Sep 19, 2013 · Cross-seeding processes may provide a mechanistic explanation for various observations in distinct diseases, including: i) the simultaneous presence of different misfolded proteins in one disease; ii) the coexistence of more than one PMD in the same individual; iii) the epidemiological observation that one PMD may be a risk factor for development of a second PMD; and iv) the …
Citation: Morales R, Moreno-Gonzalez I, Soto C (2013) Cross-Seeding of Misfolded Proteins: Implications for Etiology and Pathogenesis of Protein Misfolding Diseases.
Morales, R., Moreno-Gonzalez, I., & Soto, C. (2013). Cross-Seeding of Misfolded Proteins: Implications for Etiology and Pathogenesis of Protein Misfolding Diseases.
Misfolded proteins exist in cells together with unfolded, intermediately folded, and correctly folded species . In healthy cells, misfolded proteins are either degraded or refolded correctly by chaperone proteins that are involved in protein folding and trafficking as well as intermediate stabilization .
Morales R, Moreno-Gonzalez I, Soto C. Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. PLoS Pathog. 2013;9(9):e1003537.PubMed Google Scholar Crossref
misfolded and cellular forms of prion proteins from different species, leading to cross-seeding of prion protein aggregation.12,13 Understanding the molecular mechanism underlying the cross-seeding aggregation of prion protein could pave the way to elucidating the pathology of …
Diverse human diseases, including various neurodegenerative disorders and systemic amyloidoses, are thought to result from the misfolding and aggregation of disease-causative proteins either intracellularly, extracellularly or both, and thus are collectively called protein misfolding diseases .
All-atom Simulation of Amyloid Aggregates R. Morales, I. Moreno-Gonzalez, C. SotoCross-Seeding of Misfolded Proteins: Implications for Etiology and Pathogenesis of Protein Misfolding Diseases. PLoS Pathog, 9 (2013), p. 4.
Some of the most prevalent human degenerative diseases appear as a result of the misfolding and aggregation of proteins. Compelling evidence suggest that misfolded protein aggregates play an important role in cell dysfunction and tissue damage, leading to the disease.
Alzheimer’s disease is the most common neurodegenerative disease leading to dementia in the elderly, mostly affecting individuals over 65 years old. The deficient knowledge about Alzheimer’s etiology and the implication of risk factors in the onset and progression of the disease makes its …
Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. Morales, R.,Moreno-Gonzalez, I.,Soto, C. De novo induction of amyloid-β …
Pathophysiology. In most, if not all proteopathies, a change in 3-dimensional folding (conformation) increases the tendency of a specific protein to bind to itself. In this aggregated form, the protein is resistant to clearance and can interfere with the normal capacity of the affected organs.
A missense mutation in that protein, R345W, causes Malattia Leventinese, an autosomal dominant macular degeneration (Stone et al. 1999). Additionally, in a knockin mouse ROLE OF MISFOLDED PROTEINS IN DISEASES OF THE INNER RETINA. Retinal Involvement in Systemic Protein Misfolding Diseases.
Published in: Cold Spring Harbor Perspectives in Biology · 2011Authors: Radouil Tzekov · Linda Stein · Shalesh KaushalAffiliation: Umass Memorial Health CareAbout: Retinal degeneration · Homeostasis · Protein folding · Rhodopsin · Alzheimer’s disease
Morales R, Moreno-Gonzalez I, Soto C (2013) Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. PLOS 9: e1003537. 43.