Results 261 to 270 of about 287,910 (304)
Cellular Protein Aggregates: Formation, Biological Effects, and Ways of Elimination
International Journal of Molecular Sciences, 2023 The accumulation of protein aggregates is the hallmark of many neurodegenerative diseases. The dysregulation of protein homeostasis (or proteostasis) caused by acute proteotoxic stresses or chronic expression of mutant proteins can lead to protein ...
Xiang-Hong He +2 more
exaly +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Clinical Chemistry and Laboratory Medicine, 2001
Protein aggregation occurs in vivo as a result of improper folding or misfolding. Diverse diseases arise from protein misfolding and are now grouped under the term "protein conformational diseases", including most of the neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, the prion encephalopathies and Huntington's disease, as
MERLINI, GIAMPAOLO +6 more
openaire +3 more sources
Protein aggregation occurs in vivo as a result of improper folding or misfolding. Diverse diseases arise from protein misfolding and are now grouped under the term "protein conformational diseases", including most of the neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, the prion encephalopathies and Huntington's disease, as
MERLINI, GIAMPAOLO +6 more
openaire +3 more sources
Protein aggregation and prionopathies
Pathologie Biologie, 2014Prion protein and prion-like proteins share a number of characteristics. From the molecular point of view, they are constitutive proteins that aggregate following conformational changes into insoluble particles. These particles escape the cellular clearance machinery and amplify by recruiting the soluble for of their constituting proteins.
M, Renner, R, Melki
openaire +2 more sources
Mechanisms of Protein Aggregation
Current Pharmaceutical Biotechnology, 2009Aggregation or reversible self-association of protein therapeutics can arise through a number of different mechanisms. Five common aggregation mechanisms are described and their relations to manufacturing processes to suppress and remove aggregates are discussed.
John S, Philo, Tsutomu, Arakawa
openaire +2 more sources
Protein Misfolding and Aggregation
Biotechnology Progress, 2008Interest in the problem of protein misfolding and aggregation has exploded in recent years for two reasons: (1) the sharp rise in the number and volume of therapeutic proteins produced commercially and (2) the recognition of the central role of protein aggregates in degenerative diseases.
Regina M, Murphy, Brent S, Kendrick
openaire +2 more sources
Protein Denaturation and Aggregation
Annals of the New York Academy of Sciences, 2006Abstract: 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 ...
openaire +2 more sources
Physicochemical Principles of Protein Aggregation
2013This 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.
openaire +2 more sources
Aggregate Formation and the Structure of the Aggregates of Disulfide-Reduced Proteins
Journal of Protein Chemistry, 2002Aggregate 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 +2 more
openaire +2 more sources
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 theBahareh, Dabirmanesh +2 more
openaire +2 more sources
Reversal of Protein Aggregation Provides Evidence for Multiple Aggregated States
Journal of Molecular Biology, 2005Observations 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. +5 more
openaire +4 more sources