The amyloid state and its association with protein misfolding diseases

By Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson. Nature reviews. Molecular cell biology, 2014

977 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/2032b1581350a6c8230306d7354c713ccef169b2

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Citations in the corpus

The Amyloid-β Pathway in Alzheimer’s Disease (2021, background): “In this regard, protein solubility has emerged as a critical aspect of protein homeostasis as proteins generally evolved to maintain the solubility required for their optimal function [157, 158].”
Intrinsically Disordered Proteins Studied by NMR Spectroscopy (2015, background): “Intrinsically disordered proteins (IDPs) play crucial roles in many aspects of molecular and cell biology, as these proteins are involved in a variety of signalling and regulation processes as well as being implicated in a range of neurodegenerative and systemic disorders such as Alzheimer’s and Par”
EHRA/HRS/APHRS/SOLAECE expert consensus on atrial cardiomyopathies: definition, characterization, and clinical implication. (2016, neutral): “For organ-specific amyloidosis such as Alzheimer’s disease, there is no detectable correlation between quantity of fibrillar deposits and disease advancement.(85) Rather, disease phenotype correlates most closely with accumulation of soluble, prefibrillar protein aggregates.”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “As well as primary nucleation and fibril elongation, a number of secondary processes can be important in the kinetics of molecular self-assembly (32, 135, 139).”
Random-phase-approximation theory for sequence-dependent, biologically functional liquid-liquid phase separation of intrinsically disordered proteins (2016, background): “Droplets of these IDP-rich phase are fundamentally different from amyloids [16,37] and condensed phases of folded globular proteins [38–44].”
Structured states of disordered proteins from genomic sequences (2016, positive): “…are typically based on sequence bias that has in turn been learnt from experimental evidence from CD or NMR spectra (Alexander et al., 2009; Knowles et al., 2014; Mittag et al., 2008; Sambashivan et al., 2005; Tokuriki and Tawfik, 2009; Tompa, 2002; Uversky and Dunker, 2010; Wells et al.,…”