Amyloid fibrils from muscle myoglobin

By M. Fändrich, Matthew Fletcher, Christopher M. Dobson. Nature, 2001

763 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/8ee86075c43d3f6ef85c0671d319230a2fb0ee63

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Citations in the corpus

Conformational constraints for amyloid fibrillation: the importance of being unfolded. (2004, background): “However, under destabilizing conditions, where it is in a partially folded intermediate conformation, it will form amyloid fibrils [152].”
Folding proteins in fatal ways (2003, background): “Of particular significance is the finding that globular proteins with diverse sequences that are not currently associated with a protein-folding disease (for example, muscle myoglobin) can undergo aggregation in vitro into fibrils indistinguishable from those found in the amyloidose”
An α-helix to β-barrel domain switch transforms the transcription factor RfaH into a translationfactor (2012, neutral): “Structural interconversion between a helix and b sheet was mainly observed with artificial peptides by varying the solution conditions (Minor and Kim, 1996) or in myoglobin, where it was possible to induce a fold consisting of b strand fibrils into all-a-helical myoglobin under nonnative conditions ”
Principles of protein folding, misfolding and aggregation. (2004, background): “The most direct evidence for the latter statement is that fibrils can be formed by many different proteins that are not associated with disease, including such well-known proteins as myoglobin [56], and also by homopolymers such as polythreonine or polylysine [57].”
Unfolding the role of protein misfolding in neurodegenerative diseases (2003, background): “However, recent studies have shown that many (if not all) proteins can form amyloid-like structures under appropriate condition”
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (2002, background): “Further clues to the molecular basis of amyloid diseases and the biological significance of protein aggregation have been provided by recent observations that a range of proteins not associated with amyloid diseases are able to aggregate in vitro into fibrils indistinguishable from those found in ”
Nanomechanics of functional and pathological amyloid materials. (2011, background): “As such, amyloid nanostructures are increasingly viewed as a general alternative form of protein structure that is different from, but in many cases no less organized than, the native states of protein”