Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

By M. Stefani, Christopher M. Dobson. Journal of molecular medicine, 2003

1,657 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/02996ccedfa9c2d0d6ebb0641e017b38dca7457d

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Citations in the corpus

Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. (2005, background): “An additional term representing the stability of the native state can in principle be included to extend the approach to proteins that aggregate from a predominantly globular state, as is the case, for example, in the systemic amyloidoses associated with lysozyme and transthyretin.(10) Moreover, and”
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides (2007, positive): “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”
Towards an Understanding of the Temperature/ Pressure Configurational and Free-Energy Landscape of Biomolecules (2007, positive): “Meanwhile, a large body of literature has shown that the ability of polypeptide chains to form such structures is common, and indeed can be considered a generic feature of polypeptide chains and the thermodynamic parameters of their environment [115, 117, 118].”
Protein folding and misfolding (2003, background): “However, it is likely that the relatively disorganized prefibrillar aggregates are also harmful to cells, probably through a less specific mechanism, for example as a result of the exposure of non-native hydrophobic surfaces stimulating aberrant interactions with cell membranes or other cellular com”
New Aspects of the α-Helix to β-Sheet Transition in Stretched Hard α-Keratin Fibers (2004, background): “More recently, the discovery of harsh human diseases related to the irreversible structural transition of a-helices to b-sheets (Stefani and Dobson, 2003; Zanusso et al., 2001) has given a new impetus to the study of the a/b transition.”
Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution (2008, positive): “What is the nature of the fitness cost imposed by misfolding? Misfolded proteins manifest fitness costs unrelated to their function—such costs may involve direct toxicity, such as disruption of membrane integrity or inappropriate interactions with other cellular components (Stefani and Dobson, 2003)”
Principles of protein folding, misfolding and aggregation. (2004, background): “The answer is almost certainly that under normal circumstances the molecular chaperones and other “housekeeping” mechanism are remarkably efficient in ensuring that such potentially toxic species are neutralised[34,83].”
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011, background): “However, in a growing number of diseases, misfolding and aggregation results predominantly in a toxic gain of function (Stefani and Dobson, 2003; Winklhofer et al., 2008).”