Structure of the Aggregates of Disulfide-Reduced Proteins

Journal of Protein Chemistry, 2002
Aggregate formation and the structure of the aggregates of disulfide-reduced proteins were investigated using alpha-lactalbumin and lysozyme as model proteins. First, reducing conditions were adjusted so that only one of the four disulfide bonds present in each native protein was cleaved.
Kenji, Takase, Takahiko, Higashi, Toshihiro, Omura   +2 more
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Reversal of Protein Aggregation Provides Evidence for Multiple Aggregated States

Journal of Molecular Biology, 2005
Observations that prefibrillar aggregates from different amyloidogenic proteins can be solubilised under some conditions have raised questions as to the generality of this phenomenon and the nature of the factors that influence it. By studying aggregates formed from human muscle acylphosphatase (AcP) under mild denaturing conditions, and by using a ...
CALAMAI M., CANALE C., RELINI A., STEFANI, MASSIMO, CHITI, FABRIZIO, DOBSON C. M.   +5 more
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Prediction of protein aggregation

The scientific community is very interested in protein aggregation because of its involvement in several neurodegenerative diseases and its significance in industry. Remarkably, fibrillar aggregates are utilized naturally for constructing structural scaffolds or creating biological switches and may be intentionally designed to construct versatile ...
Kavyan, Khalili, Farnoosh, Farzam, Bahareh, Dabirmanesh, Khosro, Khajeh   +3 more
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DNAJ Proteins and Protein Aggregation Diseases

Current Topics in Medicinal Chemistry, 2013
Many neurodegenerative diseases are late onset diseases, associated with aggregation of proteins, implying that aged cells are more susceptible to proteotoxic stress. It is known that with aging, there is a decline in the functionality of chaperone networks and on the other hand, accumulation of damaged proteins occurs.
Vaishali, Kakkar, Louis C B, Prins, Harm H, Kampinga   +2 more
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Molecular simulation of protein aggregation

Biotechnology and Bioengineering, 2006
AbstractComputer simulation offers unique possibilities for investigating molecular‐level phenomena difficult to probe experimentally. Drawing from a wealth of studies concerning protein folding, computational studies of protein aggregation are emerging.
Dusan, Bratko, Troy, Cellmer, John M, Prausnitz, Harvey W, Blanch   +3 more
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Protein aggregation

International Journal of Biological Macromolecules, 2017
Ipsita, Roy, Boris I, Kurganov
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Neurodegenerative disorders of protein aggregation

Neurochemistry International, 2003
In recent years, it has become increasingly clear that many neurodegenerative diseases involve aggregation and deposition of misfolded proteins such as amyloid beta, tau, alpha-synuclein and polyglutamine containing proteins. This abnormal deposition of misfolded proteins produce malfunctioning of a distinctive set of neurons.
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