Therapeutic approaches to protein-misfolding diseases

By Fred E. Cohen, J. Kelly. Nature, 2003

810 citations recorded by the source corpus.

Subfields: Cell Biology, Genetics, Nutrition and Dietetics

View Paper: https://www.semanticscholar.org/paper/2ec1b8fb2b91a7bffdc8543f723421acf19a89d2

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In Cell Biology

1. J. Forbes
2. M. Molinari
3. M. Cooper
4. Mark P. Mattson
5. T. Magnus
6. D. Hebert

In Genetics

1. M. Cooper
2. Mark P. Mattson
3. Douglas M. Fowler
4. T. Magnus

Citations in the corpus

• Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism (2006, background): “These approaches include reduction in the production of the amyloidogenic form of proteins, increase in the clearance rate of misfolded or aggregated proteins, increase of the native state stability in amyloidogenic proteins, and direct inhibition of the self-assembly process (3).”
• Functional Amyloid Formation within Mammalian Tissue (2005, background): “The multistep process of amyloidogenesis is linked to a number of diseases, including many resulting in neurodegeneration [5–7].”
• Curli biogenesis and function. (2006, background): “Amyloid fiber formation is traditionally associated with human diseases including Alzheimer's, Parkinson's, and prion diseases; however, curli are part of a growing number of functional amyloids (15).”
• AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides (2007, neutral): “It constitutes the main bottleneck in protein production, narrowing the spectrum of relevant polypeptides obtained by recombinant techniques [3]; it reduces the shelf life and increases the immunogenicity of polypeptidic drugs [4]; and it is associated with an increasing number of critical human dis”
• EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “On basis of the mechanistic studies presented here, we conclude that EGCG and perhaps other polyphenols may have considerable potential as drug candidates for the treatment of neurodegeneration and amyloid diseases [4, 17 ].”
• Mechanisms of diabetic complications. (2013, background): “This suggests the exciting possibility that “protein misfolding” may present a common target for therapeutic intervention in diabetic complications (111).”
• EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity (2010, background): “Chafekar SM, Baas F, Scheper W (2008) Oligomer-specific Abeta toxicity in cell models is mediated by selective uptake.”
• Ageing and neuronal vulnerability (2006, background): “Abnormalities in protein chaperone mechanisms have been documented in studies of several neurodegenerative disorders, in addition to HD, AD, PD and AL”
• Functional amyloid--from bacteria to humans. (2007, background): “Alzheimer’s disease is perhaps the bestknown and most clinically relevant amyloid disease, characterized by neurodegeneration and extracellular amyloidogenesis [5, 6 ].”
• In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, background): “In any case, studies with chemical chaperones offered an important proof of principle and paved the way for characterization of several, substrate-specific pharmacological chaperones that proved efficient in cultured cells or that have already been used in animal and/or clinical trials (22, 58, 232,”