Functional amyloid--from bacteria to humans.
By Douglas M. Fowler, Atanas V. Koulov, William E. Balch, J. Kelly. TIBS -Trends in Biochemical Sciences. Regular ed, 2007
1,029 citations recorded by the source corpus.
Subfields: Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/c59560937d38304062604935b1599832dd3444fa
How researchers see this paper
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In Molecular Biology
- Christopher M. Dobson
- Michele Vendruscolo
- Tuomas P. J. Knowles
- R. Tycko
- A. Paravastu
- Richard Leapman
- S. Koide
- Matthew Biancalana
In Physiology
- Christopher M. Dobson
- Michele Vendruscolo
- Tuomas P. J. Knowles
- A. Paravastu
- Richard Leapman
- R. Tycko
- Wai-Ming Yau
- S. Linse
Citations in the corpus
- Molecular mechanisms of protein aggregation from global fitting of kinetic models (2016, methodology): “As of the time of publication, the software includes equations describing the aggregation of proteins into linear assemblies, motivated by the prevalence of amyloid fibrils in numerous diseases 1,9 as well as the functional roles of linear protein filaments 10,21 .”
- Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010, background): “Interestingly, the cross-β architecture is also shared by “functional amyloids” that play key roles in bacterial, fungal, and animal cells [19,20].”
- EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “Functionally, it is implicated in numerous physiological processes such as epigenetic inheritance, long-term memory or melanosome biogenesis [ 5 ].”
- The amyloid state and its association with protein misfolding diseases (2014, background): “Paired betasheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy.”
- Amyloid fibers provide structural integrity to Bacillus subtilis biofilms (2010, background): “However, “functional amyloids” that participate in normal biological processes in bacteria, fungi, insects, invertebrates and humans have begun to be appreciated (15).”
- Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, background): “Amyloid formation and deposition are associated with numerous human diseases, notably Alzheimer’s disease, as well as certain biological functions (1, 2).”