Role of Protein Misfolding and Proteostasis Deficiency in Protein Misfolding Diseases and Aging

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Role of Protein Misfolding and Proteostasis Deficiency in Protein Misfolding Diseases and Aging

The misfolding, aggregation, and tissue accumulation of proteins are common events in diverse chronic diseases, known as protein misfolding disorders. Many of these diseases are associated with aging, but the mechanism for this connection is unknown. Recent evidence has shown that the formation and accumulation of protein aggregates may be a process frequently occurring during normal aging, but...

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Proteostasis impairment in protein-misfolding and -aggregation diseases.

Cells possess an extensive network of components to safeguard proteome integrity and maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines in performance, as may be the case during aging, newly synthesized proteins are no longer able to fold efficiently and metastable proteins lose their functionally active conformations, particularly under conditions of cell...

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Protein Misfolding and Neurodegenerative Diseases

This special issue includes fifteen reviews and two original research articles by leading scientists in the fields of neu-ropathology, biochemistry, and cell biology, dealing with the role of protein aggregation and prion-like propagation of protein misfolding in neurodegenerative diseases. In the review article " Breaking the code of amyloid-í µí»½ oli-gomers, " available at the following link...

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Protein misfolding diseases

Protein misfolding diseases include highly debilitating degenerative disorders like Alzheimer’s and Parkinson’s diseases [1]. The healthcare and financial burden linked to these pathologies has been steadily increasing over the past decade [2]. Actually, there is currently no efficient treatment for misfolding diseases as well as no reliable early diagnostic techniques for them [3]. It is known...

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Protein Misfolding Diseases.

The majority of protein molecules must fold into defined three-dimensional structures to acquire functional activity. However, protein chains can adopt a multitude of conformational states, and their biologically active conformation is often only marginally stable. Metastable proteins tend to populate misfolded species that are prone to forming toxic aggregates, including soluble oligomers and ...

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ژورنال

عنوان ژورنال: International Journal of Cell Biology

سال: 2013

ISSN: 1687-8876,1687-8884

DOI: 10.1155/2013/638083