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Fingerprinting disease-derived protein aggregates reveals unique signature of Motor Neuron Disease

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Cox D   +9 more
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Influenza A virus propagation requires the activation of the unfolded protein response and the accumulation of insoluble protein aggregates. [PDF]

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Marques M   +13 more
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Protein Aggregation

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
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Protein aggregation and prionopathies

Pathologie Biologie, 2014
Prion 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
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Mechanisms of Protein Aggregation

Current Pharmaceutical Biotechnology, 2009
Aggregation 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
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Protein Misfolding and Aggregation

Biotechnology Progress, 2008
Interest 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
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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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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   +2 more
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