Results 271 to 280 of about 436,505 (303)

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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Protein Aggregation in Congenital Myopathies

Seminars in Pediatric Neurology, 2011
Protein aggregation in congenital myopathies may be encountered among different myofibrillar myopathies such as granulofilamentous myopathy, cytoplasmic body myopathy, or spheroid body myopathy, which are designated as αB crystallinopathy, desminopathy, and myotilinopathy, respectively, according to the respective mutant proteins.
Hans H, Goebel, Astrid, Blaschek
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Protein folding and aggregation in bacteria

Cellular and Molecular Life Sciences, 2010
Proteins might experience many conformational changes and interactions during their lifetimes, from their synthesis at ribosomes to their controlled degradation. Because, in most cases, only folded proteins are functional, protein folding in bacteria is tightly controlled genetically, transcriptionally, and at the protein sequence level.
Raimon, Sabate, Natalia S, de Groot, Salvador, Ventura   +2 more
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Effect of Additives on Protein Aggregation

Current Pharmaceutical Biotechnology, 2009
This paper overviews solution additives that affect protein stability and aggregation during refolding, heating, and freezing processes. Solution additives are mainly grouped into two classes, i.e., protein denaturants and stabilizers. The former includes guanidine, urea, strong ionic detergents, and certain chaotropic salts; the latter includes ...
Hiroyuki, Hamada, Tsutomu, Arakawa, Kentaro, Shiraki   +2 more
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Protein aggregation

International Journal of Biological Macromolecules, 2017
Ipsita, Roy, Boris I, Kurganov
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Mechanisms of Prion Protein Aggregation

Protein & Peptide Letters, 2009
The prion protein is a cell surface glycoprotein that is converted to a protease resistant abnormal isoform during the course of prion disease. The normal isoform of this protein has been shown to be an antioxidant that aids the survival of neurones.
Sarah N, Fontaine, David R, Brown
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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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Aggregated proteins in serum

In Vitro Cellular & Developmental Biology - Animal, 1996
J, Prachar, K, Hlubinova, A, Feldsamova
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Protein Folding and Aggregation

2005
R. A. Broglia, G. Tiana
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Mechanisms and pathology of protein misfolding and aggregation

Nature Reviews Molecular Cell Biology, 2023
Nikolaos Louros, Joost Schymkowitz, Frédéric Rousseau   +2 more
exaly